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Conserved domains on  [gi|1039741915|ref|XP_017170692|]
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cyclin-dependent kinase-like 1 isoform X1 [Mus musculus]

Protein Classification

cyclin-dependent kinase-like( domain architecture ID 10167602)

cyclin-dependent kinase-like (CDKL) is a serine/threonine-protein kinase that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; contains a [NKR]KIAxRE motif that seems to be a cyclin-binding region

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
2-287 0e+00

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 636.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd07847     1 EKYEKLSKIGEGSYGVVFKCRNRETGQIVAIKKFVESEDDPVIKKIALREIRMLKQLKHPNLVNLIEVFRRKRKLHLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDY 161
Cdd:cd07847    81 YCDHTVLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTGPGDDYTDY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 162 VATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDLIPRHQQVFSMNQYFSGVKIP 241
Cdd:cd07847   161 VATRWYRAPELLVGDTQYGPPVDVWAIGCVFAELLTGQPLWPGKSDVDQLYLIRKTLGDLIPRHQQIFSTNQFFKGLSIP 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1039741915 242 DPEDMETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07847   241 EPETREPLESKFPNISSPALSFLKGCLQMDPTERLSCEELLEHPYF 286
 
Name Accession Description Interval E-value
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
2-287 0e+00

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 636.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd07847     1 EKYEKLSKIGEGSYGVVFKCRNRETGQIVAIKKFVESEDDPVIKKIALREIRMLKQLKHPNLVNLIEVFRRKRKLHLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDY 161
Cdd:cd07847    81 YCDHTVLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTGPGDDYTDY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 162 VATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDLIPRHQQVFSMNQYFSGVKIP 241
Cdd:cd07847   161 VATRWYRAPELLVGDTQYGPPVDVWAIGCVFAELLTGQPLWPGKSDVDQLYLIRKTLGDLIPRHQQIFSTNQFFKGLSIP 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1039741915 242 DPEDMETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07847   241 EPETREPLESKFPNISSPALSFLKGCLQMDPTERLSCEELLEHPYF 286
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
4-287 3.66e-103

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 303.68  E-value: 3.66e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915    4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRfLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYC 83
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKV-IKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   84 DHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTdYVA 163
Cdd:smart00220  80 EGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLTT-FVG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  164 TRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLY-LIRKtlgdliprhqqvfsmnqyfsgvkiPD 242
Cdd:smart00220 159 TPEYMAPEVLLG-KGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFkKIGK------------------------PK 213
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1039741915  243 PEDMEtlelKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:smart00220 214 PPFPP----PEWDISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
4-287 1.66e-78

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 239.45  E-value: 1.66e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYC 83
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 DHTVLHELDRYQRGVPEPLVKNITWQTLQAVNfchkhncihrdvkpenilitkqsaiklcdfgfarlltgPGDYYTDYVA 163
Cdd:pfam00069  81 EGGSLFDLLSEKGAFSEREAKFIMKQILEGLE--------------------------------------SGSSLTTFVG 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 164 TRWYRSPELLvGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKtlgdliprhqqvfsmnqyfsgvkipdp 243
Cdd:pfam00069 123 TPWYMAPEVL-GGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIID--------------------------- 174
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1039741915 244 eDMETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:pfam00069 175 -QPYAFPELPSNLSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
1-294 1.96e-78

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 242.42  E-value: 1.96e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRF-LETEDDPViKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLV 79
Cdd:PLN00009    1 MDQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIrLEQEDEGV-PSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  80 FEYCDHTVLHELDRYQRGVPEP-LVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQS-AIKLCDFGFARLLTGPGDY 157
Cdd:PLN00009   80 FEYLDLDLKKHMDSSPDFAKNPrLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTnALKLADFGLARAFGIPVRT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 158 YTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGdlIPRHQQ---VFSMNQY 234
Cdd:PLN00009  160 FTHEVVTLWYRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRILG--TPNEETwpgVTSLPDY 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 235 FSGVKIPDPEDMETLelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYFDSIREVG 294
Cdd:PLN00009  238 KSAFPKWPPKDLATV---VPTLEPAGVDLLSKMLRLDPSKRITARAALEHEYFKDLGDAP 294
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
3-283 1.78e-55

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 188.30  E-value: 1.78e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFL-ETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:COG0515     8 RYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRpELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVME 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDY 161
Cdd:COG0515    88 YVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTQTGT 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 162 VA-TRWYRSPELLVGDtQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDqlyLIRKTLGDLIPRHQQVfsmnqyfsgvkI 240
Cdd:COG0515   168 VVgTPGYMAPEQARGE-PVDPRSDVYSLGVTLYELLTGRPPFDGDSPAE---LLRAHLREPPPPPSEL-----------R 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1039741915 241 PD-PEDMETLelkfpnisysalgfLKGCLHMDPAERL-TCEQLLQ 283
Cdd:COG0515   233 PDlPPALDAI--------------VLRALAKDPEERYqSAAELAA 263
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
4-208 1.88e-21

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 95.25  E-value: 1.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRnrDT--GQIVAIKRfLETE--DDPV-IKKIaLREIRMLKQLKHPNLVNLLEVFRRKRRLHL 78
Cdd:NF033483    9 YEIGERIGRGGMAEVYLAK--DTrlDRDVAVKV-LRPDlaRDPEfVARF-RREAQSAASLSHPNIVSVYDVGEDGGIPYI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYY 158
Cdd:NF033483   85 VMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARALSSTTMTQ 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039741915 159 TDYV-ATRWYRSPELLVG---DTQygppVDVWAIGCVFAELLSGVPLWPGKSDV 208
Cdd:NF033483  165 TNSVlGTVHYLSPEQARGgtvDAR----SDIYSLGIVLYEMLTGRPPFDGDSPV 214
 
Name Accession Description Interval E-value
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
2-287 0e+00

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 636.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd07847     1 EKYEKLSKIGEGSYGVVFKCRNRETGQIVAIKKFVESEDDPVIKKIALREIRMLKQLKHPNLVNLIEVFRRKRKLHLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDY 161
Cdd:cd07847    81 YCDHTVLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTGPGDDYTDY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 162 VATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDLIPRHQQVFSMNQYFSGVKIP 241
Cdd:cd07847   161 VATRWYRAPELLVGDTQYGPPVDVWAIGCVFAELLTGQPLWPGKSDVDQLYLIRKTLGDLIPRHQQIFSTNQFFKGLSIP 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1039741915 242 DPEDMETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07847   241 EPETREPLESKFPNISSPALSFLKGCLQMDPTERLSCEELLEHPYF 286
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
2-287 0e+00

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 529.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd07833     1 NKYEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKESEDDEDVKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGD-YYTD 160
Cdd:cd07833    81 YVERTLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTARPAsPLTD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 YVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDLIPRHQQVFSMNQYFSGVKI 240
Cdd:cd07833   161 YVATRWYRAPELLVGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLYLIQKCLGPLPPSHQELFSSNPRFAGVAF 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1039741915 241 PDPEDMETLELKFPNI-SYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07833   241 PEPSQPESLERRYPGKvSSPALDFLKACLRMDPKERLTCDELLQHPYF 288
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
2-287 8.73e-158

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 443.79  E-value: 8.73e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd07846     1 EKYENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMVKKIAMREIKMLKQLRHENLVNLIEVFRRKKRWYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDY 161
Cdd:cd07846    81 FVDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 162 VATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDLIPRHQQVFSMNQYFSGVKIP 241
Cdd:cd07846   161 VATRWYRAPELLVGDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIIKCLGNLIPRHQELFQKNPLFAGVRLP 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1039741915 242 DPEDMETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07846   241 EVKEVEPLERRYPKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEFF 286
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
4-287 1.37e-115

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 336.38  E-value: 1.37e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRF-LETEDDPvIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd07829     1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIrLDNEEEG-IPSTALREISLLKELKHPNIVKLLDVIHTENKLYLVFEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYV 162
Cdd:cd07829    80 CDQDLKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAFGIPLRTYTHEV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 163 ATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLG----------DLIPRHQQVFSMN 232
Cdd:cd07829   160 VTLWYRAPEILLGSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIFQILGtpteeswpgvTKLPDYKPTFPKW 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039741915 233 QYfsgvkipdpedmETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07829   240 PK------------NDLEKVLPRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
4-287 5.15e-108

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 316.10  E-value: 5.15e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLEtedDPVIKKIALREIRMLKQLK----HPNLVNLLEVFRRK--RRLH 77
Cdd:cd05118     1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKN---DFRHPKAALREIKLLKHLNdvegHPNIVKLLDVFEHRggNHLC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  78 LVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQ-SAIKLCDFGFARLLTGPgd 156
Cdd:cd05118    78 LVFELMGMNLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLElGQLKLADFGLARSFTSP-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 157 YYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGdliprhqqvfsmnqyfs 236
Cdd:cd05118   156 PYTPYVATRWYRAPEVLLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRLLG----------------- 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 237 gvkipdPEDmetlelkfpnisysALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd05118   219 ------TPE--------------ALDLLSKMLKYDPAKRITASQALAHPYF 249
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
4-287 3.66e-103

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 303.68  E-value: 3.66e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915    4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRfLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYC 83
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKV-IKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   84 DHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTdYVA 163
Cdd:smart00220  80 EGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLTT-FVG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  164 TRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLY-LIRKtlgdliprhqqvfsmnqyfsgvkiPD 242
Cdd:smart00220 159 TPEYMAPEVLLG-KGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFkKIGK------------------------PK 213
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1039741915  243 PEDMEtlelKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:smart00220 214 PPFPP----PEWDISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
4-287 1.28e-102

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 303.30  E-value: 1.28e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRF---LETEDDpvikKIALREIRMLKQLK-HPNLVNLLEVFRRKRRLHLV 79
Cdd:cd07830     1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMkkkFYSWEE----CMNLREVKSLRKLNeHPNIVKLKEVFRENDELYFV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  80 FEYCDHTvLHEL--DRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFAR-LLTGPGd 156
Cdd:cd07830    77 FEYMEGN-LYQLmkDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAReIRSRPP- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 157 yYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLG----DLIPRHQQVfsMN 232
Cdd:cd07830   155 -YTDYVSTRWYRAPEILLRSTSYSSPVDIWALGCIMAELYTLRPLFPGSSEIDQLYKICSVLGtptkQDWPEGYKL--AS 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039741915 233 QYfsGVKIPD--PEDMETLelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07830   232 KL--GFRFPQfaPTSLHQL---IPNASPEAIDLIKDMLRWDPKKRPTASQALQHPYF 283
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
3-287 1.05e-98

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 293.83  E-value: 1.05e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd07848     2 KFEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLT-GPGDYYTDY 161
Cdd:cd07848    82 VEKNMLELLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSeGSNANYTEY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 162 VATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDLIPRHQQVFSMNQYFSGVKIP 241
Cdd:cd07848   162 VATRWYRSPELLLG-APYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLGPLPAEQMKLFYSNPRFHGLRFP 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1039741915 242 DPEDMETLELKFPNISYSA-LGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07848   241 AVNHPQSLERRYLGILSGVlLDLMKNLLKLNPTDRYLTEQCLNHPAF 287
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
4-287 4.94e-95

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 284.18  E-value: 4.94e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRF-LETEDDPViKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd07835     1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIrLETEDEGV-PSTAIREISLLKELNHPNIVRLLDVVHSENKLYLVFEF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHELDR-YQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDY 161
Cdd:cd07835    80 LDLDLKKYMDSsPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAFGVPVRTYTHE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 162 VATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGdlIPRHQQ---VFSMNQYFSGV 238
Cdd:cd07835   160 VVTLWYRAPEILLGSKHYSTPVDIWSVGCIFAEMVTRRPLFPGDSEIDQLFRIFRTLG--TPDEDVwpgVTSLPDYKPTF 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1039741915 239 KIPDPEDMETLelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07835   238 PKWARQDLSKV---VPSLDEDGLDLLSQMLVYDPAKRISAKAALQHPYF 283
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
3-287 3.69e-94

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 282.54  E-value: 3.69e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRF---LETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLV 79
Cdd:cd07841     1 RYEKGKKLGEGTYAVVYKARDKETGRIVAIKKIklgERKEAKDGINFTALREIKLLQELKHPNIIGLLDVFGHKSNINLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  80 FEYCDhTVLHELDRYQRGVPEPL-VKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYY 158
Cdd:cd07841    81 FEFME-TDLEKVIKDKSIVLTPAdIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARSFGSPNRKM 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 TDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDLIPRHQQVFSMNQYFSGV 238
Cdd:cd07841   160 THQVVTRWYRAPELLFGARHYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIFEALGTPTEENWPGVTSLPDYVEF 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1039741915 239 KIPDPEDMETLelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07841   240 KPFPPTPLKQI---FPAASDDALDLLQRLLTLNPNKRITARQALEHPYF 285
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
3-287 1.91e-90

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 272.67  E-value: 1.91e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLK-HPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd07832     1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEGGIPNQALREIKALQACQgHPYVVKLRDVFPHGTGFVLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTvLHELDR-YQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDY-YT 159
Cdd:cd07832    81 YMLSS-LSEVLRdEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLFSEEDPRlYS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 160 DYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGdlIPRHQQ---VFSMNQYfs 236
Cdd:cd07832   160 HQVATRWYRAPELLYGSRKYDEGVDLWAVGCIFAELLNGSPLFPGENDIEQLAIVLRTLG--TPNEKTwpeLTSLPDY-- 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 237 gVKIPDPE-DMETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07832   236 -NKITFPEsKGIRLEEIFPDCSPEAIDLLKGLLVYNPKKRLSAEEALRHPYF 286
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
4-287 1.33e-88

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 267.89  E-value: 1.33e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRF-LETEDD--PVIkkiALREIRMLKQLKHPNLVNLLEVFRRKRR----- 75
Cdd:cd07840     1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIrMENEKEgfPIT---AIREIKLLQKLDHPNVVRLKEIVTSKGSakykg 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  76 -LHLVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGP 154
Cdd:cd07840    78 sIYMVFEYMDHDLTGLLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLARPYTKE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 155 GDY-YTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDLIPRH-QQVFSMn 232
Cdd:cd07840   158 NNAdYTNRVITLWYRPPELLLGATRYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIFELCGSPTEENwPGVSDL- 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 233 QYFSGVKiPDPEDMETLELKFPN-ISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07840   237 PWFENLK-PKKPYKRRLREVFKNvIDPSALDLLDKLLTLDPKKRISADQALQHEYF 291
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
4-287 2.08e-85

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 259.74  E-value: 2.08e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRF-LETEDDPViKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd07860     2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKIrLDTETEGV-PSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHELDRYQ-RGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDY 161
Cdd:cd07860    81 LHQDLKKFMDASAlTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 162 VATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLG----DLIPrhqQVFSMNQYFSG 237
Cdd:cd07860   161 VVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGtpdeVVWP---GVTSMPDYKPS 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039741915 238 VKIPDPEDMETLelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07860   238 FPKWARQDFSKV---VPPLDEDGRDLLSQMLHYDPNKRISAKAALAHPFF 284
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
3-287 2.87e-85

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 259.29  E-value: 2.87e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd07839     1 KYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLYDVLHSDKKLTLVFEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYV 162
Cdd:cd07839    81 CDQDLKKYFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAFGIPVRCYSAEV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 163 ATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELL-SGVPLWPGKSDVDQLYLIRKTLGdlIPRHQQVFSMNQYFSGVKIP 241
Cdd:cd07839   161 VTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELAnAGRPLFPGNDVDDQLKRIFRLLG--TPTEESWPGVSKLPDYKPYP 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1039741915 242 DPEDMETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07839   239 MYPATTSLVNVVPKLNSTGRDLLQNLLVCNPVQRISAEEALQHPYF 284
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
3-291 5.95e-85

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 260.15  E-value: 5.95e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRR-----LH 77
Cdd:cd07834     1 RYELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISNVFDDLIDAKRILREIKILRHLKHENIIGLLDILRPPSPeefndVY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  78 LVFEYCD---HTVLHEldryqrgvPEPL----VKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARL 150
Cdd:cd07834    81 IVTELMEtdlHKVIKS--------PQPLtddhIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLARG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 151 LTGPGDYY--TDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGdliprhqqv 228
Cdd:cd07834   153 VDPDEDKGflTEYVVTRWYRAPELLLSSKKYTKAIDIWSVGCIFAELLTRKPLFPGRDYIDQLNLIVEVLG--------- 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 229 fsmnqyfsgvkIPDPEDMET--------------------LELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYFD 288
Cdd:cd07834   224 -----------TPSEEDLKFissekarnylkslpkkpkkpLSEVFPGASPEAIDLLEKMLVFNPKKRITADEALAHPYLA 292

                  ...
gi 1039741915 289 SIR 291
Cdd:cd07834   293 QLH 295
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
2-287 2.37e-82

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 252.15  E-value: 2.37e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRF-LETEDD--PVIkkiALREIRMLKQLKHPNLVNLLEVFRRKR--RL 76
Cdd:cd07843     5 DEYEKLNRIEEGTYGVVYRARDKKTGEIVALKKLkMEKEKEgfPIT---SLREINILLKLQHPNIVTVKEVVVGSNldKI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  77 HLVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGD 156
Cdd:cd07843    82 YMVMEYVEHDLKSLMETMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAREYGSPLK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 157 YYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGdlIPRHQqvfSMNQYFS 236
Cdd:cd07843   162 PYTQLVVTLWYRAPELLLGAKEYSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIFKLLG--TPTEK---IWPGFSE 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039741915 237 ----GVKIPDPEDMETLELKFPNISYSALGF--LKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07843   237 lpgaKKKTFTKYPYNQLRKKFPALSLSDNGFdlLNRLLTYDPAKRISAEDALKHPYF 293
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
3-287 3.04e-82

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 251.57  E-value: 3.04e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRF-LETEDDPViKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd07861     1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIrLESEEEGV-PSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELDRYQRG--VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYT 159
Cdd:cd07861    80 FLSMDLKKYLDSLPKGkyMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAFGIPVRVYT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 160 DYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDliprhqqvfSMNQYFSGV- 238
Cdd:cd07861   160 HEVVTLWYRAPEVLLGSPRYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIFRILGT---------PTEDIWPGVt 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039741915 239 KIPDPEDM------ETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07861   231 SLPDYKNTfpkwkkGSLRTAVKNLDEDGLDLLEKMLIYDPAKRISAKKALVHPYF 285
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
2-287 7.22e-82

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 252.48  E-value: 7.22e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLK-HPNLVNLLEVFRRK--RRLHL 78
Cdd:cd07852     7 RRYEILKKLGKGAYGIVWKAIDKKTGEVVALKKIFDAFRNATDAQRTFREIMFLQELNdHPNIIKLLNVIRAEndKDIYL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDhTVLHELDRyqRGVPEPL-VKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDY 157
Cdd:cd07852    87 VFEYME-TDLHAVIR--ANILEDIhKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARSLSQLEED 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 158 Y-----TDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDliPRHQQVFSMN 232
Cdd:cd07852   164 DenpvlTDYVATRWYRAPEILLGSTRYTKGVDMWSVGCILGEMLLGKPLFPGTSTLNQLEKIIEVIGR--PSAEDIESIQ 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039741915 233 QYFSGV---KIPDPEDmETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07852   242 SPFAATmleSLPPSRP-KSLDELFPKASPDALDLLKKLLVFNPNKRLTAEEALRHPYV 298
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
4-287 7.56e-82

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 250.66  E-value: 7.56e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLK---HPNLVNLLEVFRRKRR----- 75
Cdd:cd07838     1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRVPLSEEGIPLSTIREIALLKQLEsfeHPNVVRLLDVCHGPRTdrelk 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  76 LHLVFEYCDHTVLHELDRY-QRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgp 154
Cdd:cd07838    81 LTLVFEHVDQDLATYLDKCpKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLARIYS-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 155 gdYY---TDYVATRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGdLIPRH---QQV 228
Cdd:cd07838   159 --FEmalTSVVVTLWYRAPEVLLQSS-YATPVDMWSVGCIFAELFNRRPLFRGSSEADQLGKIFDVIG-LPSEEewpRNS 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 229 FSMNQYFSGVKIPDPEDMetlelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07838   235 ALPRSSFPSYTPRPFKSF------VPEIDEEGLDLLKKMLTFNPHKRISAFEALQHPYF 287
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
3-288 3.26e-81

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 249.34  E-value: 3.26e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLEtedDPVIKKialREIRMLKQLKHPNLVNLLEVF------RRKRRL 76
Cdd:cd14137     5 SYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQ---DKRYKN---RELQIMRRLKHPNIVKLKYFFyssgekKDEVYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  77 HLVFEYCDHT---VLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAI-KLCDFGFARLLT 152
Cdd:cd14137    79 NLVMEYMPETlyrVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPETGVlKLCDFGSAKRLV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 153 gPGDYYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGdlIPRHQQVFSMN 232
Cdd:cd14137   159 -PGEPNVSYICSRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKVLG--TPTREQIKAMN 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 233 QYFSGVKIPD--PEDMETLelkFPN-ISYSALGFLKGCLHMDPAERLTCEQLLQHPYFD 288
Cdd:cd14137   236 PNYTEFKFPQikPHPWEKV---FPKrTPPDAIDLLSKILVYNPSKRLTALEALAHPFFD 291
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
4-287 1.49e-80

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 248.05  E-value: 1.49e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRF-LETEDD--PVIkkiALREIRMLKQLKHPNLVNLLEVF--RRKRRLHL 78
Cdd:cd07845     9 FEKLNRIGEGTYGIVYRARDTTSGEIVALKKVrMDNERDgiPIS---SLREITLLLNLRHPNIVELKEVVvgKHLDSIFL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYY 158
Cdd:cd07845    86 VMEYCEQDLASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLARTYGLPAKPM 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 TDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLG-----------DLIPRHQQ 227
Cdd:cd07845   166 TPKVVTLWYRAPELLLGCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIIQLLGtpnesiwpgfsDLPLVGKF 245
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 228 VFSMNQYfsgvkipdpedmETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07845   246 TLPKQPY------------NNLKHKFPWLSEAGLRLLNFLLMYDPKKRATAEEALESSYF 293
Pkinase pfam00069
Protein kinase domain;
4-287 1.66e-78

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 239.45  E-value: 1.66e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYC 83
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 DHTVLHELDRYQRGVPEPLVKNITWQTLQAVNfchkhncihrdvkpenilitkqsaiklcdfgfarlltgPGDYYTDYVA 163
Cdd:pfam00069  81 EGGSLFDLLSEKGAFSEREAKFIMKQILEGLE--------------------------------------SGSSLTTFVG 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 164 TRWYRSPELLvGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKtlgdliprhqqvfsmnqyfsgvkipdp 243
Cdd:pfam00069 123 TPWYMAPEVL-GGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIID--------------------------- 174
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1039741915 244 eDMETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:pfam00069 175 -QPYAFPELPSNLSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
1-294 1.96e-78

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 242.42  E-value: 1.96e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRF-LETEDDPViKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLV 79
Cdd:PLN00009    1 MDQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIrLEQEDEGV-PSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  80 FEYCDHTVLHELDRYQRGVPEP-LVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQS-AIKLCDFGFARLLTGPGDY 157
Cdd:PLN00009   80 FEYLDLDLKKHMDSSPDFAKNPrLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTnALKLADFGLARAFGIPVRT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 158 YTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGdlIPRHQQ---VFSMNQY 234
Cdd:PLN00009  160 FTHEVVTLWYRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRILG--TPNEETwpgVTSLPDY 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 235 FSGVKIPDPEDMETLelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYFDSIREVG 294
Cdd:PLN00009  238 KSAFPKWPPKDLATV---VPTLEPAGVDLLSKMLRLDPSKRITARAALEHEYFKDLGDAP 294
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
4-287 1.04e-76

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 238.37  E-value: 1.04e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFL---ETEDDPVIkkiALREIRMLKQLKHPNLVNLLEVF--------RR 72
Cdd:cd07866    10 YEILGKLGEGTFGEVYKARQIKTGRVVALKKILmhnEKDGFPIT---ALREIKILKKLKHPNVVPLIDMAverpdkskRK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  73 KRRLHLVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLT 152
Cdd:cd07866    87 RGSVYMVTPYMDHDLSGLLENPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLARPYD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 153 GPGDY-----------YTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGdl 221
Cdd:cd07866   167 GPPPNpkggggggtrkYTNLVVTRWYRPPELLLGERRYTTAVDIWGIGCVFAEMFTRRPILQGKSDIDQLHLIFKLCG-- 244
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039741915 222 iPRHQQVFSMNQYFSGVKIPD--PEDMETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07866   245 -TPTEETWPGWRSLPGCEGVHsfTNYPRTLEERFGKLGPEGLDLLSKLLSLDPYKRLTASDALEHPYF 311
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
4-287 6.88e-75

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 232.76  E-value: 6.88e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRF-LETEDDpvIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd07836     2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIhLDAEEG--TPSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHELDRY--QRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTD 160
Cdd:cd07836    80 MDKDLKKYMDTHgvRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAFGIPVNTFSN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 YVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLG----DLIPRHQQVFSMNQYFS 236
Cdd:cd07836   160 EVVTLWYRAPDVLLGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRIMGtpteSTWPGISQLPEYKPTFP 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 237 GVKipdPEDMETLelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07836   240 RYP---PQDLQQL---FPHADPLGIDLLHRLLQLNPELRISAHDALQHPWF 284
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
4-287 8.69e-75

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 232.55  E-value: 8.69e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDpVIKKIALREIRMLKQLK-HPNLVNLLEV-FRRKR-RLHLVF 80
Cdd:cd07831     1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKHFKS-LEQVNNLREIQALRRLSpHPNILRLIEVlFDRKTgRLALVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  81 EYCDHTvLHELDRYQRG-VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILItKQSAIKLCDFGFARLL--TGPgdy 157
Cdd:cd07831    80 ELMDMN-LYELIKGRKRpLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILI-KDDILKLADFGSCRGIysKPP--- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 158 YTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLG----DLIPRHQQVFSMNQ 233
Cdd:cd07831   155 YTEYISTRWYRAPECLLTDGYYGPKMDIWAVGCVFFEILSLFPLFPGTNELDQIAKIHDVLGtpdaEVLKKFRKSRHMNY 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039741915 234 YFsgvkiPDPEDMEtLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07831   235 NF-----PSKKGTG-LRKLLPNASAEGLDLLKKLLAYDPDERITAKQALRHPYF 282
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
2-288 1.98e-73

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 229.34  E-value: 1.98e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRF-LETEDDPViKKIALREIRMLKQLKH-PNLVNLLEV----FRRKRR 75
Cdd:cd07837     1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALKKTrLEMEEEGV-PSTALREVSLLQMLSQsIYIVRLLDVehveENGKPL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  76 LHLVFEYCDHTVLHELDRYQRG----VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAI-KLCDFGFARL 150
Cdd:cd07837    80 LYLVFEYLDTDLKKFIDSYGRGphnpLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGLlKIADLGLGRA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 151 LTGPGDYYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGdlIPRHQQvfs 230
Cdd:cd07837   160 FTIPIKSYTHEIVTLWYRAPEVLLGSTHYSTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIFRLLG--TPNEEV--- 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039741915 231 mnqyFSGV-KIPD--------PEDMETLelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYFD 288
Cdd:cd07837   235 ----WPGVsKLRDwheypqwkPQDLSRA---VPDLEPEGVDLLTKMLAYDPAKRISAKAALQHPYFD 294
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
3-287 9.83e-73

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 228.02  E-value: 9.83e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFL---ETEDDPVIkkiALREIRMLKQLKHPNLVNLLEVFRRKRR---- 75
Cdd:cd07865    13 KYEKLAKIGQGTFGEVFKARHRKTGQIVALKKVLmenEKEGFPIT---ALREIKILQLLKHENVVNLIEICRTKATpynr 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  76 ----LHLVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLL 151
Cdd:cd07865    90 ykgsIYLVFEFCEHDLAGLLSNKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLARAF 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 152 TGP----GDYYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDLIPRHQQ 227
Cdd:cd07865   170 SLAknsqPNRYTNRVVTLWYRPPELLLGERDYGPPIDMWGAGCIMAEMWTRSPIMQGNTEQHQLTLISQLCGSITPEVWP 249
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 228 VFSMNQYFSGVKIP-DPEDMETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07865   250 GVDKLELFKKMELPqGQKRKVKERLKPYVKDPYALDLIDKLLVLDPAKRIDADTALNHDFF 310
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
3-287 1.78e-71

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 225.24  E-value: 1.78e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCR--NRDTGQIVAIKRFLETEDDPV-IKKIALREIRMLKQLKHPNLVNLLEVF--RRKRRLH 77
Cdd:cd07842     1 KYEIEGCIGRGTYGRVYKAKrkNGKDGKEYAIKKFKGDKEQYTgISQSACREIALLRELKHENVVSLVEVFleHADKSVY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  78 LVFEYCDHTVLHELdRYQRG-----VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILIT----KQSAIKLCDFGFA 148
Cdd:cd07842    81 LLFDYAEHDLWQII-KFHRQakrvsIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVMgegpERGVVKIGDLGLA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 149 RLLTGP------GDyytDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSD---------VDQLYL 213
Cdd:cd07842   160 RLFNAPlkpladLD---PVVVTIWYRAPELLLGARHYTKAIDIWAIGCIFAELLTLEPIFKGREAkikksnpfqRDQLER 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 214 IRKTLG--------DLI--PRHQQvfsMNQYFSGVKIPDPeDMETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQ 283
Cdd:cd07842   237 IFEVLGtptekdwpDIKkmPEYDT---LKSDTKASTYPNS-LLAKWMHKHKKPDSQGFDLLRKLLEYDPTKRITAEEALE 312

                  ....
gi 1039741915 284 HPYF 287
Cdd:cd07842   313 HPYF 316
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
4-287 2.99e-69

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 218.40  E-value: 2.99e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIK--RFLETEDDPVIkkiALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd07844     2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKeiRLEHEEGAPFT---AIREASLLKDLKHANIVTLHDIIHTKKTLTLVFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDY 161
Cdd:cd07844    79 YLDTDLKQYMDDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARAKSVPSKTYSNE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 162 VATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDV-DQLYLIRKTLGDLIPRHQQVFSMNQYFSGVKI 240
Cdd:cd07844   159 VVTLWYRPPDVLLGSTEYSTSLDMWGVGCIFYEMATGRPLFPGSTDVeDQLHKIFRVLGTPTEETWPGVSSNPEFKPYSF 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1039741915 241 PDPEDmETLELKFPNISY--SALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07844   239 PFYPP-RPLINHAPRLDRipHGEELALKFLQYEPKKRISAAEAMKHPYF 286
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
3-285 9.99e-68

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 213.49  E-value: 9.99e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIK----RFLETEDDPVIKkialREIRMLKQLKHPNLVNLLEVFRRKRRLHL 78
Cdd:cd05117     1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKiidkKKLKSEDEEMLR----REIEILKRLDHPNIVKLYEVFEDDKNLYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYC------DHtvLHELDRYqrgvPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILIT---KQSAIKLCDFGFAR 149
Cdd:cd05117    77 VMELCtggelfDR--IVKKGSF----SEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLAskdPDSPIKIIDFGLAK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 150 LLtGPGDYYTDYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKtlGDLiprhqqvf 229
Cdd:cd05117   151 IF-EEGEKLKTVCGTPYYVAPEVLKG-KGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILK--GKY-------- 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 230 smnqyfsgvKIPDPEdmetlelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHP 285
Cdd:cd05117   219 ---------SFDSPE--------WKNVSEEAKDLIKRLLVVDPKKRLTAAEALNHP 257
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
1-287 3.88e-67

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 212.95  E-value: 3.88e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIK--RFLETEDDPVIkkiALREIRMLKQLKHPNLVNLLEVFRRKRRLHL 78
Cdd:cd07871     4 LETYVKLDKLGEGTYATVFKGRSKLTENLVALKeiRLEHEEGAPCT---AIREVSLLKNLKHANIVTLHDIIHTERCLTL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYY 158
Cdd:cd07871    81 VFEYLDSDLKQYLDNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARAKSVPTKTY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 TDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDLIPRHQQVFSMNQYFSGV 238
Cdd:cd07871   161 SNEVVTLWYRPPDVLLGSTEYSTPIDMWGVGCILYEMATGRPMFPGSTVKEELHLIFRLLGTPTEETWPGVTSNEEFRSY 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1039741915 239 KIPDPEdMETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07871   241 LFPQYR-AQPLINHAPRLDTDGIDLLSSLLLYETKSRISAEAALRHSYF 288
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
3-295 2.41e-65

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 209.92  E-value: 2.41e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRR-----LH 77
Cdd:cd07858     6 KYVPIKPIGRGAYGIVCSAKNSETNEKVAIKKIANAFDNRIDAKRTLREIKLLRHLDHENVIAIKDIMPPPHReafndVY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  78 LVFEYCDhTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDY 157
Cdd:cd07858    86 IVYELMD-TDLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARTTSEKGDF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 158 YTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDliPRHQQV-FSMNQ--- 233
Cdd:cd07858   165 MTEYVVTRWYRAPELLLNCSEYTTAIDVWSVGCIFAELLGRKPLFPGKDYVHQLKLITELLGS--PSEEDLgFIRNEkar 242
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 234 -------YFSGVKIPDpedmetlelKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYFDSIREVGE 295
Cdd:cd07858   243 ryirslpYTPRQSFAR---------LFPHANPLAIDLLEKMLVFDPSKRITVEEALAHPYLASLHDPSD 302
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
1-286 2.95e-65

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 208.50  E-value: 2.95e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRF-LETEDD--PVIkkiALREIRMLKQLKHPNLVNLLEVF------- 70
Cdd:cd07864     6 VDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVrLDNEKEgfPIT---AIREIKILRQLNHRSVVNLKEIVtdkqdal 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  71 ---RRKRRLHLVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGF 147
Cdd:cd07864    83 dfkKDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 148 ARLLTGPGDY-YTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDLIPRHQ 226
Cdd:cd07864   163 ARLYNSEESRpYTNKVITLWYRPPELLLGEERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRLCGSPCPAVW 242
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 227 QVFSMNQYFSGVKiPDPEDMETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd07864   243 PDVIKLPYFNTMK-PKKQYRRRLREEFSFIPTPALDLLDHMLTLDPSKRCTAEQALNSPW 301
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
2-287 4.14e-64

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 206.83  E-value: 4.14e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRK------RR 75
Cdd:cd07855     5 DRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVTTAKRTLRELKILRHFKHDNIIAIRDILRPKvpyadfKD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  76 LHLVFEY--CDhtvLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLL-T 152
Cdd:cd07855    85 VYVVLDLmeSD---LHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARGLcT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 153 GPGD---YYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDliPRHQQVF 229
Cdd:cd07855   162 SPEEhkyFMTEYVATRWYRAPELMLSLPEYTQAIDMWSVGCIFAEMLGRRQLFPGKNYVHQLQLILTVLGT--PSQAVIN 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 230 SMN-----QYFSGVKIPDPEDMETLelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07855   240 AIGadrvrRYIQNLPNKQPVPWETL---YPKADQQALDLLSQMLRFDPSERITVAEALQHPFL 299
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
1-292 2.79e-63

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 203.31  E-value: 2.79e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIK--RFLETEDDPVIkkiALREIRMLKQLKHPNLVNLLEVFRRKRRLHL 78
Cdd:cd07873     1 LETYIKLDKLGEGTYATVYKGRSKLTDNLVALKeiRLEHEEGAPCT---AIREVSLLKDLKHANIVTLHDIIHTEKSLTL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYY 158
Cdd:cd07873    78 VFEYLDKDLKQYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 TDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDLIPRHQQVFSMNQYFSGV 238
Cdd:cd07873   158 SNEVVTLWYRPPDILLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFRILGTPTEETWPGILSNEEFKSY 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039741915 239 KIPDPEdMETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYFDSIRE 292
Cdd:cd07873   238 NYPKYR-ADALHNHAPRLDSDGADLLSKLLQFEGRKRISAEEAMKHPYFHSLGE 290
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
10-285 6.08e-63

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 199.80  E-value: 6.08e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIaLREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLH 89
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLLEEL-LREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  90 E-LDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYVATR-WY 167
Cdd:cd00180    80 DlLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGGTTpPY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 168 RSPELLVGDTQYGPPVDVWAIGCVFAELlsgvplwpgksdvdqlylirktlgdliprhqqvfsmnqyfsgvkipdpEDME 247
Cdd:cd00180   160 YAPPELLGGRYYGPKVDIWSLGVILYEL------------------------------------------------EELK 191
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1039741915 248 TLelkfpnisysalgfLKGCLHMDPAERLTCEQLLQHP 285
Cdd:cd00180   192 DL--------------IRRMLQYDPKKRPSAKELLEHL 215
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
2-286 7.18e-63

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 203.69  E-value: 7.18e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRfLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRK-----RRL 76
Cdd:cd07849     5 PRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKK-ISPFEHQTYCLRTLREIKILLRFKHENIIGILDIQRPPtfesfKDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  77 HLVFEYCDhTVLHELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGD 156
Cdd:cd07849    84 YIVQELME-TDLYKLIKTQH-LSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARIADPEHD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 157 YY---TDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDliPrhqqvfSMNQ 233
Cdd:cd07849   162 HTgflTEYVATRWYRAPEIMLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKDYLHQLNLILGILGT--P------SQED 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 234 YFSGVKIPDPEDMETLELK--------FPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd07849   234 LNCIISLKARNYIKSLPFKpkvpwnklFPNADPKALDLLDKMLTFNPHKRITVEEALAHPY 294
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
2-289 1.07e-62

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 203.07  E-value: 1.07e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGK-IGEGSYGVVFKCRNRDTGQIVAIKRFLETE------------DDPVIKKIALREIRMLKQLKHPNLVNLLE 68
Cdd:PTZ00024    8 ERYIQKGAhLGEGTYGKVEKAYDTLTGKIVAIKKVKIIEisndvtkdrqlvGMCGIHFTTLRELKIMNEIKHENIMGLVD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  69 VFRRKRRLHLVFEYCDHTVLHELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFA 148
Cdd:PTZ00024   88 VYVEGDFINLVMDIMASDLKKVVDRKIR-LTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 149 R--------------LLTGPGDYYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLI 214
Cdd:PTZ00024  167 RrygyppysdtlskdETMQRREEMTSKVVTLWYRAPELLMGAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQLGRI 246
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 215 RKTLG----DLIPrhqQVFSMNQYFSGVKIpDPEDMETLelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYFDS 289
Cdd:PTZ00024  247 FELLGtpneDNWP---QAKKLPLYTEFTPR-KPKDLKTI---FPNASDDAIDLLQSLLKLNPLERISAKEALKHEYFKS 318
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
3-293 1.02e-61

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 200.78  E-value: 1.02e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVF-----RRKRRLH 77
Cdd:cd07859     1 RYKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHVSDATRILREIKLLRLLRHPDIVEIKHIMlppsrREFKDIY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  78 LVFEYCDhTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLL---TGP 154
Cdd:cd07859    81 VVFELME-SDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAfndTPT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 155 GDYYTDYVATRWYRSPELlVGD--TQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLG----DLIPRHQQV 228
Cdd:cd07859   160 AIFWTDYVATRWYRAPEL-CGSffSKYTPAIDIWSIGCIFAEVLTGKPLFPGKNVVHQLDLITDLLGtpspETISRVRNE 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039741915 229 fSMNQYFSGVKIPDPedmETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYFDSIREV 293
Cdd:cd07859   239 -KARRYLSSMRKKQP---VPFSQKFPNADPLALRLLERLLAFDPKDRPTAEEALADPYFKGLAKV 299
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
3-287 9.66e-61

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 195.43  E-value: 9.66e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDP-VIKKIaLREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd06606     1 RWKKGELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEeELEAL-EREIRILSSLKHPNIVRYLGTERTENTLNIFLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDH-TVLHELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLL--TGPGDYY 158
Cdd:cd06606    80 YVPGgSLASLLKKFGK-LPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLaeIATGEGT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 TDYVATRWYRSPElLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSD-VDQLYLIrkTLGDLIPRhqqvfsmnqyfsg 237
Cdd:cd06606   159 KSLRGTPYWMAPE-VIRGEGYGRAADIWSLGCTVIEMATGKPPWSELGNpVAALFKI--GSSGEPPP------------- 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039741915 238 vkIPDpedmetlelkfpNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd06606   223 --IPE------------HLSEEAKDFLRKCLQRDPKKRPTADELLQHPFL 258
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
4-287 1.16e-60

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 197.00  E-value: 1.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIK------KIALREIRMLKQLKH------PNLVNLLEVFr 71
Cdd:cd14210    15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIK---------IIRnkkrfhQQALVEVKILKHLNDndpddkHNIVRYKDSF- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  72 rKRRLHL--VFEycdhtvLHELDRYQ-------RGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQ--SAI 140
Cdd:cd14210    85 -IFRGHLciVFE------LLSINLYEllksnnfQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPskSSI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 141 KLCDFGFARLLTGPgdYYTdYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLG- 219
Cdd:cd14210   158 KVIDFGSSCFEGEK--VYT-YIQSRFYRAPEVILG-LPYDTAIDMWSLGCILAELYTGYPLFPGENEEEQLACIMEVLGv 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039741915 220 ---DLI---PRHQQVFSMN----QYFSGVKIPDPEDMETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14210   234 ppkSLIdkaSRRKKFFDSNgkprPTTNSKGKKRRPGSKSLAQVLKCDDPSFLDFLKKCLRWDPSERMTPEEALQHPWI 311
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
3-286 1.18e-60

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 195.04  E-value: 1.18e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIK----RFLETEDDPVIKkialREIRMLKQLKHPNLVNLLEVFRRKRRLHL 78
Cdd:cd14003     1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKiidkSKLKEEIEEKIK----REIEIMKLLNHPNIIKLYEVIETENKIYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGpGDYY 158
Cdd:cd14003    77 VMEYASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRG-GSLL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 TDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTlgdliprhqqvfsmnqyfsgv 238
Cdd:cd14003   156 KTFCGTPAYAAPEVLLGRKYDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKG--------------------- 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1039741915 239 KIPDPedmetlelkfPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14003   215 KYPIP----------SHLSPDARDLIRRMLVVDPSKRITIEEILNHPW 252
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
5-285 5.65e-59

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 191.27  E-value: 5.65e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   5 EKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIAlREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:cd06623     4 ERVKVLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEEFRKQLL-RELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCH-KHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYVA 163
Cdd:cd06623    83 GGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHtKRHIIHRDIKPSNLLINSKGEVKIADFGISKVLENTLDQCNTFVG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 164 TRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLSGV-PLWPgksdvdqlylirktlgdliPRHQQVFSMNQYFSGVKIPD 242
Cdd:cd06623   163 TVTYMSPERIQGES-YSYAADIWSLGLTLLECALGKfPFLP-------------------PGQPSFFELMQAICDGPPPS 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1039741915 243 PEDMETLElKFPNisysalgFLKGCLHMDPAERLTCEQLLQHP 285
Cdd:cd06623   223 LPAEEFSP-EFRD-------FISACLQKDPKKRPSAAELLQHP 257
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
2-286 2.16e-58

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 189.38  E-value: 2.16e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrFL----ETEDDpvIKKIAlREIRMLKQLKHPNLVNLLEVFRRKRRLH 77
Cdd:cd14002     1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALK-FIpkrgKSEKE--LRNLR-QEIEILRKLNHPNIIEMLDSFETKKEFV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  78 LVFEYCDhTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDY 157
Cdd:cd14002    77 VVTEYAQ-GELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMSCNTLV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 158 YTDYVATRWYRSPElLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDqlyLIRKTLGDliprhqqvfsmnqyfsG 237
Cdd:cd14002   156 LTSIKGTPLYMAPE-LVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQ---LVQMIVKD----------------P 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1039741915 238 VKIPDpedmetlelkfpNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14002   216 VKWPS------------NMSPEFKSFLQGLLNKDPSKRLSWPDLLEHPF 252
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
4-286 2.56e-58

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 191.85  E-value: 2.56e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDT--GQIVAIKRFLETEDDPVIKKIALREIRMLKQLK-HPNLVNLLE---VFRRK-RRL 76
Cdd:cd07857     2 YELIKELGQGAYGIVCSARNAETseEETVAIKKITNVFSKKILAKRALRELKLLRHFRgHKNITCLYDmdiVFPGNfNEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  77 HLVFEY--CDhtvLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLT-G 153
Cdd:cd07857    82 YLYEELmeAD---LHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARGFSeN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 154 PGD---YYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLG---DLIPRHQQ 227
Cdd:cd07857   159 PGEnagFMTEYVATRWYRAPEIMLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDYVDQLNQILQVLGtpdEETLSRIG 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 228 VFSMNQYFSGVKIPDPEDMETLelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd07857   239 SPKAQNYIRSLPNIPKKPFESI---FPNANPLALDLLEKLLAFDPTKRISVEEALEHPY 294
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
6-292 4.27e-58

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 194.10  E-value: 4.27e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   6 KIGKI-GEGSYGVVFKCRNRDTGQIVAIKRFLEtedDPVIKKialREIRMLKQLKHPNLVNL-----LEVFRRKRR---L 76
Cdd:PTZ00036   69 KLGNIiGNGSFGVVYEAICIDTSEKVAIKKVLQ---DPQYKN---RELLIMKNLNHINIIFLkdyyyTECFKKNEKnifL 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  77 HLVFEYCDHTVLHELDRYQR---GVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQS-AIKLCDFGFARLLT 152
Cdd:PTZ00036  143 NVVMEFIPQTVHKYMKHYARnnhALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNThTLKLCDFGSAKNLL 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 153 GpGDYYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGdlIPRHQQVFSMN 232
Cdd:PTZ00036  223 A-GQRSVSYICSRFYRAPELMLGATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIIQVLG--TPTEDQLKEMN 299
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 233 QYFSGVKIPD--PEDMETLelkFPN-ISYSALGFLKGCLHMDPAERLTCEQLLQHPYFDSIRE 292
Cdd:PTZ00036  300 PNYADIKFPDvkPKDLKKV---FPKgTPDDAINFISQFLKYEPLKRLNPIEALADPFFDDLRD 359
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
1-290 5.16e-58

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 190.20  E-value: 5.16e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIK--RFLETEDDPVIkkiALREIRMLKQLKHPNLVNLLEVFRRKRRLHL 78
Cdd:cd07872     5 METYIKLEKLGEGTYATVFKGRSKLTENLVALKeiRLEHEEGAPCT---AIREVSLLKDLKHANIVTLHDIVHTDKSLTL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYY 158
Cdd:cd07872    82 VFEYLDKDLKQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSVPTKTY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 TDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDLIPRHQQVFSMNQYFSGV 238
Cdd:cd07872   162 SNEVVTLWYRPPDVLLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRLLGTPTEETWPGISSNDEFKNY 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 239 KIPDPEDMETLElKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYFDSI 290
Cdd:cd07872   242 NFPKYKPQPLIN-HAPRLDTEGIELLTKFLQYESKKRISAEEAMKHAYFRSL 292
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
2-287 5.76e-58

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 190.97  E-value: 5.76e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRL----- 76
Cdd:cd07851    15 DRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRPFQSAIHAKRTYRELRLLKHMKHENVIGLLDVFTPASSLedfqd 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  77 -HLVFEYCDhTVLHELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgpg 155
Cdd:cd07851    95 vYLVTHLMG-ADLNNIVKCQK-LSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARHTD--- 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 156 DYYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGdliprhqqvfsmnqyf 235
Cdd:cd07851   170 DEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMNLVG---------------- 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 236 sgvkIPDPEDMETLELK--------------------FPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07851   234 ----TPDEELLKKISSEsarnyiqslpqmpkkdfkevFSGANPLAIDLLEKMLVLDPDKRITAAEALAHPYL 301
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
2-287 8.03e-58

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 189.09  E-value: 8.03e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRN-RDTGQIVAIKRF-LETEDD----PVIKKIALreIRMLKQLKHPNLVNLLEVFR---- 71
Cdd:cd07862     1 QQYECVAEIGEGAYGKVFKARDlKNGGRFVALKRVrVQTGEEgmplSTIREVAV--LRHLETFEHPNVVRLFDVCTvsrt 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  72 -RKRRLHLVFEYCDHTVLHELDRY-QRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFAR 149
Cdd:cd07862    79 dRETKLTLVFEHVDQDLTTYLDKVpEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLAR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 150 LLTGPGdYYTDYVATRWYRSPELLVgDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGdlIPRHQqvf 229
Cdd:cd07862   159 IYSFQM-ALTSVVVTLWYRAPEVLL-QSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKILDVIG--LPGEE--- 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 230 smnQYFSGVKIPD----PEDMETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07862   232 ---DWPRDVALPRqafhSKSAQPIEKFVTDIDELGKDLLLKCLTFNPAKRISAYSALSHPYF 290
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
3-287 1.05e-57

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 188.63  E-value: 1.05e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIK--RFLETEDDPVIKKIalREIRMLKQLK---HPNLVNLLEV-----FRR 72
Cdd:cd07863     1 QYEPVAEIGVGAYGTVYKARDPHSGHFVALKsvRVQTNEDGLPLSTV--REVALLKRLEafdHPNIVRLMDVcatsrTDR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  73 KRRLHLVFEYCDHTVLHELDRYQR-GVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLL 151
Cdd:cd07863    79 ETKVTLVFEHVDQDLRTYLDKVPPpGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARIY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 152 TGPGDyYTDYVATRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGdlIPrhqqvfSM 231
Cdd:cd07863   159 SCQMA-LTPVVVTLWYRAPEVLLQST-YATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIG--LP------PE 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 232 NQYFSGVKIP----DPEDMETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07863   229 DDWPRDVTLPrgafSPRGPRPVQSVVPEIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
1-288 3.52e-57

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 187.75  E-value: 3.52e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrfletEDDPVIKKIALREIRMLKQLK-HPNLVNLLEVFR--RKRRLH 77
Cdd:cd14132    17 QDDYEIIRKIGRGKYSEVFEGINIGNNEKVVIK-----VLKPVKKKKIKREIKILQNLRgGPNIVKLLDVVKdpQSKTPS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  78 LVFEYCDHTVLHELdrYQRGVPEPlVKNITWQTLQAVNFCHKHNCIHRDVKPENILIT-KQSAIKLCDFGFArlltgpgD 156
Cdd:cd14132    92 LIFEYVNNTDFKTL--YPTLTDYD-IRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDhEKRKLRLIDWGLA-------E 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 157 YY---TDY---VATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGV-PLWPGKSDVDQLYLIRKTLG--DLIprhqq 227
Cdd:cd14132   162 FYhpgQEYnvrVASRYYKGPELLVDYQYYDYSLDMWSLGCMLASMIFRKePFFHGHDNYDQLVKIAKVLGtdDLY----- 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039741915 228 vfsmnQYFSGVKIPDPEDMETLELKFPNISYS--------------ALGFLKGCLHMDPAERLTCEQLLQHPYFD 288
Cdd:cd14132   237 -----AYLDKYGIELPPRLNDILGRHSKKPWErfvnsenqhlvtpeALDLLDKLLRYDHQERITAKEAMQHPYFD 306
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
3-287 4.87e-57

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 185.87  E-value: 4.87e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRfLETEDDPVIKKIaLREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd05122     1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKK-INLESKEKKESI-LNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHE-LDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFA-RLLTGPGDyyTD 160
Cdd:cd05122    79 CSGGSLKDlLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSaQLSDGKTR--NT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 YVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPlwP-GKSDvdqlylIRKTLgDLIPRHQQvfsmnqyfsgVK 239
Cdd:cd05122   157 FVGTPYWMAPEVIQG-KPYGFKADIWSLGITAIEMAEGKP--PySELP------PMKAL-FLIATNGP----------PG 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1039741915 240 IPDPEDMeTLELKfpnisysalGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd05122   217 LRNPKKW-SKEFK---------DFLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
3-283 9.75e-57

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 185.10  E-value: 9.75e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFL-ETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd14014     1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRpELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDY 161
Cdd:cd14014    81 YVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQTGS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 162 VA-TRWYRSPELLVGDtQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIrktlgdlipRHQQVFSMNQYFSGVki 240
Cdd:cd14014   161 VLgTPAYMAPEQARGG-PVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKH---------LQEAPPPPSPLNPDV-- 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1039741915 241 pdPEDMETLelkfpnisysalgfLKGCLHMDPAERL-TCEQLLQ 283
Cdd:cd14014   229 --PPALDAI--------------ILRALAKDPEERPqSAAELLA 256
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
3-287 5.84e-56

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 183.18  E-value: 5.84e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDpviKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd06614     1 LYKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQN---KELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHE-LDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDY 161
Cdd:cd06614    78 MDGGSLTDiITQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKSKRNSV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 162 VATRWYRSPElLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRkTLGdliprhqqvfsmnqyfsgvkIP 241
Cdd:cd06614   158 VGTPYWMAPE-VIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLIT-TKG--------------------IP 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1039741915 242 DPEDMETLelkfpniSYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd06614   216 PLKNPEKW-------SPEFKDFLNKCLVKDPEKRPSAEELLQHPFL 254
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
3-283 1.78e-55

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 188.30  E-value: 1.78e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFL-ETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:COG0515     8 RYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRpELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVME 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDY 161
Cdd:COG0515    88 YVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTQTGT 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 162 VA-TRWYRSPELLVGDtQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDqlyLIRKTLGDLIPRHQQVfsmnqyfsgvkI 240
Cdd:COG0515   168 VVgTPGYMAPEQARGE-PVDPRSDVYSLGVTLYELLTGRPPFDGDSPAE---LLRAHLREPPPPPSEL-----------R 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1039741915 241 PD-PEDMETLelkfpnisysalgfLKGCLHMDPAERL-TCEQLLQ 283
Cdd:COG0515   233 PDlPPALDAI--------------VLRALAKDPEERYqSAAELAA 263
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
3-287 4.48e-55

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 180.74  E-value: 4.48e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd08215     1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHEL--DRYQRGV--PEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYY 158
Cdd:cd08215    81 ADGGDLAQKikKQKKKGQpfPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLESTTDLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 TDYVATRWYRSPELLVGDtQYGPPVDVWAIGCVFAELLSGVPLWPGKSdvdqlylirktLGDLIprhqqvfsmnqyfsgV 238
Cdd:cd08215   161 KTVVGTPYYLSPELCENK-PYNYKSDIWALGCVLYELCTLKHPFEANN-----------LPALV---------------Y 213
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 239 KIpdpedmetLELKFPNIS--YSAL--GFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd08215   214 KI--------VKGQYPPIPsqYSSElrDLVNSMLQKDPEKRPSANEILSSPFI 258
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
10-287 2.43e-54

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 179.29  E-value: 2.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRF--------LETEDDPVIKKIAL----REIRMLKQLKHPNLVNLLEVFR--RKRR 75
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQLYAIKIFnksrlrkrREGKNDRGKIKNALddvrREIAIMKKLDHPNIVRLYEVIDdpESDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  76 LHLVFEYCDHTVLHELDRYQRGVP--EPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTG 153
Cdd:cd14008    81 LYLVLEYCEGGPVMELDSGDRVPPlpEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSEMFED 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 154 PGDYYTDYVATRWYRSPELLVGD--TQYGPPVDVWAIGCVFAELLSGVPLWPGKSdVDQLYlirktlgDLIPRHQQVFsm 231
Cdd:cd14008   161 GNDTLQKTAGTPAFLAPELCDGDskTYSGKAADIWALGVTLYCLVFGRLPFNGDN-ILELY-------EAIQNQNDEF-- 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 232 nqyfsgvkiPDPEDMETlELKFpnisysalgFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14008   231 ---------PIPPELSP-ELKD---------LLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
2-299 1.30e-53

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 179.71  E-value: 1.30e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLH---- 77
Cdd:cd07879    15 ERYTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLSRPFQSEIFAKRAYRELTLLKHMQHENVIGLLDVFTSAVSGDefqd 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  78 --LVFEYCdHTVLHELdryqRGVP--EPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTG 153
Cdd:cd07879    95 fyLVMPYM-QTDLQKI----MGHPlsEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARHADA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 154 PgdyYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLG----DLIPRHQQVF 229
Cdd:cd07879   170 E---MTGYVVTRWYRAPEVILNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKVTGvpgpEFVQKLEDKA 246
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 230 SMNQYFSGVKIPDpEDMETLelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYFDSIREVGELTRQ 299
Cdd:cd07879   247 AKSYIKSLPKYPR-KDFSTL---FPKASPQAVDLLEKMLELDVDKRLTATEALEHPYFDSFRDADEETEQ 312
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
2-286 1.31e-53

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 179.31  E-value: 1.31e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRK-RRLHLVF 80
Cdd:cd07856    10 TRYSDLQPVGMGAFGLVCSARDQLTGQNVAVKKIMKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIFISPlEDIYFVT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  81 EYCDhTVLHELDRyQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLltgPGDYYTD 160
Cdd:cd07856    90 ELLG-TDLHRLLT-SRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARI---QDPQMTG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 YVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLG----DLIprhQQVFSMNQYFS 236
Cdd:cd07856   165 YVSTRYYRAPEIMLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELLGtppdDVI---NTICSENTLRF 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039741915 237 GVKIPDPEDMETLElKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd07856   242 VQSLPKRERVPFSE-KFKNADPDAIDLLEKMLVFDPKKRISAAEALAHPY 290
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
2-298 3.30e-53

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 178.99  E-value: 3.30e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRL----- 76
Cdd:cd07880    15 DRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYRPFQSELFAKRAYRELRLLKHMKHENVIGLLDVFTPDLSLdrfhd 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  77 -HLVFEYCDhTVLHELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPg 155
Cdd:cd07880    95 fYLVMPFMG-TDLGKLMKHEK-LSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQTDSE- 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 156 dyYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLG----DLIPRHQQVFSM 231
Cdd:cd07880   172 --MTGYVVTRWYRAPEVILNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKVTGtpskEFVQKLQSEDAK 249
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039741915 232 NqYFSGVKIPDPEDMETLelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYFDSIREVGELTR 298
Cdd:cd07880   250 N-YVKKLPRFRKKDFRSL---LPNANPLAVNVLEKMLVLDAESRITAAEALAHPYFEEFHDPEDETE 312
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
4-287 1.38e-52

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 174.76  E-value: 1.38e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIKKI------ALREIRMLKQLK------HPNLVNLLEVFR 71
Cdd:cd14133     1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALK---------IIKNNkdyldqSLDEIRLLELLNkkdkadKYHIVRLKDVFY 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  72 RKRRLHLVFEYCDHTV--LHELDRYQrGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA--IKLCDFGF 147
Cdd:cd14133    72 FKNHLCIVFELLSQNLyeFLKQNKFQ-YLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRcqIKIIDFGS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 148 ARLLTgpgDYYTDYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGdLIPRHQQ 227
Cdd:cd14133   151 SCFLT---QRLYSYIQSRYYRAPEVILG-LPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIG-IPPAHML 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 228 VFSMNqyfsgvkipdpeDMETLelkfpnisysaLGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14133   226 DQGKA------------DDELF-----------VDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
4-287 4.38e-52

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 173.99  E-value: 4.38e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRF-LETEDDpvIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd07870     2 YLNLEKLGEGSYATVYKGISRINGQLVALKVIsMKTEEG--VPFTAIREASLLKGLKHANIVLLHDIIHTKETLTFVFEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYV 162
Cdd:cd07870    80 MHTDLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKSIPSQTYSSEV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 163 ATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDV-DQLYLIRKTLGdlIPRHQQ---VFSMNQYFSGV 238
Cdd:cd07870   160 VTLWYRPPDVLLGATDYSSALDIWGAGCIFIEMLQGQPAFPGVSDVfEQLEKIWTVLG--VPTEDTwpgVSKLPNYKPEW 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1039741915 239 KIPDPEDMETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07870   238 FLPCKPQQLRVVWKRLSRPPKAEDLASQMLMMFPKDRISAQDALLHPYF 286
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
2-290 1.68e-51

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 173.34  E-value: 1.68e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIK--RFLETEDDPVIkkiALREIRMLKQLKHPNLVNLLEVFRRKRRLHLV 79
Cdd:cd07869     5 DSYEKLEKLGEGSYATVYKGKSKVNGKLVALKviRLQEEEGTPFT---AIREASLLKGLKHANIVLLHDIIHTKETLTLV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  80 FEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYT 159
Cdd:cd07869    82 FEYVHTDLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSHTYS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 160 DYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDV-DQLYLIRKTLG----DLIPrhqQVFSMNQY 234
Cdd:cd07869   162 NEVVTLWYRPPDVLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDIqDQLERIFLVLGtpneDTWP---GVHSLPHF 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 235 fsgvkipDPEDMETLELKFPNISYSALGFLKGC-------LHMDPAERLTCEQLLQHPYFDSI 290
Cdd:cd07869   239 -------KPERFTLYSPKNLRQAWNKLSYVNHAedlasklLQCFPKNRLSAQAALSHEYFSDL 294
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
9-286 8.09e-51

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 170.18  E-value: 8.09e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVAIKRF-LETEDDPVIKKIAlREIRMLKQLKHPNLVNL--LEVFRRKrrLHLVFEYCDH 85
Cdd:cd06626     7 KIGEGTFGKVYTAVNLDTGELMAMKEIrFQDNDPKTIKEIA-DEMKVLEGLDHPNLVRYygVEVHREE--VYIFMEYCQE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 TVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYT-----D 160
Cdd:cd06626    84 GTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNNTTTMApgevnS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 YVATRWYRSPELLVGDTQ--YGPPVDVWAIGCVFAELLSGVPLWpgksdvdqlylirktlgdliPRHQQVFS-MNQYFSG 237
Cdd:cd06626   164 LVGTPAYMAPEVITGNKGegHGRAADIWSLGCVVLEMATGKRPW--------------------SELDNEWAiMYHVGMG 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 238 VKIPDPEDMETlelkfpnisySALG--FLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd06626   224 HKPPIPDSLQL----------SPEGkdFLSRCLESDPKKRPTASELLDHPF 264
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
3-287 3.47e-50

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 170.73  E-value: 3.47e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETedDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRK--------- 73
Cdd:cd07854     6 RYMDLRPLGCGSNGLVFSAVDSDCDKRVAVKKIVLT--DPQSVKHALREIKIIRRLDHDNIVKVYEVLGPSgsdltedvg 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  74 -----RRLHLVFEYCDHTVLHELDryQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILI-TKQSAIKLCDFGF 147
Cdd:cd07854    84 sltelNSVYIVQEYMETDLANVLE--QGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFInTEDLVLKIGDFGL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 148 ARLLT---GPGDYYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLgDLIPR 224
Cdd:cd07854   162 ARIVDphySHKGYLSEGLVTKWYRSPRLLLSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQMQLILESV-PVVRE 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 225 HQQVFSMNQYFSGVKIPDPEDMETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07854   241 EDRNELLNVIPSFVRNDGGEPRRPLRDLLPGVNPEALDFLEQILTFNPMDRLTAEEALMHPYM 303
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
4-285 2.39e-49

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 165.73  E-value: 2.39e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIKKIAL----------REIRMLKQLKHPNLVNLLEVFRRK 73
Cdd:cd14007     2 FEIGKPLGKGKFGNVYLAREKKSGFIVALK---------VISKSQLqksglehqlrREIEIQSHLRHPNILRLYGYFEDK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  74 RRLHLVFEYCDH-TVLHELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFA---- 148
Cdd:cd14007    73 KRIYLILEYAPNgELYKELKKQKR-FDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSvhap 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 149 --RLLTGPGDYytDYVAtrwyrsPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKtlgdliprhq 226
Cdd:cd14007   152 snRRKTFCGTL--DYLP------PEMVEG-KEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQN---------- 212
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 227 qvfsmnqyfsgvkipdpedmetLELKFPN-ISYSALGFLKGCLHMDPAERLTCEQLLQHP 285
Cdd:cd14007   213 ----------------------VDIKFPSsVSPEAKDLISKLLQKDPSKRLSLEQVLNHP 250
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
2-287 3.89e-49

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 168.29  E-value: 3.89e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHlvfE 81
Cdd:cd07877    17 ERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLE---E 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCD-----HTV---LHELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARlltG 153
Cdd:cd07877    94 FNDvylvtHLMgadLNNIVKCQK-LTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLAR---H 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 154 PGDYYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLG----DLIPRHQQVF 229
Cdd:cd07877   170 TDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGtpgaELLKKISSES 249
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 230 SMNQYFSGVKIPdpedmetlELKFPNI----SYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07877   250 ARNYIQSLTQMP--------KMNFANVfigaNPLAVDLLEKMLVLDSDKRITAAQALAHAYF 303
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
10-287 1.31e-48

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 163.84  E-value: 1.31e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIKK--I--------ALREIRMLKQLKHPNLVNLLEVFRRKRRLHLV 79
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMK---------VLRKkeIikrkevehTLNERNILERVNHPFIVKLHYAFQTEEKLYLV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  80 FEYCD----HTVLHEldryQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPG 155
Cdd:cd05123    72 LDYVPggelFSHLSK----EGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 156 DYYTDYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLWPGkSDVDQLYliRKTLgdliprhqqvfsmnqyf 235
Cdd:cd05123   148 DRTYTFCGTPEYLAPEVLLG-KGYGKAVDWWSLGVLLYEMLTGKPPFYA-ENRKEIY--EKIL----------------- 206
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 236 sgvkipdpedmeTLELKFP-NISYSALGFLKGCLHMDPAERLTC---EQLLQHPYF 287
Cdd:cd05123   207 ------------KSPLKFPeYVSPEAKSLISGLLQKDPTKRLGSggaEEIKAHPFF 250
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
10-291 1.23e-47

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 164.92  E-value: 1.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRK-----RRLHLVFEYCd 84
Cdd:cd07853     8 IGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPhidpfEEIYVVTELM- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLT-GPGDYYTDYVA 163
Cdd:cd07853    87 QSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEEpDESKHMTQEVV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 164 TRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDliPRHQQVFS-----MNQYFSGV 238
Cdd:cd07853   167 TQYYRAPEILMGSRHYTSAVDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLGT--PSLEAMRSacegaRAHILRGP 244
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 239 KipDPEDMETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYFDSIR 291
Cdd:cd07853   245 H--KPPSLPVLYTLSSQATHEAVHLLCRMLVFDPDKRISAADALAHPYLDEGR 295
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
5-287 1.94e-47

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 161.36  E-value: 1.94e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   5 EKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLeTEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:cd06605     4 EYLGELGEGNGGVVSKVRHRPSGQIMAVKVIR-LEIDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEYMD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCH-KHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgpGDYYTDYVA 163
Cdd:cd06605    83 GGSLDKILKEVGRIPERILGKIAVAVVKGLIYLHeKHKIIHRDVKPSNILVNSRGQVKLCDFGVSGQLV--DSLAKTFVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 164 TRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSG---VPLW---PGKSDVDQLYLIrktlgdliprhqqvfsmnqyfsg 237
Cdd:cd06605   161 TRSYMAPERISG-GKYTVKSDIWSLGLSLVELATGrfpYPPPnakPSMMIFELLSYI----------------------- 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 238 VKIPDPedmetlelKFPN--ISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd06605   217 VDEPPP--------LLPSgkFSPDFQDFVSQCLQKDPTERPSYKELMEHPFI 260
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
9-287 4.09e-47

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 160.08  E-value: 4.09e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVAIKRfLETEDDPVIKKIALR-EIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTV 87
Cdd:cd06627     7 LIGRGAFGSVYKGLNLNTGEFVAIKQ-ISLEKIPKSDLKSVMgEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYVENGS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  88 LHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYVATRWY 167
Cdd:cd06627    86 LASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEVEKDENSVVGTPYW 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 168 RSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPlwPgksdvdqlYlirktlGDLIPrhqqvfsMNQYFSGVKIPDPedme 247
Cdd:cd06627   166 MAPEVIEM-SGVTTASDIWSVGCTVIELLTGNP--P--------Y------YDLQP-------MAALFRIVQDDHP---- 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1039741915 248 tlelKFP-NISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd06627   218 ----PLPeNISPELRDFLLQCFQKDPTLRPSAKELLKHPWL 254
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
3-287 1.82e-46

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 158.86  E-value: 1.82e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIK-----RFLETEddpviKKIALREIRMLKQLKHPNLVNLL--EVFRRKRR 75
Cdd:cd08217     1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKeidygKMSEKE-----KQQLVSEVNILRELKHPNIVRYYdrIVDRANTT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  76 LHLVFEYCDHTVLHEL-DRYQRG---VPEPLVKNITWQTLQAVNFCHKHNC-----IHRDVKPENILITKQSAIKLCDFG 146
Cdd:cd08217    76 LYIVMEYCEGGDLAQLiKKCKKEnqyIPEEFIWKIFTQLLLALYECHNRSVgggkiLHRDLKPANIFLDSDNNVKLGDFG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 147 FARLLTGPGDYYTDYVATRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLSGVPLWPGKSdvdQLYLIRKTLGDLIPRHQ 226
Cdd:cd08217   156 LARVLSHDSSFAKTYVGTPYYMSPELLNEQS-YDEKSDIWSLGCLIYELCALHPPFQAAN---QLELAKKIKEGKFPRIP 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 227 QVFSmnqyfsgvkipdpEDMETLelkfpnisysalgfLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd08217   232 SRYS-------------SELNEV--------------IKSMLNVDPDKRPSVEELLQLPLI 265
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
2-287 2.36e-46

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 160.98  E-value: 2.36e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd07878    15 ERYQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRPFQSLIHARRTYRELRLLKHMKHENVIGLLDVFTPATSIENFNE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELD-----RYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARlltGPGD 156
Cdd:cd07878    95 VYLVTNLMGADlnnivKCQK-LSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLAR---QADD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 157 YYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDLIPRHQQVFS---MNQ 233
Cdd:cd07878   171 EMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEVVGTPSPEVLKKISsehARK 250
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039741915 234 YFSGVKIPDPEDMETLelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd07878   251 YIQSLPHMPQQDLKKI---FRGANPLAIDLLEKMLVLDSDKRISASEALAHPYF 301
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
10-286 4.06e-46

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 157.38  E-value: 4.06e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLH 89
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  90 ELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA---IKLCDFGFARLLTgPGDYYTDYVATRW 166
Cdd:cd14009    81 QYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDdpvLKIADFGFARSLQ-PASMAETLCGSPL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 167 YRSPELLVGDtQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKtlgdliprhqqvfsmnqyfSGVKIPDPEDm 246
Cdd:cd14009   160 YMAPEILQFQ-KYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIER-------------------SDAVIPFPIA- 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1039741915 247 etlelkfPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14009   219 -------AQLSPDCKDLLRRLLRRDPAERISFEEFFAHPF 251
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
2-287 6.41e-46

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 159.27  E-value: 6.41e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIKKI------ALREIRMLKQLKH------PNLVNLLEV 69
Cdd:cd14134    12 NRYKILRLLGEGTFGKVLECWDRKRKRYVAVK---------IIRNVekyreaAKIEIDVLETLAEkdpngkSHCVQLRDW 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  70 FRRKRRLHLVFEYCDHTVLHELDRYQ-RGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENIL--------------- 133
Cdd:cd14134    83 FDYRGHMCIVFELLGPSLYDFLKKNNyGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILlvdsdyvkvynpkkk 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 134 ----ITKQSAIKLCDFGFArllTGPGDYYTDYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVD 209
Cdd:cd14134   163 rqirVPKSTDIKLIDFGSA---TFDDEYHSSIVSTRHYRAPEVILG-LGWSYPCDVWSIGCILVELYTGELLFQTHDNLE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 210 QLYLIRKTLGDLIPRHQQVFSMNQ---YFSGVKIPDPED--------------METLELKFPNiSYSALGFLKGCLHMDP 272
Cdd:cd14134   239 HLAMMERILGPLPKRMIRRAKKGAkyfYFYHGRLDWPEGsssgrsikrvckplKRLMLLVDPE-HRLLFDLIRKMLEYDP 317
                         330
                  ....*....|....*
gi 1039741915 273 AERLTCEQLLQHPYF 287
Cdd:cd14134   318 SKRITAKEALKHPFF 332
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
4-287 7.26e-46

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 159.34  E-value: 7.26e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIK------KIALREIRMLKQL--------KHpNLVNLLEV 69
Cdd:cd14212     1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVK---------VLKnkpayfRQAMLEIAILTLLntkydpedKH-HIVRLLDH 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  70 FRRKRRLHLVFEYCDHTvLHEL--DRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA--IKLCDF 145
Cdd:cd14212    71 FMHHGHLCIVFELLGVN-LYELlkQNQFRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDSpeIKLIDF 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 146 GFA----RLLtgpgdyYTdYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDL 221
Cdd:cd14212   150 GSAcfenYTL------YT-YIQSRFYRSPEVLLG-LPYSTAIDMWSLGCIAAELFLGLPLFPGNSEYNQLSRIIEMLGMP 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 222 iPRH----------------------------QQVFSM---------NQYFSGVKIPD--------PEDMETLELKFpNI 256
Cdd:cd14212   222 -PDWmlekgkntnkffkkvaksggrstyrlktPEEFEAenncklepgKRYFKYKTLEDiimnypmkKSKKEQIDKEM-ET 299
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1039741915 257 SYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14212   300 RLAFIDFLKGLLEYDPKKRWTPDQALNHPFI 330
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
10-286 4.44e-45

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 154.73  E-value: 4.44e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKrFLETEDDPviKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLh 89
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFAAK-FIPKRDKK--KEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGEL- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  90 eLDR-YQRG-VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILIT--KQSAIKLCDFGFARLLTgPGDYYTDYVATR 165
Cdd:cd14006    77 -LDRlAERGsLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLAdrPSPQIKIIDFGLARKLN-PGEELKEIFGTP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 166 WYRSPELLVGDTqYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDliprhqqvFSmnqyfsgvkipdped 245
Cdd:cd14006   155 EFVAPEIVNGEP-VSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVD--------FS--------------- 210
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1039741915 246 metlELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14006   211 ----EEYFSSVSQEAKDFIRKLLVKEPRKRPTAQEALQHPW 247
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
3-287 4.61e-45

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 155.16  E-value: 4.61e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVikKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd06613     1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIKLEPGDDF--EIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYV 162
Cdd:cd06613    79 CGGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTATIAKRKSFI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 163 ATRWYRSPELL-VGDTQ-YGPPVDVWAIGCVFAELLSGVP----LWPGKSdvdqLYLIRKtlgdliprhqqvfsmnqyfS 236
Cdd:cd06613   159 GTPYWMAPEVAaVERKGgYDGKCDIWALGITAIELAELQPpmfdLHPMRA----LFLIPK-------------------S 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 237 GVKIPDPEDMETLELKFPNisysalgFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd06613   216 NFDPPKLKDKEKWSPDFHD-------FIKKCLTKNPKKRPTATKLLQHPFV 259
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
2-287 3.32e-44

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 152.81  E-value: 3.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKialrEIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd06612     3 EVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQEIIK----EISILKQCDSPYIVKYYGSYFKNTDLWIVME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCD-HTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTD 160
Cdd:cd06612    79 YCGaGSVSDIMKITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMAKRNT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 YVATRWYRSPELLvGDTQYGPPVDVWAIGCVFAELLSGVPlwPgksdvdqlylirktLGDLIPrhqqvfsMNQYFsgvKI 240
Cdd:cd06612   159 VIGTPFWMAPEVI-QEIGYNNKADIWSLGITAIEMAEGKP--P--------------YSDIHP-------MRAIF---MI 211
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039741915 241 P--------DPEDMETLelkFPNisysalgFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd06612   212 PnkppptlsDPEKWSPE---FND-------FVKKCLVKDPEERPSAIQLLQHPFI 256
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
2-287 4.17e-44

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 152.32  E-value: 4.17e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIKKIAL----------REIRMLKQLKHPNLVNLLEVFR 71
Cdd:cd14099     1 KRYRRGKFLGKGGFAKCYEVTDMSTGKVYAGK---------VVPKSSLtkpkqreklkSEIKIHRSLKHPNIVKFHDCFE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  72 RKRRLHLVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLL 151
Cdd:cd14099    72 DEENVYILLELCSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 152 TGPGDYYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKsDVDQLYL-IRKtlgdliprhqqvfs 230
Cdd:cd14099   152 EYDGERKKTLCGTPNYIAPEVLEKKKGHSFEVDIWSLGVILYTLLVGKPPFETS-DVKETYKrIKK-------------- 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039741915 231 mNQYfsgvKIPdpedmetlelKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14099   217 -NEY----SFP----------SHLSISDEAKDLIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
10-286 5.02e-44

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 152.17  E-value: 5.02e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDP----VIKKIAlREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDH 85
Cdd:cd06632     8 LGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDDKksreSVKQLE-QEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVPG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 TVLHEL-DRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPgDYYTDYVAT 164
Cdd:cd06632    87 GSIHKLlQRYGA-FEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAF-SFAKSFKGS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 165 RWYRSPELLVG-DTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTlGDLIPrhqqvfsmnqyfsgvkIPDp 243
Cdd:cd06632   165 PYWMAPEVIMQkNSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNS-GELPP----------------IPD- 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1039741915 244 edmeTLELKfpnisysALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd06632   227 ----HLSPD-------AKDFIRLCLQRDPEDRPTASQLLEHPF 258
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
2-297 1.51e-43

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 151.63  E-value: 1.51e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRF-LETEDDPvIKKIAlREIRMLKQLKHPNLVNLLEVFRRKRRLHLVF 80
Cdd:cd06609     1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIdLEEAEDE-IEDIQ-QEIQFLSQCDSPYITKYYGSFLKGSKLWIIM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  81 EYCDHTVLHELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTD 160
Cdd:cd06609    79 EYCGGGSVLDLLKPGP-LDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTSTMSKRNT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 YVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPlwPgKSDVDQLYLIRktlgdLIPRHqqvfsmnqyfsgvKI 240
Cdd:cd06609   158 FVGTPFWMAPEVIKQ-SGYDEKADIWSLGITAIELAKGEP--P-LSDLHPMRVLF-----LIPKN-------------NP 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039741915 241 PdpedmeTLELkfPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYFDSIREVGELT 297
Cdd:cd06609   216 P------SLEG--NKFSKPFKDFVELCLNKDPKERPSAKELLKHKFIKKAKKTSYLT 264
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
10-290 4.00e-43

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 150.44  E-value: 4.00e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIKKIALREIRMLKQLK----------HPNLVNLLEVFRRKRRLHLV 79
Cdd:cd05579     1 ISRGAYGRVYLAKKKSTGDLYAIK---------VIKKRDMIRKNQVDSVLaernilsqaqNPFVVKLYYSFQGKKNLYLV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  80 FEYCD----HTVLHELDRYqrgvPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARL-LTGP 154
Cdd:cd05579    72 MEYLPggdlYSLLENVGAL----DEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVgLVRR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 155 GDYY--------------TDYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPlwpgksdvdqlylirktlgd 220
Cdd:cd05579   148 QIKLsiqkksngapekedRRIVGTPDYLAPEILLG-QGHGKTVDWWSLGVILYEFLVGIP-------------------- 206
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039741915 221 liPRH----QQVFSmnQYFSGvKIPDPEDmetlelkfPNISYSALGFLKGCLHMDPAERLTC---EQLLQHPYFDSI 290
Cdd:cd05579   207 --PFHaetpEEIFQ--NILNG-KIEWPED--------PEVSDEAKDLISKLLTPDPEKRLGAkgiEEIKNHPFFKGI 270
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
2-287 7.80e-43

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 149.43  E-value: 7.80e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIK------RFLETEDDPVIKKIALREIRMLKQL-KHPNLVNLLEVFRRKR 74
Cdd:cd14093     3 AKYEPKEILGRGVSSTVRRCIEKETGQEFAVKiiditgEKSSENEAEELREATRREIEILRQVsGHPNIIELHDVFESPT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  75 RLHLVFEYCDHTvlhELDRYQRGV---PEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLL 151
Cdd:cd14093    83 FIFLVFELCRKG---ELFDYLTEVvtlSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 152 TgPGDYYTDYVATRWYRSPELL---VGDTQ--YGPPVDVWAIGCVFAELLSGV-PLWPGKsdvdQLYLIRKTlgdliprh 225
Cdd:cd14093   160 D-EGEKLRELCGTPGYLAPEVLkcsMYDNApgYGKEVDMWACGVIMYTLLAGCpPFWHRK----QMVMLRNI-------- 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 226 qqvfsMNQYFSgvkIPDPEdmetlelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14093   227 -----MEGKYE---FGSPE--------WDDISDTAKDLISKLLVVDPKKRLTAEEALEHPFF 272
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
9-287 9.19e-43

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 150.60  E-value: 9.19e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTG--QIVAIKRFLETEddpvIKKIALREIRMLKQLKHPNLVNLLEVF--RRKRRLHLVFEYCD 84
Cdd:cd07867     9 KVGRGTYGHVYKAKRKDGKdeKEYALKQIEGTG----ISMSACREIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVLHeLDRYQRG---------VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILIT----KQSAIKLCDFGFARLL 151
Cdd:cd07867    85 HDLWH-IIKFHRAskankkpmqLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 152 TGPGDYYTDY---VATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKsdvdqlyliRKTLGDLIPRHQQv 228
Cdd:cd07867   164 NSPLKPLADLdpvVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCR---------QEDIKTSNPFHHD- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 229 fSMNQYFSGVKIPDPEDME---------TLELKFPNISYSALGFLK------------------GCLHMDPAERLTCEQL 281
Cdd:cd07867   234 -QLDRIFSVMGFPADKDWEdirkmpeypTLQKDFRRTTYANSSLIKymekhkvkpdskvflllqKLLTMDPTKRITSEQA 312

                  ....*.
gi 1039741915 282 LQHPYF 287
Cdd:cd07867   313 LQDPYF 318
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
4-285 2.31e-42

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 147.94  E-value: 2.31e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYC 83
Cdd:cd08529     2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 DHTVLHELDRYQRGvpEPLVKNITW----QTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYT 159
Cdd:cd08529    82 ENGDLHSLIKSQRG--RPLPEDQIWkffiQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTTNFAQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 160 DYVATRWYRSPElLVGDTQYGPPVDVWAIGCVFAELLSGvpLWPGKSDvDQLYLIRKtlgdlIPRhqqvfsmnqyfsGVK 239
Cdd:cd08529   160 TIVGTPYYLSPE-LCEDKPYNEKSDVWALGCVLYELCTG--KHPFEAQ-NQGALILK-----IVR------------GKY 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1039741915 240 IPDPEdmetlelkfpniSYSA--LGFLKGCLHMDPAERLTCEQLLQHP 285
Cdd:cd08529   219 PPISA------------SYSQdlSQLIDSCLTKDYRQRPDTTELLRNP 254
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
2-311 2.43e-42

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 148.35  E-value: 2.43e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRfLETEDDPVIKKIALrEIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd06611     5 DIWEIIGELGDGAFGKVYKAQHKETGLFAAAKI-IQIESEEELEDFMV-EIDILSECKHPNIVGLYEAYFYENKLWILIE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHEL-DRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTD 160
Cdd:cd06611    83 FCDGGALDSImLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTLQKRDT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 YVATRWYRSPELLV----GDTQYGPPVDVWAIGCVFAELLSGVPlwPgksdvdqlylirktlgdliprHQQVFSMNQYFS 236
Cdd:cd06611   163 FIGTPYWMAPEVVAcetfKDNPYDYKADIWSLGITLIELAQMEP--P---------------------HHELNPMRVLLK 219
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 237 GVKIPDPedmeTLELkfPNI-SYSALGFLKGCLHMDPAERLTCEQLLQHPYFdsirevgelTRQHDKPARKTLRQS 311
Cdd:cd06611   220 ILKSEPP----TLDQ--PSKwSSSFNDFLKSCLVKDPDDRPTAAELLKHPFV---------SDQSDNKAIKDLLAE 280
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
2-287 3.71e-42

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 147.48  E-value: 3.71e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKR---FLETEDDP-VIKKialrEIRMLKQLKHPNLVNLLEVFRRKRRLH 77
Cdd:cd14069     1 EDWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFvdmKRAPGDCPeNIKK----EVCIQKMLSHKNVVRFYGHRREGEFQY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  78 LVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFA--------- 148
Cdd:cd14069    77 LFLEYASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLAtvfrykgke 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 149 RLLTGPgdyytdyVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKtlgdliprhqqv 228
Cdd:cd14069   157 RLLNKM-------CGTLPYVAPELLAKKKYRAEPVDVWSCGIVLFAMLAGELPWDQPSDSCQEYSDWK------------ 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 229 fsmnqyfsgvkipdpEDMETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14069   218 ---------------ENKKTYLTPWKKIDTAALSLLRKILTENPNKRITIEDIKKHPWY 261
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
6-287 3.77e-42

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 147.75  E-value: 3.77e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   6 KIGK-IGEGSYGVVFKCRNRDTGQIVAIK----RFLETEddpviKKI--ALREIRMLKQLKHPNLVNLLEVFRRKRRLHL 78
Cdd:cd05581     4 KFGKpLGEGSYSTVVLAKEKETGKEYAIKvldkRHIIKE-----KKVkyVTIEKEVLSRLAHPGIVKLYYTFQDESKLYF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYY 158
Cdd:cd05581    79 VLEYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKVLGPDSSPE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 TD-----------------YVATRWYRSPELLvGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDvdqlYLIRKtlgdl 221
Cdd:cd05581   159 STkgdadsqiaynqaraasFVGTAEYVSPELL-NEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNE----YLTFQ----- 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 222 iprhqqvfsmnqyfsgvKIPDpedmetLELKFP-NISYSALGFLKGCLHMDPAERLTC------EQLLQHPYF 287
Cdd:cd05581   229 -----------------KIVK------LEYEFPeNFPPDAKDLIQKLLVLDPSKRLGVnenggyDELKAHPFF 278
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
9-287 5.92e-42

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 149.05  E-value: 5.92e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRD--TGQIVAIKRFLETEddpvIKKIALREIRMLKQLKHPNLVNLLEVF--RRKRRLHLVFEYCD 84
Cdd:cd07868    24 KVGRGTYGHVYKAKRKDgkDDKDYALKQIEGTG----ISMSACREIALLRELKHPNVISLQKVFlsHADRKVWLLFDYAE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVLHeLDRYQRG---------VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILIT----KQSAIKLCDFGFARLL 151
Cdd:cd07868   100 HDLWH-IIKFHRAskankkpvqLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLF 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 152 TGPGDYYTDY---VATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSD---------VDQLYLIRKTLG 219
Cdd:cd07868   179 NSPLKPLADLdpvVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQEdiktsnpyhHDQLDRIFNVMG 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 220 ----------DLIPRHQQV---FSMNQYFSGVKIpdpEDMETLELKfPNisYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd07868   259 fpadkdwediKKMPEHSTLmkdFRRNTYTNCSLI---KYMEKHKVK-PD--SKAFHLLQKLLTMDPIKRITSEQAMQDPY 332

                  .
gi 1039741915 287 F 287
Cdd:cd07868   333 F 333
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
10-283 6.18e-42

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 146.53  E-value: 6.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRdtGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLH 89
Cdd:cd13999     1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  90 ELDRYQRGV-PEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYVAT-RWy 167
Cdd:cd13999    79 DLLHKKKIPlSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTGVVGTpRW- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 168 RSPELLVGDtQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRktLGDLIPrhqqvfsmnqyfsgvKIPD--PED 245
Cdd:cd13999   158 MAPEVLRGE-PYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVV--QKGLRP---------------PIPPdcPPE 219
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1039741915 246 METLelkfpnisysalgfLKGCLHMDPAERLTCEQLLQ 283
Cdd:cd13999   220 LSKL--------------IKRCWNEDPEKRPSFSEIVK 243
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
3-286 8.28e-42

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 148.72  E-value: 8.28e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRL------ 76
Cdd:cd07850     1 RYQNLKPIGSGAQGIVCAAYDTVTGQNVAIKKLSRPFQNVTHAKRAYRELVLMKLVNHKNIIGLLNVFTPQKSLeefqdv 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  77 HLVFEYCDHT---VLH-ELDrYQRgvpeplVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLlT 152
Cdd:cd07850    81 YLVMELMDANlcqVIQmDLD-HER------MSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLART-A 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 153 GPGDYYTDYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLG----DLIPRHQQv 228
Cdd:cd07850   153 GTSFMMTPYVVTRYYRAPEVILG-MGYKENVDIWSVGCIMGEMIRGTVLFPGTDHIDQWNKIIEQLGtpsdEFMSRLQP- 230
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039741915 229 fSMNQY------FSGVKIPD--PEDMetlelkFPNISYS--------ALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd07850   231 -TVRNYvenrpkYAGYSFEElfPDVL------FPPDSEEhnklkasqARDLLSKMLVIDPEKRISVDDALQHPY 297
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
1-287 9.16e-42

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 148.62  E-value: 9.16e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIKK------IALREIRMLKQL-KHP-----NLVNLLE 68
Cdd:cd14226    12 MDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIK---------IIKNkkaflnQAQIEVRLLELMnKHDtenkyYIVRLKR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  69 VFRRKRRLHLVFEYCDHTvLHELDRYQ--RGVPEPLVKNITWQTLQAVNFCHKH--NCIHRDVKPENILI--TKQSAIKL 142
Cdd:cd14226    83 HFMFRNHLCLVFELLSYN-LYDLLRNTnfRGVSLNLTRKFAQQLCTALLFLSTPelSIIHCDLKPENILLcnPKRSAIKI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 143 CDFGFArllTGPGDYYTDYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGdLI 222
Cdd:cd14226   162 IDFGSS---CQLGQRIYQYIQSRFYRSPEVLLG-LPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLG-MP 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 223 PRH--QQVFSMNQYFS------------------------------GVKIPDP------EDMETLE--LKFPNisysalg 262
Cdd:cd14226   237 PVHmlDQAPKARKFFEklpdgtyylkktkdgkkykppgsrklheilGVETGGPggrragEPGHTVEdyLKFKD------- 309
                         330       340
                  ....*....|....*....|....*
gi 1039741915 263 FLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14226   310 LILRMLDYDPKTRITPAEALQHSFF 334
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
2-287 2.83e-41

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 145.07  E-value: 2.83e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRfLETEDDPViKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd06647     7 KKYTRFEKIGQGASGTVYTAIDVATGQEVAIKQ-MNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELdRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDY 161
Cdd:cd06647    85 YLAGGSLTDV-VTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTM 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 162 VATRWYRSPElLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIrKTLGDliprhqqvfsmnqyfsgvkiP 241
Cdd:cd06647   164 VGTPYWMAPE-VVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-ATNGT--------------------P 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1039741915 242 DPEDMETLELKFPNisysalgFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd06647   222 ELQNPEKLSAIFRD-------FLNRCLEMDVEKRGSAKELLQHPFL 260
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
3-286 3.10e-41

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 144.84  E-value: 3.10e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIK--RFLETEDDPVIKKIAlREIRMLKQLKHPNLVNLLEVFRRKRRLHLVF 80
Cdd:cd14073     2 RYELLETLGKGTYGKVKLAIERATGREVAIKsiKKDKIEDEQDMVRIR-REIEIMSSLNHPHIIRIYEVFENKDKIVIVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  81 EYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgPGDYYTD 160
Cdd:cd14073    81 EYASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLYS-KDKLLQT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 YVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGkSDVDQLYlirktlgdliprhQQVfSMNQYFsgvKI 240
Cdd:cd14073   160 FCGSPLYASPEIVNGTPYQGPEVDCWSLGVLLYTLVYGTMPFDG-SDFKRLV-------------KQI-SSGDYR---EP 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1039741915 241 PDPEDmetlelkfpnisysALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14073   222 TQPSD--------------ASGLIRWMLTVNPKRRATIEDIANHWW 253
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
3-286 3.94e-41

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 144.93  E-value: 3.94e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIK-----RFLETEDDPvikKIALREIRMLKQLKHPNLVNLLEVFRRKRRLH 77
Cdd:cd14098     1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKqivkrKVAGNDKNL---QLFQREINILKSLEHPGIVRLIDWYEDDQHIY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  78 LVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA--IKLCDFGFARlLTGPG 155
Cdd:cd14098    78 LVMEYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPviVKISDFGLAK-VIHTG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 156 DYYTDYVATRWYRSPELLVGDTQYGPP-----VDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTlgdliprhqqvfs 230
Cdd:cd14098   157 TFLVTFCGTMAYLAPEILMSKEQNLQGgysnlVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKG------------- 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 231 mnqyfsgvKIPDPEDMETlelkfpNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14098   224 --------RYTQPPLVDF------NISEEAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
3-283 7.44e-41

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 144.42  E-value: 7.44e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFL-----ETEDDPVIKKIALREIRMLKQL-KHPNLVNLLEVFRRKRRL 76
Cdd:cd13993     1 RYQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYksgpnSKDGNDFQKLPQLREIDLHRRVsRHPNIITLHDVFETEVAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  77 HLVFEYCDHTVLHEL---DRYQRGVPEpLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQS-AIKLCDFGFARllt 152
Cdd:cd13993    81 YIVLEYCPNGDLFEAiteNRIYVGKTE-LIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEgTVKLCDFGLAT--- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 153 gPGDYYTDY-VATRWYRSPELLVGDTQYGP-----PVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLirktlgdliprhq 226
Cdd:cd13993   157 -TEKISMDFgVGSEFYMAPECFDEVGRSLKgypcaAGDIWSLGIILLNLTFGRNPWKIASESDPIFY------------- 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039741915 227 qvfsmnqYFSGvkipdpeDMETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQ 283
Cdd:cd13993   223 -------DYYL-------NSPNLFDVILPMSDDFYNLLRQIFTVNPNNRILLPELQL 265
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
9-283 7.69e-41

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 143.84  E-value: 7.69e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915    9 KIGEGSYGVVFKCR----NRDTGQIVAIKRFLETEDDPVIKKIaLREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:smart00221   6 KLGEGAFGEVYKGTlkgkGDGKEVEVAVKTLKEDASEQQIEEF-LREARIMRKLDHPNIVKLLGVCTEEEPLMIVMEYMP 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   85 HTVLHELDRYQRGVPEPLVK--NITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgPGDYYTDYV 162
Cdd:smart00221  85 GGDLLDYLRKNRPKELSLSDllSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLY-DDDYYKVKG 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  163 A---TRWYrSPELLVgDTQYGPPVDVWAIGCVFAELLS-GVPLWPGKSDVDQLYLIRKtlGDLIPRhqqvfsmnqyfsgv 238
Cdd:smart00221 164 GklpIRWM-APESLK-EGKFTSKSDVWSFGVLLWEIFTlGEEPYPGMSNAEVLEYLKK--GYRLPK-------------- 225
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1039741915  239 kiPD--PEDMETLelkfpnisysalgfLKGCLHMDPAERLTCEQLLQ 283
Cdd:smart00221 226 --PPncPPELYKL--------------MLQCWAEDPEDRPTFSELVE 256
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
9-283 1.03e-40

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 143.44  E-value: 1.03e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915    9 KIGEGSYGVVFKCR----NRDTGQIVAIKRFLETEDDPVIKKIaLREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:smart00219   6 KLGEGAFGEVYKGKlkgkGGKKKVEVAVKTLKEDASEQQIEEF-LREARIMRKLDHPNVVKLLGVCTEEEPLYIVMEYME 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   85 HTVLHELDRYQRG-VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgPGDYYTDYVA 163
Cdd:smart00219  85 GGDLLSYLRKNRPkLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLY-DDDYYRKRGG 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  164 ---TRWYrSPELLVgDTQYGPPVDVWAIGCVFAELLS-GVPLWPGKSDVDQLYLIRKtlGDLIPRhqqvfsmnqyfsgvk 239
Cdd:smart00219 164 klpIRWM-APESLK-EGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEYLKN--GYRLPQ--------------- 224
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1039741915  240 iPD--PEDMETLelkfpnisysalgfLKGCLHMDPAERLTCEQLLQ 283
Cdd:smart00219 225 -PPncPPELYDL--------------MLQCWAEDPEDRPTFSELVE 255
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
3-287 1.59e-40

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 145.23  E-value: 1.59e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIK------RFLETeddpvikkiALREIRMLKQLKHP------NLVNLLEVF 70
Cdd:cd14225    44 RYEILEVIGKGSFGQVVKALDHKTNEHVAIKiirnkkRFHHQ---------ALVEVKILDALRRKdrdnshNVIHMKEYF 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  71 RRKRRLHLVFEYCDHTvLHEL---DRYQrGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITK--QSAIKLCDF 145
Cdd:cd14225   115 YFRNHLCITFELLGMN-LYELikkNNFQ-GFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQrgQSSIKVIDF 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 146 G-----FARLLTgpgdyytdYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGD 220
Cdd:cd14225   193 GsscyeHQRVYT--------YIQSRFYRSPEVILG-LPYSMAIDMWSLGCILAELYTGYPLFPGENEVEQLACIMEVLGL 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 221 LIPRHQQVFSMNQYFSGVK--------------IPDPEDMeTLELKFPNISYsaLGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14225   264 PPPELIENAQRRRLFFDSKgnprcitnskgkkrRPNSKDL-ASALKTSDPLF--LDFIRRCLEWDPSKRMTPDEALQHEW 340

                  .
gi 1039741915 287 F 287
Cdd:cd14225   341 I 341
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
4-287 3.33e-40

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 142.15  E-value: 3.33e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETE-DDPVIKKIaLREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd14071     2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQlDEENLKKI-YREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgPGDYYTDYV 162
Cdd:cd14071    81 ASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFK-PGELLKTWC 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 163 ATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGV-PLwpgksDVDQLYLIRKTLgdLIPRHQQVFSMNqyfsgvkip 241
Cdd:cd14071   160 GSPPYAAPEVFEGKEYEGPQLDIWSLGVVLYVLVCGAlPF-----DGSTLQTLRDRV--LSGRFRIPFFMS--------- 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1039741915 242 dpEDMETLelkfpnisysalgfLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14071   224 --TDCEHL--------------IRRMLVLDPSKRLTIEQIKKHKWM 253
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
6-287 9.99e-40

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 140.85  E-value: 9.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   6 KIGK-IGEGSYGVVFKCRNRDTGQIVAIK----RFLETEDdpVIKKIAlREIRMLKQLKHPNLVNLLEVFRRKRRLHLVF 80
Cdd:cd14081     4 RLGKtLGKGQTGLVKLAKHCVTGQKVAIKivnkEKLSKES--VLMKVE-REIAIMKLIEHPNVLKLYDVYENKKYLYLVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  81 EYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARlLTGPGDYYTD 160
Cdd:cd14081    81 EYVSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMAS-LQPEGSLLET 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 YVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSG-VPLwpGKSDVDQLYLIRKtlgdliprhQQVFSMNQYFSgvk 239
Cdd:cd14081   160 SCGSPHYACPEVIKGEKYDGRKADIWSCGVILYALLVGaLPF--DDDNLRQLLEKVK---------RGVFHIPHFIS--- 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1039741915 240 iPDPEDMetlelkfpnisysalgfLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14081   226 -PDAQDL-----------------LRRMLEVNPEKRITIEEIKKHPWF 255
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
2-286 3.30e-39

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 140.13  E-value: 3.30e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDpvIKKIALrEIRMLKQL-KHPNLVNLLEVFRRKR------ 74
Cdd:cd06608     6 GIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDE--EEEIKL-EINILRKFsNHPNIATFYGAFIKKDppggdd 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  75 RLHLVFEYCDHTVLHEL----DRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARL 150
Cdd:cd06608    83 QLWLVMEYCGGGSVTDLvkglRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVSAQ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 151 LTGPGDYYTDYVATRWYRSPELLVGDTQ----YGPPVDVWAIGCVFAELLSGVPlwPgksdvdqlylirktLGDLIPrhq 226
Cdd:cd06608   163 LDSTLGRRNTFIGTPYWMAPEVIACDQQpdasYDARCDVWSLGITAIELADGKP--P--------------LCDMHP--- 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 227 qvfsMNQYFSGVKIPDPedmetlELKFP-NISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd06608   224 ----MRALFKIPRNPPP------TLKSPeKWSKEFNDFISECLIKNYEQRPFTEELLEHPF 274
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
3-286 5.44e-39

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 139.00  E-value: 5.44e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIKKIALR--------EIRMLKQLKHPNLVNLLEVFRRKR 74
Cdd:cd14095     1 KYDIGRVIGDGNFAVVKECRDKATDKEYALK---------IIDKAKCKgkehmienEVAILRRVKHPNIVQLIEEYDTDT 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  75 RLHLVFEYCDHTVLHELDRYQRGVPEP----LVKNITwqtlQAVNFCHKHNCIHRDVKPENILITKQS----AIKLCDFG 146
Cdd:cd14095    72 ELYLVMELVKGGDLFDAITSSTKFTERdasrMVTDLA----QALKYLHSLSIVHRDIKPENLLVVEHEdgskSLKLADFG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 147 FARLLTGPgdYYT-----DYVAtrwyrsPELLvGDTQYGPPVDVWAIGCVFAELLSGVPlwPGKS-DVDQLYLIRKTLgd 220
Cdd:cd14095   148 LATEVKEP--LFTvcgtpTYVA------PEIL-AETGYGLKVDIWAAGVITYILLCGFP--PFRSpDRDQEELFDLIL-- 214
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 221 liprhqqvfsmnqyfSGvkipdpedmetlELKFP-----NISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14095   215 ---------------AG------------EFEFLspywdNISDSAKDLISRMLVVDPEKRYSAGQVLDHPW 258
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
2-297 6.00e-39

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 140.24  E-value: 6.00e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRfLETEDDPViKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd06655    19 KKYTRYEKIGQGASGTVFTAIDVATGQEVAIKQ-INLQKQPK-KELIINEILVMKELKNPNIVNFLDSFLVGDELFVVME 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELdRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDY 161
Cdd:cd06655    97 YLAGGSLTDV-VTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSKRSTM 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 162 VATRWYRSPElLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTlgdliprhqqvfsmnqyfsgvKIP 241
Cdd:cd06655   176 VGTPYWMAPE-VVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATN---------------------GTP 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 242 DPEDMETLELKFPNisysalgFLKGCLHMDPAERLTCEQLLQHPYFDSIREVGELT 297
Cdd:cd06655   234 ELQNPEKLSPIFRD-------FLNRCLEMDVEKRGSAKELLQHPFLKLAKPLSSLT 282
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
10-286 6.26e-39

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 139.44  E-value: 6.26e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLETE-----DDPVIKKI--ALR-EIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd06629     9 IGKGTYGRVYLAMNATTGEMLAVKQVELPKtssdrADSRQKTVvdALKsEIDTLKDLDHPNIVQYLGFEETEDYFSIFLE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDH-TVLHELDRYqRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARlltGPGDYYTD 160
Cdd:cd06629    89 YVPGgSIGSCLRKY-GKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISK---KSDDIYGN 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 YVATR-----WYRSPELLVGDTQ-YGPPVDVWAIGCVFAELLSGVPLWpgkSDVDQLYLIRKtlgdliprhqqVFSMNQy 234
Cdd:cd06629   165 NGATSmqgsvFWMAPEVIHSQGQgYSAKVDIWSLGCVVLEMLAGRRPW---SDDEAIAAMFK-----------LGNKRS- 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 235 fsgvKIPDPEDMetlelkfpNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd06629   230 ----APPVPEDV--------NLSPEALDFLNACFAIDPRDRPTAAELLSHPF 269
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
9-284 9.62e-39

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 138.44  E-value: 9.62e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCR---NRDTGQIVAIKRFLETEDDPVIKKIaLREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDH 85
Cdd:cd00192     2 KLGEGAFGEVYKGKlkgGDGKTVDVAVKTLKEDASESERKDF-LKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYMEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 TVLHE-LDRYQRGVPEPLVKNITWQTLqaVNFC----------HKHNCIHRDVKPENILITKQSAIKLCDFGFARLLtgp 154
Cdd:cd00192    81 GDLLDfLRKSRPVFPSPEPSTLSLKDL--LSFAiqiakgmeylASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDI--- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 155 gDYYTDYVAT-------RWYrSPELLVgDTQYGPPVDVWAIGCVFAELLS--GVPlWPGKSDVDQLYLIRKtlgdliprh 225
Cdd:cd00192   156 -YDDDYYRKKtggklpiRWM-APESLK-DGIFTSKSDVWSFGVLLWEIFTlgATP-YPGLSNEEVLEYLRK--------- 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 226 qqvfsmnqyfsGVKIPDPEDMetlelkfPNISYSalgFLKGCLHMDPAERLTCEQLLQH 284
Cdd:cd00192   223 -----------GYRLPKPENC-------PDELYE---LMLSCWQLDPEDRPTFSELVER 260
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
2-287 1.02e-38

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 138.64  E-value: 1.02e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRfLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd06610     1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKR-IDLEKCQTSMDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELDRY---QRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYY 158
Cdd:cd06610    80 LLSGGSLLDIMKSsypRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSASLATGGDRT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 ----TDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPlwPGkSDVDQLYLIRKTLGDliprhqqvfsmnqy 234
Cdd:cd06610   160 rkvrKTFVGTPCWMAPEVMEQVRGYDFKADIWSFGITAIELATGAA--PY-SKYPPMKVLMLTLQN-------------- 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039741915 235 fsgvkipDPEDMETlelkfpNISYSALG-----FLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd06610   223 -------DPPSLET------GADYKKYSksfrkMISLCLQKDPSKRPTAEELLKHKFF 267
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
4-283 1.52e-38

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 138.38  E-value: 1.52e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRF-LETEDDPV--IKkialREIRMLKQLKH---PNLVNLLEVFRRKRRLH 77
Cdd:cd06917     3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLnLDTDDDDVsdIQ----KEVALLSQLKLgqpKNIIKYYGSYLKGPSLW 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  78 LVFEYCDHTVLHELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDY 157
Cdd:cd06917    79 IIMDYCEGGSIRTLMRAGP-IAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSSK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 158 YTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWpgkSDVDQLYLIRktlgdLIPRHQQvfsmnqyfsg 237
Cdd:cd06917   158 RSTFVGTPYWMAPEVITEGKYYDTKADIWSLGITTYEMATGNPPY---SDVDALRAVM-----LIPKSKP---------- 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1039741915 238 vkiPdpedmetlelKFPNISYSAL--GFLKGCLHMDPAERLTCEQLLQ 283
Cdd:cd06917   220 ---P----------RLEGNGYSPLlkEFVAACLDEEPKDRLSADELLK 254
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
10-286 2.15e-38

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 137.54  E-value: 2.15e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLH 89
Cdd:cd14074    11 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDDVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLILELGDGGDMY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  90 E-LDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILI-TKQSAIKLCDFGFARLLTgPGDYYTDYVATRWY 167
Cdd:cd14074    91 DyIMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQ-PGEKLETSCGSLAY 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 168 RSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIrktlgdliprhqqvfsMNQYFSgvkIPDpedme 247
Cdd:cd14074   170 SAPEILLGDEYDAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMI----------------MDCKYT---VPA----- 225
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1039741915 248 tlelkfpNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14074   226 -------HVSPECKDLIRRMLIRDPKKRASLEEIENHPW 257
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
3-286 2.35e-38

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 140.65  E-value: 2.35e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIK------RFleteddpviKKIALREIRMLKQLKHP------NLVNLLEVF 70
Cdd:cd14224    66 RYEVLKVIGKGSFGQVVKAYDHKTHQHVALKmvrnekRF---------HRQAAEEIRILEHLKKQdkdntmNVIHMLESF 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  71 RRKRRLHLVFEYCDHTvLHEL---DRYQrGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQ--SAIKLCDF 145
Cdd:cd14224   137 TFRNHICMTFELLSMN-LYELikkNKFQ-GFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQgrSGIKVIDF 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 146 GFA-----RLLTgpgdyytdYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLG- 219
Cdd:cd14224   215 GSScyehqRIYT--------YIQSRFYRAPEVILG-ARYGMPIDMWSFGCILAELLTGYPLFPGEDEGDQLACMIELLGm 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 220 ------DLIPRHQQVFSMN---QYFSGVKIPD-----------------PEDMETLELKFPNISYSA-LGFLKGCLHMDP 272
Cdd:cd14224   286 ppqkllETSKRAKNFISSKgypRYCTVTTLPDgsvvlnggrsrrgkmrgPPGSKDWVTALKGCDDPLfLDFLKRCLEWDP 365
                         330
                  ....*....|....
gi 1039741915 273 AERLTCEQLLQHPY 286
Cdd:cd14224   366 AARMTPSQALRHPW 379
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
3-197 4.64e-38

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 136.48  E-value: 4.64e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd08218     1 KYVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHELDRYQRGVPEPLVKNITW--QTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTD 160
Cdd:cd08218    81 CDGGDLYKRINAQRGVLFPEDQILDWfvQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVELART 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1039741915 161 YVATRWYRSPElLVGDTQYGPPVDVWAIGCVFAELLS 197
Cdd:cd08218   161 CIGTPYYLSPE-ICENKPYNNKSDIWALGCVLYEMCT 196
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
3-287 5.35e-38

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 138.12  E-value: 5.35e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTG-QIVAIK--RfleteDDPVIKKIALREIRMLKQL--------KHpnLVNLLEVFR 71
Cdd:cd14135     1 RYRVYGYLGKGVFSNVVRARDLARGnQEVAIKiiR-----NNELMHKAGLKELEILKKLndadpddkKH--CIRLLRHFE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  72 RKRRLHLVFEyCDHTVLHE-LDRYQRGV--PEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILIT-KQSAIKLCDFGF 147
Cdd:cd14135    74 HKNHLCLVFE-SLSMNLREvLKKYGKNVglNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNeKKNTLKLCDFGS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 148 ArLLTGPGDYyTDYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLG----DLIP 223
Cdd:cd14135   153 A-SDIGENEI-TPYLVSRFYRAPEIILG-LPYDYPIDMWSVGCTLYELYTGKILFPGKTNNHMLKLMMDLKGkfpkKMLR 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 224 RHQQV---FSMNQYFSGVKIpDP----EDMETLELKFPN-------ISYSALG------------FLKGCLHMDPAERLT 277
Cdd:cd14135   230 KGQFKdqhFDENLNFIYREV-DKvtkkEVRRVMSDIKPTkdlktllIGKQRLPdedrkkllqlkdLLDKCLMLDPEKRIT 308
                         330
                  ....*....|
gi 1039741915 278 CEQLLQHPYF 287
Cdd:cd14135   309 PNEALQHPFI 318
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
2-297 2.10e-37

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 136.00  E-value: 2.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRfLETEDDPViKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd06656    19 KKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQ-MNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELdRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDY 161
Cdd:cd06656    97 YLAGGSLTDV-VTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTM 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 162 VATRWYRSPElLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTlgdliprhqqvfsmnqyfsgvKIP 241
Cdd:cd06656   176 VGTPYWMAPE-VVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATN---------------------GTP 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 242 DPEDMETLELKFPNisysalgFLKGCLHMDPAERLTCEQLLQHPYFDSIREVGELT 297
Cdd:cd06656   234 ELQNPERLSAVFRD-------FLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLT 282
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
4-286 2.34e-37

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 135.03  E-value: 2.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDtGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKH-PNLVNLL--EVFRRKRRLHLVF 80
Cdd:cd14131     3 YEILKQLGKGGSSKVYKVLNPK-KKIYALKRVDLEGADEQTLQSYKNEIELLKKLKGsDRIIQLYdyEVTDEDDYLYMVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  81 EYCDHTVLHELDRYQ-RGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSaIKLCDFGFARLLtgPGD--- 156
Cdd:cd14131    82 ECGEIDLATILKKKRpKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVKGR-LKLIDFGIAKAI--QNDtts 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 157 -YYTDYVATRWYRSPELLVGDTQY---------GPPVDVWAIGCVFAELLSGVPlwPGKSDVDQlylIRKTlgdliprhq 226
Cdd:cd14131   159 iVRDSQVGTLNYMSPEAIKDTSASgegkpkskiGRPSDVWSLGCILYQMVYGKT--PFQHITNP---IAKL--------- 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 227 qvfsmnqyfsgVKIPDPedmeTLELKFPNISY-SALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14131   225 -----------QAIIDP----NHEIEFPDIPNpDLIDVMKRCLQRDPKKRPSIPELLNHPF 270
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
10-286 6.25e-37

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 133.81  E-value: 6.25e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRF------LETEDDPVIKKIAL-REIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd06628     8 IGSGSFGSVYLGMNASSGELMAVKQVelpsvsAENKDRKKSMLDALqREIALLRELQHENIVQYLGSSSDANHLNIFLEY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 C-DHTVLHELDRYQrGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFA------RLLTGPG 155
Cdd:cd06628    88 VpGGSVATLLNNYG-AFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISkkleanSLSTKNN 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 156 DYYTDYVATRWYRSPElLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPgksDVDQLylirktlgdliprhQQVFSMNQYF 235
Cdd:cd06628   167 GARPSLQGSVFWMAPE-VVKQTSYTRKADIWSLGCLVVEMLTGTHPFP---DCTQM--------------QAIFKIGENA 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 236 SgvkiPDPEdmetlelkfPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd06628   229 S----PTIP---------SNISSEARDFLEKTFEIDHNKRPTADELLKHPF 266
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
2-287 7.34e-37

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 133.94  E-value: 7.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIK------RFLETEDDPVIKKIALREIRMLKQLK-HPNLVNLLEVFRRKR 74
Cdd:cd14181    10 QKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKiievtaERLSPEQLEEVRSSTLKEIHILRQVSgHPSIITLIDSYESST 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  75 RLHLVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLtGP 154
Cdd:cd14181    90 FIFLVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHL-EP 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 155 GDYYTDYVATRWYRSPELL---VGDTQ--YGPPVDVWAIGCVFAELLSGV-PLWPGKsdvdQLYLIRktlgdLIPRHQQV 228
Cdd:cd14181   169 GEKLRELCGTPGYLAPEILkcsMDETHpgYGKEVDLWACGVILFTLLAGSpPFWHRR----QMLMLR-----MIMEGRYQ 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 229 FSmnqyfsgvkipDPEdmetlelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14181   240 FS-----------SPE--------WDDRSSTVKDLISRLLVVDPEIRLTAEQALQHPFF 279
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
4-191 8.16e-37

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 133.46  E-value: 8.16e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKC--RNRDTGQIVAIK---RFLETEDDpvIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHL 78
Cdd:cd14080     2 YRLGKTIGEGSYSKVKLAeyTKSGLKEKVACKiidKKKAPKDF--LEKFLPRELEILRKLRHPNIIQVYSIFERGSKVFI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYY 158
Cdd:cd14080    80 FMEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLCPDDDGDV 159
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1039741915 159 TD--YVATRWYRSPELLVGdTQYGPPV-DVWAIGCV 191
Cdd:cd14080   160 LSktFCGSAAYAAPEILQG-IPYDPKKyDIWSLGVI 194
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
4-286 1.16e-36

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 133.15  E-value: 1.16e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGK-IGEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIKKIALR--------EIRMLKQLKHPNLVNLLEVFRRKR 74
Cdd:cd14185     1 HYEIGRtIGDGNFAVVKECRHWNENQEYAMK---------IIDKSKLKgkedmiesEILIIKSLSHPNIVKLFEVYETEK 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  75 RLHLVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILIT----KQSAIKLCDFGFARL 150
Cdd:cd14185    72 EIYLILEYVRGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQhnpdKSTTLKLADFGLAKY 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 151 LTGPgdYYTdYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPlwPGKS---DVDQLYlirktlgdliprhqQ 227
Cdd:cd14185   152 VTGP--IFT-VCGTPTYVAPEILSE-KGYGLEVDMWAAGVILYILLCGFP--PFRSperDQEELF--------------Q 211
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 228 VFSMNQYfsgvkipdpedmETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14185   212 IIQLGHY------------EFLPPYWDNISEAAKDLISRLLVVDPEKRYTAKQVLQHPW 258
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
4-285 1.47e-36

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 132.51  E-value: 1.47e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLK-HPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd13997     2 FHELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKKPFRGPKERARALREVEAHAALGqHPNIVRYYSSWEEGGHLYIQMEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDH----TVLHELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFA-RLLTGPGDY 157
Cdd:cd13997    82 CENgslqDALEELSPISK-LSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLAtRLETSGDVE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 158 YTDYVatrwYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLwpgksdvdqlylirktlgdliPRHQQvfSMNQYFSG 237
Cdd:cd13997   161 EGDSR----YLAPELLNENYTHLPKADIFSLGVTVYEAATGEPL---------------------PRNGQ--QWQQLRQG 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1039741915 238 vKIPDPEDmetlelkfPNISYSALGFLKGCLHMDPAERLTCEQLLQHP 285
Cdd:cd13997   214 -KLPLPPG--------LVLSQELTRLLKVMLDPDPTRRPTADQLLAHD 252
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
10-287 3.43e-36

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 132.09  E-value: 3.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVA---IKRFLETEDdpVIKKIaLREIRMLKQLK-HPNLVNLLEVFRRKRRLHLVFEYCDH 85
Cdd:cd14106    16 LGRGKFAVVRKCIHKETGKEYAakfLRKRRRGQD--CRNEI-LHEIAVLELCKdCPRVVNLHEVYETRSELILILELAAG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 TVL-HELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA---IKLCDFGFARLLtGPGDYYTDY 161
Cdd:cd14106    93 GELqTLLDEEEC-LTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPlgdIKLCDFGISRVI-GEGEEIREI 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 162 VATRWYRSPELLvgdtQYGP---PVDVWAIGCVFAELLSGVPLWPGKSDvdqlylirktlgdliprhQQVFsMNqyFSGV 238
Cdd:cd14106   171 LGTPDYVAPEIL----SYEPislATDMWSIGVLTYVLLTGHSPFGGDDK------------------QETF-LN--ISQC 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1039741915 239 KIPDPEDMetlelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14106   226 NLDFPEEL------FKDVSPLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
3-287 4.33e-36

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 133.09  E-value: 4.33e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIK------RFLETeddpvikkiALREIRMLKQL-----KHP---NLVNLLE 68
Cdd:cd14136    11 RYHVVRKLGWGHFSTVWLCWDLQNKRFVALKvvksaqHYTEA---------ALDEIKLLKCVreadpKDPgreHVVQLLD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  69 VFRRK----RRLHLVFEYCDHTVLHELDRYQ-RGVPEPLVKNITWQTLQAVNFCHKhNC--IHRDVKPENILIT-KQSAI 140
Cdd:cd14136    82 DFKHTgpngTHVCMVFEVLGPNLLKLIKRYNyRGIPLPLVKKIARQVLQGLDYLHT-KCgiIHTDIKPENVLLCiSKIEV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 141 KLCDFGFArllTGPGDYYTDYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLW---PGKS---DVDQLYLI 214
Cdd:cd14136   161 KIADLGNA---CWTDKHFTEDIQTRQYRSPEVILG-AGYGTPADIWSTACMAFELATGDYLFdphSGEDysrDEDHLALI 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 215 RKTLGDlIPRH--------QQVFSMN---QYFSGVKIPDPEDMETLELKFPNISYSAL-GFLKGCLHMDPAERLTCEQLL 282
Cdd:cd14136   237 IELLGR-IPRSiilsgkysREFFNRKgelRHISKLKPWPLEDVLVEKYKWSKEEAKEFaSFLLPMLEYDPEKRATAAQCL 315

                  ....*
gi 1039741915 283 QHPYF 287
Cdd:cd14136   316 QHPWL 320
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
1-288 4.34e-36

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 134.06  E-value: 4.34e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRL---- 76
Cdd:cd07874    16 LKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKSLeefq 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  77 --HLVFEYCDHTVLHELdryQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARlLTGP 154
Cdd:cd07874    96 dvYLVMELMDANLCQVI---QMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR-TAGT 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 155 GDYYTDYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDLIPRHQQVF--SMN 232
Cdd:cd07874   172 SFMMTPYVVTRYYRAPEVILG-MGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLqpTVR 250
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 233 QY------FSGVKIPD-------PEDMETLELKfpniSYSALGFLKGCLHMDPAERLTCEQLLQHPYFD 288
Cdd:cd07874   251 NYvenrpkYAGLTFPKlfpdslfPADSEHNKLK----ASQARDLLSKMLVIDPAKRISVDEALQHPYIN 315
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
2-297 5.69e-36

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 132.16  E-value: 5.69e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRfLETEDDPViKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd06654    20 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQ-MNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELdRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDY 161
Cdd:cd06654    98 YLAGGSLTDV-VTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTM 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 162 VATRWYRSPElLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTlgdliprhqqvfsmnqyfsgvKIP 241
Cdd:cd06654   177 VGTPYWMAPE-VVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATN---------------------GTP 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 242 DPEDMETLELKFPNisysalgFLKGCLHMDPAERLTCEQLLQHPYFDSIREVGELT 297
Cdd:cd06654   235 ELQNPEKLSAIFRD-------FLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLT 283
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
10-287 6.48e-36

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 130.84  E-value: 6.48e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIK----RFLeteddpviKKIA------LREIRMLKQLKHPNLVNLLEVFR--RKRRLH 77
Cdd:cd14119     1 LGEGSYGKVKEVLDTETLCRRAVKilkkRKL--------RRIPngeanvKREIQILRRLNHRNVIKLVDVLYneEKQKLY 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  78 LVFEYCDHTVLHELDRyqrgvpEPLVKNITWQT-------LQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARL 150
Cdd:cd14119    73 MVMEYCVGGLQEMLDS------APDKRLPIWQAhgyfvqlIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 151 LT--GPGDYYTDYVATRWYRSPELLVGDTQY-GPPVDVWAIGCVFAELLSGvpLWPGKSDvdqlylirktlgdliprhqq 227
Cdd:cd14119   147 LDlfAEDDTCTTSQGSPAFQPPEIANGQDSFsGFKVDIWSAGVTLYNMTTG--KYPFEGD-------------------- 204
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 228 vfsmNQY--FsgvkipdpEDMETLELKFP-NISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14119   205 ----NIYklF--------ENIGKGEYTIPdDVDPDLQDLLRGMLEKDPEKRFTIEQIRQHPWF 255
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
5-287 8.73e-36

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 131.41  E-value: 8.73e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   5 EKIGKIGEGSYGVVFKCRNRDTGQIVAiKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKR-RLHLVFEYC 83
Cdd:cd06620     8 ETLKDLGAGNGGSVSKVLHIPTGTIMA-KKVIHIDAKSSVRKQILRELQILHECHSPYIVSFYGAFLNENnNIIICMEYM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 DHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCH-KHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgpGDYYTDYV 162
Cdd:cd06620    87 DCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYnVHRIIHRDIKPSNILVNSKGQIKLCDFGVSGELI--NSIADTFV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 163 ATRWYRSPELLVGDtQYGPPVDVWAIGCVFAELLSG-VPLWpGKSDVDQLYLIRKTLGDLIprhQQVfsmnqyfsgVKIP 241
Cdd:cd06620   165 GTSTYMSPERIQGG-KYSVKSDVWSLGLSIIELALGeFPFA-GSNDDDDGYNGPMGILDLL---QRI---------VNEP 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1039741915 242 DPedmeTL--ELKFPNIsysALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd06620   231 PP----RLpkDRIFPKD---LRDFVDRCLLKDPRERPSPQLLLDHDPF 271
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
9-286 1.19e-35

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 130.10  E-value: 1.19e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKC-RNRDTGQIVAIKRFLETEddpvIKKIA----LREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYC 83
Cdd:cd14121     2 KLGSGTYATVYKAyRKSGAREVVAVKCVSKSS----LNKAStenlLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 DHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITK--QSAIKLCDFGFARLLTgPGDYYTDY 161
Cdd:cd14121    78 SGGDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSryNPVLKLADFGFAQHLK-PNDEAHSL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 162 VATRWYRSPELLVGDtQYGPPVDVWAIGCVFAELLSGVPlwPGKSdvdqlylirKTLGDLIprhqqvfsmnqyfsgVKIP 241
Cdd:cd14121   157 RGSPLYMAPEMILKK-KYDARVDLWSVGVILYECLFGRA--PFAS---------RSFEELE---------------EKIR 209
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1039741915 242 DPEDMETleLKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14121   210 SSKPIEI--PTRPELSADCRDLLLRLLQRDPDRRISFEEFFAHPF 252
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
2-312 1.19e-35

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 130.92  E-value: 1.19e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGqIVAIKRFLETEDDPVIKKIALrEIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd06643     5 DFWEIVGELGDGAFGKVYKAQNKETG-ILAAAKVIDTKSEEELEDYMV-EIDILASCDHPNIVKLLDAFYYENNLWILIE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCD----HTVLHELdryQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDY 157
Cdd:cd06643    83 FCAggavDAVMLEL---ERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTLQR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 158 YTDYVATRWYRSPELLVGDTQYGPP----VDVWAIGCVFAELlsgvplwpgksdvdqlylirktlGDLIPRHQQVFSMNQ 233
Cdd:cd06643   160 RDSFIGTPYWMAPEVVMCETSKDRPydykADVWSLGVTLIEM-----------------------AQIEPPHHELNPMRV 216
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 234 YFSGVKiPDPEDMETLELKFPNISysalGFLKGCLHMDPAERLTCEQLLQHPYFDSIREvgeltrqhDKPARKTLRQSR 312
Cdd:cd06643   217 LLKIAK-SEPPTLAQPSRWSPEFK----DFLRKCLEKNVDARWTTSQLLQHPFVSVLVS--------NKPLRELIAEAK 282
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
3-198 1.22e-35

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 130.33  E-value: 1.22e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd14072     1 NYRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 C------DHTVLHelDRYQRgvPEPLVKniTWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgPGD 156
Cdd:cd14072    81 AsggevfDYLVAH--GRMKE--KEARAK--FRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFT-PGN 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1039741915 157 YYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSG 198
Cdd:cd14072   154 KLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSG 195
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
2-286 1.60e-35

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 131.72  E-value: 1.60e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAiKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd06650     5 DDFEKISELGAGNGGVVFKVSHKPSGLVMA-RKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICME 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFC-HKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgpGDYYTD 160
Cdd:cd06650    84 HMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLrEKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLI--DSMANS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 YVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSG-VPLWPGKSDVDQLYLIRKTLGDLIPRHQQVFSMNQYFSGVK 239
Cdd:cd06650   162 FVGTRSYMSPERLQG-THYSVQSDIWSMGLSLVEMAVGrYPIPPPDAKELELMFGCQVEGDAAETPPRPRTPGRPLSSYG 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 240 IPDPEDMETLEL----------KFPNISYSA--LGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd06650   241 MDSRPPMAIFELldyivnepppKLPSGVFSLefQDFVNKCLIKNPAERADLKQLMVHAF 299
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
2-290 1.94e-35

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 130.54  E-value: 1.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrFLETEDDPVIKKIALrEIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd06644    12 EVWEIIGELGDGAFGKVYKAKNKETGALAAAK-VIETKSEEELEDYMV-EIEILATCNHPYIVKLLGAFYWDGKLWIMIE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YC-----DHTVLhELDRyqrGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGD 156
Cdd:cd06644    90 FCpggavDAIML-ELDR---GLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQ 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 157 YYTDYVATRWYRSPELLV----GDTQYGPPVDVWAIGCVFAELlsgvplwpgksdvdqlylirktlGDLIPRHQQVFSMN 232
Cdd:cd06644   166 RRDSFIGTPYWMAPEVVMcetmKDTPYDYKADIWSLGITLIEM-----------------------AQIEPPHHELNPMR 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 233 QYFSGVKiPDPEDMET---LELKFPNisysalgFLKGCLHMDPAERLTCEQLLQHPYFDSI 290
Cdd:cd06644   223 VLLKIAK-SEPPTLSQpskWSMEFRD-------FLKTALDKHPETRPSAAQLLEHPFVSSV 275
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
2-310 1.94e-35

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 130.62  E-value: 1.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIK----RFLETEDdpvIKKIAlREIRMLKQLKHPNLVNLLEVFRRKRRLH 77
Cdd:cd14086     1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKiintKKLSARD---HQKLE-REARICRLLKHPNIVRLHDSISEEGFHY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  78 LVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILI---TKQSAIKLCDFGFARLLTGP 154
Cdd:cd14086    77 LVFDLVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIEVQGD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 155 GDYYTDYVATRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLSGV-PLWpgKSDVDQLYlirktlgdliprhQQVFSMNQ 233
Cdd:cd14086   157 QQAWFGFAGTPGYLSPEVLRKDP-YGKPVDIWACGVILYILLVGYpPFW--DEDQHRLY-------------AQIKAGAY 220
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039741915 234 YFsgvkiPDPE-DMETLELKfpnisysalGFLKGCLHMDPAERLTCEQLLQHPYFdsirevgeltRQHDKPARKTLRQ 310
Cdd:cd14086   221 DY-----PSPEwDTVTPEAK---------DLINQMLTVNPAKRITAAEALKHPWI----------CQRDRVASMVHRQ 274
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
2-315 2.21e-35

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 130.74  E-value: 2.21e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQ-----IVAIKRF-----LETEDdpvIKkialREIRMLKQLKHPNLVNLLEVFR 71
Cdd:cd14094     3 DVYELCEVIGKGPFSVVRRCIHRETGQqfavkIVDVAKFtsspgLSTED---LK----REASICHMLKHPHIVELLETYS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  72 RKRRLHLVFEYCDHTVLHeLDRYQRGV-----PEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILI--TKQSA-IKLC 143
Cdd:cd14094    76 SDGMLYMVFEFMDGADLC-FEIVKRADagfvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLasKENSApVKLG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 144 DFGFARLLTGPGDYYTDYVATRWYRSPELLVGDtQYGPPVDVWAIGCVFAELLSGVPLWPGkSDVDQLYLIRKTLGDLIP 223
Cdd:cd14094   155 GFGVAIQLGESGLVAGGRVGTPHFMAPEVVKRE-PYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNP 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 224 RhqqvfsmnqyfsgvkipdpedmetlelKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYfdsIREvgeltRQHDKP 303
Cdd:cd14094   233 R---------------------------QWSHISESAKDLVRRMLMLDPAERITVYEALNHPW---IKE-----RDRYAY 277
                         330
                  ....*....|..
gi 1039741915 304 arktlrqsRKHL 315
Cdd:cd14094   278 --------RIHL 281
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
2-286 3.52e-35

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 129.11  E-value: 3.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIK-KIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVF 80
Cdd:cd06607     1 KIFEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTEKwQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  81 EYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgPGdyyTD 160
Cdd:cd06607    81 EYCLGSASDIVEVHKKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSASLVC-PA---NS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 YVATRWYRSPE--LLVGDTQYGPPVDVWAIGCVFAELLSgvplwpgksdvdqlylirktlgdlipRHQQVFSMNQYFSGV 238
Cdd:cd06607   157 FVGTPYWMAPEviLAMDEGQYDGKVDVWSLGITCIELAE--------------------------RKPPLFNMNAMSALY 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039741915 239 KIP--DPEDMETLELkfpniSYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd06607   211 HIAqnDSPTLSSGEW-----SDDFRNFVDSCLQKIPQDRPSAEDLLKHPF 255
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
3-287 6.29e-35

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 128.27  E-value: 6.29e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIK-----RFLET--EDDPVIKKIALrEIRMLKQLK---HPNLVNLLEVFRR 72
Cdd:cd14004     1 DYTILKEMGEGAYGQVNLAIYKSKGKEVVIKfifkeRILVDtwVRDRKLGTVPL-EIHILDTLNkrsHPNIVKLLDFFED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  73 KRRLHLVFEyCDHTVLHELDRYQR--GVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARL 150
Cdd:cd14004    80 DEFYYLVME-KHGSGMDLFDFIERkpNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSAAY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 151 LTgPGDYYTdYVATRWYRSPELLVGDTQYGPPVDVWAIGCVfaellsgvplwpgksdvdqLYLIrktlgdliprhqqVFS 230
Cdd:cd14004   159 IK-SGPFDT-FVGTIDYAAPEVLRGNPYGGKEQDIWALGVL-------------------LYTL-------------VFK 204
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039741915 231 MNQYFSGVKIPDPedmetlELKFPN-ISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14004   205 ENPFYNIEEILEA------DLRIPYaVSEDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
3-287 1.04e-34

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 129.34  E-value: 1.04e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYE---KIGKIGEGSYGVVFKCRNRDTGQIVAIKrfleteddPVIKKI-ALREIRMLKQLK-HPNLVNLLEVFRRKRRLH 77
Cdd:cd14092     4 NYEldlREEALGDGSFSVCRKCVHKKTGQEFAVK--------IVSRRLdTSREVQLLRLCQgHPNIVKLHEVFQDELHTY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  78 LVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILIT---KQSAIKLCDFGFARLLTGP 154
Cdd:cd14092    76 LVMELLRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTdedDDAEIKIVDFGFARLKPEN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 155 GDYYTDyVATRWYRSPELLVGDTQ---YGPPVDVWAIGCVFAELLSG-VPLWPGKSDVDQLYLIRK-TLGDliprhqqvF 229
Cdd:cd14092   156 QPLKTP-CFTLPYAAPEVLKQALStqgYDESCDLWSLGVILYTMLSGqVPFQSPSRNESAAEIMKRiKSGD--------F 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039741915 230 SmnqyFSGvkipdpedmetleLKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14092   227 S----FDG-------------EEWKNVSSEAKSLIQGLLTVDPSKRLTMSELRNHPWL 267
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
4-285 1.06e-34

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 127.42  E-value: 1.06e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLK-HPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd14050     3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDRKRKLEEVERHEKLGeHPNCVRFIKAWEEKGILYIQTEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYV 162
Cdd:cd14050    83 CDTSLQQYCEETHS-LPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVELDKEDIHDAQEG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 163 ATRwYRSPELLVGDtqYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLylirktlgdlipRHQQvfsmnqyfsgvkIPD 242
Cdd:cd14050   162 DPR-YMAPELLQGS--FTKAADIFSLGITILELACNLELPSGGDGWHQL------------RQGY------------LPE 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1039741915 243 PedmetlelkFPN-ISYSALGFLKGCLHMDPAERLTCEQLLQHP 285
Cdd:cd14050   215 E---------FTAgLSPELRSIIKLMMDPDPERRPTAEDLLALP 249
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
9-286 1.59e-34

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 127.66  E-value: 1.59e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVL 88
Cdd:cd14097     8 KLGQGSFGVVIEATHKETQTKWAIKKINREKAGSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMELCEDGEL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  89 HELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA-------IKLCDFGFARLLTGPG-DYYTD 160
Cdd:cd14097    88 KELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIIdnndklnIKVTDFGLSVQKYGLGeDMLQE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 YVATRWYRSPELLVGDtQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKtlGDLiprhqqvfsmnqYFSgvki 240
Cdd:cd14097   168 TCGTPIYMAPEVISAH-GYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRK--GDL------------TFT---- 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1039741915 241 pdpedmetlELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14097   229 ---------QSVWQSVSDAAKNVLQQLLKVDPAHRMTASELLDNPW 265
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
1-286 1.93e-34

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 129.76  E-value: 1.93e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEKIGKIGEGSYGVVfkCRNRDT--GQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRL-- 76
Cdd:cd07876    20 LKRYQQLKPIGSGAQGIV--CAAFDTvlGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKSLee 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  77 ----HLVFEYCDHT---VLH-ELDrYQRgvpeplVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFA 148
Cdd:cd07876    98 fqdvYLVMELMDANlcqVIHmELD-HER------MSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 149 RllTGPGDY-YTDYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLG----DLIP 223
Cdd:cd07876   171 R--TACTNFmMTPYVVTRYYRAPEVILG-MGYKENVDIWSVGCIMGELVKGSVIFQGTDHIDQWNKVIEQLGtpsaEFMN 247
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039741915 224 RHQQV---FSMNQ-YFSGVK----IPD---PEDMETLELKfpniSYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd07876   248 RLQPTvrnYVENRpQYPGISfeelFPDwifPSESERDKLK----TSQARDLLSKMLVIDPDKRISVDEALRHPY 317
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
2-287 4.97e-34

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 125.80  E-value: 4.97e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDT-------GQIVAIKRFLETEDDPVIkkiaLREIRMLKQLK-HPNLVNLLEVFRRK 73
Cdd:cd14019     1 NKYRIIEKIGEGTFSSVYKAEDKLHdlydrnkGRLVALKHIYPTSSPSRI----LNELECLERLGgSNNVSGLITAFRNE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  74 RRLHLVFEYCDHTVLHEldrYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAI-KLCDFGFARLLT 152
Cdd:cd14019    77 DQVVAVLPYIEHDDFRD---FYRKMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNRETGKgVLVDFGLAQREE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 153 GPGDYYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGV-PLWPGKSDVDQLYLIRKTLGdliprhqqvfsm 231
Cdd:cd14019   154 DRPEQRAPRAGTRGFRAPEVLFKCPHQTTAIDIWSAGVILLSILSGRfPFFFSSDDIDALAEIATIFG------------ 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 232 nqyfsgvkipdpedmetlelkfpniSYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14019   222 -------------------------SDEAYDLLDKLLELDPSKRITAEEALKHPFF 252
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
9-320 5.99e-34

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 127.46  E-value: 5.99e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIK-KIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTV 87
Cdd:cd06633    28 EIGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKwQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEYCLGSA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  88 LHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgPGDyytDYVATRWY 167
Cdd:cd06633   108 SDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIAS-PAN---SFVGTPYW 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 168 RSPELLVG--DTQYGPPVDVWAIGCVFAELLSgvplwpgksdvdqlylirktlgdlipRHQQVFSMNQYFSGVKIPDpED 245
Cdd:cd06633   184 MAPEVILAmdEGQYDGKVDIWSLGITCIELAE--------------------------RKPPLFNMNAMSALYHIAQ-ND 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 246 METLELKfpNISYSALGFLKGCLHMDPAERLTCEQLLQHpyfDSIREvgeltrqhDKPAR------KTLRQSRKHLTGLQ 319
Cdd:cd06633   237 SPTLQSN--EWTDSFRGFVDYCLQKIPQERPSSAELLRH---DFVRR--------ERPPRvlidliQRTKDAVRELDNLQ 303

                  .
gi 1039741915 320 Y 320
Cdd:cd06633   304 Y 304
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
3-195 6.10e-34

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 125.86  E-value: 6.10e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKR------FLETEDdpvikkiALREIRMLKQLKHPNLVNLLEVFRRKRRL 76
Cdd:cd08219     1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEirlpksSSAVED-------SRKEAVLLAKMKHPNIVAFKESFEADGHL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  77 HLVFEYCDHTVLHELDRYQRG--VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGP 154
Cdd:cd08219    74 YIVMEYCDGGDLMQKIKLQRGklFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSP 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1039741915 155 GDYYTDYVATRWYRSPELLvGDTQYGPPVDVWAIGCVFAEL 195
Cdd:cd08219   154 GAYACTYVGTPYYVPPEIW-ENMPYNNKSDIWSLGCILYEL 193
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
5-284 9.63e-34

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 125.30  E-value: 9.63e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   5 EKIGKIGEGSYGVVFKCR----NRDTGQIVAIKRFLETEDDPVIKKIaLREIRMLKQLKHPNLVNLLEVFRRKRRLHLVF 80
Cdd:pfam07714   2 TLGEKLGEGAFGEVYKGTlkgeGENTKIKVAVKTLKEGADEEEREDF-LEEASIMKKLDHPNIVKLLGVCTQGEPLYIVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  81 EYCDHTVLHE-LDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYT 159
Cdd:pfam07714  81 EYMPGGDLLDfLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYDDDYYRK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 160 D---YVATRWYrSPELLVgDTQYGPPVDVWAIGCVFAELLS-GVPLWPGKSDvdqlylirktlgdliprhQQVfsMNQYF 235
Cdd:pfam07714 161 RgggKLPIKWM-APESLK-DGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSN------------------EEV--LEFLE 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1039741915 236 SGVKIPDPEDMeTLELKfpnisysalGFLKGCLHMDPAERLTCEQLLQH 284
Cdd:pfam07714 219 DGYRLPQPENC-PDELY---------DLMKQCWAYDPEDRPTFSELVED 257
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
6-198 1.54e-33

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 124.72  E-value: 1.54e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   6 KIGK-IGEGSYGVVFKCRNRDTGQIVAIK---RFLETEDdpVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd14162     3 IVGKtLGHGSYAVVKKAYSTKHKCKVAIKivsKKKAPED--YLQKFLPREIEVIKGLKHPNLICFYEAIETTSRVYIIME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYT-- 159
Cdd:cd14162    81 LAENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARGVMKTKDGKPkl 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1039741915 160 --DYVATRWYRSPELLVGDTqYGPPV-DVWAIGCVFAELLSG 198
Cdd:cd14162   161 seTYCGSYAYASPEILRGIP-YDPFLsDIWSMGVVLYTMVYG 201
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
2-287 2.62e-33

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 125.24  E-value: 2.62e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAiKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd06615     1 DDFEKLGELGAGNGGVVTKVLHRPSGLIMA-RKLIHLEIKPAIRNQIIRELKVLHECNSPYIVGFYGAFYSDGEISICME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCH-KHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgpGDYYTD 160
Cdd:cd06615    80 HMDGGSLDQVLKKAGRIPENILGKISIAVLRGLTYLReKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLI--DSMANS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 YVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGV-PLWPGKSdvdqlylirKTLGDLIPRHQQ--VFSMNQYFSG 237
Cdd:cd06615   158 FVGTRSYMSPERLQG-THYTVQSDIWSLGLSLVEMAIGRyPIPPPDA---------KELEAMFGRPVSegEAKESHRPVS 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 238 VKIPD-PEDMETLEL----------KFPNISYSA--LGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd06615   228 GHPPDsPRPMAIFELldyivnepppKLPSGAFSDefQDFVDKCLKKNPKERADLKELTKHPFI 290
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
2-286 4.28e-33

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 123.64  E-value: 4.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIKKIALR--------EIRMLKQLKHPNLVNLLEVFRRK 73
Cdd:cd14083     3 DKYEFKEVLGTGAFSEVVLAEDKATGKLVAIK---------CIDKKALKgkedslenEIAVLRKIKHPNIVQLLDIYESK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  74 RRLHLVFEYCDHTVLheLDR-YQRGV-PEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILI---TKQSAIKLCDFGFA 148
Cdd:cd14083    74 SHLYLVMELVTGGEL--FDRiVEKGSyTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYyspDEDSKIMISDFGLS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 149 RlLTGPGDYYTDyVATRWYRSPELLvGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTlgdliprhqqv 228
Cdd:cd14083   152 K-MEDSGVMSTA-CGTPGYVAPEVL-AQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKA----------- 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 229 fsmnQYfsgvkipdpedmetlELKFP---NISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14083   218 ----EY---------------EFDSPywdDISDSAKDFIRHLMEKDPNKRYTCEQALEHPW 259
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
10-287 1.37e-32

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 122.54  E-value: 1.37e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIK-----RFLETEDDPVIKKIaLREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY-C 83
Cdd:cd06630     8 LGTGAFSSCYQARDVKTGTLMAVKqvsfcRNSSSEQEEVVEAI-REEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWmA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 DHTVLHELDRYQrGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILI--TKQSaIKLCDFGFA-RL---LTGPGDY 157
Cdd:cd06630    87 GGSVASLLSKYG-AFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVdsTGQR-LRIADFGAAaRLaskGTGAGEF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 158 YTDYVATRWYRSPELLVGDtQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKtlgdlIPRHQQVFSMNQYFSg 237
Cdd:cd06630   165 QGQLLGTIAFMAPEVLRGE-QYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFK-----IASATTPPPIPEHLS- 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039741915 238 vkiPDPEDmetlelkfpnisysalgFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd06630   238 ---PGLRD-----------------VTLRCLELQPEDRPPARELLKHPVF 267
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
9-287 1.42e-32

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 122.17  E-value: 1.42e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPviKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVL 88
Cdd:cd06648    14 KIGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQR--RELLFNEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGGAL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  89 HELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYVATRWYR 168
Cdd:cd06648    92 TDIVTHTR-MNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWM 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 169 SPElLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRktlgDLIPRHqqvfsmnqyfsgvkipdpedmet 248
Cdd:cd06648   171 APE-VISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIR----DNEPPK----------------------- 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1039741915 249 leLKFP-NISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd06648   223 --LKNLhKVSPRLRSFLDRMLVRDPAQRATAAELLNHPFL 260
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
4-286 1.58e-32

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 122.16  E-value: 1.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFR-RKRRLHLVFEY 82
Cdd:cd08223     2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEgEDGFLYIVMGF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHELDRYQRGVPEPLVKNITW--QTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTD 160
Cdd:cd08223    82 CEGGDLYTRLKEQKGVLLEERQVVEWfvQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSDMATT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 YVATRWYRSPELLvGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKsdvDQLYLIRKTLGDLIPrhqqvfsmnqyfsgvKI 240
Cdd:cd08223   162 LIGTPYYMSPELF-SNKPYNHKSDVWALGCCVYEMATLKHAFNAK---DMNSLVYKILEGKLP---------------PM 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1039741915 241 PDPEDMETLELkfpnisysalgfLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd08223   223 PKQYSPELGEL------------IKAMLHQDPEKRPSVKRILRQPY 256
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
6-287 1.66e-32

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 121.99  E-value: 1.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   6 KIGK-IGEGSYGVVFKCRNRDTGQIVAIK----RFLETEDdpVIKKIAlREIRMLKQLKHPNLVNLLEVFRRKRRLHLVF 80
Cdd:cd14079     5 ILGKtLGVGSFGKVKLAEHELTGHKVAVKilnrQKIKSLD--MEEKIR-REIQILKLFRHPHIIRLYEVIETPTDIFMVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  81 EYCDHTvlhELDRY--QRG-VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGpGDY 157
Cdd:cd14079    82 EYVSGG---ELFDYivQKGrLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNIMRD-GEF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 158 YTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSG-VPLwpgkSDVDQLYLIRKTLGDliprhqqVFSMNQYFS 236
Cdd:cd14079   158 LKTSCGSPNYAAPEVISGKLYAGPEVDVWSCGVILYALLCGsLPF----DDEHIPNLFKKIKSG-------IYTIPSHLS 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 237 gvkiPDPEDMetlelkfpnisysalgfLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14079   227 ----PGARDL-----------------IKRMLVVDPLKRITIPEIRQHPWF 256
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
1-288 2.39e-32

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 124.00  E-value: 2.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRL---- 76
Cdd:cd07875    23 LKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLeefq 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  77 --HLVFEYCDHTVLHELdryQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARlLTGP 154
Cdd:cd07875   103 dvYIVMELMDANLCQVI---QMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR-TAGT 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 155 GDYYTDYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLG--------DLIPRHQ 226
Cdd:cd07875   179 SFMMTPYVVTRYYRAPEVILG-MGYKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVIEQLGtpcpefmkKLQPTVR 257
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 227 QVFSMNQYFSGVK----IPD---PEDMETLELKfpniSYSALGFLKGCLHMDPAERLTCEQLLQHPYFD 288
Cdd:cd07875   258 TYVENRPKYAGYSfeklFPDvlfPADSEHNKLK----ASQARDLLSKMLVIDASKRISVDEALQHPYIN 322
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
2-286 2.46e-32

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 122.55  E-value: 2.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCR-NRDTGQIVAIK--RFLETEDDPV----IKKIaLREIRMLKQLKHPNLVNLLEVFRRKR 74
Cdd:cd14096     1 ENYRLINKIGEGAFSNVYKAVpLRNTGKPVAIKvvRKADLSSDNLkgssRANI-LKEVQIMKRLSHPNIVKLLDFQESDE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  75 RLHLVFEYCDH-TVLHELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILI------------------- 134
Cdd:cd14096    80 YYYIVLELADGgEIFHQIVRLTY-FSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFepipfipsivklrkaddde 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 135 TKQSA--------------IKLCDFGFARLLTgPGDYYTDyVATRWYRSPElLVGDTQYGPPVDVWAIGCVFAELLSGVP 200
Cdd:cd14096   159 TKVDEgefipgvggggigiVKLADFGLSKQVW-DSNTKTP-CGTVGYTAPE-VVKDERYSKKVDMWALGCVLYTLLCGFP 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 201 LWPGKSdvdqlyliRKTLGDLIPRHQQVFsmnqyfsgvkipdpedmetLELKFPNISYSALGFLKGCLHMDPAERLTCEQ 280
Cdd:cd14096   236 PFYDES--------IETLTEKISRGDYTF-------------------LSPWWDEISKSAKDLISHLLTVDPAKRYDIDE 288

                  ....*.
gi 1039741915 281 LLQHPY 286
Cdd:cd14096   289 FLAHPW 294
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
2-286 4.83e-32

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 121.38  E-value: 4.83e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLeTEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKR--RLHLV 79
Cdd:cd06621     1 DKIVELSSLGEGAGGSVTKCRLRNTKTIFALKTIT-TDPNPDVQKQILRELEINKSCASPYIVKYYGAFLDEQdsSIGIA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  80 FEYCDHTVLHEL-----DRYQRGVPEPLVKnITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGP 154
Cdd:cd06621    80 MEYCEGGSLDSIykkvkKKGGRIGEKVLGK-IAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSGELVNS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 155 GDyyTDYVATRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLSG-VPLWPGKSdvDQLYLIrktlgDLIprhqqvfsmnQ 233
Cdd:cd06621   159 LA--GTFTGTSYYMAPERIQGGP-YSITSDVWSLGLTLLEVAQNrFPFPPEGE--PPLGPI-----ELL----------S 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 234 YFSGVKIPDPEDMETLELKFpniSYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd06621   219 YIVNMPNPELKDEPENGIKW---SESFKDFIEKCLEKDGTRRPGPWQMLAHPW 268
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
4-287 5.36e-32

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 121.59  E-value: 5.36e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIKKiALREIR-----MLKQLKHPNLVNLLEVFRRKRRLHL 78
Cdd:cd14091     2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVK---------IIDK-SKRDPSeeieiLLRYGQHPNIITLRDVYDDGNSVYL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTVLheLDR--YQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA----IKLCDFGFAR--- 149
Cdd:cd14091    72 VTELLRGGEL--LDRilRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGdpesLRICDFGFAKqlr 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 150 ----LLTGPgdYYT-DYVAtrwyrsPELLvgDTQ-YGPPVDVWAIGCVFAELLSGV-PLWPGKSDVDQLYLIRKTLGDli 222
Cdd:cd14091   150 aengLLMTP--CYTaNFVA------PEVL--KKQgYDAACDIWSLGVLLYTMLAGYtPFASGPNDTPEVILARIGSGK-- 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039741915 223 prhqqvFSMNqyfSGVkipdpedmetlelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14091   218 ------IDLS---GGN--------------WDHVSDSAKDLVRKMLHVDPSQRPTAAQVLQHPWI 259
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
2-286 8.18e-32

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 120.54  E-value: 8.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIK--RFLETEDDPVIKKialrEIRMLKQLKHPNLVNLLEVFRRKRRLHLV 79
Cdd:cd06645    11 EDFELIQRIGSGTYGDVYKARNVNTGELAAIKviKLEPGEDFAVVQQ----EIIMMKDCKHSNIVAYFGSYLRRDKLWIC 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  80 FEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYT 159
Cdd:cd06645    87 MEFCGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAKRK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 160 DYVATRWYRSPELLVGDTQ--YGPPVDVWAIGCVFAELLSGVPlwpgksdvdqlylirkTLGDLIPRHQQVFSMNQYFSG 237
Cdd:cd06645   167 SFIGTPYWMAPEVAAVERKggYNQLCDIWAVGITAIELAELQP----------------PMFDLHPMRALFLMTKSNFQP 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1039741915 238 VKIPDpedmetlELKFPNisySALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd06645   231 PKLKD-------KMKWSN---SFHHFVKMALTKNPKKRPTAEKLLQHPF 269
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
6-287 1.54e-31

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 119.38  E-value: 1.54e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   6 KIGK-IGEGSYGVVFKCRNRDTGQIVAIKRF-LETEDDPVIKKI-AL-REIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd06625     3 KQGKlLGQGAFGQVYLCYDADTGRELAVKQVeIDPINTEASKEVkALeCEIQLLKNLQHERIVQYYGCLQDEKSLSIFME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLL----TGPGdy 157
Cdd:cd06625    83 YMPGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKRLqticSSTG-- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 158 YTDYVATRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLSGVPLWpgkSDVDQLYLIRKtlgdlIPRHQQVFsmnqyfsg 237
Cdd:cd06625   161 MKSVTGTPYWMSPEVINGEG-YGRKADIWSVGCTVVEMLTTKPPW---AEFEPMAAIFK-----IATQPTNP-------- 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039741915 238 vKIPdpedmetlelkfPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd06625   224 -QLP------------PHVSEDARDFLSLIFVRNKKQRPSAEELLSHSFV 260
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
2-286 1.64e-31

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 119.37  E-value: 1.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYeKIGK-IGEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIKKIALR--------EIRMLKQLKHPNLVNLLEVFRR 72
Cdd:cd14184     1 EKY-KIGKvIGDGNFAVVKECVERSTGKEFALK---------IIDKAKCCgkehlienEVSILRRVKHPNIIMLIEEMDT 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  73 KRRLHLVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILI----TKQSAIKLCDFGFA 148
Cdd:cd14184    71 PAELYLVMELVKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 149 RLLTGPgdYYTdYVATRWYRSPElLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQlylirktlgDLiprhqqv 228
Cdd:cd14184   151 TVVEGP--LYT-VCGTPTYVAPE-IIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNLQE---------DL------- 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 229 fsMNQYFSG-VKIPDPedmetlelKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14184   211 --FDQILLGkLEFPSP--------YWDNITDSAKELISHMLQVNVEARYTAEQILSHPW 259
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
10-284 1.66e-31

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 119.68  E-value: 1.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRnRDTGQIVAIKRfLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLH 89
Cdd:cd14066     1 IGSGGFGTVYKGV-LENGTVVAVKR-LNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  90 ELDRYQRGVPE---PLVKNITWQTLQAVNFCH---KHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTD--- 160
Cdd:cd14066    79 DRLHCHKGSPPlpwPQRLKIAKGIARGLEYLHeecPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSESVSKTsav 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 -----YVATRWYRSPELLVGdtqygppVDVWAIGCVFAELLSGVPlwpgKSDVDQLYLIRKTLGDLIPRHQQVfsmnqyf 235
Cdd:cd14066   159 kgtigYLAPEYIRTGRVSTK-------SDVYSFGVVLLELLTGKP----AVDENRENASRKDLVEWVESKGKE------- 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 236 SGVKIPDPEdmetLELKFPNISYSALGFLK---GCLHMDPAERLTCEQLLQH 284
Cdd:cd14066   221 ELEDILDKR----LVDDDGVEEEEVEALLRlalLCTRSDPSLRPSMKEVVQM 268
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
2-286 1.75e-31

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 119.81  E-value: 1.75e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIK----RFLETEDDPVIKKIA--LREIRMLKQLKHPNLVNLLEVFRRKRR 75
Cdd:cd14084     6 KKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKiinkRKFTIGSRREINKPRniETEIEILKKLSHPCIIKIEDFFDAEDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  76 LHLVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA---IKLCDFGFARLLt 152
Cdd:cd14084    86 YYIVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEeclIKITDFGLSKIL- 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 153 GPGDYYTDYVATRWYRSPELLV--GDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDvdqlyliRKTLGDLIPRHQQVFS 230
Cdd:cd14084   165 GETSLMKTLCGTPTYLAPEVLRsfGTEGYTRAVDCWSLGVILFICLSGYPPFSEEYT-------QMSLKEQILSGKYTFI 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 231 MNQYfsgvkipdpedmetlelkfPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14084   238 PKAW-------------------KNVSEEAKDLVKKMLVVDPSRRPSIEEALEHPW 274
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
3-195 1.80e-31

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 119.30  E-value: 1.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETE-DDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd08224     1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFEmMDAKARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNIVLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELDRY----QRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDY 157
Cdd:cd08224    81 LADAGDLSRLIKHfkkqKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGRFFSSKTTA 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1039741915 158 YTDYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAEL 195
Cdd:cd08224   161 AHSLVGTPYYMSPERIRE-QGYDFKSDIWSLGCLLYEM 197
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
3-197 2.80e-31

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 118.68  E-value: 2.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRF----LETEDdpviKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHL 78
Cdd:cd08220     1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIpveqMTKEE----RQAALNEVKVLSMLHHPNIIEYYESFLEDKALMI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTVLHELDRYQRGV--PEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITK-QSAIKLCDFGFARLLTGPG 155
Cdd:cd08220    77 VMEYAPGGTLFEYIQQRKGSllSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKkRTVVKIGDFGISKILSSKS 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1039741915 156 DYYTdYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLS 197
Cdd:cd08220   157 KAYT-VVGTPCYISPELCEG-KPYNQKSDIWALGCVLYELAS 196
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
3-287 3.15e-31

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 118.49  E-value: 3.15e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDD---------PVIKKIALreIRMLKQLKHPNLVNLLEVFRRK 73
Cdd:cd14005     1 QYEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTewamingpvPVPLEIAL--LLKASKPGVPGVIRLLDWYERP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  74 RRLHLVFEY-----------CDHTVLheldryqrgvPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA-IK 141
Cdd:cd14005    79 DGFLLIMERpepcqdlfdfiTERGAL----------SENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRTGeVK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 142 LCDFGFARLLTgpGDYYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGvplwpgksdvdqlylirktlgdl 221
Cdd:cd14005   149 LIDFGCGALLK--DSVYTDFDGTRVYSPPEWIRHGRYHGRPATVWSLGILLYDMLCG----------------------- 203
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 222 iprhqqvfsmnqyfsgvKIPDPEDMETLELKF---PNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14005   204 -----------------DIPFENDEQILRGNVlfrPRLSKECCDLISRCLQFDPSKRPSLEQILSHPWF 255
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
3-198 3.59e-31

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 118.52  E-value: 3.59e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRdTGQIVAIK--RFLETEDDPVIKKIAlREIRMLKQLKHPNLVNLLEVFRRKRRLHLVF 80
Cdd:cd14161     4 RYEFLETLGKGTYGRVKKARDS-SGRLVAIKsiRKDRIKDEQDLLHIR-REIEIMSSLNHPHIISVYEVFENSSKIVIVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  81 EYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGpGDYYTD 160
Cdd:cd14161    82 EYASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLYNQ-DKFLQT 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1039741915 161 YVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSG 198
Cdd:cd14161   161 YCGSPLYASPEIVNGRPYIGPEVDSWSLGVLLYILVHG 198
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
8-284 4.22e-31

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 118.21  E-value: 4.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   8 GKIGEGSYGVVfKCRNRD-TGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHT 86
Cdd:cd14075     8 GELGSGNFSQV-KLGIHQlTKEKVAIKILDKTKLDQKTQRLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVMEYASGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  87 vlhELDRY--QRG-VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgPGDYYTDYVA 163
Cdd:cd14075    87 ---ELYTKisTEGkLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAK-RGETLNTFCG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 164 TRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVplWPGKSDvdqlylirkTLGDLiprhQQVFSMNQYFsgvkIPdp 243
Cdd:cd14075   163 SPPYAAPELFKDEHYIGIYVDIWALGVLLYFMVTGV--MPFRAE---------TVAKL----KKCILEGTYT----IP-- 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1039741915 244 edmetlelkfPNISYSALGFLKGCLHMDPAERLTCEQLLQH 284
Cdd:cd14075   222 ----------SYVSEPCQELIRGILQPVPSDRYSIDEIKNS 252
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
5-286 4.31e-31

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 120.31  E-value: 4.31e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   5 EKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIAlREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:PLN00034   77 ERVNRIGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTVRRQIC-REIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMD 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVLHEldryQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYVAT 164
Cdd:PLN00034  156 GGSLEG----THIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQTMDPCNSSVGT 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 165 RWYRSPELLVGDTQYGP----PVDVWAIGCVFAELLSG-VPLWPGKSdvdqlylirktlGDLIPRHQQVfSMNQyfsgvk 239
Cdd:PLN00034  232 IAYMSPERINTDLNHGAydgyAGDIWSLGVSILEFYLGrFPFGVGRQ------------GDWASLMCAI-CMSQ------ 292
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1039741915 240 ipDPEDMETLELKFPNisysalgFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:PLN00034  293 --PPEAPATASREFRH-------FISCCLQREPAKRWSAMQLLQHPF 330
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
1-287 4.61e-31

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 118.07  E-value: 4.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrFLETEDdPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVF 80
Cdd:cd14114     1 YDHYDILEELGTGAFGVVHRCTERATGNNFAAK-FIMTPH-ESDKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLIL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  81 EYCDHTVLHE-LDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA--IKLCDFGFARLLTgPGDY 157
Cdd:cd14114    79 EFLSGGELFErIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRSneVKLIDFGLATHLD-PKES 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 158 YTDYVATRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTlgdliprhqqvfsmnqyfsg 237
Cdd:cd14114   158 VKVTTGTAEFAAPEIVEREP-VGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSC-------------------- 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039741915 238 vkipdpeDMETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14114   217 -------DWNFDDSAFSGISEEAKDFIRKLLLADPNKRMTIHQALEHPWL 259
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
4-225 9.58e-31

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 119.09  E-value: 9.58e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFletEDDPVIKKIALREIRMLKQLKHP-----NLVNLLEVFRRKRRLHL 78
Cdd:cd14211     1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKIL---KNHPSYARQGQIEVSILSRLSQEnadefNFVRAYECFQHKNHTCL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTvLHELDRYQRGVPEPL--VKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA----IKLCDFGFARLLT 152
Cdd:cd14211    78 VFEMLEQN-LYDFLKQNKFSPLPLkyIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVRqpyrVKVIDFGSASHVS 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 153 GPgdYYTDYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGdLIPRH 225
Cdd:cd14211   157 KA--VCSTYLQSRYYRAPEIILG-LPFCEAIDMWSLGCVIAELFLGWPLYPGSSEYDQIRYISQTQG-LPAEH 225
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
2-290 9.91e-31

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 119.31  E-value: 9.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEddpVIKK------IALREIrmLKQLKHPNLVNLLEVFRRKRR 75
Cdd:cd05573     1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSD---MLKReqiahvRAERDI--LADADSPWIVRLHYAFQDEDH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  76 LHLVFEYC---DhtVLHELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLL- 151
Cdd:cd05573    76 LYLVMEYMpggD--LMNLLIKYDV-FPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMn 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 152 -TGPGDYYTDY---------------------------VATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPlwP 203
Cdd:cd05573   153 kSGDRESYLNDsvntlfqdnvlarrrphkqrrvraysaVGTPDYIAPEVLRG-TGYGPECDWWSLGVILYEMLYGFP--P 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 204 GKSDvdqlylirktlgdliprhqqvfSMNQYFSgvKIPDPEDmetlELKFP---NISYSALGFLKGCLhMDPAERLTC-E 279
Cdd:cd05573   230 FYSD----------------------SLVETYS--KIMNWKE----SLVFPddpDVSPEAIDLIRRLL-CDPEDRLGSaE 280
                         330
                  ....*....|.
gi 1039741915 280 QLLQHPYFDSI 290
Cdd:cd05573   281 EIKAHPFFKGI 291
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
10-286 1.04e-30

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 117.54  E-value: 1.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFkCRNRDTGQIVAIKRFLETEDDPVI-----KKIAlREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:cd06631     9 LGKGAYGTVY-CGLTSTGQLIAVKQVELDTSDKEKaekeyEKLQ-EEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEFVP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLT------GPGDYY 158
Cdd:cd06631    87 GGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRLCinlssgSQSQLL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 TDYVATRWYRSPElLVGDTQYGPPVDVWAIGCVFAELLSGVPLWpgkSDVDQLYLIrktlgdliprhqqvFSMNqyfSGV 238
Cdd:cd06631   167 KSMRGTPYWMAPE-VINETGHGRKSDIWSIGCTVFEMATGKPPW---ADMNPMAAI--------------FAIG---SGR 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1039741915 239 KIpdpedMETLELKFpniSYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd06631   226 KP-----VPRLPDKF---SPEARDFVHACLTRDQDERPSAEQLLKHPF 265
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
10-290 1.08e-30

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 118.07  E-value: 1.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFletEDDPVIK----KIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDH 85
Cdd:cd05580     9 LGTGSFGRVRLVKHKDSGKYYALKIL---KKAKIIKlkqvEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVMEYVPG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 TVL-HELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLtgPGDYYT----- 159
Cdd:cd05580    86 GELfSLLRRSGR-FPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRV--KDRTYTlcgtp 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 160 DYVAtrwyrsPELLVGdTQYGPPVDVWAIGCVFAELLSGVPlwPGKsDVDQLYLIRKTLGDliprhqqvfsmnqyfsgvk 239
Cdd:cd05580   163 EYLA------PEIILS-KGHGKAVDWWALGILIYEMLAGYP--PFF-DENPMKIYEKILEG------------------- 213
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039741915 240 ipdpedmetlELKFP-NISYSALGFLKGCLHMDPAERLTC-----EQLLQHPYFDSI 290
Cdd:cd05580   214 ----------KIRFPsFFDPDAKDLIKRLLVVDLTKRLGNlkngvEDIKNHPWFAGI 260
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
4-286 1.16e-30

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 117.68  E-value: 1.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIKKIALR--------EIRMLKQLKHPNLVNLLEVFRRKRR 75
Cdd:cd14169     5 YELKEKLGEGAFSEVVLAQERGSQRLVALK---------CIPKKALRgkeamvenEIAVLRRINHENIVSLEDIYESPTH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  76 LHLVFEYCDHTVLheLDR-YQRG-VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILIT---KQSAIKLCDFGFARL 150
Cdd:cd14169    76 LYLAMELVTGGEL--FDRiIERGsYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFGLSKI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 151 ltGPGDYYTDYVATRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLSGVPLWPGKSDvDQLYlirktlgDLIPRHQQVFS 230
Cdd:cd14169   154 --EAQGMLSTACGTPGYVAPELLEQKP-YGKAVDVWAIGVISYILLCGYPPFYDEND-SELF-------NQILKAEYEFD 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 231 mNQYFSgvkipdpedmetlelkfpNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14169   223 -SPYWD------------------DISESAKDFIRHLLERDPEKRFTCEQALQHPW 259
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
4-285 1.16e-30

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 117.11  E-value: 1.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRF-------LETEDdpvikkiALREIRMLKQLKHPNLVNLLEVFRRKRRL 76
Cdd:cd08530     2 FKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVnlgslsqKERED-------SVNEIRLLASVNHPNIIRYKEAFLDGNRL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  77 HLVFEYCDHTVL-HELDRYQ---RGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLT 152
Cdd:cd08530    75 CIVMEYAPFGDLsKLISKRKkkrRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 153 GpGDYYTDyVATRWYRSPELLvGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDqlyLIRKTLGDLIPRHQQVFSmn 232
Cdd:cd08530   155 K-NLAKTQ-IGTPLYAAPEVW-KGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQE---LRYKVCRGKFPPIPPVYS-- 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 233 qyfsgvkipdpEDMETlelkfpnisysalgFLKGCLHMDPAERLTCEQLLQHP 285
Cdd:cd08530   227 -----------QDLQQ--------------IIRSLLQVNPKKRPSCDKLLQSP 254
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
4-286 1.53e-30

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 116.78  E-value: 1.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIK-------RFLETEDDPVIKKIALREIRMLKQ------LKHPNLVNLLEVF 70
Cdd:cd14077     3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKiiprasnAGLKKEREKRLEKEISRDIRTIREaalsslLNHPHICRLRDFL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  71 RRKRRLHLVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARL 150
Cdd:cd14077    83 RTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGLSNL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 151 LTgPGDYYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGvplwpgksdvdqlylirktlgdliprhqqvfs 230
Cdd:cd14077   163 YD-PRRLLRTFCGSLYFAAPELLQAQPYTGPEVDVWSFGVVLYVLVCG-------------------------------- 209
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039741915 231 mnqyfsgvKIP-DPEDMETLE-------LKFPN-ISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14077   210 --------KVPfDDENMPALHakikkgkVEYPSyLSSECKSLISRMLVVDPKKRATLEQVLNHPW 266
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
10-290 1.75e-30

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 116.81  E-value: 1.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIKK---IALREIR--------MLKQLKHPNLVNLLEVFRRKRRLHL 78
Cdd:cd05611     4 ISKGAFGSVYLAKKRSTGDYFAIK---------VLKKsdmIAKNQVTnvkaeraiMMIQGESPYVAKLYYSFQSKDYLYL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgPGDYY 158
Cdd:cd05611    75 VMEYLNGGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGL-EKRHN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 TDYVATRWYRSPELL--VGDTQYGppvDVWAIGCVFAELLSGVPLWPGKSdVDQLYlirktlgDLIPRHqqvfsmnqyfs 236
Cdd:cd05611   154 KKFVGTPDYLAPETIlgVGDDKMS---DWWSLGCVIFEFLFGYPPFHAET-PDAVF-------DNILSR----------- 211
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039741915 237 gvKIPDPEDmetlelKFPNISYSALGFLKGCLHMDPAERLTC---EQLLQHPYFDSI 290
Cdd:cd05611   212 --RINWPEE------VKEFCSPEAVDLINRLLCMDPAKRLGAngyQEIKSHPFFKSI 260
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
10-286 1.95e-30

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 116.17  E-value: 1.95e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRF-LETEDDpviKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYC----- 83
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIkCRKAKD---REDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVaggel 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 ------DHTVLHELD--RYQRgvpeplvknitwQTLQAVNFCHKHNCIHRDVKPENILITKQSA--IKLCDFGFARLLtG 153
Cdd:cd14103    78 fervvdDDFELTERDciLFMR------------QICEGVQYMHKQGILHLDLKPENILCVSRTGnqIKIIDFGLARKY-D 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 154 PGDYYTDYVATRWYRSPELLVGDtQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTlgdliprhqqvfsmnQ 233
Cdd:cd14103   145 PDKKLKVLFGTPEFVAPEVVNYE-PISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRA---------------K 208
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 234 YfsgvkipDPEDMEtlelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14103   209 W-------DFDDEA-----FDDISDEAKDFISKLLVKDPRKRMSAAQCLQHPW 249
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
3-286 2.43e-30

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 115.96  E-value: 2.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIK-----RFLETEDDPVIKkialREIRMLKQLKHPNLVNLLEVFRRKRRLH 77
Cdd:cd14663     1 RYELGRTLGEGTFAKVKFARNTKTGESVAIKiidkeQVAREGMVEQIK----REIAIMKLLRHPNIVELHEVMATKTKIF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  78 LVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARL---LTGP 154
Cdd:cd14663    77 FVMELVTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSALseqFRQD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 155 GDYYTdYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGvplwpgksdvdqlYLirktlgdliPRHQQVFsMNQY 234
Cdd:cd14663   157 GLLHT-TCGTPNYVAPEVLARRGYDGAKADIWSCGVILFVLLAG-------------YL---------PFDDENL-MALY 212
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 235 fsgVKIpdpedmETLELKFPN-ISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14663   213 ---RKI------MKGEFEYPRwFSPGAKSLIKRILDPNPSTRITVEQIMASPW 256
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
2-286 2.65e-30

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 116.28  E-value: 2.65e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIK----RFLETEDDPVIKKIALreirmLKQLKHPNLVNLLEVFRRKRRLH 77
Cdd:cd14167     3 DIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKciakKALEGKETSIENEIAV-----LHKIKHPNIVALDDIYESGGHLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  78 LVFEYCDHTVLheLDR-YQRGV-PEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENIL---ITKQSAIKLCDFGFARlLT 152
Cdd:cd14167    78 LIMQLVSGGEL--FDRiVEKGFyTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSK-IE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 153 GPGDYYTDYVATRWYRSPELLvGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVdQLYlirktlgdliprhQQVFSMN 232
Cdd:cd14167   155 GSGSVMSTACGTPGYVAPEVL-AQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDA-KLF-------------EQILKAE 219
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039741915 233 QYFSGvkiPDPEDmetlelkfpnISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14167   220 YEFDS---PYWDD----------ISDSAKDFIQHLMEKDPEKRFTCEQALQHPW 260
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
4-286 2.95e-30

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 117.46  E-value: 2.95e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIK-KIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd06635    27 FSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKwQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEY 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgPGDyytDYV 162
Cdd:cd06635   107 CLGSASDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIAS-PAN---SFV 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 163 ATRWYRSPELLVG--DTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDLIprhqQVFSMNQYFSgvki 240
Cdd:cd06635   183 GTPYWMAPEVILAmdEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPTL----QSNEWSDYFR---- 254
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1039741915 241 pdpedmetlelkfpnisysalGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd06635   255 ---------------------NFVDSCLQKIPQDRPTSEELLKHMF 279
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
10-287 5.40e-30

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 115.05  E-value: 5.40e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIK-----RFLETEddpVIKKIaLREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:cd05578     8 IGKGSFGKVCIVQKKDTKKMFAMKymnkqKCIEKD---SVRNV-LNELEILQELEHPFLVNLWYSFQDEEDMYMVVDLLL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVLheldRY--QRGVP--EPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgPGDYYTD 160
Cdd:cd05578    84 GGDL----RYhlQQKVKfsEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLT-DGTLATS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 YVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLWPGKSdvdqlylirKTLGDLIpRHQQVFSMNQYFSGvki 240
Cdd:cd05578   159 TSGTKPYMAPEVFMR-AGYSFAVDWWSLGVTAYEMLRGKRPYEIHS---------RTSIEEI-RAKFETASVLYPAG--- 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1039741915 241 pDPEDMETlelkfpnisysalgFLKGCLHMDPAERLTC-EQLLQHPYF 287
Cdd:cd05578   225 -WSEEAID--------------LINKLLERDPQKRLGDlSDLKNHPYF 257
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
10-198 6.12e-30

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 114.96  E-value: 6.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDP-VIKKIALREIRMLKQLKHPNLVNLLEVFR-RKRRLHLVFEYCDHTV 87
Cdd:cd14164     8 IGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPdFVQKFLPRELSILRRVNHPNIVQMFECIEvANGRLYIVMEAAATDL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  88 LHELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILIT-KQSAIKLCDFGFARLLTGPGDYYTDYVATRW 166
Cdd:cd14164    88 LQKIQEVHH-IPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSaDDRKIKIADFGFARFVEDYPELSTTFCGSRA 166
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1039741915 167 YRSPELLVGdTQYGP-PVDVWAIGCVFAELLSG 198
Cdd:cd14164   167 YTPPEVILG-TPYDPkKYDVWSLGVVLYVMVTG 198
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
3-195 9.80e-30

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 114.67  E-value: 9.80e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd08225     1 RYEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHN--CIHRDVKPENILITKQSAI-KLCDFGFARLLTGPGDYYT 159
Cdd:cd08225    81 CDGGDLMKRINRQRGVLFSEDQILSWFVQISLGLKHIHDrkILHRDIKSQNIFLSKNGMVaKLGDFGIARQLNDSMELAY 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1039741915 160 DYVATRWYRSPElLVGDTQYGPPVDVWAIGCVFAEL 195
Cdd:cd08225   161 TCVGTPYYLSPE-ICQNRPYNNKTDIWSLGCVLYEL 195
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
3-286 9.88e-30

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 114.44  E-value: 9.88e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNrdtgqivaiKRFLETEDDPVIKKI------------ALREIRMLKQLKHPNLVNLLEVF 70
Cdd:cd08222     1 RYRVVRKLGSGNFGTVYLVSD---------LKATADEELKVLKEIsvgelqpdetvdANREAKLLSKLDHPAIVKFHDSF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  71 RRKRRLHLVFEYCD----HTVLHELDRYQRGVPEPLVknITW--QTLQAVNFCHKHNCIHRDVKPENILItKQSAIKLCD 144
Cdd:cd08222    72 VEKESFCIVTEYCEggdlDDKISEYKKSGTTIDENQI--LDWfiQLLLAVQYMHERRILHRDLKAKNIFL-KNNVIKVGD 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 145 FGFARLLTGPGDYYTDYVATRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKtlGDlIPr 224
Cdd:cd08222   149 FGISRILMGTSDLATTFTGTPYYMSPEVLKHEG-YNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVE--GE-TP- 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 225 hqqvfsmnqyfsgvKIPDPEDMEtLELkfpnisysalgFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd08222   224 --------------SLPDKYSKE-LNA-----------IYSRMLNKDPALRPSAAEILKIPF 259
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
2-286 1.38e-29

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 114.19  E-value: 1.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFleteDDPVIKKIAL-----REIRMLKQLKHPNLVNLLEVFRRKRRL 76
Cdd:cd14186     1 EDFKVLNLLGKGSFACVYRARSLHTGLEVAIKMI----DKKAMQKAGMvqrvrNEVEIHCQLKHPSILELYNYFEDSNYV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  77 HLVFEYCDHTvlhELDRYQRGVPEPLVKN----ITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLT 152
Cdd:cd14186    77 YLVLEMCHNG---EMSRYLKNRKKPFTEDearhFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 153 GPGDYYTDYVATRWYRSPELlVGDTQYGPPVDVWAIGCVFAELLSGVPlwPGKSDVDQLYLIRKTLGDLI-PRHqqvfsm 231
Cdd:cd14186   154 MPHEKHFTMCGTPNYISPEI-ATRSAHGLESDVWSLGCMFYTLLVGRP--PFDTDTVKNTLNKVVLADYEmPAF------ 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039741915 232 nqyfsgvkipdpedmetlelkfpnISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14186   225 ------------------------LSREAQDLIHQLLRKNPADRLSLSSVLDHPF 255
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
10-287 1.50e-29

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 114.33  E-value: 1.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKC--RNRDTGQIVAIKRF---LETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRR-KRRLHLVFEYC 83
Cdd:cd13994     1 IGKGATSVVRIVtkKNPRSGVLYAVKEYrrrDDESKRKDYVKRLTSEYIISSKLHHPNIVKVLDLCQDlHGKWCLVMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 DHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDY-- 161
Cdd:cd13994    81 PGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVFGMPAEKESPMsa 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 162 --VATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDliprhqqvFSMNQYfSGVK 239
Cdd:cd13994   161 glCGSEPYMAPEVFTSGSYDGRAVDVWSCGIVLFALFTGRFPWRSAKKSDSAYKAYEKSGD--------FTNGPY-EPIE 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1039741915 240 IPDPEDMETLELKFpnisysalgflkgcLHMDPAERLTCEQLLQHPYF 287
Cdd:cd13994   232 NLLPSECRRLIYRM--------------LHPDPEKRITIDEALNDPWV 265
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
10-288 1.52e-29

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 114.70  E-value: 1.52e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIKKIAL-------REIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd14166    11 LGSGAFSEVYLVKQRSTGKLYALK---------CIKKSPLsrdssleNEIAVLKRIKHENIVTLEDIYESTTHYYLVMQL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLheLDR-YQRGV-PEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILI---TKQSAIKLCDFGFARLltGPGDY 157
Cdd:cd14166    82 VSGGEL--FDRiLERGVyTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLSKM--EQNGI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 158 YTDYVATRWYRSPELLvGDTQYGPPVDVWAIGCVFAELLSGVPlwpgksdvdqlylirktlgdliPRHQQVFSmnQYFSG 237
Cdd:cd14166   158 MSTACGTPGYVAPEVL-AQKPYSKAVDCWSIGVITYILLCGYP----------------------PFYEETES--RLFEK 212
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 238 VKipdpEDMETLELKF-PNISYSALGFLKGCLHMDPAERLTCEQLLQHPYFD 288
Cdd:cd14166   213 IK----EGYYEFESPFwDDISESAKDFIRHLLEKNPSKRYTCEKALSHPWII 260
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
2-286 1.97e-29

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 114.73  E-value: 1.97e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVikkialREIRMLKQL-KHPNLVNLLEVFRRKRRLHLVF 80
Cdd:cd14177     4 DVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPS------EEIEILMRYgQHPNIITLKDVYDDGRYVYLVT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  81 EYCDHTVLheLDRY--QRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA----IKLCDFGFARLLTGP 154
Cdd:cd14177    78 ELMKGGEL--LDRIlrQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSAnadsIRICDFGFAKQLRGE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 155 GDYYTDYVATRWYRSPELLVgDTQYGPPVDVWAIGCVFAELLSG-VPLWPGKSDVDQLYLIRKTLGDliprhqqvFSMnq 233
Cdd:cd14177   156 NGLLLTPCYTANFVAPEVLM-RQGYDAACDIWSLGVLLYTMLAGyTPFANGPNDTPEEILLRIGSGK--------FSL-- 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 234 yfSGVkipdpedmetlelKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14177   225 --SGG-------------NWDTVSDAAKDLLSHMLHVDPHQRYTAEQVLKHSW 262
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
4-219 2.21e-29

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 115.51  E-value: 2.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFletEDDPVIKKIALREIRMLKQLKHPN-----LVNLLEVFRRKRRLHL 78
Cdd:cd14229     2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKIL---KNHPSYARQGQIEVGILARLSNENadefnFVRAYECFQHRNHTCL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTvLHELDRYQRGVPEPL--VKNITWQTLQAVNFCHKHNCIHRDVKPENILIT----KQSAIKLCDFGFARLLT 152
Cdd:cd14229    79 VFEMLEQN-LYDFLKQNKFSPLPLkvIRPILQQVATALKKLKSLGLIHADLKPENIMLVdpvrQPYRVKVIDFGSASHVS 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039741915 153 GPgdYYTDYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLG 219
Cdd:cd14229   158 KT--VCSTYLQSRYYRAPEIILG-LPFCEAIDMWSLGCVIAELFLGWPLYPGALEYDQIRYISQTQG 221
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
4-286 3.72e-29

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 113.56  E-value: 3.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPviKKIALrEIRMLKQLKH-PNLVNLLEVFRRKR------RL 76
Cdd:cd06636    18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEE--EEIKL-EINMLKKYSHhRNIATYYGAFIKKSppghddQL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  77 HLVFEYCDHTVLHELDRYQRG--VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGP 154
Cdd:cd06636    95 WLVMEFCGAGSVTDLVKNTKGnaLKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 155 GDYYTDYVATRWYRSPELLV----GDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYlirktlgdLIPRHqqvfs 230
Cdd:cd06636   175 VGRRNTFIGTPYWMAPEVIAcdenPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALF--------LIPRN----- 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 231 mnqyfsgvkiPDPedmetlELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd06636   242 ----------PPP------KLKSKKWSKKFIDFIEGCLVKNYLSRPSTEQLLKHPF 281
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
2-286 4.24e-29

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 113.57  E-value: 4.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFletedDPV--IKKIALREIRMLKQLK-HPNLVNLLEVFRRKR---- 74
Cdd:cd06638    18 DTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKIL-----DPIhdIDEEIEAEYNILKALSdHPNVVKFYGMYYKKDvkng 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  75 -RLHLVFEYCDHTVLHELDR--YQRG--VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFAR 149
Cdd:cd06638    93 dQLWLVLELCNGGSVTDLVKgfLKRGerMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSA 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 150 LLTGPGDYYTDYVATRWYRSPELLVG----DTQYGPPVDVWAIGCVFAELLSGVPlwpgksdvdqlylirkTLGDLIPrh 225
Cdd:cd06638   173 QLTSTRLRRNTSVGTPFWMAPEVIACeqqlDSTYDARCDVWSLGITAIELGDGDP----------------PLADLHP-- 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 226 qqvfsMNQYFSGVKIPDPedmetlELKFPNISYSALG-FLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd06638   235 -----MRALFKIPRNPPP------TLHQPELWSNEFNdFIRKCLTKDYEKRPTVSDLLQHVF 285
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
4-286 4.45e-29

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 113.16  E-value: 4.45e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKigeGSYGVVFKCRNRDTGQIVAIKRfLETEDDPVIkkiaLREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYC 83
Cdd:cd14010     5 YDEIGR---GKHSVVYKGRRKGTIEFVAIKC-VDKSKRPEV----LNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 DHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLT----------- 152
Cdd:cd14010    77 TGGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARREGeilkelfgqfs 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 153 -----GPGDYYTDYVATRWYRSPELLVGDtQYGPPVDVWAIGCVFAELLSGVPlwPGKSDvDQLYLIRKTLGDLIPRhqq 227
Cdd:cd14010   157 degnvNKVSKKQAKRGTPYYMAPELFQGG-VHSFASDLWALGCVLYEMFTGKP--PFVAE-SFTELVEKILNEDPPP--- 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 228 vfsMNQYFSGVKIPDPEDMetlelkfpnisysalgfLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14010   230 ---PPPKVSSKPSPDFKSL-----------------LKGLLEKDPAKRLSWDELVKHPF 268
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
4-286 5.14e-29

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 112.97  E-value: 5.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIK----RFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLV 79
Cdd:cd14105     7 YDIGEELGSGQFAVVKKCREKSTGLEYAAKfikkRRSKASRRGVSREDIEREVSILRQVLHPNIITLHDVFENKTDVVLI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  80 FEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA----IKLCDFGFARLLTgPG 155
Cdd:cd14105    87 LELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVpiprIKLIDFGLAHKIE-DG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 156 DYYTDYVATRWYRSPElLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLylirktlgdliprhQQVFSMNQYF 235
Cdd:cd14105   166 NEFKNIFGTPEFVAPE-IVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETL--------------ANITAVNYDF 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 236 SgvkipdpedmetlELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14105   231 D-------------DEYFSNTSELAKDFIRQLLVKDPRKRMTIQESLRHPW 268
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
2-287 6.45e-29

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 113.95  E-value: 6.45e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQI-VAIKrfleteddpVIKKI------ALREIRMLKQLKHPNLVN------LLE 68
Cdd:cd14214    13 ERYEIVGDLGEGTFGKVVECLDHARGKSqVALK---------IIRNVgkyreaARLEINVLKKIKEKDKENkflcvlMSD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  69 VFRRKRRLHLVFEYCDHTVLhELDRYQRGVPEPL--VKNITWQTLQAVNFCHKHNCIHRDVKPENILIT----------- 135
Cdd:cd14214    84 WFNFHGHMCIAFELLGKNTF-EFLKENNFQPYPLphIRHMAYQLCHALKFLHENQLTHTDLKPENILFVnsefdtlynes 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 136 --------KQSAIKLCDFGFArllTGPGDYYTDYVATRWYRSPELLVgDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSD 207
Cdd:cd14214   163 ksceeksvKNTSIRVADFGSA---TFDHEHHTTIVATRHYRPPEVIL-ELGWAQPCDVWSLGCILFEYYRGFTLFQTHEN 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 208 VDQLYLIRKTLGDlIPRHQQVFSMNQ--YFSGVKIPDPEDMETLELK---FPNISYSA---------LGFLKGCLHMDPA 273
Cdd:cd14214   239 REHLVMMEKILGP-IPSHMIHRTRKQkyFYKGSLVWDENSSDGRYVSencKPLMSYMLgdslehtqlFDLLRRMLEFDPA 317
                         330
                  ....*....|....
gi 1039741915 274 ERLTCEQLLQHPYF 287
Cdd:cd14214   318 LRITLKEALLHPFF 331
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1-286 1.09e-28

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 112.61  E-value: 1.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEKIGK-IGEGSYGVVFKCRNRDTGQIVAIKRFLETEDdpviKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLV 79
Cdd:cd14085     1 LEDFFEIESeLGRGATSVVYRCRQKGTQKPYAVKKLKKTVD----KKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  80 FEYCDHTVLheLDR-YQRGV-PEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILIT---KQSAIKLCDFGFARLLtgP 154
Cdd:cd14085    77 LELVTGGEL--FDRiVEKGYySERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYAtpaPDAPLKIADFGLSKIV--D 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 155 GDYYTDYV-ATRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLSGV-PLWPGKSDVdqlYLIRKTLGdliprhqqvfsmn 232
Cdd:cd14085   153 QQVTMKTVcGTPGYCAPEILRGCA-YGPEVDMWSVGVITYILLCGFePFYDERGDQ---YMFKRILN------------- 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039741915 233 qyfsgvkipdpEDMETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14085   216 -----------CDYDFVSPWWDDVSLNAKDLVKKLIVLDPKKRLTTQQALQHPW 258
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
2-286 1.13e-28

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 112.03  E-value: 1.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIK----RFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLH 77
Cdd:cd14194     5 DYYDTGEELGSGQFAVVKKCREKSTGLQYAAKfikkRRTKSSRRGVSREDIEREVSILKEIQHPNVITLHEVYENKTDVI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  78 LVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA----IKLCDFGFARLLTG 153
Cdd:cd14194    85 LILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVpkprIKIIDFGLAHKIDF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 154 pGDYYTDYVATRWYRSPElLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDvdqlyliRKTLGDLiprhqqvfsmnq 233
Cdd:cd14194   165 -GNEFKNIFGTPEFVAPE-IVNYEPLGLEADMWSIGVITYILLSGASPFLGDTK-------QETLANV------------ 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 234 yfSGVkipdpeDMETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14194   224 --SAV------NYEFEDEYFSNTSALAKDFIRRLLVKDPKKRMTIQDSLQHPW 268
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
5-291 1.28e-28

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 112.25  E-value: 1.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   5 EKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIaLREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:cd06622     4 EVLDELGKGNYGSVYKVLHRPTGVTMAMKEIRLELDESKFNQI-IMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVLHEL---DRYQRGVPEPLVKNITWQTLQAVNFC-HKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgpGDYYTD 160
Cdd:cd06622    83 AGSLDKLyagGVATEGIPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLV--ASLAKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 YVATRWYRSPELLVGDTQYGPPV-----DVWAIGCVFAELLSGVPLWPGKSdvdqlylirktlgdliprHQQVFSMnqyF 235
Cdd:cd06622   161 NIGCQSYMAPERIKSGGPNQNPTytvqsDVWSLGLSILEMALGRYPYPPET------------------YANIFAQ---L 219
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 236 SGVKIPDPEDMEtlelkfPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYFDSIR 291
Cdd:cd06622   220 SAIVDGDPPTLP------SGYSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWLVKYK 269
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
4-286 1.70e-28

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 111.66  E-value: 1.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRF-LETEDDPVIKKialREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd06646    11 YELIQRVGSGTYGDVYKARNLHTGELAAVKIIkLEPGDDFSLIQ---QEIFMVKECKHCNIVAYFGSYLSREKLWICMEY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYV 162
Cdd:cd06646    88 CGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKITATIAKRKSFI 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 163 ATRWYRSPELLVGDTQ--YGPPVDVWAIGCVFAELLSGVPlwpgksdvdqlylirkTLGDLIPRhQQVFSMNQyfSGVKI 240
Cdd:cd06646   168 GTPYWMAPEVAAVEKNggYNQLCDIWAVGITAIELAELQP----------------PMFDLHPM-RALFLMSK--SNFQP 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1039741915 241 PDPEDMETLELKFPNisysalgFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd06646   229 PKLKDKTKWSSTFHN-------FVKISLTKNPKKRPTAERLLTHLF 267
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
2-286 2.68e-28

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 110.85  E-value: 2.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYeKIGK-IGEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIKKIALR--------EIRMLKQLKHPNLVNLLEVFRR 72
Cdd:cd14183     6 ERY-KVGRtIGDGNFAVVKECVERSTGREYALK---------IINKSKCRgkehmiqnEVSILRRVKHPNIVLLIEEMDM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  73 KRRLHLVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQS----AIKLCDFGFA 148
Cdd:cd14183    76 PTELYLVMELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQdgskSLKLGDFGLA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 149 RLLTGPgdYYTdYVATRWYRSPElLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDvDQLYLIRKTLgdliprhqqv 228
Cdd:cd14183   156 TVVDGP--LYT-VCGTPTYVAPE-IIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGD-DQEVLFDQIL---------- 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039741915 229 fsMNQyfsgVKIPDPedmetlelKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14183   221 --MGQ----VDFPSP--------YWDNVSDSAKELITMMLQVDVDQRYSALQVLEHPW 264
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
4-286 2.86e-28

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 112.04  E-value: 2.86e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIK-KIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd06634    17 FSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKwQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgPGDyytDYV 162
Cdd:cd06634    97 CLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASIMA-PAN---SFV 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 163 ATRWYRSPELLVG--DTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDLIPRHQqvfsMNQYFSgvki 240
Cdd:cd06634   173 GTPYWMAPEVILAmdEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPALQSGH----WSEYFR---- 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1039741915 241 pdpedmetlelkfpnisysalGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd06634   245 ---------------------NFVDSCLQKIPQDRPTSDVLLKHRF 269
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
10-290 3.47e-28

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 111.92  E-value: 3.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIK---RFLETEDDPVikKIALREIRML-KQLKHPNLVNLLEVFRRKRRLHLVFEYC-- 83
Cdd:cd05570     3 LGKGSFGKVMLAERKKTDELYAIKvlkKEVIIEDDDV--ECTMTEKRVLaLANRHPFLTGLHACFQTEDRLYFVMEYVng 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 -DhtVLHELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYV 162
Cdd:cd05570    81 gD--LMFHIQRARR-FTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGIWGGNTTSTFC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 163 ATRWYRSPELLVGDtQYGPPVDVWAIGCVFAELLSGVPLWPGKsDVDQLYliRKTLGD--LIPRHqqvfsmnqyfsgvki 240
Cdd:cd05570   158 GTPDYIAPEILREQ-DYGFSVDWWALGVLLYEMLAGQSPFEGD-DEDELF--EAILNDevLYPRW--------------- 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039741915 241 pdpedmetlelkfpnISYSALGFLKGCLHMDPAERLTC-----EQLLQHPYFDSI 290
Cdd:cd05570   219 ---------------LSREAVSILKGLLTKDPARRLGCgpkgeADIKAHPFFRNI 258
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
4-286 3.92e-28

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 110.39  E-value: 3.92e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDpviKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYC 83
Cdd:cd14110     5 YAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYKPED---KQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 D-HTVLHELDRyQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTG----PGDYY 158
Cdd:cd14110    82 SgPELLYNLAE-RNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFNQgkvlMTDKK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 TDYVATrwyRSPELLVGDTQyGPPVDVWAIGCVFAELLSGVplWPGKSDV--DQLYLIRKTLgdliprhqqvfsmnqyfs 236
Cdd:cd14110   161 GDYVET---MAPELLEGQGA-GPQTDIWAIGVTAFIMLSAD--YPVSSDLnwERDRNIRKGK------------------ 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039741915 237 gVKipdpedmetLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14110   217 -VQ---------LSRCYAGLSGGAVNFLKSTLCAKPWGRPTASECLQNPW 256
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
10-288 5.54e-28

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 110.01  E-value: 5.54e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRF-----LETEDDPVIKkialREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTFALKCVkkrhiVQTRQQEHIF----SEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 ----HTVLHELDRYqrgvPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTd 160
Cdd:cd05572    77 ggelWTILRDRGLF----DEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGSGRKTWT- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 YVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPlwPgksdvdqlylirktlgdliprhqqvfsmnqyFSGvki 240
Cdd:cd05572   152 FCGTPEYVAPEIILN-KGYDFSVDYWSLGILLYELLTGRP--P-------------------------------FGG--- 194
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 241 PDPEDMETLE--------LKFPN-ISYSALGFLKGCLHMDPAERLTCEQ-----LLQHPYFD 288
Cdd:cd05572   195 DDEDPMKIYNiilkgidkIEFPKyIDKNAKNLIKQLLRRNPEERLGYLKggirdIKKHKWFE 256
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
10-191 6.22e-28

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 110.12  E-value: 6.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKR--FLETEDDPVIKKialrEIRMLKQL-KHPNLVNLL--EVFRRKRRLH--LVFEY 82
Cdd:cd13985     8 LGEGGFSYVYLAHDVNTGRRYALKRmyFNDEEQLRVAIK----EIEIMKRLcGHPNIVQYYdsAILSSEGRKEvlLLMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHELD-RYQRGVPEPLVKNITWQTLQAVNFCHKHN--CIHRDVKPENILITKQSAIKLCDFGFARlltgpgdyYT 159
Cdd:cd13985    84 CPGSLVDILEkSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGSAT--------TE 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 160 DYVATRW-----------------YRSPEL--LVGDTQYGPPVDVWAIGCV 191
Cdd:cd13985   156 HYPLERAeevniieeeiqknttpmYRAPEMidLYSKKPIGEKADIWALGCL 206
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
2-286 8.70e-28

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 109.14  E-value: 8.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQ-IVAIKRFLETEDdpviKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVF 80
Cdd:cd14111     3 KPYTFLDEKARGRFGVIRRCRENATGKnFPAKIVPYQAEE----KQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  81 EYC-DHTVLHEL-DRYQRGvpEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFAR----LLTGP 154
Cdd:cd14111    79 EFCsGKELLHSLiDRFRYS--EDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQsfnpLSLRQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 155 GDYYTdyvATRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLSGvplwpgksdvdqlyliRKTLGDLIPRHQQVFSMNQY 234
Cdd:cd14111   157 LGRRT---GTLEYMAPEMVKGEP-VGPPADIWSIGVLTYIMLSG----------------RSPFEDQDPQETEAKILVAK 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 235 FSGVKIpdpedmetlelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14111   217 FDAFKL------------YPNVSQSASLFLKKVLSSYPWSRPTTKDCFAHAW 256
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
5-287 1.09e-27

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 109.82  E-value: 1.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   5 EKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALR-EIRMlKQLKHPNLVNLLEVFRRKRRLHLVFEYC 83
Cdd:cd06617     4 EVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRATVNSQEQKRLLMDlDISM-RSVDCPYTVTFYGALFREGDVWICMEVM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 DhTVLHELDR--YQRG--VPEPLVKNITWQTLQAVNFCH-KHNCIHRDVKPENILITKQSAIKLCDFGfarlLTGpgdYY 158
Cdd:cd06617    83 D-TSLDKFYKkvYDKGltIPEDILGKIAVSIVKALEYLHsKLSVIHRDVKPSNVLINRNGQVKLCDFG----ISG---YL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 TDYVA------TRWYRSPELLVGDT---QYGPPVDVWAIGCVFAELLSG-VPLWPGKSDVDQLylirktlgdliprhQQV 228
Cdd:cd06617   155 VDSVAktidagCKPYMAPERINPELnqkGYDVKSDVWSLGITMIELATGrFPYDSWKTPFQQL--------------KQV 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 229 fsmnqyfsgVKIPDPedmetlelKFPNISYSA--LGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd06617   221 ---------VEEPSP--------QLPAEKFSPefQDFVNKCLKKNYKERPNYPELLQHPFF 264
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
2-286 1.17e-27

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 110.52  E-value: 1.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAiKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd06649     5 DDFERISELGAGNGGVVTKVQHKPSGLIMA-RKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICME 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFC-HKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgpGDYYTD 160
Cdd:cd06649    84 HMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLrEKHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLI--DSMANS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 YVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSG-VPLWPGKSDVDQLYLIRKTLG-------DLIPRHQqvfSMN 232
Cdd:cd06649   162 FVGTRSYMSPERLQG-THYSVQSDIWSMGLSLVELAIGrYPIPPPDAKELEAIFGRPVVDgeegephSISPRPR---PPG 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 233 QYFSGVKIPDPEDMETLEL----------KFPNISYSA--LGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd06649   238 RPVSGHGMDSRPAMAIFELldyivnepppKLPNGVFTPdfQEFVNKCLIKNPAERADLKMLMNHTF 303
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
10-290 1.61e-27

Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 109.97  E-value: 1.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLETEddpVIKKI----ALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDH 85
Cdd:cd05585     2 IGKGSFGKVMQVRKKDTSRIYALKTIRKAH---IVSRSevthTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFING 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 TVL-HELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYVAT 164
Cdd:cd05585    79 GELfHHLQREGR-FDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKDDDKTNTFCGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 165 RWYRSPELLVGDTqYGPPVDVWAIGCVFAELLSGVPLWPGKsDVDQLYliRKTLGDLIprhqqvfsmnqyfsgvKIPDPE 244
Cdd:cd05585   158 PEYLAPELLLGHG-YTKAVDWWTLGVLLYEMLTGLPPFYDE-NTNEMY--RKILQEPL----------------RFPDGF 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1039741915 245 DMETLELkfpnisysalgfLKGCLHMDPAERL---TCEQLLQHPYFDSI 290
Cdd:cd05585   218 DRDAKDL------------LIGLLNRDPTKRLgynGAQEIKNHPFFDQI 254
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
10-290 1.67e-27

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 110.10  E-value: 1.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFletEDDPVIKK------IALREIrMLKQLKHPNLVNLLEVFRRKRRLHLVFEYC 83
Cdd:cd05575     3 IGKGSFGKVLLARHKAEGKLYAVKVL---QKKAILKRnevkhiMAERNV-LLKNVKHPFLVGLHYSFQTKDKLYFVLDYV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 DHTVL--HeLDRyQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDY 161
Cdd:cd05575    79 NGGELffH-LQR-ERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEPSDTTSTF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 162 VATRWYRSPELLVGDtQYGPPVDVWAIGCVFAELLSGVPlwPGKS-DVDQLYliRKTLgdliprHQQvfsmnqyfsgvki 240
Cdd:cd05575   157 CGTPEYLAPEVLRKQ-PYDRTVDWWCLGAVLYEMLYGLP--PFYSrDTAEMY--DNIL------HKP------------- 212
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039741915 241 pdpedmetLELKfPNISYSALGFLKGCLHMDPAERLTC----EQLLQHPYFDSI 290
Cdd:cd05575   213 --------LRLR-TNVSPSARDLLEGLLQKDRTKRLGSgndfLEIKNHSFFRPI 257
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
10-224 1.79e-27

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 108.56  E-value: 1.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLH 89
Cdd:cd14202    10 IGHGAFAVVFKGRHKEKHDLEVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDFQEIANSVYLVMEYCNGGDLA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  90 ELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA---------IKLCDFGFARLLTGPGDYYTd 160
Cdd:cd14202    90 DYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGGrksnpnnirIKIADFGFARYLQNNMMAAT- 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 161 YVATRWYRSPELLVGDtQYGPPVDVWAIGCVFAELLSGVPLWPGKS--DVDQLYLIRKTLGDLIPR 224
Cdd:cd14202   169 LCGSPMYMAPEVIMSQ-HYDAKADLWSIGTIIYQCLTGKAPFQASSpqDLRLFYEKNKSLSPNIPR 233
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
10-286 3.14e-27

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 107.88  E-value: 3.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVikKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLH 89
Cdd:cd06624    16 LGKGTFGVVYAARDLSTQVRIAIKEIPERDSREV--QPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGGSLS 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  90 ELDRYQRGvP----EPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILI-TKQSAIKLCDFGFARLLTGPGDYYTDYVAT 164
Cdd:cd06624    94 ALLRSKWG-PlkdnENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVnTYSGVVKISDFGTSKRLAGINPCTETFTGT 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 165 RWYRSPELL-VGDTQYGPPVDVWAIGCVFAELLSGVPlwpgksdvdqlylirkTLGDLIPRHQQVFSMNQYFSGVKIPDp 243
Cdd:cd06624   173 LQYMAPEVIdKGQRGYGPPADIWSLGCTIIEMATGKP----------------PFIELGEPQAAMFKVGMFKIHPEIPE- 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1039741915 244 edmetlelkfpNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd06624   236 -----------SLSEEAKSFILRCFEPDPDKRATASDLLQDPF 267
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
4-219 3.78e-27

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 109.79  E-value: 3.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFletEDDPVIKKIALREIRMLKQLKHP-----NLVNLLEVFRRKRRLHL 78
Cdd:cd14227    17 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKIL---KNHPSYARQGQIEVSILARLSTEsaddyNFVRAYECFQHKNHTCL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTvLHELDRYQRGVPEPL--VKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA----IKLCDFGFARLLT 152
Cdd:cd14227    94 VFEMLEQN-LYDFLKQNKFSPLPLkyIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPSRqpyrVKVIDFGSASHVS 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039741915 153 GPgdYYTDYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLG 219
Cdd:cd14227   173 KA--VCSTYLQSRYYRAPEIILG-LPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQG 236
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
10-290 4.26e-27

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 108.00  E-value: 4.26e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFleteDDPVIKK-----IALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:cd05577     1 LGRGGFGEVCACQVKATGKMYACKKL----DKKRIKKkkgetMALNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVL--HELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGpGDYYTDYV 162
Cdd:cd05577    77 GGDLkyHIYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFKG-GKKIKGRV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 163 ATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSG-VPLWPGKSDVDQLYLIRKTLgdliprhqqvfsmnqyfsgvkip 241
Cdd:cd05577   156 GTHGYMAPEVLQKEVAYDFSVDWFALGCMLYEMIAGrSPFRQRKEKVDKEELKRRTL----------------------- 212
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039741915 242 dpEDMETLELKFpniSYSALGFLKGCLHMDPAERLTC-----EQLLQHPYFDSI 290
Cdd:cd05577   213 --EMAVEYPDSF---SPEARSLCEGLLQKDPERRLGCrggsaDEVKEHPFFRSL 261
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
9-286 5.89e-27

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 107.93  E-value: 5.89e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVAIKRFLEteddpviKKIALREIRMLKQLK-HPNLVNLLEVFRR----------KRRLH 77
Cdd:cd14171    13 KLGTGISGPVRVCVKKSTGERFALKILLD-------RPKARTEVRLHMMCSgHPNIVQIYDVYANsvqfpgesspRARLL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  78 LVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQS---AIKLCDFGFARLltGP 154
Cdd:cd14171    86 IVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSedaPIKLCDFGFAKV--DQ 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 155 GDYYTDYVaTRWYRSPELL----------VGDTQYGPP------VDVWAIGCVFAELLSGVPlwPGKSDVdqlylirktl 218
Cdd:cd14171   164 GDLMTPQF-TPYYVAPQVLeaqrrhrkerSGIPTSPTPytydksCDMWSLGVIIYIMLCGYP--PFYSEH---------- 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039741915 219 gdliPRHQQVFSMNQYFSGVKIPDPEDmetlELKFpnISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14171   231 ----PSRTITKDMKRKIMTGSYEFPEE----EWSQ--ISEMAKDIVRKLLCVDPEERMTIEEVLHHPW 288
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
4-286 6.94e-27

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 107.40  E-value: 6.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIK----RFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLV 79
Cdd:cd14195     7 YEMGEELGSGQFAIVRKCREKGTGKEYAAKfikkRRLSSSRRGVSREEIEREVNILREIQHPNIITLHDIFENKTDVVLI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  80 FEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA----IKLCDFGFARLLTGpG 155
Cdd:cd14195    87 LELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVpnprIKLIDFGIAHKIEA-G 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 156 DYYTDYVATRWYRSPElLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLylirktlgdliprhQQVFSMNQYF 235
Cdd:cd14195   166 NEFKNIFGTPEFVAPE-IVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETL--------------TNISAVNYDF 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 236 SgvkipdpedmetlELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14195   231 D-------------EEYFSNTSELAKDFIRRLLVKDPKKRMTIAQSLEHSW 268
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
9-287 7.78e-27

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 106.52  E-value: 7.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVAIKrFLETEDDPviKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVL 88
Cdd:cd14108     9 EIGRGAFSYLRRVKEKSSDLSFAAK-FIPVRAKK--KTSARRELALLAELDHKSIVRFHDAFEKRRVVIIVTELCHEELL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  89 HELDRyQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA--IKLCDFGFARLLTGPGDYYTDYvATRW 166
Cdd:cd14108    86 ERITK-RPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTdqVRICDFGNAQELTPNEPQYCKY-GTPE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 167 YRSPElLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRktlgdliprhqqvfSMNQYFSgvkipdpedm 246
Cdd:cd14108   164 FVAPE-IVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIR--------------NYNVAFE---------- 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1039741915 247 etlELKFPNISYSALGFLKGCLHMDPAeRLTCEQLLQHPYF 287
Cdd:cd14108   219 ---ESMFKDLCREAKGFIIKVLVSDRL-RPDAEETLEHPWF 255
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
9-287 8.19e-27

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 107.42  E-value: 8.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVAIKRF-LETEDDpviKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTV 87
Cdd:cd06657    27 KIGEGSTGIVCIATVKSSGKLVAVKKMdLRKQQR---RELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  88 LHELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYVATRWY 167
Cdd:cd06657   104 LTDIVTHTR-MNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYW 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 168 RSPElLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLgdliprhqqvfsmnqyfsgvkipdPEDME 247
Cdd:cd06657   183 MAPE-LISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNL------------------------PPKLK 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1039741915 248 TLElkfpNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd06657   238 NLH----KVSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 273
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
9-286 9.10e-27

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 106.60  E-value: 9.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDdpvikkiALREIRM-LKQLKHPNLVNLLEVF----RRKRRLHLVFEYC 83
Cdd:cd14089     8 VLGLGINGKVLECFHKKTGEKFALKVLRDNPK-------ARREVELhWRASGCPHIVRIIDVYentyQGRKCLLVVMECM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 DHTvlhEL-----DRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITK---QSAIKLCDFGFAR------ 149
Cdd:cd14089    81 EGG---ELfsriqERADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSkgpNAILKLTDFGFAKetttkk 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 150 LLTGPgdYYTDYvatrwYRSPELLvGDTQYGPPVDVWAIGCVFAELLSGVPlwPGKSDvdqlylirktlgdliprHQQVF 229
Cdd:cd14089   158 SLQTP--CYTPY-----YVAPEVL-GPEKYDKSCDMWSLGVIMYILLCGYP--PFYSN-----------------HGLAI 210
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039741915 230 S--------MNQYfsgvKIPDPEdmetlelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14089   211 SpgmkkrirNGQY----EFPNPE--------WSNVSEEAKDLIRGLLKTDPSERLTIEEVMNHPW 263
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
4-195 9.82e-27

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 107.07  E-value: 9.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIaLREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYC 83
Cdd:cd14046     8 FEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIKLRSESKNNSRI-LREVMLLSRLNHQHVVRYYQAWIERANLYIQMEYC 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 DHTVLHELdrYQRGVPEPlvKNITW----QTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFAR-------LLT 152
Cdd:cd14046    87 EKSTLRDL--IDSGLFQD--TDRLWrlfrQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATsnklnveLAT 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039741915 153 GPGDYYTDY-----------VATRWYRSPELLVGDT-QYGPPVDVWAIGCVFAEL 195
Cdd:cd14046   163 QDINKSTSAalgssgdltgnVGTALYVAPEVQSGTKsTYNEKVDMYSLGIIFFEM 217
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
18-200 9.87e-27

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 106.65  E-value: 9.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  18 VFKCRNRDTGQIVAIKRFLEtEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLHELDRYQRG 97
Cdd:cd14088    17 IFRAKDKTTGKLYTCKKFLK-RDGRKVRKAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLELATGREVFDWILDQGY 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  98 VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILI---TKQSAIKLCDFGFARLLTGpgdYYTDYVATRWYRSPELlV 174
Cdd:cd14088    96 YSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYynrLKNSKIVISDFHLAKLENG---LIKEPCGTPEYLAPEV-V 171
                         170       180
                  ....*....|....*....|....*.
gi 1039741915 175 GDTQYGPPVDVWAIGCVFAELLSGVP 200
Cdd:cd14088   172 GRQRYGRPVDCWAIGVIMYILLSGNP 197
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
9-287 1.26e-26

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 106.56  E-value: 1.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLK-HPNLVNLLEVFRRKRRLHLVFEYC---- 83
Cdd:cd14197    16 ELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRMEIIHEIAVLELAQaNPWVINLHEVYETASEMILVLEYAagge 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 --DHTVLhelDRyQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA---IKLCDFGFARLLTGpGDYY 158
Cdd:cd14197    96 ifNQCVA---DR-EEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPlgdIKIVDFGLSRILKN-SEEL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 TDYVATRWYRSPELLvgdtQYGP---PVDVWAIGCVFAELLSGVPLWPGkSDVDQLYLirktlgdliprhqQVFSMNQYF 235
Cdd:cd14197   171 REIMGTPEYVAPEIL----SYEPistATDMWSIGVLAYVMLTGISPFLG-DDKQETFL-------------NISQMNVSY 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 236 SGvkipdpEDMEtlelkfpNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14197   233 SE------EEFE-------HLSESAIDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
4-287 1.50e-26

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 105.97  E-value: 1.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYG-VVFKCRNRDTGQIV----AIKRFLETEddpviKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHL 78
Cdd:cd08221     2 YIPVRVLGRGAFGeAVLYRKTEDNSLVVwkevNLSRLSEKE-----RRDALNEIDILSLLNHDNIITYYNHFLDGESLFI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTVLHELDRYQRG--VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGD 156
Cdd:cd08221    77 EMEYCNGGNLHDKIAQQKNqlFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSESS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 157 YYTDYVATRWYRSPELLVGDtQYGPPVDVWAIGCVFAELLSgvplwpgksdvdqlylIRKTLGdliprhqqvfSMNQYFS 236
Cdd:cd08221   157 MAESIVGTPYYMSPELVQGV-KYNFKSDIWAVGCVLYELLT----------------LKRTFD----------ATNPLRL 209
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 237 GVKIPDPEDMETLELKFPNIsysaLGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd08221   210 AVKIVQGEYEDIDEQYSEEI----IQLVHDCLHQDPEDRPTAEELLERPLL 256
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
10-286 1.50e-26

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 106.29  E-value: 1.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLETEddpVIKKIAL------------------------REIRMLKQLKHPNLVN 65
Cdd:cd14118     2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKK---LLKQAGFfrrppprrkpgalgkpldpldrvyREIAILKKLDHPNVVK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  66 LLEVFR--RKRRLHLVFEYCDHTVLHEldryqrgVP--EPLVKNITW----QTLQAVNFCHKHNCIHRDVKPENILITKQ 137
Cdd:cd14118    79 LVEVLDdpNEDNLYMVFELVDKGAVME-------VPtdNPLSEETARsyfrDIVLGIEYLHYQKIIHRDIKPSNLLLGDD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 138 SAIKLCDFGFARLLTGPGDYYTDYVATRWYRSPELLVG--DTQYGPPVDVWAIGCVFAELLSG-VPLwpgkSDVDQLYLI 214
Cdd:cd14118   152 GHVKIADFGVSNEFEGDDALLSSTAGTPAFMAPEALSEsrKKFSGKALDIWAMGVTLYCFVFGrCPF----EDDHILGLH 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 215 RKTlgdlipRHQQvfsmnqyfsgVKIPDPedmetlelkfPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14118   228 EKI------KTDP----------VVFPDD----------PVVSEQLKDLILRMLDKNPSERITLPEIKEHPW 273
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
4-219 1.64e-26

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 107.87  E-value: 1.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFletEDDPVIKKIALREIRMLKQLKHPN-----LVNLLEVFRRKRRLHL 78
Cdd:cd14228    17 YEVLEFLGRGTFGQVAKCWKRSTKEIVAIKIL---KNHPSYARQGQIEVSILSRLSSENadeynFVRSYECFQHKNHTCL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTvLHELDRYQRGVPEPL--VKNITWQTLQAVNFCHKHNCIHRDVKPENILIT----KQSAIKLCDFGFARLLT 152
Cdd:cd14228    94 VFEMLEQN-LYDFLKQNKFSPLPLkyIRPILQQVATALMKLKSLGLIHADLKPENIMLVdpvrQPYRVKVIDFGSASHVS 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039741915 153 GPgdYYTDYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLG 219
Cdd:cd14228   173 KA--VCSTYLQSRYYRAPEIILG-LPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQG 236
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
4-196 1.76e-26

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 106.22  E-value: 1.76e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIaLREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYC 83
Cdd:cd13996     8 FEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSASEKV-LREVKALAKLNHPNIVRYYTAWVEEPPLYIQMELC 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 DHTVLHELDRYQRGVP---EPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQS-AIKLCDFGFARLL-------- 151
Cdd:cd13996    87 EGGTLRDWIDRRNSSSkndRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDlQVKIGDFGLATSIgnqkreln 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 152 -----TGPGD-YYTDYVATRWYRSPELLVGDtQYGPPVDVWAIGCVFAELL 196
Cdd:cd13996   167 nlnnnNNGNTsNNSVGIGTPLYASPEQLDGE-NYNEKADIYSLGIILFEML 216
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
1-286 1.94e-26

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 105.81  E-value: 1.94e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEkIGK-IGEGSYGVVFKCRNRDTGQIVAIKRFLETE-DDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHL 78
Cdd:cd14116     4 LEDFE-IGRpLGKGKFGNVYLAREKQSKFILALKVLFKAQlEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDH-TVLHELDRYQRGVPEPLVKNITwQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFArlLTGPGDY 157
Cdd:cd14116    83 ILEYAPLgTVYRELQKLSKFDEQRTATYIT-ELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWS--VHAPSSR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 158 YTDYVATRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLSGVPLWPGKSdvdqlylirktlgdliprHQQVFsmnqyfsg 237
Cdd:cd14116   160 RTTLCGTLDYLPPEMIEGRM-HDEKVDLWSLGVLCYEFLVGKPPFEANT------------------YQETY-------- 212
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039741915 238 vkipdpEDMETLELKFPN-ISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14116   213 ------KRISRVEFTFPDfVTEGARDLISRLLKHNPSQRPMLREVLEHPW 256
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
2-286 2.01e-26

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 105.54  E-value: 2.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIKKIAL--------REIRMLKQLKHPNLVNLLEVFRRK 73
Cdd:cd14078     3 KYYELHETIGSGGFAKVKLATHILTGEKVAIK---------IMDKKALgddlprvkTEIEALKNLSHQHICRLYHVIETD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  74 RRLHLVFEYC------DHTVlhELDRyqrgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGf 147
Cdd:cd14078    74 NKIFMVLEYCpggelfDYIV--AKDR----LSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFG- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 148 arLLTGPGDYYTDYVAT----RWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSG-VPLwpgksDVDQLY-LIRKTLgdl 221
Cdd:cd14078   147 --LCAKPKGGMDHHLETccgsPAYAAPELIQGKPYIGSEADVWSMGVLLYALLCGfLPF-----DDDNVMaLYRKIQ--- 216
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 222 iprhqqvfsmnqyfSGV-KIPDPEDMETLELkfpnisysalgfLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14078   217 --------------SGKyEEPEWLSPSSKLL------------LDQMLQVDPKKRITVKELLNHPW 256
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
4-315 2.82e-26

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 106.34  E-value: 2.82e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKialREIRMLKQLKH-PNLVNLLEVFRRKR------RL 76
Cdd:cd06637     8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEIK---QEINMLKKYSHhRNIATYYGAFIKKNppgmddQL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  77 HLVFEYCDHTVLHELDRYQRG--VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGP 154
Cdd:cd06637    85 WLVMEFCGAGSVTDLIKNTKGntLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 155 GDYYTDYVATRWYRSPELLV----GDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYlirktlgdLIPRHqqvfs 230
Cdd:cd06637   165 VGRRNTFIGTPYWMAPEVIAcdenPDATYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRALF--------LIPRN----- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 231 mnqyfsgvkiPDPedmetlELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYFdsirevgeltrqHDKPARKTLR- 309
Cdd:cd06637   232 ----------PAP------RLKSKKWSKKFQSFIESCLVKNHSQRPSTEQLMKHPFI------------RDQPNERQVRi 283

                  ....*.
gi 1039741915 310 QSRKHL 315
Cdd:cd06637   284 QLKDHI 289
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
3-285 3.06e-26

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 105.58  E-value: 3.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNR-DTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLK---HPNLVNLLEVFRRKRRLHL 78
Cdd:cd14052     1 RFANVELIGSGEFSQVYKVSERvPTGKVYAVKKLKPNYAGAKDRLRRLEEVSILRELTldgHDNIVQLIDSWEYHGHLYI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDH----TVLHELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFA------ 148
Cdd:cd14052    81 QTELCENgsldVFLSELGLLGR-LDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMAtvwpli 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 149 RLLTGPGDyytdyvatRWYRSPELLvGDTQYGPPVDVWAIGCVFAELLSGVPL------WP-----GKSDVDQLYLIRKT 217
Cdd:cd14052   160 RGIEREGD--------REYIAPEIL-SEHMYDKPADIFSLGLILLEAAANVVLpdngdaWQklrsgDLSDAPRLSSTDLH 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039741915 218 LGDLIPRHQQVFSMNqyfsgvKIPDPEDMETLelkfpnisysalgfLKGCLHMDPAERLTCEQLLQHP 285
Cdd:cd14052   231 SASSPSSNPPPDPPN------MPILSGSLDRV--------------VRWMLSPEPDRRPTADDVLATP 278
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
10-286 3.07e-26

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 105.88  E-value: 3.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVikkialREIRMLKQL-KHPNLVNLLEVFRRKRRLHLVFEYCDHTVL 88
Cdd:cd14175     9 IGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPS------EEIEILLRYgQHPNIITLKDVYDDGKHVYLVTELMRGGEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  89 heLDRY--QRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQS----AIKLCDFGFARLLTGPGDYYTDYV 162
Cdd:cd14175    83 --LDKIlrQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESgnpeSLRICDFGFAKQLRAENGLLMTPC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 163 ATRWYRSPELLvGDTQYGPPVDVWAIGCVFAELLSG-VPLWPGKSDVDQLYLIRKTLGDliprhqqvFSMNqyfSGvkip 241
Cdd:cd14175   161 YTANFVAPEVL-KRQGYDEGCDIWSLGILLYTMLAGyTPFANGPSDTPEEILTRIGSGK--------FTLS---GG---- 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1039741915 242 dpedmetlelKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14175   225 ----------NWNTVSDAAKDLVSKMLHVDPHQRLTAKQVLQHPW 259
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
10-281 3.16e-26

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 106.11  E-value: 3.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIK---RFLETEDDpvikkialREIRMLKQLK-HPNLVNLLEVFRRKRRLHLVFEYCDH 85
Cdd:cd14180    14 LGEGSFSVCRKCRHRQSGQEYAVKiisRRMEANTQ--------REVAALRLCQsHPNIVALHEVLHDQYHTYLVMELLRG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 TVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILI---TKQSAIKLCDFGFARLLTGPGDYYTDYV 162
Cdd:cd14180    86 GELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYadeSDGAVLKVIDFGFARLRPQGSRPLQTPC 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 163 ATRWYRSPELLvGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDV-------DQLYLIRKtlGDliprhqqvFSMnqyf 235
Cdd:cd14180   166 FTLQYAAPELF-SNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGKmfhnhaaDIMHKIKE--GD--------FSL---- 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1039741915 236 sgvkipdpeDMETLElkfpNISYSALGFLKGCLHMDPAERLTCEQL 281
Cdd:cd14180   231 ---------EGEAWK----GVSEEAKDLVRGLLTVDPAKRLKLSEL 263
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
2-287 3.37e-26

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 105.38  E-value: 3.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIK-------RFLETEDDPVIKKIALREIRMLKQLK-HPNLVNLLEVFRRK 73
Cdd:cd14182     3 EKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKiiditggGSFSPEEVQELREATLKEIDILRKVSgHPNIIQLKDTYETN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  74 RRLHLVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTg 153
Cdd:cd14182    83 TFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQLD- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 154 PGDYYTDYVATRWYRSPELL---VGDTQ--YGPPVDVWAIGCVFAELLSGV-PLWPGKsdvdQLYLIRktlgdliprhqQ 227
Cdd:cd14182   162 PGEKLREVCGTPGYLAPEIIecsMDDNHpgYGKEVDMWSTGVIMYTLLAGSpPFWHRK----QMLMLR-----------M 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 228 VFSMNQYFSGVKIPDPED-METLELKFpnisysalgflkgcLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14182   227 IMSGNYQFGSPEWDDRSDtVKDLISRF--------------LVVQPQKRYTAEEALAHPFF 273
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
4-292 5.12e-26

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 107.04  E-value: 5.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFletEDDPVIKKIALREIRM----LKQLKHPNLVNLLEVFRRKRRLHLV 79
Cdd:cd05600    13 FQILTQVGQGGYGSVFLARKKDTGEICALKIM---KKKVLFKLNEVNHVLTerdiLTTTNSPWLVKLLYAFQDPENVYLA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  80 FEY----------CDHTVLHEldRYQRGVpeplvknITwQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFA- 148
Cdd:cd05600    90 MEYvpggdfrtllNNSGILSE--EHARFY-------IA-EMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLAs 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 149 ----------------RLLTGPGDYYTDY--------------------VATRWYRSPELLVGDtQYGPPVDVWAIGCVF 192
Cdd:cd05600   160 gtlspkkiesmkirleEVKNTAFLELTAKerrniyramrkedqnyansvVGSPDYMAPEVLRGE-GYDLTVDYWSLGCIL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 193 AELLSGVPLWPGKSDVD---QLYLIRKTLGDliPRHQQvfsmnqyfsgvkiPDPEdmetlelkfPNISYSALGFLKGCLh 269
Cdd:cd05600   239 FECLVGFPPFSGSTPNEtwaNLYHWKKTLQR--PVYTD-------------PDLE---------FNLSDEAWDLITKLI- 293
                         330       340
                  ....*....|....*....|....*....
gi 1039741915 270 MDPAERL-TCEQLLQHPYF-----DSIRE 292
Cdd:cd05600   294 TDPQDRLqSPEQIKNHPFFknidwDRLRE 322
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
9-286 6.21e-26

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 104.51  E-value: 6.21e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVAIKRF--LETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDH- 85
Cdd:cd14070     9 KLGEGSFAKVREGLHAVTGEKVAIKVIdkKKAKKDSYVTKNLRREGRIQQMIRHPNITQLLDILETENSYYLVMELCPGg 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 TVLHELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGdyYTDYVATR 165
Cdd:cd14070    89 NLMHRIYDKKR-LEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAGILG--YSDPFSTQ 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 166 W----YRSPELLvGDTQYGPPVDVWAIGCVFAELLSGVplwpgksdvdqlylirktlgdlIPRHQQVFSMNQYFSgvKIP 241
Cdd:cd14070   166 CgspaYAAPELL-ARKKYGPKVDVWSIGVNMYAMLTGT----------------------LPFTVEPFSLRALHQ--KMV 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1039741915 242 DPEdMETLElkfPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14070   221 DKE-MNPLP---TDLSPGAISFLRSLLEPDPLKRPNIKQALANRW 261
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
3-286 7.64e-26

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 104.15  E-value: 7.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrFLETEDDPviKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd14087     2 KYDIKALIGRGSFSRVVRVEHRVTRQPYAIK-MIETKCRG--REVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITK---QSAIKLCDFGFARLLT-GPGDYY 158
Cdd:cd14087    79 ATGGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHpgpDSKIMITDFGLASTRKkGPNCLM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 TDYVATRWYRSPELLVgDTQYGPPVDVWAIGCVFAELLSGVplWPGKSDVdqlyliRKTLGDLIPRHQQVFSmnqyfsgv 238
Cdd:cd14087   159 KTTCGTPEYIAPEILL-RKPYTQSVDMWAVGVIAYILLSGT--MPFDDDN------RTRLYRQILRAKYSYS-------- 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1039741915 239 kiPDPedmetlelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14087   222 --GEP---------WPSVSNLAKDFIDRLLTVNPGERLSATQALKHPW 258
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
4-286 7.81e-26

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 104.27  E-value: 7.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrFLETEDDP-----VIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHL 78
Cdd:cd14196     7 YDIGEELGSGQFAIVKKCREKSTGLEYAAK-FIKKRQSRasrrgVSREEIEREVSILRQVLHPNIITLHDVYENRTDVVL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA----IKLCDFGFARLLTgP 154
Cdd:cd14196    86 ILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIE-D 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 155 GDYYTDYVATRWYRSPElLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDqlylirkTLGDLIprhqqvfSMNQY 234
Cdd:cd14196   165 GVEFKNIFGTPEFVAPE-IVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQE-------TLANIT-------AVSYD 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 235 FSgvkipdpedmetlELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14196   230 FD-------------EEFFSHTSELAKDFIRKLLVKETRKRLTIQEALRHPW 268
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
2-286 8.71e-26

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 104.76  E-value: 8.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIaLREIR-MLKQLKHPNLVNLLEVFRRKRRLHLVF 80
Cdd:cd06618    15 NDLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRSGNKEENKRI-LMDLDvVLKSHDCPYIVKCYGYFITDSDVFICM 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  81 EyCDHTVLHEL-DRYQRGVPEPLVKNITWQTLQAVNFC-HKHNCIHRDVKPENILITKQSAIKLCDFGFARLLtgpgdyy 158
Cdd:cd06618    94 E-LMSTCLDKLlKRIQGPIPEDILGKMTVSIVKALHYLkEKHGVIHRDVKPSNILLDESGNVKLCDFGISGRL------- 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 TDYVA-TRW-----YRSPELLVGDT--QYGPPVDVWAIGCVFAELLSGVPLWPG-KSDVDQLyliRKTLGDLIPRhqqvF 229
Cdd:cd06618   166 VDSKAkTRSagcaaYMAPERIDPPDnpKYDIRADVWSLGISLVELATGQFPYRNcKTEFEVL---TKILNEEPPS----L 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039741915 230 SMNQYFSgvkiPDPEDmetlelkfpnisysalgFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd06618   239 PPNEGFS----PDFCS-----------------FVDLCLTKDHRYRPKYRELLQHPF 274
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
10-287 9.25e-26

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 103.85  E-value: 9.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKrfLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLH 89
Cdd:cd14190    12 LGGGKFGKVHTCTEKRTGLKLAAK--VINKQNSKDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGGELF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  90 EL---DRYQRGVPEPLVknITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA--IKLCDFGFARLLTgPGDYYTDYVAT 164
Cdd:cd14190    90 ERivdEDYHLTEVDAMV--FVRQICEGIQFMHQMRVLHLDLKPENILCVNRTGhqVKIIDFGLARRYN-PREKLKVNFGT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 165 RWYRSPELLVGDtQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLylirktlgdliprhQQVFSMNQYFsgvkipdpe 244
Cdd:cd14190   167 PEFLSPEVVNYD-QVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETL--------------NNVLMGNWYF--------- 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1039741915 245 DMETLElkfpNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14190   223 DEETFE----HVSDEAKDFVSNLIIKERSARMSATQCLKHPWL 261
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
1-290 9.88e-26

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 105.87  E-value: 9.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLE--TEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHL 78
Cdd:cd05617    14 LQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKelVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYY 158
Cdd:cd05617    94 VIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTT 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 TDYVATRWYRSPELLVGDtQYGPPVDVWAIGCVFAELLSGvplwpgksdvdqlylirKTLGDLIPRHQQVfSMNQYFSGV 238
Cdd:cd05617   174 STFCGTPNYIAPEILRGE-EYGFSVDWWALGVLMFEMMAG-----------------RSPFDIITDNPDM-NTEDYLFQV 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 239 KIPDPedmetleLKFPN-ISYSALGFLKGCLHMDPAERLTCE------QLLQHPYFDSI 290
Cdd:cd05617   235 ILEKP-------IRIPRfLSVKASHVLKGFLNKDPKERLGCQpqtgfsDIKSHTFFRSI 286
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
10-209 1.04e-25

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 103.65  E-value: 1.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIK-----RFLETEDDpvikkiALR-EIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYC 83
Cdd:cd14082    11 LGSGQFGIVYGGKHRKTGRDVAIKvidklRFPTKQES------QLRnEVAILQQLSHPGVVNLECMFETPERVFVVMEKL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 DHTVLHELDRYQRG-VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA---IKLCDFGFARLLtGPGDYYT 159
Cdd:cd14082    85 HGDMLEMILSSEKGrLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPfpqVKLCDFGFARII-GEKSFRR 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039741915 160 DYVATRWYRSPELLVgDTQYGPPVDVWAIGCVFAELLSGVplWPGKSDVD 209
Cdd:cd14082   164 SVVGTPAYLAPEVLR-NKGYNRSLDMWSVGVIIYVSLSGT--FPFNEDED 210
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
10-286 1.10e-25

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 104.19  E-value: 1.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKrFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTvlh 89
Cdd:cd06619     9 LGHGNGGTVYKAYHLLTRRILAVK-VIPLDITVELQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFMDGG--- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  90 ELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgpGDYYTDYVATRWYRS 169
Cdd:cd06619    85 SLDVYRK-IPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLV--NSIAKTYVGTNAYMA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 170 PELLVGDtQYGPPVDVWAIGCVFAELLSGVPLWPGksdvdqlylIRKTLGDLIPRhqqvfsmnQYFSGVKIPDPEDMETL 249
Cdd:cd06619   162 PERISGE-QYGIHSDVWSLGISFMELALGRFPYPQ---------IQKNQGSLMPL--------QLLQCIVDEDPPVLPVG 223
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1039741915 250 ELkfpniSYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd06619   224 QF-----SEKFVHFITQCMRKQPKERPAPENLMDHPF 255
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
2-286 1.19e-25

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 105.49  E-value: 1.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVikkialREIR-MLKQLKHPNLVNLLEVFRRKRRLHLVF 80
Cdd:cd14176    19 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPT------EEIEiLLRYGQHPNIITLKDVYDDGKYVYVVT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  81 EYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQS----AIKLCDFGFARLLTGPGD 156
Cdd:cd14176    93 ELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQLRAENG 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 157 YYTDYVATRWYRSPELLvGDTQYGPPVDVWAIGCVFAELLSG-VPLWPGKSDVDQLYLIRKTLGDliprhqqvFSMNQYF 235
Cdd:cd14176   173 LLMTPCYTANFVAPEVL-ERQGYDAACDIWSLGVLLYTMLTGyTPFANGPDDTPEEILARIGSGK--------FSLSGGY 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 236 sgvkipdpedmetlelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14176   244 -----------------WNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPW 277
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
9-287 1.21e-25

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 104.30  E-value: 1.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVAIKRF-LETEDDpviKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTV 87
Cdd:cd06659    28 KIGEGSTGVVCIAREKHSGRQVAVKMMdLRKQQR---RELLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGGA 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  88 LHELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYVATRWY 167
Cdd:cd06659   105 LTDIVSQTR-LNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISKDVPKRKSLVGTPYW 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 168 RSPElLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTlgdliprhqqvfsmnqyfsgvkiPDPedme 247
Cdd:cd06659   184 MAPE-VISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDS-----------------------PPP---- 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1039741915 248 tlELK-FPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd06659   236 --KLKnSHKASPVLRDFLERMLVRDPQERATAQELLDHPFL 274
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
4-287 1.24e-25

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 103.43  E-value: 1.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrFLETEDDpvIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYC 83
Cdd:cd14107     4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAK-FIPLRSS--TRARAFQERDILARLSHRRLTCLLDQFETRKTLILILELC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 DHTVLheLDR-YQRG-VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILIT--KQSAIKLCDFGFARLLTGPGDYYT 159
Cdd:cd14107    81 SSEEL--LDRlFLKGvVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVspTREDIKICDFGFAQEITPSEHQFS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 160 DyvatrwYRSPELLVGDTQYGPPV----DVWAIGCVFAELLSGVPLWPGKSDvdqlyliRKTLgdliprhqqvfsMNQYF 235
Cdd:cd14107   159 K------YGSPEFVAPEIVHQEPVsaatDIWALGVIAYLSLTCHSPFAGEND-------RATL------------LNVAE 213
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 236 SGVKIPDPEdmetlelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14107   214 GVVSWDTPE--------ITHLSEDAKDFIKRVLQPDPEKRPSASECLSHEWF 257
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
10-286 1.28e-25

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 103.94  E-value: 1.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKI-----ALREIRMLKQLKHPNLVNLLEVFR-RKRRLHLVFEYC 83
Cdd:cd13990     8 LGKGGFSEVYKAFDLVEQRYVACKIHQLNKDWSEEKKQnyikhALREYEIHKSLDHPRIVKLYDVFEiDTDSFCTVLEYC 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 DHtvlHELDRY---QRGVPEPLVKNITWQTLQAVNFC--HKHNCIHRDVKPENILITKQS---AIKLCDFGFARLLtgPG 155
Cdd:cd13990    88 DG---NDLDFYlkqHKSIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSGNvsgEIKITDFGLSKIM--DD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 156 DYYTDY--------VATRWYRSPE-LLVGDTqygPP-----VDVWAIGCVFAELLSGvplwpgksdvdqlyliRKTLGDL 221
Cdd:cd13990   163 ESYNSDgmeltsqgAGTYWYLPPEcFVVGKT---PPkisskVDVWSVGVIFYQMLYG----------------RKPFGHN 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039741915 222 IPRHQQVFSmnqyfsgvKIPdpedMETLELKFPN---ISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd13990   224 QSQEAILEE--------NTI----LKATEVEFPSkpvVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
10-212 1.43e-25

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 104.67  E-value: 1.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFletEDDPVIKK------IALREIrMLKQLKHPNLVNLLEVFRRKRRLHLVFEYC 83
Cdd:cd05603     3 IGKGSFGKVLLAKRKCDGKFYAVKVL---QKKTILKKkeqnhiMAERNV-LLKNLKHPFLVGLHYSFQTSEKLYFVLDYV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 DHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYVA 163
Cdd:cd05603    79 NGGELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPEETTSTFCG 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1039741915 164 TRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLSGVPLWPGKsDVDQLY 212
Cdd:cd05603   159 TPEYLAPEVLRKEP-YDRTVDWWCLGAVLYEMLYGLPPFYSR-DVSQMY 205
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
10-286 1.45e-25

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 103.53  E-value: 1.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLETEDdpvikkiALREIRMLKQLKH-PNLVNLLEVF----RRKRRLHLVFEYCD 84
Cdd:cd14172    12 LGLGVNGKVLECFHRRTGQKCALKLLYDSPK-------ARREVEHHWRASGgPHIVHILDVYenmhHGKRCLLIIMECME 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVLHE--LDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILIT---KQSAIKLCDFGFARLLTGPGDYYT 159
Cdd:cd14172    85 GGELFSriQERGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTskeKDAVLKLTDFGFAKETTVQNALQT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 160 DyVATRWYRSPELLvGDTQYGPPVDVWAIGCVFAELLSGVPlwPGKSDVDQLylirktlgdLIPRHQQVFSMNQYfsgvK 239
Cdd:cd14172   165 P-CYTPYYVAPEVL-GPEKYDKSCDMWSLGVIMYILLCGFP--PFYSNTGQA---------ISPGMKRRIRMGQY----G 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1039741915 240 IPDPEdmetlelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14172   228 FPNPE--------WAEVSEEAKQLIRHLLKTDPTERMTITQFMNHPW 266
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
10-290 3.06e-25

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 103.98  E-value: 3.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIKK---IA-------LREIRMLKQLKHPNLVNLLEVFRRKRRLHLV 79
Cdd:cd05571     3 LGKGTFGKVILCREKATGELYAIK---------ILKKeviIAkdevahtLTENRVLQNTRHPFLTSLKYSFQTNDRLCFV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  80 FEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYT 159
Cdd:cd05571    74 MEYVNGGELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGATTK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 160 DYVATRWYRSPELLVgDTQYGPPVDVWAIGCVFAELLSG-VPLWPGKSDVdqlylirktLGDLIPrhqqvfsmnqyfsgv 238
Cdd:cd05571   154 TFCGTPEYLAPEVLE-DNDYGRAVDWWGLGVVMYEMMCGrLPFYNRDHEV---------LFELIL--------------- 208
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039741915 239 kipdpedMEtlELKFP-NISYSALGFLKGCLHMDPAERL-----TCEQLLQHPYFDSI 290
Cdd:cd05571   209 -------ME--EVRFPsTLSPEAKSLLAGLLKKDPKKRLgggprDAKEIMEHPFFASI 257
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
10-198 3.06e-25

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 102.45  E-value: 3.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRD-TGQIVAIKrfleteddpVIKKIAL--------REIRMLKQLKHPNLVNLLEVFRRKRRLHLVF 80
Cdd:cd14120     1 IGHGAFAVVFKGRHRKkPDLPVAIK---------CITKKNLsksqnllgKEIKILKELSHENVVALLDCQETSSSVYLVM 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  81 EYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA---------IKLCDFGFARLL 151
Cdd:cd14120    72 EYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGrkpspndirLKIADFGFARFL 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1039741915 152 TGpGDYYTDYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSG 198
Cdd:cd14120   152 QD-GMMAATLCGSPMYMAPEVIMS-LQYDAKADLWSIGTIVYQCLTG 196
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
10-191 3.56e-25

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 102.97  E-value: 3.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPviKKIALREIRMLKQLK-HPNLVNLLEV--FRRKRRLHLVFEYCDHT 86
Cdd:cd14036     8 IAEGGFAFVYEAQDVGTGKEYALKRLLSNEEEK--NKAIIQEINFMKKLSgHPNIVQFCSAasIGKEESDQGQAEYLLLT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  87 VLHE---LDR-YQRGVPEPL----VKNITWQTLQAVNFCHKHN--CIHRDVKPENILITKQSAIKLCDFGFARLLTgpgd 156
Cdd:cd14036    86 ELCKgqlVDFvKKVEAPGPFspdtVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGSATTEA---- 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 157 YYTDY----------------VATRWYRSPELLVGDTQY--GPPVDVWAIGCV 191
Cdd:cd14036   162 HYPDYswsaqkrslvedeitrNTTPMYRTPEMIDLYSNYpiGEKQDIWALGCI 214
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
9-195 4.74e-25

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 102.03  E-value: 4.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVAIKRFLETED-DPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTV 87
Cdd:cd08228     9 KIGRGQFSEVYRATCLLDRKPVALKKVQIFEMmDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLELADAGD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  88 LHELDRY----QRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYVA 163
Cdd:cd08228    89 LSQMIKYfkkqKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVG 168
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1039741915 164 TRWYRSPElLVGDTQYGPPVDVWAIGCVFAEL 195
Cdd:cd08228   169 TPYYMSPE-RIHENGYNFKSDIWSLGCLLYEM 199
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
4-286 5.04e-25

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 102.49  E-value: 5.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKI-GEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIKKIA-------LREIRMLKQLK-HPNLVNLLEVFRRKR 74
Cdd:cd14090     3 YKLTGELlGEGAYASVQTCINLYTGKEYAVK---------IIEKHPghsrsrvFREVETLHQCQgHPNILQLIEYFEDDE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  75 RLHLVFEYCDH-TVLHELDRyQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILIT---KQSAIKLCDFGFArl 150
Cdd:cd14090    74 RFYLVFEKMRGgPLLSHIEK-RVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCEsmdKVSPVKICDFDLG-- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 151 lTGPGD--YYTDYVATrwyrsPELL--VGDTQYGPP----------------VDVWAIGCVFAELLSGVPLWPGKSDVDQ 210
Cdd:cd14090   151 -SGIKLssTSMTPVTT-----PELLtpVGSAEYMAPevvdafvgealsydkrCDLWSLGVILYIMLCGYPPFYGRCGEDC 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 211 LYlirkTLGDLIPRHQqvfsmNQYFSGVK-----IPDPEdmetlelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHP 285
Cdd:cd14090   225 GW----DRGEACQDCQ-----ELLFHSIQegeyeFPEKE--------WSHISAEAKDLISHLLVRDASQRYTAEQVLQHP 287

                  .
gi 1039741915 286 Y 286
Cdd:cd14090   288 W 288
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
6-202 5.14e-25

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 102.04  E-value: 5.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   6 KIGKI-GEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKK--IALR-EIRMLKQLKHPNLVNLLEVFR--RKRRLHLV 79
Cdd:cd06652     5 RLGKLlGQGAFGRVYLCYDADTGRELAVKQVQFDPESPETSKevNALEcEIQLLKNLLHERIVQYYGCLRdpQERTLSIF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  80 FEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFAR-----LLTGP 154
Cdd:cd06652    85 MEYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKrlqtiCLSGT 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1039741915 155 GdyYTDYVATRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLSGVPLW 202
Cdd:cd06652   165 G--MKSVTGTPYWMSPEVISGEG-YGRKADIWSVGCTVVEMLTEKPPW 209
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
10-286 6.58e-25

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 102.41  E-value: 6.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFletEDDP-VIKKIALREIRMLKQLK-HPNLVNLLEVFRRKRRLHLVFE-YCDHT 86
Cdd:cd14173    10 LGEGAYARVQTCINLITNKEYAVKII---EKRPgHSRSRVFREVEMLYQCQgHRNVLELIEFFEEEDKFYLVFEkMRGGS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  87 VLHELDRyQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILI---TKQSAIKLCDFGFARLLTGPGDyyTDYVA 163
Cdd:cd14173    87 ILSHIHR-RRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCehpNQVSPVKICDFDLGSGIKLNSD--CSPIS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 164 TrwyrsPELLV--GDTQYGPP----------------VDVWAIGCVFAELLSGVPLWPGKSDVDQLYlirkTLGDLIPRH 225
Cdd:cd14173   164 T-----PELLTpcGSAEYMAPevveafneeasiydkrCDLWSLGVILYIMLSGYPPFVGRCGSDCGW----DRGEACPAC 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 226 QQVFSMNQYFSGVKIPDPEdmetlelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14173   235 QNMLFESIQEGKYEFPEKD--------WAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPW 287
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
9-200 7.36e-25

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 102.19  E-value: 7.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTgqIVAIKRFLETEDDPV--IKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHT 86
Cdd:cd14158    22 KLGEGGFGVVFKGYINDK--NVAVKKLAAMVDISTedLTKQFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMPNG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  87 VLheLDRY--QRGVPePLVK----NITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARllTGPGDYYTD 160
Cdd:cd14158   100 SL--LDRLacLNDTP-PLSWhmrcKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLAR--ASEKFSQTI 174
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1039741915 161 Y----VATRWYRSPELLVGDTQygPPVDVWAIGCVFAELLSGVP 200
Cdd:cd14158   175 MteriVGTTAYMAPEALRGEIT--PKSDIFSFGVVLLEIITGLP 216
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
2-305 9.73e-25

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 101.69  E-value: 9.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIAlREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd06641     4 ELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEIEDIQ-QEITVLSQCDSPYVTKYYGSYLKDTKLWIIME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTvlHELDRYQRG-VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTD 160
Cdd:cd06641    83 YLGGG--SALDLLEPGpLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRN* 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 YVATRWYRSPELlVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIrktlgdliPRHQQVFSMNQYFSGVKi 240
Cdd:cd06641   161 FVGTPFWMAPEV-IKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLI--------PKNNPPTLEGNYSKPLK- 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 241 pdpedmetlelkfpnisysalGFLKGCLHMDPAERLTCEQLLQHPY-FDSIREVGELTRQHDKPAR 305
Cdd:cd06641   231 ---------------------EFVEACLNKEPSFRPTAKELLKHKFiLRNAKKTSYLTELIDRYKR 275
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
3-286 9.87e-25

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 101.22  E-value: 9.87e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrFLETEDDpvIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd14665     1 RYELVKDIGSGNFGVARLMRDKQTKELVAVK-YIERGEK--IDENVQREIINHRSLRHPNIVRFKEVILTPTHLAIVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA--IKLCDFGFAR---LLTGPgdy 157
Cdd:cd14665    78 AAGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAprLKICDFGYSKssvLHSQP--- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 158 yTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVplWPGKsDVDQLYLIRKTLGDLIprhqqvfsmnqyfsG 237
Cdd:cd14665   155 -KSTVGTPAYIAPEVLLKKEYDGKIADVWSCGVTLYVMLVGA--YPFE-DPEEPRNFRKTIQRIL--------------S 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1039741915 238 VKIPDPEDMetlelkfpNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14665   217 VQYSIPDYV--------HISPECRHLISRIFVADPATRITIPEIRNHEW 257
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
2-287 1.87e-24

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 101.85  E-value: 1.87e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRD-TGQIVAIKrfleteddpVIKKI------ALREIRMLKQL--KHPN----LVNLLE 68
Cdd:cd14213    12 ARYEIVDTLGEGAFGKVVECIDHKmGGMHVAVK---------IVKNVdryreaARSEIQVLEHLntTDPNstfrCVQMLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  69 VFRRKRRLHLVFEYCDHTVlHELDRYQRGVPEPL--VKNITWQTLQAVNFCHKHNCIHRDVKPENILIT----------- 135
Cdd:cd14213    83 WFDHHGHVCIVFELLGLST-YDFIKENSFLPFPIdhIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVqsdyvvkynpk 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 136 --------KQSAIKLCDFGFArllTGPGDYYTDYVATRWYRSPELLVgDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSD 207
Cdd:cd14213   162 mkrdertlKNPDIKVVDFGSA---TYDDEHHSTLVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVFQTHDS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 208 VDQLYLIRKTLGDlIPRH-------QQVFSMNQ-----------YFSGVKIPDPEDMETLELKFPNIsysaLGFLKGCLH 269
Cdd:cd14213   238 KEHLAMMERILGP-LPKHmiqktrkRKYFHHDQldwdehssagrYVRRRCKPLKEFMLSQDVDHEQL----FDLIQKMLE 312
                         330
                  ....*....|....*...
gi 1039741915 270 MDPAERLTCEQLLQHPYF 287
Cdd:cd14213   313 YDPAKRITLDEALKHPFF 330
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
3-288 2.02e-24

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 100.47  E-value: 2.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRD-TGQIVAIKRFleTEDDPVIKKIAL-REIRMLKQLKHPNLVNLLEVFRRKRRLHLVF 80
Cdd:cd14201     7 EYSRKDLVGHGAFAVVFKGRHRKkTDWEVAIKSI--NKKNLSKSQILLgKEIKILKELQHENIVALYDVQEMPNSVFLVM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  81 EYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILIT----KQSA-----IKLCDFGFARLL 151
Cdd:cd14201    85 EYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSyasrKKSSvsgirIKIADFGFARYL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 152 TGPGDYYTdYVATRWYRSPELLVGDtQYGPPVDVWAIGCVFAELLSGVPLWPGKS--DVDQLYLIRKTLGDLIPRHQQVF 229
Cdd:cd14201   165 QSNMMAAT-LCGSPMYMAPEVIMSQ-HYDAKADLWSIGTVIYQCLVGKPPFQANSpqDLRMFYEKNKNLQPSIPRETSPY 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 230 SMNqyfsgvkipdpedmetlelkfpnisysalgFLKGCLHMDPAERLTCEQLLQHPYFD 288
Cdd:cd14201   243 LAD------------------------------LLLGLLQRNQKDRMDFEAFFSHPFLE 271
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
2-287 2.09e-24

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 101.63  E-value: 2.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRN-RDTGQIVAIKRFLETEDdpvIKKIALREIRMLKQL--KHPN----LVNLLEVFRRKR 74
Cdd:cd14215    12 ERYEIVSTLGEGTFGRVVQCIDhRRGGARVALKIIKNVEK---YKEAARLEINVLEKIneKDPEnknlCVQMFDWFDYHG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  75 RLHLVFEYCDHTVLHELdRYQRGVPEPL--VKNITWQTLQAVNFCHKHNCIHRDVKPENILI------------------ 134
Cdd:cd14215    89 HMCISFELLGLSTFDFL-KENNYLPYPIhqVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFvnsdyeltynlekkrder 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 135 -TKQSAIKLCDFGFArllTGPGDYYTDYVATRWYRSPELLVgDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYL 213
Cdd:cd14215   168 sVKSTAIRVVDFGSA---TFDHEHHSTIVSTRHYRAPEVIL-ELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREHLAM 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 214 IRKTLGDLIPRHQQVFSMNQYFSGVKIPDPEDMETLELKFPNIS-------------YSALGFLKGCLHMDPAERLTCEQ 280
Cdd:cd14215   244 MERILGPIPSRMIRKTRKQKYFYHGRLDWDENTSAGRYVRENCKplrryltseaeehHQLFDLIESMLEYEPSKRLTLAA 323

                  ....*..
gi 1039741915 281 LLQHPYF 287
Cdd:cd14215   324 ALKHPFF 330
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
10-290 2.14e-24

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 101.62  E-value: 2.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKrFLETE----DDPVIKKIAlrEIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDH 85
Cdd:cd05595     3 LGKGTFGKVILVREKATGRYYAMK-ILRKEviiaKDEVAHTVT--ESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 -TVLHELDRyQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYVAT 164
Cdd:cd05595    80 gELFFHLSR-ERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGATMKTFCGT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 165 RWYRSPELLvGDTQYGPPVDVWAIGCVFAELLSG-VPLWpgKSDvdqlylirktlgdliprHQQVFSMNQyfsgvkipdp 243
Cdd:cd05595   159 PEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGrLPFY--NQD-----------------HERLFELIL---------- 208
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 244 edMEtlELKFP-NISYSALGFLKGCLHMDPAERL-----TCEQLLQHPYFDSI 290
Cdd:cd05595   209 --ME--EIRFPrTLSPEAKSLLAGLLKKDPKQRLgggpsDAKEVMEHRFFLSI 257
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
10-290 2.35e-24

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 101.62  E-value: 2.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIKKIAL----------REIRMLKQLKHPNLVNLLEVFRRKRRLHLV 79
Cdd:cd05601     9 IGRGHFGEVQVVKEKATGDIYAMK---------VLKKSETlaqeevsffeEERDIMAKANSPWITKLQYAFQDSENLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  80 FEYcdHT---VLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGD 156
Cdd:cd05601    80 MEY--HPggdLLSLLSRYDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLSSDKT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 157 YYTDY-VATRWYRSPELL-----VGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSdvdqlylIRKTLGDLIpRHQQVFS 230
Cdd:cd05601   158 VTSKMpVGTPDYIAPEVLtsmngGSKGTYGVECDWWSLGIVAYEMLYGKTPFTEDT-------VIKTYSNIM-NFKKFLK 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 231 MnqyfsgvkipdPEDmetlelkfPNISYSALGFLKGCLhMDPAERLTCEQLLQHPYFDSI 290
Cdd:cd05601   230 F-----------PED--------PKVSESAVDLIKGLL-TDAKERLGYEGLCCHPFFSGI 269
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
1-290 2.40e-24

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 102.03  E-value: 2.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLE--TEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHL 78
Cdd:cd05618    19 LQDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKelVNDDEDIDWVQTEKHVFEQASNHPFLVGLHSCFQTESRLFF 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYY 158
Cdd:cd05618    99 VIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTT 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 TDYVATRWYRSPELLVGDtQYGPPVDVWAIGCVFAELLSGVPLW--------PGKSDVDQLYlirktlgdliprhqQVFS 230
Cdd:cd05618   179 STFCGTPNYIAPEILRGE-DYGFSVDWWALGVLMFEMMAGRSPFdivgssdnPDQNTEDYLF--------------QVIL 243
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 231 MNQyfsgVKIPDpedmetlelkfpNISYSALGFLKGCLHMDPAERLTC------EQLLQHPYFDSI 290
Cdd:cd05618   244 EKQ----IRIPR------------SLSVKAASVLKSFLNKDPKERLGChpqtgfADIQGHPFFRNV 293
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
10-286 2.70e-24

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 100.89  E-value: 2.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIKKIALR--------EIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd14168    18 LGTGAFSEVVLAEERATGKLFAVK---------CIPKKALKgkessienEIAVLRKIKHENIVALEDIYESPNHLYLVMQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQ---SAIKLCDFGFARlLTGPGDYY 158
Cdd:cd14168    89 LVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQdeeSKIMISDFGLSK-MEGKGDVM 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 TDYVATRWYRSPELLvGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDvDQLYlirktlgdliprhQQVFSMNQYFSGv 238
Cdd:cd14168   168 STACGTPGYVAPEVL-AQKPYSKAVDCWSIGVIAYILLCGYPPFYDEND-SKLF-------------EQILKADYEFDS- 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1039741915 239 kiPDPEDmetlelkfpnISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14168   232 --PYWDD----------ISDSAKDFIRNLMEKDPNKRYTCEQALRHPW 267
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
10-290 3.14e-24

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 101.19  E-value: 3.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFletEDDPVIKKIALREIR-----MLKQLKHPNLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:cd05604     4 IGKGSFGKVLLAKRKRDGKYYAVKVL---QKKVILNRKEQKHIMaernvLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYVAT 164
Cdd:cd05604    81 GGELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDTTTTFCGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 165 RWYRSPELLVgDTQYGPPVDVWAIGCVFAELLSGVPLWPGKsDVDQLY--LIRKtlgDLIPRhqqvfsmnqyfsgvkipd 242
Cdd:cd05604   161 PEYLAPEVIR-KQPYDNTVDWWCLGSVLYEMLYGLPPFYCR-DTAEMYenILHK---PLVLR------------------ 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 243 pedmetlelkfPNISYSALGFLKGCLHMDPAERLTC----EQLLQHPYFDSI 290
Cdd:cd05604   218 -----------PGISLTAWSILEELLEKDRQLRLGAkedfLEIKNHPFFESI 258
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
10-286 3.35e-24

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 99.87  E-value: 3.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVV-----FKCRNRDTGQIVAIKRFLETEDDPVIKKIAL-REIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYC 83
Cdd:cd14076     9 LGEGEFGKVklgwpLPKANHRSGVQVAIKLIRRDTQQENCQTSKImREINILKGLTHPNIVRLLDVLKTKKYIGIVLEFV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 DHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFA-RLLTGPGDYYTDYV 162
Cdd:cd14076    89 SGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFAnTFDHFNGDLMSTSC 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 163 ATRWYRSPELLVGDTQY-GPPVDVWAIGCVFAELLSGVPLW------PGKSDVDQLYlirktlgdliprhqqvfsmnQYF 235
Cdd:cd14076   169 GSPCYAAPELVVSDSMYaGRKADIWSCGVILYAMLAGYLPFdddphnPNGDNVPRLY--------------------RYI 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 236 sgvkipdpedMETlELKFPN-ISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14076   229 ----------CNT-PLIFPEyVTPKARDLLRRILVPNPRKRIRLSAIMRHAW 269
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
3-287 3.68e-24

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK1 binds with high affinity the alternative splicing factor, SRSF1 (serine/arginine-rich splicing factor 1), and regiospecifically phosphorylates 10-12 serines in its RS domain. It plays a role in the regulation of pre-mRNA splicing, chromatin structure, and germ cell development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271118 [Multi-domain]  Cd Length: 349  Bit Score: 101.26  E-value: 3.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDdpvIKKIALREIRMLKQLKH-----PN---LVNLLEVFR--- 71
Cdd:cd14216    11 RYHVIRKLGWGHFSTVWLSWDIQGKRFVAMKVVKSAEH---YTETALDEIKLLKSVRNsdpndPNremVVQLLDDFKisg 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  72 -RKRRLHLVFEYCDHTVLHEL--DRYQrGVPEPLVKNITWQTLQAVNFCH-KHNCIHRDVKPENILIT------------ 135
Cdd:cd14216    88 vNGTHICMVFEVLGHHLLKWIikSNYQ-GLPLPCVKKIIRQVLQGLDYLHtKCRIIHTDIKPENILLSvneqyirrlaae 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 136 ------------------KQSAIKLCDFGFARLLTgpgDYYTDYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLS 197
Cdd:cd14216   167 atewqrnflvnplepknaEKLKVKIADLGNACWVH---KHFTEDIQTRQYRSLEVLIG-SGYNTPADIWSTACMAFELAT 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 198 GVPLWPGKS------DVDQLYLIRKTLGdLIPRH--------QQVFSMNQYFSGVKIPDPEDM-ETLELKFPNISYSALG 262
Cdd:cd14216   243 GDYLFEPHSgedysrDEDHIALIIELLG-KVPRKlivagkysKEFFTKKGDLKHITKLKPWGLfEVLVEKYEWSQEEAAG 321
                         330       340
                  ....*....|....*....|....*...
gi 1039741915 263 ---FLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14216   322 ftdFLLPMLELIPEKRATAAECLRHPWL 349
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
4-286 3.83e-24

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 100.09  E-value: 3.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVikkialREIR-MLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd14178     5 YEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPS------EEIEiLLRYGQHPNIITLKDVYDDGKFVYLVMEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLheLDRY--QRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQS----AIKLCDFGFARLLTGPGD 156
Cdd:cd14178    79 MRGGEL--LDRIlrQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESgnpeSIRICDFGFAKQLRAENG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 157 YYTDYVATRWYRSPELLvGDTQYGPPVDVWAIGCVFAELLSG-VPLWPGKSDVDQLYLIRktlgdliprhqqVFSMNQYF 235
Cdd:cd14178   157 LLMTPCYTANFVAPEVL-KRQGYDAACDIWSLGILLYTMLAGfTPFANGPDDTPEEILAR------------IGSGKYAL 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 236 SGVkipdpedmetlelKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14178   224 SGG-------------NWDSISDAAKDIVSKMLHVDPHQRLTAPQVLRHPW 261
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
4-287 5.34e-24

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 99.28  E-value: 5.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRfleteddpVIKKIALR-----EIRMLKQLKHPNLVNLLEVFRRKRRLHL 78
Cdd:cd14113     9 YSEVAELGRGRFSVVKKCDQRGTKRAVATKF--------VNKKLMKRdqvthELGVLQSLQHPQLVGLLDTFETPTSYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA---IKLCDFGFA-RLLTGP 154
Cdd:cd14113    81 VLEMADQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSkptIKLADFGDAvQLNTTY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 155 gdYYTDYVATRWYRSPELLVGDtqygpPV----DVWAIGCVFAELLSGVPLWPGKSdVDQLYLIRKTLGDLIPrhqqvfs 230
Cdd:cd14113   161 --YIHQLLGSPEFAAPEIILGN-----PVsltsDLWSIGVLTYVLLSGVSPFLDES-VEETCLNICRLDFSFP------- 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039741915 231 mNQYFSGVkipdpedmetlelkfpniSYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14113   226 -DDYFKGV------------------SQKAKDFVCFLLQMDPAKRPSAALCLQEQWL 263
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
4-196 6.63e-24

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 99.18  E-value: 6.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIaLREIRMLKQLKHPNLVNLL--------EVFRRKRR 75
Cdd:cd14048     8 FEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLPNNELAREKV-LREVRALAKLDHPGIVRYFnawlerppEGWQEKMD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  76 ---LHLVFEYCDHTVLHELDRYQRGV---PEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFA- 148
Cdd:cd14048    87 evyLYIQMQLCRKENLKDWMNRRCTMesrELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFGLVt 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 149 ---------RLLTGPGDY--YTDYVATRWYRSPELLVGDtQYGPPVDVWAIGCVFAELL 196
Cdd:cd14048   167 amdqgepeqTVLTPMPAYakHTGQVGTRLYMSPEQIHGN-QYSEKVDIFALGLILFELI 224
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
45-286 8.06e-24

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 98.59  E-value: 8.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  45 KKIAL--REIRMLKQLKHPNLVNLLE--VFRRKR----RLHLVFEYCDHTVLHE-LDRYqRGVPEPLVKNITWQTLQAVN 115
Cdd:cd14012    40 KQIQLleKELESLKKLRHPNLVSYLAfsIERRGRsdgwKVYLLTEYAPGGSLSElLDSV-GSVPLDTARRWTLQLLEALE 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 116 FCHKHNCIHRDVKPENILITKQSA---IKLCDFGF-ARLLTGPGDYYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCV 191
Cdd:cd14012   119 YLHRNGVVHKSLHAGNVLLDRDAGtgiVKLTDYSLgKTLLDMCSRGSLDEFKQTYWLPPELAQGSKSPTRKTDVWDLGLL 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 192 FAELLSGVPLWpgksdvdqlylirktlgdliprhqqvfsmnQYFSGvkiPDPEdMETLELkfpniSYSALGFLKGCLHMD 271
Cdd:cd14012   199 FLQMLFGLDVL------------------------------EKYTS---PNPV-LVSLDL-----SASLQDFLSKCLSLD 239
                         250
                  ....*....|....*
gi 1039741915 272 PAERLTCEQLLQHPY 286
Cdd:cd14012   240 PKKRPTALELLPHEF 254
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
10-287 8.45e-24

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 98.70  E-value: 8.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKrFLETEDDP--VIKKIALREIRMLKQLKHPNLVNLLEVFRRKR-RLHLVFEYCDHT 86
Cdd:cd14165     9 LGEGSYAKVKSAYSERLKCNVAIK-IIDKKKAPddFVEKFLPRELEILARLNHKSIIKTYEIFETSDgKVYIVMELGVQG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  87 VLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLL----TGPGDYYTDYV 162
Cdd:cd14165    88 DLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRClrdeNGRIVLSKTFC 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 163 ATRWYRSPELLVGdTQYGPPV-DVWAIGCVFAELLSG-VPLwpGKSDVDQLYLIRKTLGDLIPRhqqvfSMNQyfsgvki 240
Cdd:cd14165   168 GSAAYAAPEVLQG-IPYDPRIyDIWSLGVILYIMVCGsMPY--DDSNVKKMLKIQKEHRVRFPR-----SKNL------- 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1039741915 241 pdpedmeTLELKfpNISYSAlgflkgcLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14165   233 -------TSECK--DLIYRL-------LQPDVSQRLCIDEVLSHPWL 263
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
2-286 9.20e-24

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 99.30  E-value: 9.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFletedDPV--IKKIALREIRMLKQL-KHPNLVNLLEVFRRKRR--- 75
Cdd:cd06639    22 DTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKIL-----DPIsdVDEEIEAEYNILRSLpNHPNVVKFYGMFYKADQyvg 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  76 --LHLVFEYCDHTVLHEL-----DRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFA 148
Cdd:cd06639    97 gqLWLVLELCNGGSVTELvkgllKCGQR-LDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 149 RLLTGPGDYYTDYVATRWYRSPELLVGDTQYGPP----VDVWAIGCVFAELLSGVPLWPGKSDVDQLYlirktlgdLIPR 224
Cdd:cd06639   176 AQLTSARLRRNTSVGTPFWMAPEVIACEQQYDYSydarCDVWSLGITAIELADGDPPLFDMHPVKALF--------KIPR 247
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 225 HqqvfsmnqyfsgvkiPDPedmetlELKFPNISYSALG-FLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd06639   248 N---------------PPP------TLLNPEKWCRGFShFISQCLIKDFEKRPSVTHLLEHPF 289
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
4-195 1.01e-23

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 98.73  E-value: 1.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQ-IVAIK---------RFLETEDDPVIKKIaLREIRMLK-QLKHPNLVNLLEVFRR 72
Cdd:cd08528     2 YAVLELLGSGAFGCVYKVRKKSNGQtLLALKeinmtnpafGRTEQERDKSVGDI-ISEVNIIKeQLRHPNIVRYYKTFLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  73 KRRLHLVFEYCDHTVLHE----LDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCI-HRDVKPENILITKQSAIKLCDFGF 147
Cdd:cd08528    81 NDRLYIVMELIEGAPLGEhfssLKEKNEHFTEDRIWNIFVQMVLALRYLHKEKQIvHRDLKPNNIMLGEDDKVTITDFGL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1039741915 148 ARLLTGPGDYYTDYVATRWYRSPElLVGDTQYGPPVDVWAIGCVFAEL 195
Cdd:cd08528   161 AKQKGPESSKMTSVVGTILYSCPE-IVQNEPYGEKADIWALGCILYQM 207
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
10-287 1.12e-23

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 99.51  E-value: 1.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKrFLETEDDPVIKKI--ALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYcdhTV 87
Cdd:PTZ00263   26 LGTGSFGRVRIAKHKGTGEYYAIK-CLKKREILKMKQVqhVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEF---VV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  88 LHELDRYQRGV---PEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgpgDYYTDYVAT 164
Cdd:PTZ00263  102 GGELFTHLRKAgrfPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVP---DRTFTLCGT 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 165 RWYRSPElLVGDTQYGPPVDVWAIGCVFAELLSGVPlwpgksdvdqlylirktlgdliprhqqvfsmnQYFSGVKIPDPE 244
Cdd:PTZ00263  179 PEYLAPE-VIQSKGHGKAVDWWTMGVLLYEFIAGYP--------------------------------PFFDDTPFRIYE 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1039741915 245 DMETLELKFPN-ISYSALGFLKGCLHMDPAERLTC-----EQLLQHPYF 287
Cdd:PTZ00263  226 KILAGRLKFPNwFDGRARDLVKGLLQTDHTKRLGTlkggvADVKNHPYF 274
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
9-287 1.13e-23

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 98.96  E-value: 1.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVAIKRF-LETEDDpviKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTV 87
Cdd:cd06658    29 KIGEGSTGIVCIATEKHTGKQVAVKKMdLRKQQR---RELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGA 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  88 LHELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYVATRWY 167
Cdd:cd06658   106 LTDIVTHTR-MNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSLVGTPYW 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 168 RSPElLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDLIPRHQQVFSMNQyfsgvkipdpedme 247
Cdd:cd06658   185 MAPE-VISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDNLPPRVKDSHKVSSVLR-------------- 249
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1039741915 248 tlelkfpnisysalGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd06658   250 --------------GFLDLMLVREPSQRATAQELLQHPFL 275
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
9-287 1.20e-23

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 98.15  E-value: 1.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVA---IKRFLETEDDPVikkiaLREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDH 85
Cdd:cd14191     9 RLGSGKFGQVFRLVEKKTKKVWAgkfFKAYSAKEKENI-----RQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMVSG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 TVLHE--LDRYQRGVPEPLVKNITwQTLQAVNFCHKHNCIHRDVKPENILITKQ--SAIKLCDFGFARLLTGPGDYYTDY 161
Cdd:cd14191    84 GELFEriIDEDFELTERECIKYMR-QISEGVEYIHKQGIVHLDLKPENIMCVNKtgTKIKLIDFGLARRLENAGSLKVLF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 162 vATRWYRSPElLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDLiprhqqvfsmnqyfsgvkip 241
Cdd:cd14191   163 -GTPEFVAPE-VINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDF-------------------- 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1039741915 242 DPEdmetlelKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14191   221 DDE-------AFDEISDDAKDFISNLLKKDMKARLTCTQCLQHPWL 259
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
2-200 1.24e-23

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 98.63  E-value: 1.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrFLETEDDPVIKKIA--LREIRMLKQLKHPNLVNLLEVFRRKRRLHLV 79
Cdd:cd14209     1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMK-ILDKQKVVKLKQVEhtLNEKRILQAINFPFLVKLEYSFKDNSNLYMV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  80 FEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGpgdYYT 159
Cdd:cd14209    80 MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKG---RTW 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1039741915 160 DYVATRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLSGVP 200
Cdd:cd14209   157 TLCGTPEYLAPEIILSKG-YNKAVDWWALGVLIYEMAAGYP 196
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
10-201 1.61e-23

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 98.96  E-value: 1.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIK---RFLETEDDpvikkialREIRMLKQLK-HPNLVNLLEVFRRKRRLHLVFEYCDH 85
Cdd:cd14179    15 LGEGSFSICRKCLHKKTNQEYAVKivsKRMEANTQ--------REIAALKLCEgHPNIVKLHEVYHDQLHTFLVMELLKG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 TVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQ---SAIKLCDFGFARLLTGPGDYYTDYV 162
Cdd:cd14179    87 GELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDEsdnSEIKIIDFGFARLKPPDNQPLKTPC 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1039741915 163 ATRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLSG-VPL 201
Cdd:cd14179   167 FTLHYAAPELLNYNG-YDESCDLWSLGVILYTMLSGqVPF 205
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
7-286 1.64e-23

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 98.01  E-value: 1.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   7 IGK-IGEGSYGVVFKCRNRDTGQIVAIKRFLET--EDDPVIKKIAlREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYC 83
Cdd:cd14117    10 IGRpLGKGKFGNVYLAREKQSKFIVALKVLFKSqiEKEGVEHQLR-REIEIQSHLRHPNILRLYNYFHDRKRIYLILEYA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 DHTVLH-ELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFArlLTGPGDYYTDYV 162
Cdd:cd14117    89 PRGELYkELQKHGR-FDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWS--VHAPSLRRRTMC 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 163 ATRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKtlgdliprhqqvfsmnqyfsgvkipd 242
Cdd:cd14117   166 GTLDYLPPEMIEGRT-HDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVK-------------------------- 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1039741915 243 pedmetLELKFP-NISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14117   219 ------VDLKFPpFLSDGSRDLISKLLRYHPSERLPLKGVMEHPW 257
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
10-197 1.83e-23

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 97.51  E-value: 1.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDtgQIVAIKRFlETEDdpvIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLH 89
Cdd:cd14058     1 VGRGSFGVVCKARWRN--QIVAVKII-ESES---EKKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  90 ELDRYQRGVPEPLVKN-ITW--QTLQAVNFCHKHN---CIHRDVKPENILITKQ-SAIKLCDFGFArllTGPGDYYTDYV 162
Cdd:cd14058    75 NVLHGKEPKPIYTAAHaMSWalQCAKGVAYLHSMKpkaLIHRDLKPPNLLLTNGgTVLKICDFGTA---CDISTHMTNNK 151
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1039741915 163 ATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLS 197
Cdd:cd14058   152 GSAAWMAPEVFEG-SKYSEKCDVFSWGIILWEVIT 185
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
10-198 2.04e-23

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 96.79  E-value: 2.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFkcRNRDTGQIVAIKRFLETEDDpvikkialrEIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLH 89
Cdd:cd14059     1 LGSGAQGAVF--LGKFRGEEVAVKKVRDEKET---------DIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLY 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  90 ELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTdYVATRWYRS 169
Cdd:cd14059    70 EVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKSTKMS-FAGTVAWMA 148
                         170       180
                  ....*....|....*....|....*....
gi 1039741915 170 PElLVGDTQYGPPVDVWAIGCVFAELLSG 198
Cdd:cd14059   149 PE-VIRNEPCSEKVDIWSFGVVLWELLTG 176
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
10-198 2.27e-23

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 97.45  E-value: 2.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRdtGQIVAIKRfLETEDDPVIKKIALREIRMLKQLKHPNLVNLL--EVFRRKRRLHLV-FEYCDHT 86
Cdd:cd13979    11 LGSGGFGSVYKATYK--GETVAVKI-VRRRRKNRASRQSFWAELNAARLRHENIVRVLaaETGTDFASLGLIiMEYCGNG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  87 VLHELdRYQRGVPEPLVK--NITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGP---GDYYTDY 161
Cdd:cd13979    88 TLQQL-IYEGSEPLPLAHriLISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKLGEGnevGTPRSHI 166
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1039741915 162 VATRWYRSPELLVGDTQyGPPVDVWAIGCVFAELLSG 198
Cdd:cd13979   167 GGTYTYRAPELLKGERV-TPKADIYSFGITLWQMLTR 202
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
10-290 2.37e-23

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 97.46  E-value: 2.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCR---NRDTGQIVAIKrfleteddpVIKKIALreIRMLKQLKH--------------PNLVNLLEVFRR 72
Cdd:cd05583     2 LGTGAYGKVFLVRkvgGHDAGKLYAMK---------VLKKATI--VQKAKTAEHtmterqvleavrqsPFLVTLHYAFQT 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  73 KRRLHLVFEYCD----HTVLHELDRYQrgvpEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFA 148
Cdd:cd05583    71 DAKLHLILDYVNggelFTHLYQREHFT----ESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLS 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 149 RLLTGPGDYYT-DYVATRWYRSPELLVGDTQ-YGPPVDVWAIGCVFAELLSGV-PLWPGKSDVDQLYLIRKTLGDLIPrh 225
Cdd:cd05583   147 KEFLPGENDRAySFCGTIEYMAPEVVRGGSDgHDKAVDWWSLGVLTYELLTGAsPFTVDGERNSQSEISKRILKSHPP-- 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 226 qqvfsmnqyfsgvkIPdpedmetlelkfPNISYSALGFLKGCLHMDPAERLTC-----EQLLQHPYFDSI 290
Cdd:cd05583   225 --------------IP------------KTFSAEAKDFILKLLEKDPKKRLGAgprgaHEIKEHPFFKGL 268
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
10-286 2.56e-23

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 97.23  E-value: 2.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIK-----RFLETEDDPVIKKIALrEIRMLKQL----KHPNLVNLLEVFRRKRRLHLVF 80
Cdd:cd14101     8 LGKGGFGTVYAGHRISDGLQVAIKqisrnRVQQWSKLPGVNPVPN-EVALLQSVgggpGHRGVIRLLDWFEIPEGFLLVL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  81 EYCDHTvlHELDRY--QRG-VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILI-TKQSAIKLCDFGFARLLTgpGD 156
Cdd:cd14101    87 ERPQHC--QDLFDYitERGaLDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVdLRTGDIKLIDFGSGATLK--DS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 157 YYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGvplwpgksdvdqlylirktlgdliprhqqvfsmnqyfs 236
Cdd:cd14101   163 MYTDFDGTRVYSPPEWILYHQYHALPATVWSLGILLYDMVCG-------------------------------------- 204
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 237 gvKIPDPEDMETL--ELKFP-NISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14101   205 --DIPFERDTDILkaKPSFNkRVSNDCRSLIRSCLAYNPSDRPSLEQILLHPW 255
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
2-286 2.62e-23

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 97.43  E-value: 2.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIAlREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd06640     4 ELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEDEIEDIQ-QEITVLSQCDSPYVTKYYGSYLKGTKLWIIME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTvlHELDRYQRG-VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTD 160
Cdd:cd06640    83 YLGGG--SALDLLRAGpFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 YVATRWYRSPELlVGDTQYGPPVDVWAIGCVFAELLSGVPlwpGKSDVDQLYLIRktlgdLIPrhqqvfsmnqyfsgvKI 240
Cdd:cd06640   161 FVGTPFWMAPEV-IQQSAYDSKADIWSLGITAIELAKGEP---PNSDMHPMRVLF-----LIP---------------KN 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1039741915 241 PDPedmeTLELKFpniSYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd06640   217 NPP----TLVGDF---SKPFKEFIDACLNKDPSFRPTAKELLKHKF 255
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
6-202 4.17e-23

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 96.63  E-value: 4.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   6 KIGKI-GEGSYGVVFKCRNRDTGQIVAIKRF-LETEDDPVIKKI-ALR-EIRMLKQLKHPNLVNLLEVFR--RKRRLHLV 79
Cdd:cd06653     5 RLGKLlGRGAFGEVYLCYDADTGRELAVKQVpFDPDSQETSKEVnALEcEIQLLKNLRHDRIVQYYGCLRdpEEKKLSIF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  80 FEYC-DHTVLHELDRYQrGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFAR-----LLTG 153
Cdd:cd06653    85 VEYMpGGSVKDQLKAYG-ALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKriqtiCMSG 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1039741915 154 PGdyYTDYVATRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLSGVPLW 202
Cdd:cd06653   164 TG--IKSVTGTPYWMSPEVISGEG-YGRKADVWSVACTVVEMLTEKPPW 209
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
2-286 5.29e-23

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 96.66  E-value: 5.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIAlREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd06642     4 ELFTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAEDEIEDIQ-QEITVLSQCDSPYITRYYGSYLKGTKLWIIME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTvlHELDRYQRG-VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTD 160
Cdd:cd06642    83 YLGGG--SALDLLKPGpLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 YVATRWYRSPELlVGDTQYGPPVDVWAIGCVFAELLSGVPLWpgkSDVDQLYLIRktlgdLIPRHQQVFSMNQYFSGVKi 240
Cdd:cd06642   161 FVGTPFWMAPEV-IKQSAYDFKADIWSLGITAIELAKGEPPN---SDLHPMRVLF-----LIPKNSPPTLEGQHSKPFK- 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1039741915 241 pdpedmetlelkfpnisysalGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd06642   231 ---------------------EFVEACLNKDPRFRPTAKELLKHKF 255
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
4-290 6.60e-23

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 96.71  E-value: 6.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRfleteddpvIKK--IALR--------EIRMLKQLKHPNLVNLLEVFRRK 73
Cdd:cd05609     2 FETIKLISNGAYGAVYLVRHRETRQRFAMKK---------INKqnLILRnqiqqvfvERDILTFAENPFVVSMYCSFETK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  74 RRLHLVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFAR--LL 151
Cdd:cd05609    73 RHLCMVMEYVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKigLM 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 152 TGPGDYYTDY-------------VATRWYRSPELLVgDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDqlyLIRKTL 218
Cdd:cd05609   153 SLTTNLYEGHiekdtrefldkqvCGTPEYIAPEVIL-RQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEE---LFGQVI 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039741915 219 GDLIprhqqvfsmnqyfsgvKIPDPEDMetlelkfpnISYSALGFLKGCLHMDPAERL---TCEQLLQHPYFDSI 290
Cdd:cd05609   229 SDEI----------------EWPEGDDA---------LPDDAQDLITRLLQQNPLERLgtgGAEEVKQHPFFQDL 278
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
9-287 1.36e-22

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 95.37  E-value: 1.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLK-HPNLVNLLEVFRRKRRLHLVFEYC---- 83
Cdd:cd14198    15 ELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAEILHEIAVLELAKsNPRVVNLHEVYETTSEIILILEYAagge 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 --DHTVLHELDRyqrgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA---IKLCDFGFARLLTGPGDyY 158
Cdd:cd14198    95 ifNLCVPDLAEM----VSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPlgdIKIVDFGMSRKIGHACE-L 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 TDYVATRWYRSPELLvgdtQYGP---PVDVWAIGCVFAELLSGVPLWPGkSDVDQLYLirktlgdliprhqQVFSMNQYF 235
Cdd:cd14198   170 REIMGTPEYLAPEIL----NYDPittATDMWNIGVIAYMLLTHESPFVG-EDNQETFL-------------NISQVNVDY 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 236 SgvkipdpedmetlELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14198   232 S-------------EETFSSVSQLATDFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
9-287 2.17e-22

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 94.60  E-value: 2.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVA-----IKRFLETEddpvIKKIAlREIRMLKQLKHPNLVNLLEVFRRKRRLHLVF--E 81
Cdd:cd13983     8 VLGRGSFKTVYRAFDTEEGIEVAwneikLRKLPKAE----RQRFK-QEIEILKSLKHPNIIKFYDSWESKSKKEVIFitE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHE-LDRYQRgVPEPLVKNITWQTLQAVNFCHKHN--CIHRDVKPENILIT-KQSAIKLCDFGFARLLTgpGDY 157
Cdd:cd13983    83 LMTSGTLKQyLKRFKR-LKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINgNTGEVKIGDLGLATLLR--QSF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 158 YTDYVATRWYRSPELLvgDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYliRKTLGDLIPrhqqvfsmnQYFSG 237
Cdd:cd13983   160 AKSVIGTPEFMAPEMY--EEHYDEKVDIYAFGMCLLEMATGEYPYSECTNAAQIY--KKVTSGIKP---------ESLSK 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039741915 238 VKIPDPEDmetlelkfpnisysalgFLKGCLhMDPAERLTCEQLLQHPYF 287
Cdd:cd13983   227 VKDPELKD-----------------FIEKCL-KPPDERPSARELLEHPFF 258
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
10-290 2.29e-22

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 96.24  E-value: 2.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFletEDDPVIKKIALREIR-----MLKQLKHPNLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:cd05602    15 IGKGSFGKVLLARHKSDEKFYAVKVL---QKKAILKKKEEKHIMsernvLLKNVKHPFLVGLHFSFQTTDKLYFVLDYIN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYVAT 164
Cdd:cd05602    92 GGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEPNGTTSTFCGT 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 165 RWYRSPELLvGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDqlylirktlgdliprhqqvfsmnQYFSGVKIPdpe 244
Cdd:cd05602   172 PEYLAPEVL-HKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAE-----------------------MYDNILNKP--- 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039741915 245 dmetLELKfPNISYSALGFLKGCLHMDPAERLTCE----QLLQHPYFDSI 290
Cdd:cd05602   225 ----LQLK-PNITNSARHLLEGLLQKDRTKRLGAKddftEIKNHIFFSPI 269
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
10-287 2.55e-22

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 94.64  E-value: 2.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTG-----QIVAIKRFLETEDdpvIKKialrEIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:cd14192    12 LGGGRFGQVHKCTELSTGltlaaKIIKVKGAKEREE---VKN----EINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVLHEL---DRYQrgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA--IKLCDFGFARLLTgPGDYYT 159
Cdd:cd14192    85 GGELFDRitdESYQ--LTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNSTGnqIKIIDFGLARRYK-PREKLK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 160 DYVATRWYRSPELLVGD-TQYgpPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDLiprhqqvfsmnqyfsgv 238
Cdd:cd14192   162 VNFGTPEFLAPEVVNYDfVSF--PTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDF----------------- 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1039741915 239 kipdpeDMETLElkfpNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14192   223 ------DAEAFE----NLSEEAKDFISRLLVKEKSCRMSATQCLKHEWL 261
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
10-290 2.78e-22

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 95.74  E-value: 2.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLET---EDDPVikKIALREIRMLK-QLKHPNLVNLLEVFRRKRRLHLVFEYCDH 85
Cdd:cd05590     3 LGKGSFGKVMLARLKESGRLYAVKVLKKDvilQDDDV--ECTMTEKRILSlARNHPFLTQLYCCFQTPDRLFFVMEFVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 TVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYVATR 165
Cdd:cd05590    81 GDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKTTSTFCGTP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 166 WYRSPELLvGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDqlyLIRKTLGDliprhqqvfsmnqyfsgvkipdped 245
Cdd:cd05590   161 DYIAPEIL-QEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDD---LFEAILND------------------------- 211
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 246 metlELKFPN-ISYSALGFLKGCLHMDPAERLTC------EQLLQHPYFDSI 290
Cdd:cd05590   212 ----EVVYPTwLSQDAVDILKAFMTKNPTMRLGSltlggeEAILRHPFFKEL 259
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
10-290 3.09e-22

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 95.71  E-value: 3.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLETE---DDPVIKKIALREIRMLKQLKH-PNLVNLLEVFRRKRRLHLVFEY-CD 84
Cdd:cd05586     1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVivaKKEVAHTIGERNILVRTALDEsPFIVGLKFSFQTPTDLYLVTDYmSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVLHELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYVAT 164
Cdd:cd05586    81 GELFWHLQKEGR-FSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADLTDNKTTNTFCGT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 165 RWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSG-VPLWpgKSDVDQLYlirktlgdliprhqqvfsMNQYFSGVKIpdP 243
Cdd:cd05586   160 TEYLAPEVLLDEKGYTKMVDFWSLGVLVFEMCCGwSPFY--AEDTQQMY------------------RNIAFGKVRF--P 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 244 EDMETLELKfpnisysalGFLKGCLHMDPAERL----TCEQLLQHPYFDSI 290
Cdd:cd05586   218 KDVLSDEGR---------SFVKGLLNRNPKHRLgahdDAVELKEHPFFADI 259
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
10-290 3.72e-22

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 95.18  E-value: 3.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIKKIALRE---IRMLKQLKH--------PNLVNLLEVFRRKRRLHL 78
Cdd:cd05588     3 IGRGSYAKVLMVELKKTKRIYAMK---------VIKKELVNDdedIDWVQTEKHvfetasnhPFLVGLHSCFQTESRLFF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYY 158
Cdd:cd05588    74 VIEFVNGGDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 TDYVATRWYRSPELLVGDtQYGPPVDVWAIGCVFAELLSG--------VPLWPGKSDVDQLY--LIRKTLgdLIPRhqqv 228
Cdd:cd05588   154 STFCGTPNYIAPEILRGE-DYGFSVDWWALGVLMFEMLAGrspfdivgSSDNPDQNTEDYLFqvILEKPI--RIPR---- 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039741915 229 fsmnqyfsgvkipdpedmetlelkfpNISYSALGFLKGCLHMDPAERLTCE------QLLQHPYFDSI 290
Cdd:cd05588   227 --------------------------SLSVKAASVLKGFLNKNPAERLGCHpqtgfaDIQSHPFFRTI 268
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
10-212 4.18e-22

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 93.93  E-value: 4.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFleteDDPVIK-KIALREIRMLKQLK-HPNLVNLLEVFRRKRRlHLVF--EYCDH 85
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTKMALKFV----PKPSTKlKDFLREYNISLELSvHPHIIKTYDVAFETED-YYVFaqEYAPY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 TVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA--IKLCDFGFAR---LLTGPGDYYTD 160
Cdd:cd13987    76 GDLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCrrVKLCDFGLTRrvgSTVKRVSGTIP 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 161 YVAtrwyrsPELL----VGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLY 212
Cdd:cd13987   156 YTA------PEVCeakkNEGFVVDPSIDVWAFGVLLFCCLTGNFPWEKADSDDQFY 205
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
4-200 4.47e-22

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 94.42  E-value: 4.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEddpvikKIALREI-------RMLKQLKHPNLVNLLEVFRRKRRL 76
Cdd:cd05612     3 FERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPE------VIRLKQEqhvhnekRVLKEVSHPFIIRLFWTEHDQRFL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  77 HLVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgpgD 156
Cdd:cd05612    77 YMLMEYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLR---D 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1039741915 157 YYTDYVATRWYRSPELLvGDTQYGPPVDVWAIGCVFAELLSGVP 200
Cdd:cd05612   154 RTWTLCGTPEYLAPEVI-QSKGHNKAVDWWALGILIYEMLVGYP 196
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
10-286 4.98e-22

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 93.99  E-value: 4.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKK--IALR-EIRMLKQLKHPNLVNLLEVFRRK--RRLHLVFEYCD 84
Cdd:cd06651    15 LGQGAFGRVYLCYDVDTGRELAAKQVQFDPESPETSKevSALEcEIQLLKNLQHERIVQYYGCLRDRaeKTLTIFMEYMP 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTG---PGDYYTDY 161
Cdd:cd06651    95 GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicmSGTGIRSV 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 162 VATRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTlgdliPRHQQVFSmnqyfsgvkip 241
Cdd:cd06651   175 TGTPYWMSPEVISGEG-YGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQ-----PTNPQLPS----------- 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1039741915 242 dpedmetlelkfpNISYSALGFLkGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd06651   238 -------------HISEHARDFL-GCIFVEARHRPSAEELLRHPF 268
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
2-200 5.13e-22

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 95.14  E-value: 5.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEddpVIKK--IAL----REIrmlkqLKHPN---LVNLLEVFRR 72
Cdd:cd05596    26 EDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFE---MIKRsdSAFfweeRDI-----MAHANsewIVQLHYAFQD 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  73 KRRLHLVFEYC---DHTVLheLDRYQrgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFAR 149
Cdd:cd05596    98 DKYLYMVMDYMpggDLVNL--MSNYD--VPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCM 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039741915 150 LLTGPGDYYTDY-VATRWYRSPELLV---GDTQYGPPVDVWAIGCVFAELLSGVP 200
Cdd:cd05596   174 KMDKDGLVRSDTaVGTPDYISPEVLKsqgGDGVYGRECDWWSVGVFLYEMLVGDT 228
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
10-312 5.42e-22

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 94.87  E-value: 5.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLE---TEDDPVikKIALREIRMLK-QLKHPNLVNLLEVFRRKRRLHLVFEYCDH 85
Cdd:cd05591     3 LGKGSFGKVMLAERKGTDEVYAIKVLKKdviLQDDDV--DCTMTEKRILAlAAKHPFLTALHSCFQTKDRLFFVMEYVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 TVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYVATR 165
Cdd:cd05591    81 GDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGKTTTTFCGTP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 166 WYRSPELLvGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDqlyLIRKTLGDliprhqqvfsmnqyfsgvkipdped 245
Cdd:cd05591   161 DYIAPEIL-QELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDD---LFESILHD------------------------- 211
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039741915 246 metlELKFPN-ISYSALGFLKGCLHMDPAERLTC-------EQLLQHPYFDSIREVGELTRQHDKPARKTLRQSR 312
Cdd:cd05591   212 ----DVLYPVwLSKEAVSILKAFMTKNPAKRLGCvasqggeDAIRQHPFFREIDWEALEQRKVKPPFKPKIKTKR 282
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
3-287 5.98e-22

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK3 is highly expressed in the heart and skeletal muscles, and is controlled by a muscle-specific enhancer that is regulated by MEF2. It may play an important role in muscle development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271120 [Multi-domain]  Cd Length: 365  Bit Score: 95.47  E-value: 5.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIK------KIALREIRMLKQL--------KHPNLVNLLE 68
Cdd:cd14218    11 RYHVVRKLGWGHFSTVWLCWDIQRKRFVALK---------VVKsavhytETAVDEIKLLKCVrdsdpsdpKRETIVQLID 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  69 VFR----RKRRLHLVFEYCDHTVLHEL--DRYQrGVPEPLVKNITWQTLQAVNFCH-KHNCIHRDVKPENIL-------- 133
Cdd:cd14218    82 DFKisgvNGVHVCMVLEVLGHQLLKWIikSNYQ-GLPLPCVKSILRQVLQGLDYLHtKCKIIHTDIKPENILmcvdegyv 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 134 --------ITKQSAI-----KLCDFGFARLLTGPGD----------------------YYTDYVATRWYRSPELLVGdTQ 178
Cdd:cd14218   161 rrlaaeatIWQQAGApppsgSSVSFGASDFLVNPLEpqnadkirvkiadlgnacwvhkHFTEDIQTRQYRALEVLIG-AE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 179 YGPPVDVWAIGCVFAELLSGVPLWPGKS------DVDQLYLIRKTLGDlIPRH--------QQVFSMNQYFSGVKIPDPE 244
Cdd:cd14218   240 YGTPADIWSTACMAFELATGDYLFEPHSgedytrDEDHIAHIVELLGD-IPPHfalsgrysREYFNRRGELRHIKNLKHW 318
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1039741915 245 DM-ETLELKFP-----NISYSAlgFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14218   319 GLyEVLVEKYEwpleqAAQFTD--FLLPMMEFLPEKRATAAQCLQHPWL 365
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
4-197 6.18e-22

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 93.71  E-value: 6.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFleteddPVIKKIALREIRMLKQLKHPNLVNLLEVF------------- 70
Cdd:cd14047     8 FKEIELIGSGGFGQVFKAKHRIDGKTYAIKRV------KLNNEKAEREVKALAKLDHPNIVRYNGCWdgfdydpetsssn 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  71 --RRKRR-LHLVFEYCDHTVLHELDRYQRGVP-EPL-VKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDF 145
Cdd:cd14047    82 ssRSKTKcLFIQMEFCEKGTLESWIEKRNGEKlDKVlALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDF 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 146 GFARLLTGPGDyYTDYVATRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLS 197
Cdd:cd14047   162 GLVTSLKNDGK-RTKSKGTLSYMSPEQISSQD-YGKEVDIYALGLILFELLH 211
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
1-198 6.55e-22

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 97.12  E-value: 6.55e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915    1 MEKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIK----RFLETEDdpviKKIALREIRMLKQLKHPNLVNLLEVFRRK--R 74
Cdd:PTZ00266    12 LNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKaisyRGLKERE----KSQLVIEVNVMRELKHKNIVRYIDRFLNKanQ 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   75 RLHLVFEYCDHTVL----HELDRYQRGVPEPLVKNITWQTLQAVNFCHK-------HNCIHRDVKPENIL---------- 133
Cdd:PTZ00266    88 KLYILMEFCDAGDLsrniQKCYKMFGKIEEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFlstgirhigk 167
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039741915  134 ITKQS-------AIKLCDFGFARLLtGPGDYYTDYVATRWYRSPELLVGDTQ-YGPPVDVWAIGCVFAELLSG 198
Cdd:PTZ00266   168 ITAQAnnlngrpIAKIGDFGLSKNI-GIESMAHSCVGTPYYWSPELLLHETKsYDDKSDMWALGCIIYELCSG 239
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
2-196 7.63e-22

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 93.50  E-value: 7.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYekigkIGEGSYGVVFKCRNRDTGQIVAIKRFLeTEDDPVIKkIALREIRMLKQLK-HPNLVNLLE--VFRRKRRLHL 78
Cdd:cd14037     8 EKY-----LAEGGFAHVYLVKTSNGGNRAALKRVY-VNDEHDLN-VCKREIEIMKRLSgHKNIVGYIDssANRSGNGVYE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VF---EYCDHTVLHEL--DRYQRGVPEPLVKNITWQTLQAVNFCH--KHNCIHRDVKPENILITKQSAIKLCDFGFA-RL 150
Cdd:cd14037    81 VLllmEYCKGGGVIDLmnQRLQTGLTESEILKIFCDVCEAVAAMHylKPPLIHRDLKVENVLISDSGNYKLCDFGSAtTK 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039741915 151 LTGPGDYYT-DYVA-------TRWYRSPELLvgDTQYGPPV----DVWAIGCVFAELL 196
Cdd:cd14037   161 ILPPQTKQGvTYVEedikkytTLQYRAPEMI--DLYRGKPIteksDIWALGCLLYKLC 216
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
3-312 9.62e-22

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 93.39  E-value: 9.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKialREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd14104     1 KYMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGADQVLVK---KEISILNIARHRNILRLHESFESHEELVMIFEF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHE-LDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILIT--KQSAIKLCDFGFARLLTgPGDYYT 159
Cdd:cd14104    78 ISGVDIFErITTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCtrRGSYIKIIEFGQSRQLK-PGDKFR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 160 DYVATRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLylirktlgdliprhQQVFSMNQYFsgvk 239
Cdd:cd14104   157 LQYTSAEFYAPEVHQHES-VSTATDMWSLGCLVYVLLSGINPFEAETNQQTI--------------ENIRNAEYAF---- 217
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 240 ipDPEdmetlelKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYfdsirevgeLTRQHDKPARKTLRQSR 312
Cdd:cd14104   218 --DDE-------AFKNISIEALDFVDRLLVKERKSRMTAQEALNHPW---------LKQGMETVSSKDIKTTR 272
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
1-290 1.10e-21

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 94.56  E-value: 1.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIKKIALREIRMLKQL----------KHPNLVNLLEVF 70
Cdd:cd05610     3 IEEFVIVKPISRGAFGKVYLGRKKNNSKLYAVK---------VVKKADMINKNMVHQVqaerdalalsKSPFIVHLYYSL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  71 RRKRRLHLVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFAR- 149
Cdd:cd05610    74 QSANNVYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKv 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 150 ----------LLTGPG------DYY------------------TDY------------------VATRWYRSPELLVGDT 177
Cdd:cd05610   154 tlnrelnmmdILTTPSmakpknDYSrtpgqvlslisslgfntpTPYrtpksvrrgaarvegeriLGTPDYLAPELLLGKP 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 178 qYGPPVDVWAIGCVFAELLSGVPlwpgksdvdqlylirkTLGDLIPrhQQVFsmnQYFSGVKIPDPEDMETLELKfpniS 257
Cdd:cd05610   234 -HGPAVDWWALGVCLFEFLTGIP----------------PFNDETP--QQVF---QNILNRDIPWPEGEEELSVN----A 287
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1039741915 258 YSALGFLkgcLHMDPAERLTCEQLLQHPYFDSI 290
Cdd:cd05610   288 QNAIEIL---LTMDPTKRAGLKELKQHPLFHGV 317
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
2-283 1.38e-21

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 93.25  E-value: 1.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFK-----CRNRDTGQI-VAIKRFLETEDDPVIKKIaLREIRMLKQL-KHPNLVNLLEVFRRKR 74
Cdd:cd05053    12 DRLTLGKPLGEGAFGQVVKaeavgLDNKPNEVVtVAVKMLKDDATEKDLSDL-VSEMEMMKMIgKHKNIINLLGACTQDG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  75 RLHLVFEYCDHTVLHELDRYQRGVPE--------PLVKNIT--------WQTLQAVNFCHKHNCIHRDVKPENILITKQS 138
Cdd:cd05053    91 PLYVVVEYASKGNLREFLRARRPPGEeaspddprVPEEQLTqkdlvsfaYQVARGMEYLASKKCIHRDLAARNVLVTEDN 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 139 AIKLCDFGFARLLTGPgDYY---TD-YVATRWYrSPELLVgDTQYGPPVDVWAIGCVFAEL--LSGVPlWPGksdvdqly 212
Cdd:cd05053   171 VMKIADFGLARDIHHI-DYYrktTNgRLPVKWM-APEALF-DRVYTHQSDVWSFGVLLWEIftLGGSP-YPG-------- 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 213 lirktlgdlIPrhqqvfsMNQYFSGVKipDPEDMEtlelKFPNISYSALGFLKGCLHMDPAERLTCEQLLQ 283
Cdd:cd05053   239 ---------IP-------VEELFKLLK--EGHRME----KPQNCTQELYMLMRDCWHEVPSQRPTFKQLVE 287
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
9-287 1.40e-21

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 92.72  E-value: 1.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYG-VVFKCR--NRDtgqiVAIKRFLeteddPVIKKIALREIRMLKQL-KHPNLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:cd13982     8 VLGYGSEGtIVFRGTfdGRP----VAVKRLL-----PEFFDFADREVQLLRESdEHPNVIRYFCTEKDRQFLYIALELCA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVLHELDRYQRG----VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA-----IKLCDFGFARLLTGpG 155
Cdd:cd13982    79 ASLQDLVESPRESklflRPGLEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILISTPNAhgnvrAMISDFGLCKKLDV-G 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 156 DY---YTDYVA-TRWYRSPELLVGDTQYGP--PVDVWAIGCVFAELLSGvplwpGKsdvdqlylirKTLGDLIPRHQQVF 229
Cdd:cd13982   158 RSsfsRRSGVAgTSGWIAPEMLSGSTKRRQtrAVDIFSLGCVFYYVLSG-----GS----------HPFGDKLEREANIL 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 230 S-----MNQYFSGVKIPDPEDMetlelkfpnisysalgfLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd13982   223 KgkyslDKLLSLGEHGPEAQDL-----------------IERMIDFDPEKRPSAEEVLNHPFF 268
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
2-200 1.67e-21

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 93.45  E-value: 1.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEddpVIKKIALREIR----MLKQLKHPNLVNLLEVFRRKRRLH 77
Cdd:cd05599     1 EDFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSE---MLEKEQVAHVRaerdILAEADNPWVVKLYYSFQDEENLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  78 LVFEYC---DHTVLheLDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGfarLLTGP 154
Cdd:cd05599    78 LIMEFLpggDMMTL--LMKKDT-LTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFG---LCTGL 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1039741915 155 GDYYTDY--VATRWYRSPELLvGDTQYGPPVDVWAIGCVFAELLSGVP 200
Cdd:cd05599   152 KKSHLAYstVGTPDYIAPEVF-LQKGYGKECDWWSLGVIMYEMLIGYP 198
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
6-293 1.78e-21

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 93.13  E-value: 1.78e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   6 KIGKIGEGSyGVVFKCRNRDTGQIVAIKRF-LETEDDPVIKKIaLREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:cd08216     5 EIGKCFKGG-GVVHLAKHKPTNTLVAVKKInLESDSKEDLKFL-QQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPLMA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVLHELDR--YQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPG------- 155
Cdd:cd08216    83 YGSCRDLLKthFPEGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSMVKHGkrqrvvh 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 156 DYYTDYVATRWYRSPELLVGDTQ-YGPPVDVWAIGCVFAELLSGVPlwPGKSDVDQLYLIRKTLGDLiprhQQVFSMNQY 234
Cdd:cd08216   163 DFPKSSEKNLPWLSPEVLQQNLLgYNEKSDIYSVGITACELANGVV--PFSDMPATQMLLEKVRGTT----PQLLDCSTY 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039741915 235 fsgvkiPDPED----METLELKFPNIS--YSALG----------FLKGCLHMDPAERLTCEQLLQHPYFDSIREV 293
Cdd:cd08216   237 ------PLEEDsmsqSEDSSTEHPNNRdtRDIPYqrtfseafhqFVELCLQRDPELRPSASQLLAHSFFKQCRRS 305
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
1-287 1.84e-21

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 92.23  E-value: 1.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEKIgKIGEGSYGVVFKCRNRDTGqivaiKRFLEteddpviKKIALR-----EIrMLKQL--KHPNLVNLLEVFRRK 73
Cdd:PHA03390   16 CEIVKKL-KLIDGKFGKVSVLKHKPTQ-----KLFVQ-------KIIKAKnfnaiEP-MVHQLmkDNPNFIKLYYSVTTL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  74 RRLHLVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILIT-KQSAIKLCDFGFARLLT 152
Cdd:PHA03390   82 KGHVLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDrAKDRIYLCDYGLCKIIG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 153 GPGDYytDyvATRWYRSPELLVGDtQYGPPVDVWAIGCVFAELLSGVplWPGKSDVDQlYLirkTLGDLIPRHQQvfsmn 232
Cdd:PHA03390  162 TPSCY--D--GTLDYFSPEKIKGH-NYDVSFDWWAVGVLTYELLTGK--HPFKEDEDE-EL---DLESLLKRQQK----- 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 233 qyfsgvKIPdpedmetlelKFPNISYSALGFLKGCLHMDPAERL-TCEQLLQHPYF 287
Cdd:PHA03390  226 ------KLP----------FIKNVSKNANDFVQSMLKYNINYRLtNYNEIIKHPFL 265
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
4-208 1.88e-21

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 95.25  E-value: 1.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRnrDT--GQIVAIKRfLETE--DDPV-IKKIaLREIRMLKQLKHPNLVNLLEVFRRKRRLHL 78
Cdd:NF033483    9 YEIGERIGRGGMAEVYLAK--DTrlDRDVAVKV-LRPDlaRDPEfVARF-RREAQSAASLSHPNIVSVYDVGEDGGIPYI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYY 158
Cdd:NF033483   85 VMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARALSSTTMTQ 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039741915 159 TDYV-ATRWYRSPELLVG---DTQygppVDVWAIGCVFAELLSGVPLWPGKSDV 208
Cdd:NF033483  165 TNSVlGTVHYLSPEQARGgtvDAR----SDIYSLGIVLYEMLTGRPPFDGDSPV 214
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
10-230 1.90e-21

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 92.66  E-value: 1.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFleteDDPVIKK-----IALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:cd05607    10 LGKGGFGEVCAVQVKNTGQMYACKKL----DKKRLKKksgekMALLEKEILEKVNSPFIVSLAYAFETKTHLCLVMSLMN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVL--HELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGpGDYYTDYV 162
Cdd:cd05607    86 GGDLkyHIYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKE-GKPITQRA 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 163 ATRWYRSPELLVgDTQYGPPVDVWAIGCVFAELLSG-VPLWPGKSDVDQLYLIRKTLGDLIPRHQQVFS 230
Cdd:cd05607   165 GTNGYMAPEILK-EESYSYPVDWFAMGCSIYEMVAGrTPFRDHKEKVSKEELKRRTLEDEVKFEHQNFT 232
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
3-286 1.92e-21

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 92.14  E-value: 1.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFletEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd14662     1 RYELVKDIGSGNFGVARLMRNKETKELVAVKYI---ERGLKIDENVQREIINHRSLRHPNIIRFKEVVLTPTHLAIVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA--IKLCDFGFAR---LLTGPgdy 157
Cdd:cd14662    78 AAGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAprLKICDFGYSKssvLHSQP--- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 158 yTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVplWPGKsDVDQLYLIRKTLgdliprhQQVFSMnQYfsg 237
Cdd:cd14662   155 -KSTVGTPAYIAPEVLSRKEYDGKVADVWSCGVTLYVMLVGA--YPFE-DPDDPKNFRKTI-------QRIMSV-QY--- 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1039741915 238 vKIPDpedmetlelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14662   220 -KIPD----------YVRVSQDCRHLLSRIFVANPAKRITIPEIKNHPW 257
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
9-202 3.29e-21

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 91.95  E-value: 3.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVAIKRfLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLH------LVFEY 82
Cdd:cd14038     1 RLGTGGFGNVLRWINQETGEQVAIKQ-CRQELSPKNRERWCLEIQIMKRLNHPNVVAARDVPEGLQKLApndlplLAMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHE-LDRYQR--GVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITK--QSAI-KLCDFGFARLLTgPGD 156
Cdd:cd14038    80 CQGGDLRKyLNQFENccGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQgeQRLIhKIIDLGYAKELD-QGS 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039741915 157 YYTDYVATRWYRSPELLvGDTQYGPPVDVWAIGCVFAELLSG----VPLW 202
Cdd:cd14038   159 LCTSFVGTLQYLAPELL-EQQKYTVTVDYWSFGTLAFECITGfrpfLPNW 207
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
10-203 4.93e-21

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 91.36  E-value: 4.93e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRF-LETEDDPVIKKIALREIRMLKQLKHPNLVNL------LEVFRRKRRLHLVFEY 82
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTGEYVAIKKCrQELSPSDKNRERWCLEVQIMKKLNHPNVVSArdvppeLEKLSPNDLPLLAMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVL-HELDRYQR--GVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITK---QSAIKLCDFGFARLLTgPGD 156
Cdd:cd13989    81 CSGGDLrKVLNQPENccGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQgggRVIYKLIDLGYAKELD-QGS 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 157 YYTDYVATRWYRSPELLVGDtQYGPPVDVWAIGCVFAELLSGV----PLWP 203
Cdd:cd13989   160 LCTSFVGTLQYLAPELFESK-KYTCTVDYWSFGTLAFECITGYrpflPNWQ 209
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
1-289 5.01e-21

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 91.15  E-value: 5.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETE-DDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLV 79
Cdd:cd14187     6 RRRYVRGRFLGKGGFAKCYEITDADTKEVFAGKIVPKSLlLKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  80 FEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYT 159
Cdd:cd14187    86 LELCRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDGERKK 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 160 DYVATRWYRSPELLvGDTQYGPPVDVWAIGCVFAELLSGVPLWPgKSDVDQLYLIRKTLGDLIPRHqqvfsmnqyfsgvk 239
Cdd:cd14187   166 TLCGTPNYIAPEVL-SKKGHSFEVDIWSIGCIMYTLLVGKPPFE-TSCLKETYLRIKKNEYSIPKH-------------- 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039741915 240 ipdpedmetlelkfpnISYSALGFLKGCLHMDPAERLTCEQLLQHPYFDS 289
Cdd:cd14187   230 ----------------INPVAASLIQKMLQTDPTARPTINELLNDEFFTS 263
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
10-286 6.41e-21

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 90.41  E-value: 6.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIK-----RFLETEDDPVIKKIALrEIRMLKQLKH--PNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd14100     8 LGSGGFGSVYSGIRVADGAPVAIKhvekdRVSEWGELPNGTRVPM-EIVLLKKVGSgfRGVIRLLDWFERPDSFVLVLER 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDhtVLHELDRY--QRG-VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILIT-KQSAIKLCDFGFARLLTgpGDYY 158
Cdd:cd14100    87 PE--PVQDLFDFitERGaLPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGELKLIDFGSGALLK--DTVY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 TDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGvplwpgksdvdqlylirktlgdliprhqqvfsmnqyfsgv 238
Cdd:cd14100   163 TDFDGTRVYSPPEWIRFHRYHGRSAAVWSLGILLYDMVCG---------------------------------------- 202
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 239 KIPDPEDMETLELKF---PNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14100   203 DIPFEHDEEIIRGQVffrQRVSSECQHLIKWCLALRPSDRPSFEDIQNHPW 253
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
1-290 9.46e-21

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 91.68  E-value: 9.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrFLETEDDPVIKKIA--LREIRMLKQLKHPNLVNLLEVFRRKRRLHL 78
Cdd:cd05593    14 MNDFDYLKLLGKGTFGKVILVREKASGKYYAMK-ILKKEVIIAKDEVAhtLTESRVLKNTRHPFLTSLKYSFQTKDRLCF 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYY 158
Cdd:cd05593    93 VMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATM 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 TDYVATRWYRSPELLvGDTQYGPPVDVWAIGCVFAELLSG-VPLWPGKsdvdqlylirktlgdliprHQQVFSMnqyfsg 237
Cdd:cd05593   173 KTFCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGrLPFYNQD-------------------HEKLFEL------ 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 238 vkipdpedMETLELKFP-NISYSALGFLKGCLHMDPAERL-----TCEQLLQHPYFDSI 290
Cdd:cd05593   227 --------ILMEDIKFPrTLSADAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFTGV 277
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
5-287 1.01e-20

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 90.50  E-value: 1.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   5 EKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIaLREIRMLKQLKH-PNLVnllevfrrkRRLHLVFEYC 83
Cdd:cd06616     9 KDLGEIGRGAFGTVNKMLHKPSGTIMAVKRIRSTVDEKEQKRL-LMDLDVVMRSSDcPYIV---------KFYGALFREG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 DHTVLHEL-------------DRYQRGVPEPLVKNITWQTLQAVNFCHK-HNCIHRDVKPENILITKQSAIKLCDFGFAr 149
Cdd:cd06616    79 DCWICMELmdisldkfykyvyEVLDSVIPEEILGKIAVATVKALNYLKEeLKIIHRDVKPSNILLDRNGNIKLCDFGIS- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 150 lltgpgDYYTDYVAT------RWYRSPELLVGDTQ---YGPPVDVWAIGCVFAELLSGVPLWPG-KSDVDQLylirktlg 219
Cdd:cd06616   158 ------GQLVDSIAKtrdagcRPYMAPERIDPSASrdgYDVRSDVWSLGITLYEVATGKFPYPKwNSVFDQL-------- 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039741915 220 dliprhQQVfsmnqyfsgVKIPDPEDMETLELKFpniSYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd06616   224 ------TQV---------VKGDPPILSNSEEREF---SPSFVNFVNLCLIKDESKRPKYKELLKHPFI 273
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
9-195 1.09e-20

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 90.48  E-value: 1.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVAIKRfLETED--DPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHT 86
Cdd:cd08229    31 KIGRGQFSEVYRATCLLDGVPVALKK-VQIFDlmDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAG 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  87 VLHELDRY----QRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYV 162
Cdd:cd08229   110 DLSRMIKHfkkqKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLV 189
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1039741915 163 ATRWYRSPElLVGDTQYGPPVDVWAIGCVFAEL 195
Cdd:cd08229   190 GTPYYMSPE-RIHENGYNFKSDIWSLGCLLYEM 221
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
10-309 1.50e-20

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 90.93  E-value: 1.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCR---NRDTGQIVAIKrfleteddpVIKKIAL-----------REIRMLKQLKHPNLVNLLEVFRRKRR 75
Cdd:cd05584     4 LGKGGYGKVFQVRkttGSDKGKIFAMK---------VLKKASIvrnqkdtahtkAERNILEAVKHPFIVDLHYAFQTGGK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  76 LHLVFEY-CDHTVLHELDRyqRGV-PEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTG 153
Cdd:cd05584    75 LYLILEYlSGGELFMHLER--EGIfMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKESIH 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 154 PGDYYTDYVATRWYRSPELLVgDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSdvdqlyliRKTLGDLIPRhqqvfsmnq 233
Cdd:cd05584   153 DGTVTHTFCGTIEYMAPEILT-RSGHGKAVDWWSLGALMYDMLTGAPPFTAEN--------RKKTIDKILK--------- 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 234 yfsgVKIPDPedmetlelkfPNISYSALGFLKGCLHMDPAERL-----TCEQLLQHPYFDSIREVGELTRQHDKPARKTL 308
Cdd:cd05584   215 ----GKLNLP----------PYLTNEARDLLKKLLKRNVSSRLgsgpgDAEEIKAHPFFRHINWDDLLAKKVEPPFKPLL 280

                  .
gi 1039741915 309 R 309
Cdd:cd05584   281 Q 281
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
4-287 1.57e-20

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 89.60  E-value: 1.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETE-DDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd14189     3 YCKGRLLGKGGFARCYEMTDLATNKTYAVKVIPHSRvAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYV 162
Cdd:cd14189    83 CSRKSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQRKKTIC 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 163 ATRWYRSPELLVgDTQYGPPVDVWAIGCVFAELLSGVPLWPgKSDVDQLYLIRKTLGDLIPrhqqvfsmnqyfsgvkipd 242
Cdd:cd14189   163 GTPNYLAPEVLL-RQGHGPESDVWSLGCVMYTLLCGNPPFE-TLDLKETYRCIKQVKYTLP------------------- 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1039741915 243 pedmetlelkfPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14189   222 -----------ASLSLPARHLLAGILKRNPGDRLTLDQILEHEFF 255
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
1-290 2.03e-20

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 90.86  E-value: 2.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrFLETEDDPVIKKIA--LREIRMLKQLKHPNLVNLLEVFRRKRRLHL 78
Cdd:cd05594    24 MNDFEYLKLLGKGTFGKVILVKEKATGRYYAMK-ILKKEVIVAKDEVAhtLTENRVLQNSRHPFLTALKYSFQTHDRLCF 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCH-KHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDY 157
Cdd:cd05594   103 VMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGAT 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 158 YTDYVATRWYRSPELLvGDTQYGPPVDVWAIGCVFAELLSG-VPLWPGKsdvdqlylirktlgdliprHQQVFSMNQyfs 236
Cdd:cd05594   183 MKTFCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGrLPFYNQD-------------------HEKLFELIL--- 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 237 gvkipdpedMEtlELKFP-NISYSALGFLKGCLHMDPAERL-----TCEQLLQHPYFDSI 290
Cdd:cd05594   240 ---------ME--EIRFPrTLSPEAKSLLSGLLKKDPKQRLgggpdDAKEIMQHKFFAGI 288
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
10-290 2.86e-20

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 89.56  E-value: 2.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLETEddpvIKK-----IALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:cd05608     9 LGKGGFGEVSACQMRATGKLYACKKLNKKR----LKKrkgyeGAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTIMN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVL----HELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTD 160
Cdd:cd05608    85 GGDLryhiYNVDEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQTKTKG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 YVATRWYRSPELLVGDtQYGPPVDVWAIGCVFAELLSGV-PLWPGKSDVDQLYLIRKTLGDLIprhqqvfsmnqyfsgvk 239
Cdd:cd05608   165 YAGTPGFMAPELLLGE-EYDYSVDYFTLGVTLYEMIAARgPFRARGEKVENKELKQRILNDSV----------------- 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 240 ipdpedmeTLELKFpniSYSALGFLKGCLHMDPAERL-----TCEQLLQHPYFDSI 290
Cdd:cd05608   227 --------TYSEKF---SPASKSICEALLAKDPEKRLgfrdgNCDGLRTHPFFRDI 271
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
9-207 4.52e-20

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 87.88  E-value: 4.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVAIKRFLETeDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVL 88
Cdd:cd05041     2 KIGRGNFGDVYRGVLKPDNTEVAVKTCRET-LPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  89 heLDRYQRGVPEPLVKNITWQTLQAVN---FCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGpGDYY----TDY 161
Cdd:cd05041    81 --LTFLRKKGARLTVKQLLQMCLDAAAgmeYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREEED-GEYTvsdgLKQ 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1039741915 162 VATRWyRSPE-LLVGdtQYGPPVDVWAIGCVFAELLS-GVPLWPGKSD 207
Cdd:cd05041   158 IPIKW-TAPEaLNYG--RYTSESDVWSFGILLWEIFSlGATPYPGMSN 202
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
2-287 5.77e-20

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 87.95  E-value: 5.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEkIGK--IGEGSYGVVFKCRNRDTG-----QIVAIKRFLeteddpvikkiaLREIRMLKQLKHPNLVNLLEVFRRKR 74
Cdd:cd14109     3 ELYE-IGEedEKRAAQGAPFHVTERSTGrnflaQLRYGDPFL------------MREVDIHNSLDHPNIVQMHDAYDDEK 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  75 RLHLVFEYCDHTVLHELDRYQRG---VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILItKQSAIKLCDFGFARLL 151
Cdd:cd14109    70 LAVTVIDNLASTIELVRDNLLPGkdyYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILL-QDDKLKLADFGQSRRL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 152 TgpgdyyTDYVATRWYRSPELLVGDTQYGPPV----DVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDLiprhqq 227
Cdd:cd14109   149 L------RGKLTTLIYGSPEFVSPEIVNSYPVtlatDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWSF------ 216
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 228 vfsmnqyfsgvkipdpeDMETLElkfpNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14109   217 -----------------DSSPLG----NISDDARDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
4-284 6.78e-20

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 88.12  E-value: 6.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVikKIALREIRMLKQLKHPNLVNLL-----EVFRRKRRLHL 78
Cdd:cd13986     2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILCHSKEDV--KEAMREIENYRLFNHPNILRLLdsqivKEAGGKKEVYL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDH-TVLHELDRYQRG---VPEPLVKNITWQTLQAVNFCHKHNCI---HRDVKPENILITKQSAIKLCDFGFAR-- 149
Cdd:cd13986    80 LLPYYKRgSLQDEIERRLVKgtfFPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLLSEDDEPILMDLGSMNpa 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 150 --LLTGPGDYYT--DYVATRW---YRSPELLVGDTQ--YGPPVDVWAIGCVFAELLSGVPlwPGKSDVDQlylirktlGD 220
Cdd:cd13986   160 riEIEGRREALAlqDWAAEHCtmpYRAPELFDVKSHctIDEKTDIWSLGCTLYALMYGES--PFERIFQK--------GD 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039741915 221 liPRHQQVFSMNqyfsgVKIPDPedmetlelkfPNISYSALGFLKGCLHMDPAERLTCEQLLQH 284
Cdd:cd13986   230 --SLALAVLSGN-----YSFPDN----------SRYSEELHQLVKSMLVVNPAERPSIDDLLSR 276
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
6-287 1.20e-19

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 86.97  E-value: 1.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   6 KIGK-IGEGSYGVVFKCRNRDTGQIVAIKrFLETEDDP--VIKKIALREIRMLKQLKHPNLVNLLEVFRRKR-RLHLVFE 81
Cdd:cd14163     3 QLGKtIGEGTYSKVKEAFSKKHQRKVAIK-IIDKSGGPeeFIQRFLPRELQIVERLDHKNIIHVYEMLESADgKIYLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSaIKLCDFGFARLL-TGPGDYYTD 160
Cdd:cd14163    82 LAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGFT-LKLTDFGFAKQLpKGGRELSQT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 YVATRWYRSPELLVG---DTQYGppvDVWAIGCVFAELL-SGVPLwpgkSDVDqlylirktlgdlIPR---HQQvfsmnq 233
Cdd:cd14163   161 FCGSTAYAAPEVLQGvphDSRKG---DIWSMGVVLYVMLcAQLPF----DDTD------------IPKmlcQQQ------ 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039741915 234 yfSGVKIPdpedmetlelKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14163   216 --KGVSLP----------GHLGVSRTCQDLLKRLLEPDMVLRPSIEEVSWHPWL 257
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
2-198 1.28e-19

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 88.90  E-value: 1.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEddpVIKK----IALREIRMLKQLKHPNLVNLLEVFRRKRRLH 77
Cdd:cd05621    52 EDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFE---MIKRsdsaFFWEERDIMAFANSPWVVQLFCAFQDDKYLY 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  78 LVFEYCDHTVLHEL-DRYQrgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGD 156
Cdd:cd05621   129 MVMEYMPGGDLVNLmSNYD--VPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMKMDETGM 206
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1039741915 157 YYTDY-VATRWYRSPELLV---GDTQYGPPVDVWAIGCVFAELLSG 198
Cdd:cd05621   207 VHCDTaVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLFEMLVG 252
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
4-309 1.32e-19

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 88.05  E-value: 1.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVF---KCRNRDTGQIVAIKrfleteddpVIKKIAL-----------REIRMLKQLKH-PNLVNLLE 68
Cdd:cd05614     2 FELLKVLGTGAYGKVFlvrKVSGHDANKLYAMK---------VLRKAALvqkaktvehtrTERNVLEHVRQsPFLVTLHY 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  69 VFRRKRRLHLVFEYCD----HTVLHELDRYQrgvpEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCD 144
Cdd:cd05614    73 AFQTDAKLHLILDYVSggelFTHLYQRDHFS----EDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTD 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 145 FGFAR-LLTGPGDYYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDvdqlyliRKTLGDLIP 223
Cdd:cd05614   149 FGLSKeFLTEEKERTYSFCGTIEYMAPEIIRGKSGHGKAVDWWSLGILMFELLTGASPFTLEGE-------KNTQSEVSR 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 224 RhqqVFSMNQYFSGVKIPDPEDMetlelkfpnisysalgfLKGCLHMDPAERL-----TCEQLLQHPYFDSIREVGELTR 298
Cdd:cd05614   222 R---ILKCDPPFPSFIGPVARDL-----------------LQKLLCKDPKKRLgagpqGAQEIKEHPFFKGLDWEALALR 281
                         330
                  ....*....|.
gi 1039741915 299 QHDKPARKTLR 309
Cdd:cd05614   282 KVNPPFRPSIR 292
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
9-287 1.35e-19

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 86.98  E-value: 1.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVAikrFLETEDDPVIKKIALR---EIRMLKQLKHPNLVNLLEVFRRKRRLH----LVFE 81
Cdd:cd14033     8 EIGRGSFKTVYRGLDTETTVEVA---WCELQTRKLSKGERQRfseEVEMLKGLQHPNIVRFYDSWKSTVRGHkciiLVTE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHN--CIHRDVKPENILITKQSA-IKLCDFGFARLLTGpgDYY 158
Cdd:cd14033    85 LMTSGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFITGPTGsVKIGDLGLATLKRA--SFA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 TDYVATRWYRSPELLvgDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYliRKTLGDLIPrhqqvfsmnQYFSGV 238
Cdd:cd14033   163 KSVIGTPEFMAPEMY--EEKYDEAVDVYAFGMCILEMATSEYPYSECQNAAQIY--RKVTSGIKP---------DSFYKV 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1039741915 239 KIPdpedmetlELKfpnisysalGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14033   230 KVP--------ELK---------EIIEGCIRTDKDERFTIQDLLEHRFF 261
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
10-198 1.43e-19

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 86.73  E-value: 1.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVF--KCRNRDTGQIVAIKRFLETEDDpvikkiALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTV 87
Cdd:cd05059    12 LGSGQFGVVHlgKWRGKIDVAIKMIKEGSMSEDD------FIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMANGC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  88 LHELDRYQRGV-PEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgpGDYYTDYVATRW 166
Cdd:cd05059    86 LLNYLRERRGKfQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVL--DDEYTSSVGTKF 163
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1039741915 167 ---YRSPELLVgDTQYGPPVDVWAIGCVFAELLSG 198
Cdd:cd05059   164 pvkWSPPEVFM-YSKFSSKSDVWSFGVLMWEVFSE 197
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
4-200 1.87e-19

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 87.76  E-value: 1.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrFLETEDdpVIKK------IALREIrmLKQLKHPNLVNLLEVFRRKRRLH 77
Cdd:cd05598     3 FEKIKTIGVGAFGEVSLVRKKDTNALYAMK-TLRKKD--VLKRnqvahvKAERDI--LAEADNEWVVKLYYSFQDKENLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  78 LVFEYCDHTVLHELdRYQRGV-PEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGfarLLTG--- 153
Cdd:cd05598    78 FVMDYIPGGDLMSL-LIKKGIfEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFG---LCTGfrw 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 154 --PGDYYTDY--VATRWYRSPELLVgDTQYGPPVDVWAIGCVFAELLSGVP 200
Cdd:cd05598   154 thDSKYYLAHslVGTPNYIAPEVLL-RTGYTQLCDWWSVGVILYEMLVGQP 203
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
2-284 1.99e-19

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 86.43  E-value: 1.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKC--RNRDTGQIVAIKRFLETEDDPVikkiALREIRMLKQLKHPNLVNLLEVFRRKRRLHLV 79
Cdd:cd14112     3 GRFSFGSEIFRGRFSVIVKAvdSTTETDAHCAVKIFEVSDEASE----AVREFESLRTLQHENVQRLIAAFKPSNFAYLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  80 FEYCDHTVLHELDrYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILIT--KQSAIKLCDFGFARLLTGPGDY 157
Cdd:cd14112    79 MEKLQEDVFTRFS-SNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQsvRSWQVKLVDFGRAQKVSKLGKV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 158 YTDyVATRWyRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPlwPGKSDVDQLYLIRKTLgdliprhqqvfsmnqyfSG 237
Cdd:cd14112   158 PVD-GDTDW-ASPEFHNPETPITVQSDIWGLGVLTFCLLSGFH--PFTSEYDDEEETKENV-----------------IF 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1039741915 238 VKIpDPedmetlELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQH 284
Cdd:cd14112   217 VKC-RP------NLIFVEATQEALRFATWALKKSPTRRMRTDEALEH 256
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
4-291 2.29e-19

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 87.29  E-value: 2.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIK-KIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd05574     3 FKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKvKRVLTEREILATLDHPFLPTLYASFQTSTHLCFVMDY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHELDRYQRG--VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFA------------ 148
Cdd:cd05574    83 CPGGELFRLLQKQPGkrLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSkqssvtpppvrk 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 149 ----------------RLLTGPGDYYT-DYVATRWYRSPELLVGDTQyGPPVDVWAIGCVFAELLSGVPLWPGKSdvdql 211
Cdd:cd05574   163 slrkgsrrssvksiekETFVAEPSARSnSFVGTEEYIAPEVIKGDGH-GSAVDWWTLGILLYEMLYGTTPFKGSN----- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 212 ylIRKTLGDLIPRhqqvfsmnqyfsgvkipdpedmetlELKFP---NISYSALGFLKGCLHMDPAERLTC----EQLLQH 284
Cdd:cd05574   237 --RDETFSNILKK-------------------------ELTFPespPVSSEAKDLIRKLLVKDPSKRLGSkrgaSEIKRH 289

                  ....*..
gi 1039741915 285 PYFDSIR 291
Cdd:cd05574   290 PFFRGVN 296
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
6-281 2.78e-19

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 86.67  E-value: 2.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   6 KIGKIGEGSYGVVFKCR---NRD-TGQIVAIKRfLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVF--RRKRRLHLV 79
Cdd:cd05038     8 FIKQLGEGHFGSVELCRydpLGDnTGEQVAVKS-LQPSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCesPGRRSLRLI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  80 FEYCDHTVL-HELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYY 158
Cdd:cd05038    87 MEYLPSGSLrDYLQRHRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKVLPEDKEYY 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 T----DYVATRWYrSPELLVGDTQYGPPvDVWAIGCVFAELLSgvplwPGKSDVDQLYLIRKTLGDLIPRHQQVFSMNQY 234
Cdd:cd05038   167 YvkepGESPIFWY-APECLRESRFSSAS-DVWSFGVTLYELFT-----YGDPSQSPPALFLRMIGIAQGQMIVTRLLELL 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1039741915 235 FSGVKIPDPEDMetlelkfPNISYSalgFLKGCLHMDPAERLTCEQL 281
Cdd:cd05038   240 KSGERLPRPPSC-------PDEVYD---LMKECWEYEPQDRPSFSDL 276
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
10-284 2.95e-19

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 85.62  E-value: 2.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIkkiaLREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLH 89
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGKVMVMKELKRFDEQRSF----LKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  90 E-LDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIK---LCDFGFARLL----TGPGDYYTDY 161
Cdd:cd14065    77 ElLKSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRnavVADFGLAREMpdekTKKPDRKKRL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 162 --VATRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLSGVPLWPgksdvdqlylirktlgDLIPRHQQvFSMN-QYFSGV 238
Cdd:cd14065   157 tvVGSPYWMAPEMLRGES-YDEKVDVFSFGIVLCEIIGRVPADP----------------DYLPRTMD-FGLDvRAFRTL 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1039741915 239 KIPDpedmetLELKFPNISYSalgflkgCLHMDPAERLTCEQLLQH 284
Cdd:cd14065   219 YVPD------CPPSFLPLAIR-------CCQLDPEKRPSFVELEHH 251
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
10-286 5.20e-19

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 85.35  E-value: 5.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKrfLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLH 89
Cdd:cd14193    12 LGGGRFGQVHKCEEKSSGLKLAAK--IIKARSQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGGELF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  90 E--LDRYQRGVPEPLVKNITwQTLQAVNFCHKHNCIHRDVKPENILITKQSA--IKLCDFGFARLLTgPGDYYTDYVATR 165
Cdd:cd14193    90 DriIDENYNLTELDTILFIK-QICEGIQYMHQMYILHLDLKPENILCVSREAnqVKIIDFGLARRYK-PREKLRVNFGTP 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 166 WYRSPELLVGDTqYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDLiprhqqvfsmnqyfsgvkipdpED 245
Cdd:cd14193   168 EFLAPEVVNYEF-VSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDF----------------------ED 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1039741915 246 MEtlelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14193   225 EE-----FADISEEAKDFISKLLIKEKSWRMSASEALKHPW 260
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
10-216 5.31e-19

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 85.50  E-value: 5.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCR-----NRDTGQIVAIKRfLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:cd05048    13 LGEGAFGKVYKGEllgpsSEESAISVAIKT-LKENASPKTQQDFRREAELMSDLQHPNIVCLLGVCTKEQPQCMLFEYMA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVLHEL------------DRYQRGVPEPLVK----NITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFA 148
Cdd:cd05048    92 HGDLHEFlvrhsphsdvgvSSDDDGTASSLDQsdflHIAIQIAAGMEYLSSHHYVHRDLAARNCLVGDGLTVKISDFGLS 171
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 149 RLLTGpGDYY----TDYVATRWYRSPELLVGdtQYGPPVDVWAIGCVFAELLS-GVPLWPGKSDVDQLYLIRK 216
Cdd:cd05048   172 RDIYS-SDYYrvqsKSLLPVRWMPPEAILYG--KFTTESDVWSFGVVLWEIFSyGLQPYYGYSNQEVIEMIRS 241
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
10-293 5.96e-19

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 85.86  E-value: 5.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFletEDDPVikkiALREIRM-LKQLKHPNLVNLLEVF----RRKRRLHLVFEYCD 84
Cdd:cd14170    10 LGLGINGKVLQIFNKRTQEKFALKML---QDCPK----ARREVELhWRASQCPHIVRIVDVYenlyAGRKCLLIVMECLD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVLHE--LDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQ---SAIKLCDFGFARLLTGPGDYYT 159
Cdd:cd14170    83 GGELFSriQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKrpnAILKLTDFGFAKETTSHNSLTT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 160 DyVATRWYRSPELLvGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVdqlylirktlgDLIPRHQQVFSMNQYfsgvK 239
Cdd:cd14170   163 P-CYTPYYVAPEVL-GPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGL-----------AISPGMKTRIRMGQY----E 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039741915 240 IPDPEdmetlelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYFDSIREV 293
Cdd:cd14170   226 FPNPE--------WSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQSTKV 271
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
10-286 6.18e-19

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 85.01  E-value: 6.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLE---TEDDPVIKKIALREIRMLKQLKHP--NLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:cd14102     8 LGSGGFGTVYAGSRIADGLPVAVKHVVKervTEWGTLNGVMVPLEIVLLKKVGSGfrGVIKLLDWYERPDGFLIVMERPE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 htVLHELDRY--QRG-VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILI-TKQSAIKLCDFGFARLLTgpGDYYTD 160
Cdd:cd14102    88 --PVKDLFDFitEKGaLDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVdLRTGELKLIDFGSGALLK--DTVYTD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 YVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGvplwpgksdvdqlylirktlgdliprhqqvfsmnqyfsgvKI 240
Cdd:cd14102   164 FDGTRVYSPPEWIRYHRYHGRSATVWSLGVLLYDMVCG----------------------------------------DI 203
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1039741915 241 PDPEDMETLELKF---PNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14102   204 PFEQDEEILRGRLyfrRRVSPECQQLIKWCLSLRPSDRPTLEQIFDHPW 252
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
10-214 6.30e-19

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 86.01  E-value: 6.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRF-----LETEDdpvikkIALREIRMLKQLKHPNLVNLLEVFRRKRRLH--LVFEY 82
Cdd:cd13988     1 LGQGATANVFRGRHKKTGDLYAVKVFnnlsfMRPLD------VQMREFEVLKKLNHKNIVKLFAIEEELTTRHkvLVMEL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CD----HTVLHE-LDRYqrGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILIT----KQSAIKLCDFGFARLLtG 153
Cdd:cd13988    75 CPcgslYTVLEEpSNAY--GLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRVigedGQSVYKLTDFGAAREL-E 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 154 PGDYYTDYVATRWYRSPEL-----LVGDTQ--YGPPVDVWAIGCVFAELLSG-VPLWP---GKSDVDQLYLI 214
Cdd:cd13988   152 DDEQFVSLYGTEEYLHPDMyeravLRKDHQkkYGATVDLWSIGVTFYHAATGsLPFRPfegPRRNKEVMYKI 223
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
10-291 7.25e-19

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 85.25  E-value: 7.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPviKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLH 89
Cdd:cd14154     1 LGKGFFGQAIKVTHRETGEVMVMKELIRFDEEA--QRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTLK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  90 ELdryQRGVPEPLvkniTWQtlQAVNFC----------HKHNCIHRDVKPENILITKQSAIKLCDFGFARLL-------- 151
Cdd:cd14154    79 DV---LKDMARPL----PWA--QRVRFAkdiasgmaylHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLIveerlpsg 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 152 ----------TGPGDYYTDY--VATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLWPgksdvdqlylirktlg 219
Cdd:cd14154   150 nmspsetlrhLKSPDRKKRYtvVGNPYWMAPEMLNG-RSYDEKVDIFSFGIVLCEIIGRVEADP---------------- 212
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 220 DLIPRHQQvFSMNQyfsgvkipdpedmETLELKF----PNiSYSALGFLkgCLHMDPAERLTCEQLlqHPYFDSIR 291
Cdd:cd14154   213 DYLPRTKD-FGLNV-------------DSFREKFcagcPP-PFFKLAFL--CCDLDPEKRPPFETL--EEWLEALY 269
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
3-192 7.28e-19

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 86.07  E-value: 7.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFleTEDDPVIKKIALREIRMLKQLK--HPNLVNLLE-------VFRR- 72
Cdd:cd13977     1 KYSLIREVGRGSYGVVYEAVVRRTGARVAVKKI--RCNAPENVELALREFWALSSIQrqHPNVIQLEEcvlqrdgLAQRm 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  73 -----KRRLHL-----------------------VFEYCDHTVLHELDRYQRgvPEPLVKNITWQTL-QAVNFCHKHNCI 123
Cdd:cd13977    79 shgssKSDLYLllvetslkgercfdprsacylwfVMEFCDGGDMNEYLLSRR--PDRQTNTSFMLQLsSALAFLHRNQIV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 124 HRDVKPENILITKQSA---IKLCDFGFARLLTGPGD-----------YYTDYVATRWYRSPELLVGdtQYGPPVDVWAIG 189
Cdd:cd13977   157 HRDLKPDNILISHKRGepiLKVADFGLSKVCSGSGLnpeepanvnkhFLSSACGSDFYMAPEVWEG--HYTAKADIFALG 234

                  ...
gi 1039741915 190 CVF 192
Cdd:cd13977   235 III 237
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
4-290 9.09e-19

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 85.05  E-value: 9.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVF---KCRNRDTGQIVAIKRFLETEddpVIKKIALRE-IRMLKQ-LKH----PNLVNLLEVFRRKR 74
Cdd:cd05613     2 FELLKVLGTGAYGKVFlvrKVSGHDAGKLYAMKVLKKAT---IVQKAKTAEhTRTERQvLEHirqsPFLVTLHYAFQTDT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  75 RLHLVFEYCD----HTVLHELDRYQrgvpEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFAR- 149
Cdd:cd05613    79 KLHLILDYINggelFTHLSQRERFT----ENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKe 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 150 LLTGPGDYYTDYVATRWYRSPELLV-GDTQYGPPVDVWAIGCVFAELLSGV-PLWPGKSDVDQLYLIRKTLGDliprhqq 227
Cdd:cd05613   155 FLLDENERAYSFCGTIEYMAPEIVRgGDSGHDKAVDWWSLGVLMYELLTGAsPFTVDGEKNSQAEISRRILKS------- 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039741915 228 vfsmnqyfsgvKIPDPEDMETLelkfpnisysALGFLKGCLHMDPAERLTC-----EQLLQHPYFDSI 290
Cdd:cd05613   228 -----------EPPYPQEMSAL----------AKDIIQRLLMKDPKKRLGCgpngaDEIKKHPFFQKI 274
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
10-198 1.51e-18

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 84.04  E-value: 1.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLH 89
Cdd:cd13978     1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  90 EL-DRYQRGVPEPLVKNITWQTLQAVNFCHKHN--CIHRDVKPENILITKQSAIKLCDFGFARL----------LTGPGD 156
Cdd:cd13978    81 SLlEREIQDVPWSLRFRIIHEIALGMNFLHNMDppLLHHDLKPENILLDNHFHVKISDFGLSKLgmksisanrrRGTENL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1039741915 157 YYTDYvatrwYRSPELLvGDTQYGPPV--DVWAIGCVFAELLSG 198
Cdd:cd13978   161 GGTPI-----YMAPEAF-DDFNKKPTSksDVYSFAIVIWAVLTR 198
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
2-198 1.58e-18

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 85.83  E-value: 1.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEddpVIKK----IALREIRMLKQLKHPNLVNLLEVFRRKRRLH 77
Cdd:cd05622    73 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFE---MIKRsdsaFFWEERDIMAFANSPWVVQLFYAFQDDRYLY 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  78 LVFEYC-DHTVLHELDRYQrgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGD 156
Cdd:cd05622   150 MVMEYMpGGDLVNLMSNYD--VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGM 227
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1039741915 157 YYTDY-VATRWYRSPELLV---GDTQYGPPVDVWAIGCVFAELLSG 198
Cdd:cd05622   228 VRCDTaVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVG 273
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
10-198 1.76e-18

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 84.20  E-value: 1.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRfLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRL-----HLVFEYCD 84
Cdd:cd14039     1 LGTGGFGNVCLYQNQETGEKIAIKS-CRLELSVKNKDRWCHEIQIMKKLNHPNVVKACDVPEEMNFLvndvpLLAMEYCS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVLHELDRYQR---GVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAI---KLCDFGFARLLTgPGDYY 158
Cdd:cd14039    80 GGDLRKLLNKPEnccGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKivhKIIDLGYAKDLD-QGSLC 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1039741915 159 TDYVATRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLSG 198
Cdd:cd14039   159 TSFVGTLQYLAPELFENKS-YTVTVDYWSFGTMVFECIAG 197
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
10-286 1.90e-18

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 84.31  E-value: 1.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIKKIA-------LREIRMLKQLK-HPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd14174    10 LGEGAYAKVQGCVSLQNGKEYAVK---------IIEKNAghsrsrvFREVETLYQCQgNKNILELIEFFEDDTRFYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YC-DHTVLHELDRyQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILIT---KQSAIKLCDFGFAR-------- 149
Cdd:cd14174    81 KLrGGSILAHIQK-RKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCEspdKVSPVKICDFDLGSgvklnsac 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 150 -LLTGPgdYYTDYVATRWYRSPELLVGDTQ----YGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLY----LIRKTLGD 220
Cdd:cd14174   160 tPITTP--ELTTPCGSAEYMAPEVVEVFTDeatfYDKRCDLWSLGVILYIMLSGYPPFVGHCGTDCGWdrgeVCRVCQNK 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 221 LIPRHQQvfsmNQYfsgvKIPDPEdmetlelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14174   238 LFESIQE----GKY----EFPDKD--------WSHISSEAKDLISKLLVRDAKERLSAAQVLQHPW 287
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
9-215 2.01e-18

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 84.30  E-value: 2.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTG-----QIVAIKRFLETEDDPVIKKIAlREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYC 83
Cdd:cd05091    13 ELGEDRFGKVYKGHLFGTApgeqtQAVAIKTLKDKAEGPLREEFR-HEAMLRSRLQHPNIVCLLGVVTKEQPMSMIFSYC 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 DHTVLHEL---------------DRYQRGVPEPL-VKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGF 147
Cdd:cd05091    92 SHGDLHEFlvmrsphsdvgstddDKTVKSTLEPAdFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVFDKLNVKISDLGL 171
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 148 ARLLTGpGDYY----TDYVATRWYRSPELLVGdtQYGPPVDVWAIGCVFAELLS-GVPLWPGKSDVDQLYLIR 215
Cdd:cd05091   172 FREVYA-ADYYklmgNSLLPIRWMSPEAIMYG--KFSIDSDIWSYGVVLWEVFSyGLQPYCGYSNQDVIEMIR 241
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
7-283 2.45e-18

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 84.25  E-value: 2.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   7 IGK-IGEGSYGVVFKCR-------NRDTGQIVAIKRFletEDDPVIKKIA--LREIRMLKQL-KHPNLVNLLEVFRRKRR 75
Cdd:cd05099    16 LGKpLGEGCFGQVVRAEaygidksRPDQTVTVAVKML---KDNATDKDLAdlISEMELMKLIgKHKNIINLLGVCTQEGP 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  76 LHLVFEYCDHTVLHELDRYQR-----------GVPE-----PLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA 139
Cdd:cd05099    93 LYVIVEYAAKGNLREFLRARRppgpdytfditKVPEeqlsfKDLVSCAYQVARGMEYLESRRCIHRDLAARNVLVTEDNV 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 140 IKLCDFGFARlltgpGDYYTDY--------VATRWYrSPELLVgDTQYGPPVDVWAIGCVFAEL--LSGVPlWPGksdvd 209
Cdd:cd05099   173 MKIADFGLAR-----GVHDIDYykktsngrLPVKWM-APEALF-DRVYTHQSDVWSFGILMWEIftLGGSP-YPG----- 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039741915 210 qlylirktlgdlIPrHQQVFSMNQyfSGVKIPDPedmetlelkfPNISYSALGFLKGCLHMDPAERLTCEQLLQ 283
Cdd:cd05099   240 ------------IP-VEELFKLLR--EGHRMDKP----------SNCTHELYMLMRECWHAVPTQRPTFKQLVE 288
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
9-212 3.13e-18

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 83.24  E-value: 3.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVAIKRFLEtedDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDH-TV 87
Cdd:cd05052    13 KLGGGQYGEVYEGVWKKYNLTVAVKTLKE---DTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYgNL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  88 LHELDRYQRGVPEPLV-KNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgpGDYYTDYVATRW 166
Cdd:cd05052    90 LDYLRECNREELNAVVlLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMT--GDTYTAHAGAKF 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039741915 167 ---YRSPELLVGDTqYGPPVDVWAIGCVFAELLS-GVPLWPGkSDVDQLY 212
Cdd:cd05052   168 pikWTAPESLAYNK-FSIKSDVWAFGVLLWEIATyGMSPYPG-IDLSQVY 215
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
8-197 5.75e-18

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 82.32  E-value: 5.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   8 GKIGEGSYGVVFK--CRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRrLHLVFEYCDH 85
Cdd:cd05116     1 GELGSGNFGTVKKgyYQMKKVVKTVAVKILKNEANDPALKDELLREANVMQQLDNPYIVRMIGICEAES-WMLVMEMAEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 TVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYVATR 165
Cdd:cd05116    80 GPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENYYKAQTHGK 159
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1039741915 166 W---YRSPELLvGDTQYGPPVDVWAIGCVFAELLS 197
Cdd:cd05116   160 WpvkWYAPECM-NYYKFSSKSDVWSFGVLMWEAFS 193
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
10-217 6.25e-18

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 82.31  E-value: 6.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDpvIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLh 89
Cdd:cd14221     1 LGKGCFGQAIKVTHRETGEVMVMKELIRFDEE--TQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTL- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  90 eldryqRGVPEPLVKNITWQtlQAVNFC----------HKHNCIHRDVKPENILITKQSAIKLCDFGFARLL----TGPG 155
Cdd:cd14221    78 ------RGIIKSMDSHYPWS--QRVSFAkdiasgmaylHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMvdekTQPE 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 156 DYYTDYVATR----------WYRSPELLVGDTqYGPPVDVWAIGCVFAELLsgvplwpGKSDVDQLYLIRKT 217
Cdd:cd14221   150 GLRSLKKPDRkkrytvvgnpYWMAPEMINGRS-YDEKVDVFSFGIVLCEII-------GRVNADPDYLPRTM 213
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
3-197 8.08e-18

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 82.25  E-value: 8.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYekIGKIGEGSYGVVFKCR----NRDTGQIVAIKRFleTEDDPVIKKIALREIRMLKQLKHPNLVNLLEVF--RRKRRL 76
Cdd:cd05081     7 KY--ISQLGKGNFGSVELCRydplGDNTGALVAVKQL--QHSGPDQQRDFQREIQILKALHSDFIVKYRGVSygPGRRSL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  77 HLVFEYCDHTVLHE-LDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPG 155
Cdd:cd05081    83 RLVMEYLPSGCLRDfLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLPLDK 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1039741915 156 DYYT----DYVATRWYrSPELLvGDTQYGPPVDVWAIGCVFAELLS 197
Cdd:cd05081   163 DYYVvrepGQSPIFWY-APESL-SDNIFSRQSDVWSFGVVLYELFT 206
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
10-290 1.28e-17

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 82.33  E-value: 1.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFleteDDPVIKK-----IALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:cd05632    10 LGKGGFGEVCACQVRATGKMYACKRL----EKKRIKKrkgesMALNEKQILEKVNSQFVVNLAYAYETKDALCLVLTIMN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVL--HELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFArLLTGPGDYYTDYV 162
Cdd:cd05632    86 GGDLkfHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLA-VKIPEGESIRGRV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 163 ATRWYRSPELLvGDTQYGPPVDVWAIGCVFAELLSG-VPLWPGKSDVDQLYLIRKTLgdliprhqqvfsmnqyfsgvkip 241
Cdd:cd05632   165 GTVGYMAPEVL-NNQRYTLSPDYWGLGCLIYEMIEGqSPFRGRKEKVKREEVDRRVL----------------------- 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039741915 242 dpEDMETLELKFpniSYSALGFLKGCLHMDPAERLTCE-----QLLQHPYFDSI 290
Cdd:cd05632   221 --ETEEVYSAKF---SEEAKSICKMLLTKDPKQRLGCQeegagEVKRHPFFRNM 269
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
9-197 1.32e-17

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 81.15  E-value: 1.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFK--CRNRDTGQIVAIKRFLETEDDpvikkiALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHT 86
Cdd:cd05112    11 EIGSGQFGLVHLgyWLNKDKVAIKTIREGAMSEED------FIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  87 VLHELDRYQRGV--PEPLVkNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgpGDYYTDYVAT 164
Cdd:cd05112    85 CLSDYLRTQRGLfsAETLL-GMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVL--DDQYTSSTGT 161
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1039741915 165 RW---YRSPElLVGDTQYGPPVDVWAIGCVFAELLS 197
Cdd:cd05112   162 KFpvkWSSPE-VFSFSRYSSKSDVWSFGVLMWEVFS 196
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
7-285 1.41e-17

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 81.68  E-value: 1.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   7 IGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQL-KHPNLVNLLEVFRRKRRLHLVFEYCDH 85
Cdd:cd14051     5 VEKIGSGEFGSVYKCINRLDGCVYAIKKSKKPVAGSVDEQNALNEVYAHAVLgKHPHVVRYYSAWAEDDHMIIQNEYCNG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 TVLHEL--DRYQRG--VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAI-KLC--DFGFARLLTGPGDYY 158
Cdd:cd14051    85 GSLADAisENEKAGerFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISRTPNPvSSEeeEEDFEGEEDNPESNE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 TDYV------ATRwYRSPELLVGDTQY------------GPPVDVWAIGCVFAELLSGVPLwpgKSDVDQLYLIRKtlGD 220
Cdd:cd14051   165 VTYKigdlghVTS-ISNPQVEEGDCRFlaneilqenyshLPKADIFALALTVYEAAGGGPL---PKNGDEWHEIRQ--GN 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039741915 221 LIPrhqqvfsmnqyfsgvkipdpedmetlelkFPNISYSALGFLKGCLHMDPAERLTCEQLLQHP 285
Cdd:cd14051   239 LPP-----------------------------LPQCSPEFNELLRSMIHPDPEKRPSAAALLQHP 274
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
9-197 1.45e-17

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 81.60  E-value: 1.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCR----NRDTGQIVAIKRFLETEDDPVikKIALREIRMLKQLKHPNLVNLLEVFRR--KRRLHLVFEY 82
Cdd:cd14205    11 QLGKGNFGSVEMCRydplQDNTGEVVAVKKLQHSTEEHL--RDFEREIEILKSLQHDNIVKYKGVCYSagRRNLRLIMEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHE-LDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYT-- 159
Cdd:cd14205    89 LPYGSLRDyLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKEYYKvk 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1039741915 160 --DYVATRWYrSPELLVgDTQYGPPVDVWAIGCVFAELLS 197
Cdd:cd14205   169 epGESPIFWY-APESLT-ESKFSVASDVWSFGVVLYELFT 206
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
10-290 1.50e-17

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 81.61  E-value: 1.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRfLETEDdpvIKK-----IALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:cd05630     8 LGKGGFGEVCACQVRATGKMYACKK-LEKKR---IKKrkgeaMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVL--HELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFArLLTGPGDYYTDYV 162
Cdd:cd05630    84 GGDLkfHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLA-VHVPEGQTIKGRV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 163 ATRWYRSPElLVGDTQYGPPVDVWAIGCVFAELLSG-VPLWPGKSDVDqlyliRKTLGDLIPRHQQVFSmnQYFSgvkiP 241
Cdd:cd05630   163 GTVGYMAPE-VVKNERYTFSPDWWALGCLLYEMIAGqSPFQQRKKKIK-----REEVERLVKEVPEEYS--EKFS----P 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039741915 242 DpedmetlelkfpnisysALGFLKGCLHMDPAERLTCE-----QLLQHPYFDSI 290
Cdd:cd05630   231 Q-----------------ARSLCSMLLCKDPAERLGCRgggarEVKEHPLFKKL 267
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
10-290 1.60e-17

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 81.63  E-value: 1.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRfLETEDdpvIKK-----IALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:cd05605     8 LGKGGFGEVCACQVRATGKMYACKK-LEKKR---IKKrkgeaMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTIMN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVL--HELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgPGDYYTDYV 162
Cdd:cd05605    84 GGDLkfHIYNMGNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIP-EGETIRGRV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 163 ATRWYRSPElLVGDTQYGPPVDVWAIGCVFAELLSGVPLW------PGKSDVDQLylirktlgdliprhqqvfsmnqyfs 236
Cdd:cd05605   163 GTVGYMAPE-VVKNERYTFSPDWWGLGCLIYEMIEGQAPFrarkekVKREEVDRR------------------------- 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 237 gVKipdpEDMETLELKFpniSYSALGFLKGCLHMDPAERLTC-----EQLLQHPYFDSI 290
Cdd:cd05605   217 -VK----EDQEEYSEKF---SEEAKSICSQLLQKDPKTRLGCrgegaEDVKSHPFFKSI 267
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
3-196 1.96e-17

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 81.40  E-value: 1.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFL--ETEDDPVIKkiALREIRMLKQLKHPNLVNLLEVFRR--KRRLHL 78
Cdd:cd14049     7 EFEEIARLGKGGYGKVYKVRNKLDGQYYAIKKILikKVTKRDCMK--VLREVKVLAGLQHPNIVGYHTAWMEhvQLMLYI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTVLHEL-DRYQRGVPEPLVKN------------ITWQTLQAVNFCHKHNCIHRDVKPENILITKQS-AIKLCD 144
Cdd:cd14049    85 QMQLCELSLWDWIvERNKRPCEEEFKSApytpvdvdvttkILQQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDiHVRIGD 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039741915 145 FGFA--RLLTGPGDY----------YTDYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELL 196
Cdd:cd14049   165 FGLAcpDILQDGNDSttmsrlngltHTSGVGTCLYAAPEQLEG-SHYDFKSDMYSIGVILLELF 227
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
1-189 2.81e-17

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 80.78  E-value: 2.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEKIGKIGEGSYGVVFKCRNRDTG-----QIVAIKRFLETEDDP--------------------VIKKIaLREIRML 55
Cdd:cd14199     1 LNQYKLKDEIGKGSYGVVKLAYNEDDNtyyamKVLSKKKLMRQAGFPrrppprgaraapegctqprgPIERV-YQEIAIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  56 KQLKHPNLVNLLEVFR--RKRRLHLVFEYCDHTVLHEldryqrgVP--EPLVKN---ITWQTL-QAVNFCHKHNCIHRDV 127
Cdd:cd14199    80 KKLDHPNVVKLVEVLDdpSEDHLYMVFELVKQGPVME-------VPtlKPLSEDqarFYFQDLiKGIEYLHYQKIIHRDV 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039741915 128 KPENILITKQSAIKLCDFGFARLLTGPGDYYTDYVATRWYRSPELLvGDTQ---YGPPVDVWAIG 189
Cdd:cd14199   153 KPSNLLVGEDGHIKIADFGVSNEFEGSDALLTNTVGTPAFMAPETL-SETRkifSGKALDVWAMG 216
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
3-244 4.10e-17

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 80.07  E-value: 4.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQL-KHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd14138     6 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHSHVVRYYSAWAEDDHMLIQNE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCD----HTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA------------------ 139
Cdd:cd14138    86 YCNggslADAISENYRIMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRTSIpnaaseegdedewasnkv 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 140 -IKLCDFGFARLLTGP----GDyyTDYVATrwyrspELLVGDTQYGPPVDVWAIGCVFAELLSGVPLwpgKSDVDQLYLI 214
Cdd:cd14138   166 iFKIGDLGHVTRVSSPqveeGD--SRFLAN------EVLQENYTHLPKADIFALALTVVCAAGAEPL---PTNGDQWHEI 234
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1039741915 215 RKtlgDLIPRHQQVFSmNQYFSGVKI---PDPE 244
Cdd:cd14138   235 RQ---GKLPRIPQVLS-QEFLDLLKVmihPDPE 263
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
3-196 4.38e-17

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 81.43  E-value: 4.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDtgqivaikrflETEDDPVIKKIAL------REIRMLKQLKHPNLVNLLEVFRRKRRL 76
Cdd:PHA03207   93 QYNILSSLTPGSEGEVFVCTKHG-----------DEQRKKVIVKAVTggktpgREIDILKTISHRAIINLIHAYRWKSTV 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  77 HLVFEYCDHTVLHELDRYQrgvPEPLVKNITWQT--LQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGP 154
Cdd:PHA03207  162 CMVMPKYKCDLFTYVDRSG---PLPLEQAITIQRrlLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAACKLDAH 238
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1039741915 155 GDYYTDY--VATRWYRSPELLVGDTqYGPPVDVWAIGCVFAELL 196
Cdd:PHA03207  239 PDTPQCYgwSGTLETNSPELLALDP-YCAKTDIWSAGLVLFEMS 281
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
4-293 4.64e-17

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 80.85  E-value: 4.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEddpVIKK---IALREIR-MLKQLKHPNLVNLLEVFRRKRRLHLV 79
Cdd:cd05597     3 FEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWE---MLKRaetACFREERdVLVNGDRRWITKLHYAFQDENYLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  80 FE-YCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFA-RLLTGPGDY 157
Cdd:cd05597    80 MDyYCGGDLLTLLSKFEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSClKLREDGTVQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 158 YTDYVATRWYRSPELLV----GDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDqlylirkTLGDlIPRHQQVFSmnq 233
Cdd:cd05597   160 SSVAVGTPDYISPEILQamedGKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVE-------TYGK-IMNHKEHFS--- 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039741915 234 yfsgvkIPDPEDmetlelkfpNISYSALGFLKGcLHMDPAERL---TCEQLLQHPYF-----DSIREV 293
Cdd:cd05597   229 ------FPDDED---------DVSEEAKDLIRR-LICSRERRLgqnGIDDFKKHPFFegidwDNIRDS 280
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
8-200 6.18e-17

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 79.29  E-value: 6.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   8 GKI-GEGSYGVVFKCRNRDTGQIVAIKRFLETE-DDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDH 85
Cdd:cd14188     6 GKVlGKGGFAKCYEMTDLTTNKVYAAKIIPHSRvSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 TVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYVATR 165
Cdd:cd14188    86 RSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRRTICGTP 165
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1039741915 166 WYRSPELLvGDTQYGPPVDVWAIGCVFAELLSGVP 200
Cdd:cd14188   166 NYLSPEVL-NKQGHGCESDIWALGCVMYTMLLGRP 199
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
9-287 7.53e-17

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 79.38  E-value: 7.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVAikrFLETEDDPVIKKIALR---EIRMLKQLKHPNLVNLLE----VFRRKRRLHLVFE 81
Cdd:cd14031    17 ELGRGAFKTVYKGLDTETWVEVA---WCELQDRKLTKAEQQRfkeEAEMLKGLQHPNIVRFYDswesVLKGKKCIVLVTE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHE-LDRYQRGVPEpLVKNITWQTLQAVNFCHKHN--CIHRDVKPENILITKQS-AIKLCDFGFARLLTGpgDY 157
Cdd:cd14031    94 LMTSGTLKTyLKRFKVMKPK-VLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTgSVKIGDLGLATLMRT--SF 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 158 YTDYVATRWYRSPELLvgDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYliRKTLGDLIPRhqqvfSMNqyfsg 237
Cdd:cd14031   171 AKSVIGTPEFMAPEMY--EEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIY--RKVTSGIKPA-----SFN----- 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039741915 238 vKIPDPEDMETLElkfpnisysalgflkGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14031   237 -KVTDPEVKEIIE---------------GCIRQNKSERLSIKDLLNHAFF 270
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
8-202 8.66e-17

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 79.09  E-value: 8.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   8 GKIGEGSYGVVFKCRNRDTGQIVAIKRFleteddpVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTV 87
Cdd:cd13991    12 LRIGRGSFGEVHRMEDKQTGFQCAVKKV-------RLEVFRAEELMACAGLTSPRVVPLYGAVREGPWVNIFMDLKEGGS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  88 LHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQ-SAIKLCDFGFARLL--TGPGD--YYTDYV 162
Cdd:cd13991    85 LGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDgSDAFLCDFGHAECLdpDGLGKslFTGDYI 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1039741915 163 -ATRWYRSPELLVGDTQyGPPVDVWAIGCVFAELLSGVPLW 202
Cdd:cd13991   165 pGTETHMAPEVVLGKPC-DAKVDVWSSCCMMLHMLNGCHPW 204
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
2-287 9.34e-17

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 79.72  E-value: 9.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIK-----RFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFR-RKRR 75
Cdd:cd14040     6 ERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKihqlnKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSlDTDT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  76 LHLVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCH--KHNCIHRDVKPENILITKQSA---IKLCDFGFARL 150
Cdd:cd14040    86 FCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGTAcgeIKITDFGLSKI 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 151 LTGPG------DYYTDYVATRWYRSPELLVGDTQygPP-----VDVWAIGCVFAELLSGvplwpgksdvdqlyliRKTLG 219
Cdd:cd14040   166 MDDDSygvdgmDLTSQGAGTYWYLPPECFVVGKE--PPkisnkVDVWSVGVIFFQCLYG----------------RKPFG 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039741915 220 DlIPRHQQVFSMNQYFSGVKIPDPEDmetlelkfPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14040   228 H-NQSQQDILQENTILKATEVQFPVK--------PVVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYL 286
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
2-198 1.02e-16

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 80.44  E-value: 1.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLkqlkhpnLVN--------LLEVFRRK 73
Cdd:cd05624    72 DDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERNV-------LVNgdcqwittLHYAFQDE 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  74 RRLHLVFEY-CDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLT 152
Cdd:cd05624   145 NYLYLVMDYyVGGDLLTLLSKFEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSCLKMN 224
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 153 GPGDYYTDY-VATRWYRSPELLV----GDTQYGPPVDVWAIGCVFAELLSG 198
Cdd:cd05624   225 DDGTVQSSVaVGTPDYISPEILQamedGMGKYGPECDWWSLGVCMYEMLYG 275
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
10-207 1.63e-16

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 78.12  E-value: 1.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQiVAIKRFleTEDDPVIKKIA-LREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVL 88
Cdd:cd05085     4 LGKGNFGEVYKGTLKDKTP-VAVKTC--KEDLPQELKIKfLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGGDF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  89 heLDRYQRGVPEPLVKNITWQTLQAVN---FCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGpGDYYTD---YV 162
Cdd:cd05085    81 --LSFLRKKKDELKTKQLVKFSLDAAAgmaYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQEDD-GVYSSSglkQI 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1039741915 163 ATRWyRSPELLvGDTQYGPPVDVWAIGCVFAELLS-GVPLWPGKSD 207
Cdd:cd05085   158 PIKW-TAPEAL-NYGRYSSESDVWSFGILLWETFSlGVCPYPGMTN 201
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
9-197 1.64e-16

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 78.05  E-value: 1.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDdPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYC---DH 85
Cdd:cd05084     3 RIGRGNFGEVFSGRLRADNTPVAVKSCRETLP-PDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVqggDF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 TVLHELDRYQRGVPEpLVKnITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARlLTGPGDYYTD----Y 161
Cdd:cd05084    82 LTFLRTEGPRLKVKE-LIR-MVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSR-EEEDGVYAATggmkQ 158
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1039741915 162 VATRWyRSPELLvGDTQYGPPVDVWAIGCVFAELLS 197
Cdd:cd05084   159 IPVKW-TAPEAL-NYGRYSSESDVWSFGILLWETFS 192
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
10-306 2.13e-16

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 78.89  E-value: 2.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIK---RFLETEDDPVikKIALREIRMLK-QLKHPNLVNLLEVFRRKRRLHLVFEYCDH 85
Cdd:cd05616     8 LGKGSFGKVMLAERKGTDELYAVKilkKDVVIQDDDV--ECTMVEKRVLAlSGKPPFLTQLHSCFQTMDRLYFVMEYVNG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 -TVLHELDRYQRgVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYVAT 164
Cdd:cd05616    86 gDLMYHIQQVGR-FKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 165 RWYRSPElLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKsDVDQLYlirktlgdliprhQQVFSMNQYFsgvkipdPE 244
Cdd:cd05616   165 PDYIAPE-IIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGE-DEDELF-------------QSIMEHNVAY-------PK 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039741915 245 DMetlelkfpniSYSALGFLKGCLHMDPAERLTC-----EQLLQHPYFDSIrEVGELTRQHDKPARK 306
Cdd:cd05616   223 SM----------SKEAVAICKGLMTKHPGKRLGCgpegeRDIKEHAFFRYI-DWEKLERKEIQPPYK 278
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
10-290 2.62e-16

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 78.89  E-value: 2.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIK---RFLETEDDPVikKIALREIRMLKQL-KHPNLVNLLEVFRRKRRLHLVFEYCDH 85
Cdd:cd05615    18 LGKGSFGKVMLAERKGSDELYAIKilkKDVVIQDDDV--ECTMVEKRVLALQdKPPFLTQLHSCFQTVDRLYFVMEYVNG 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 TVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYVATR 165
Cdd:cd05615    96 GDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMVEGVTTRTFCGTP 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 166 WYRSPElLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKsDVDQLYlirktlgdliprhQQVFSMNQYFSgvkipdped 245
Cdd:cd05615   176 DYIAPE-IIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGE-DEDELF-------------QSIMEHNVSYP--------- 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039741915 246 metlelkfPNISYSALGFLKGCLHMDPAERLTCEQ-----LLQHPYFDSI 290
Cdd:cd05615   232 --------KSLSKEAVSICKGLMTKHPAKRLGCGPegerdIREHAFFRRI 273
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
10-211 3.00e-16

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 77.43  E-value: 3.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTgqiVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRrKRRLHLVFEYCDHTVL- 88
Cdd:cd14062     1 IGSGSFGTVYKGRWHGD---VAVKKLNVTDPTPSQLQAFKNEVAVLRKTRHVNILLFMGYMT-KPQLAIVTQWCEGSSLy 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  89 HELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARlltgpgdyytdyVATRW-- 166
Cdd:cd14062    77 KHLHVLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLAT------------VKTRWsg 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 167 ------------YRSPEL--LVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQL 211
Cdd:cd14062   145 sqqfeqptgsilWMAPEVirMQDENPYSFQSDVYAFGIVLYELLTGQLPYSHINNRDQI 203
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
21-283 3.52e-16

Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein 15; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Vps15 is a large protein consisting of an N-terminal kinase domain, a C-terminal WD-repeat containing domain, and an intermediate bridge domain that contain HEAT repeats. The kinase domain is necessary for the signaling functions of Vps15. Human Vps15 was previously called p150. It associates and regulates Vps34, also called Class III phosphoinositide 3-kinase (PI3K), which catalyzes the phosphorylation of D-myo-phosphatidylinositol (PtdIns). Vps34 is the only PI3K present in yeast. It plays an important role in the regulation of protein and vesicular trafficking and sorting, autophagy, trimeric G-protein signaling, and phagocytosis. The Vps15 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 77.68  E-value: 3.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  21 CRNRDTGQIVAIKRFLETEDDPVIK--KIALREIRMlKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVlheldrYQRGV 98
Cdd:cd13980    17 ARARHDEGLVVVKVFVKPDPALPLRsyKQRLEEIRD-RLLELPNVLPFQKVIETDKAAYLIRQYVKYNL------YDRIS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  99 PEPLVKN-----ITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFAR--LLTG--PGD--YYTDYVATR-W 166
Cdd:cd13980    90 TRPFLNLiekkwIAFQLLHALNQCHKRGVCHGDIKTENVLVTSWNWVYLTDFASFKptYLPEdnPADfsYFFDTSRRRtC 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 167 YRSPELLVGDTQYG-----------PPVDVWAIGCVFAEL-LSGVPLWpgksDVDQLYLIRKtlgdliprhqqvfsmNQY 234
Cdd:cd13980   170 YIAPERFVDALTLDaeserrdgeltPAMDIFSLGCVIAELfTEGRPLF----DLSQLLAYRK---------------GEF 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 235 fsgvkipDPEDMetLElKFPNISYSALgflkgCLHM---DPAERLTCEQLLQ 283
Cdd:cd13980   231 -------SPEQV--LE-KIEDPNIREL-----ILHMiqrDPSKRLSAEDYLK 267
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
4-197 3.73e-16

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 78.38  E-value: 3.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFkcrnrdtgqiVAIKrflETEDDPVIKKIA-----LREIRMLKQLKHPNLVNLLEVFRRKRRLHL 78
Cdd:PHA03209   68 YTVIKTLTPGSEGRVF----------VATK---PGQPDPVVLKIGqkgttLIEAMLLQNVNHPSVIRMKDTLVSGAITCM 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARL-LTGPGDY 157
Cdd:PHA03209  135 VLPHYSSDLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQFpVVAPAFL 214
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1039741915 158 ytDYVATRWYRSPELLVGDtQYGPPVDVWAIGCVFAELLS 197
Cdd:PHA03209  215 --GLAGTVETNAPEVLARD-KYNSKADIWSAGIVLFEMLA 251
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
2-287 3.99e-16

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 77.79  E-value: 3.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIK-----RFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFR-RKRR 75
Cdd:cd14041     6 DRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKihqlnKNWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSlDTDS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  76 LHLVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCH--KHNCIHRDVKPENILITKQSA---IKLCDFGFARL 150
Cdd:cd14041    86 FCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNeiKPPIIHYDLKPGNILLVNGTAcgeIKITDFGLSKI 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 151 LTGPGDYYTDYV-------ATRWYRSPELLVGDTQygPP-----VDVWAIGCVFAELLSGvplwpgksdvdqlyliRKTL 218
Cdd:cd14041   166 MDDDSYNSVDGMeltsqgaGTYWYLPPECFVVGKE--PPkisnkVDVWSVGVIFYQCLYG----------------RKPF 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 219 GDlIPRHQQVFSMNQYFSGVKIPDPEDmetlelkfPNISYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14041   228 GH-NQSQQDILQENTILKATEVQFPPK--------PVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYL 287
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
3-149 4.85e-16

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 77.11  E-value: 4.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrfLETEDDPVikKIALREIRMLKQLKH----PNLV-------------- 64
Cdd:cd14016     1 RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIK--IEKKDSKH--PQLEYEAKVYKLLQGgpgiPRLYwfgqegdynvmvmd 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  65 ----NLLEVFRR-KRRLHLvfeycdHTVLheldryqrgvpeplvkNITWQTLQAVNFCHKHNCIHRDVKPENILI---TK 136
Cdd:cd14016    77 llgpSLEDLFNKcGRKFSL------KTVL----------------MLADQMISRLEYLHSKGYIHRDIKPENFLMglgKN 134
                         170
                  ....*....|...
gi 1039741915 137 QSAIKLCDFGFAR 149
Cdd:cd14016   135 SNKVYLIDFGLAK 147
STKc_SRPK2 cd14217
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs ...
3-287 5.55e-16

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK2 mediates neuronal cell cycle and cell death through regulation of nuclear cyclin D1. It has also been found to promote leukemia cell proliferation by regulating cyclin A1. SRPK2 also plays a role in regulating pre-mRNA splicing and is required for spliceosomal B complex formation. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271119 [Multi-domain]  Cd Length: 366  Bit Score: 78.15  E-value: 5.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDdpvIKKIALREIRMLKQLKH-----PN---LVNLLEVFR--- 71
Cdd:cd14217    13 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQH---YTETALDEIKLLRCVREsdpedPNkdmVVQLIDDFKisg 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  72 -RKRRLHLVFEYCDHTVLHEL--DRYQrGVPEPLVKNITWQTLQAVNFCH-KHNCIHRDVKPENILI------TKQSAIK 141
Cdd:cd14217    90 mNGIHVCMVFEVLGHHLLKWIikSNYQ-GLPIRCVKSIIRQVLQGLDYLHsKCKIIHTDIKPENILMcvddayVRRMAAE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 142 LCDFGFA--------------RLLTGPGD----------------------YYTDYVATRWYRSPELLVGdTQYGPPVDV 185
Cdd:cd14217   169 ATEWQKAgapppsgsavstapDLLVNPLDprnadkirvkiadlgnacwvhkHFTEDIQTRQYRSIEVLIG-AGYSTPADI 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 186 WAIGCVFAELLSGVPLWPGKS------DVDQLYLIRKTLGDlIPRHqqvFSMNQYFSGVKIPDPEDMETLELKFPNISYS 259
Cdd:cd14217   248 WSTACMAFELATGDYLFEPHSgedysrDEDHIAHIIELLGC-IPRH---FALSGKYSREFFNRRGELRHITKLKPWSLFD 323
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1039741915 260 AL---------------GFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14217   324 VLvekygwphedaaqftDFLIPMLEMVPEKRASAGECLRHPWL 366
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
2-198 6.16e-16

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 78.13  E-value: 6.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIR-MLKQLKHPNLVNLLEVFRRKRRLHLVF 80
Cdd:cd05623    72 EDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERdVLVNGDSQWITTLHYAFQDDNNLYLVM 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  81 EY-CDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYT 159
Cdd:cd05623   152 DYyVGGDLLTLLSKFEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKLMEDGTVQS 231
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1039741915 160 DY-VATRWYRSPELLV----GDTQYGPPVDVWAIGCVFAELLSG 198
Cdd:cd05623   232 SVaVGTPDYISPEILQamedGKGKYGPECDWWSLGVCMYEMLYG 275
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
2-200 8.41e-16

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 77.33  E-value: 8.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTG-QIVAIKRFletEDDPVIKKI----ALREIRMLKQLKHPNLVNLLEVFRRKRRL 76
Cdd:PTZ00426   30 EDFNFIRTLGTGSFGRVILATYKNEDfPPVAIKRF---EKSKIIKQKqvdhVFSERKILNYINHPFCVNLYGSFKDESYL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  77 HLVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgpGD 156
Cdd:PTZ00426  107 YLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVVD--TR 184
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1039741915 157 YYTdYVATRWYRSPELLVgDTQYGPPVDVWAIGCVFAELLSGVP 200
Cdd:PTZ00426  185 TYT-LCGTPEYIAPEILL-NVGHGKAADWWTLGIFIYEILVGCP 226
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
7-283 1.01e-15

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 76.98  E-value: 1.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   7 IGK-IGEGSYGVVFKCR----NRDTGQ---IVAIKRFletEDDPVIKKIA--LREIRMLKQL-KHPNLVNLLEVFRRKRR 75
Cdd:cd05101    28 LGKpLGEGCFGQVVMAEavgiDKDKPKeavTVAVKML---KDDATEKDLSdlVSEMEMMKMIgKHKNIINLLGACTQDGP 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  76 LHLVFEYCDHTVLHELDRYQRG-----------VP-EPL----VKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA 139
Cdd:cd05101   105 LYVIVEYASKGNLREYLRARRPpgmeysydinrVPeEQMtfkdLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNV 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 140 IKLCDFGFARLLTGPgDYYTDYVATRW---YRSPELLVgDTQYGPPVDVWAIGCVFAEL--LSGVPlWPGKSdVDQLYLI 214
Cdd:cd05101   185 MKIADFGLARDINNI-DYYKKTTNGRLpvkWMAPEALF-DRVYTHQSDVWSFGVLMWEIftLGGSP-YPGIP-VEELFKL 260
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 215 RKtlgdliprhqqvfsmnqyfSGVKIPDPEDMeTLELKFpnisysalgFLKGCLHMDPAERLTCEQLLQ 283
Cdd:cd05101   261 LK-------------------EGHRMDKPANC-TNELYM---------MMRDCWHAVPSQRPTFKQLVE 300
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
10-200 1.47e-15

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 75.51  E-value: 1.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRdtGQIVAIKRFLETEDDPVIKKIA--LREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDhtv 87
Cdd:cd14061     2 IGVGGFGKVYRGIWR--GEEVAVKAARQDPDEDISVTLEnvRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYAR--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  88 LHELDRY--QRGVPEPLVKNITWQTLQAVNFCHKHN---CIHRDVKPENILITK--------QSAIKLCDFGFARLLtgp 154
Cdd:cd14061    77 GGALNRVlaGRKIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILEaienedleNKTLKITDFGLAREW--- 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039741915 155 gdYYT---DYVATRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLSG-VP 200
Cdd:cd14061   154 --HKTtrmSAAGTYAWMAPEVIKSST-FSKASDVWSYGVLLWELLTGeVP 200
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
13-194 1.60e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 77.24  E-value: 1.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  13 GSYGVVFKCRNRDTGQIVAIKRFLETEddpvikkiALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLHELD 92
Cdd:PHA03211  180 GSEGCVFESSHPDYPQRVVVKAGWYAS--------SVHEARLLRRLSHPAVLALLDVRVVGGLTCLVLPKYRSDLYTYLG 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  93 RYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTG--PGDYYTDYVATRWYRSP 170
Cdd:PHA03211  252 ARLRPLGLAQVTAVARQLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFGAACFARGswSTPFHYGIAGTVDTNAP 331
                         170       180
                  ....*....|....*....|....
gi 1039741915 171 ELLVGDTqYGPPVDVWAIGCVFAE 194
Cdd:PHA03211  332 EVLAGDP-YTPSVDIWSAGLVIFE 354
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
10-290 1.82e-15

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 75.90  E-value: 1.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVF---KCRNRDTGQIVAIKrfleteddpVIKKIALR---------EIRMLKQLKHPNLVNLLEVFRRKRRLH 77
Cdd:cd05582     3 LGQGSFGKVFlvrKITGPDAGTLYAMK---------VLKKATLKvrdrvrtkmERDILADVNHPFIVKLHYAFQTEGKLY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  78 LVFEYcdhtvLHELDRYQRGVPEPL-----VKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLT 152
Cdd:cd05582    74 LILDF-----LRGGDLFTRLSKEVMfteedVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 153 GPGDYYTDYVATRWYRSPElLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSdvdqlyliRKTLGDLIPRHQqvFSMN 232
Cdd:cd05582   149 DHEKKAYSFCGTVEYMAPE-VVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKD--------RKETMTMILKAK--LGMP 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 233 QYFSgvkipdPEdmetlelkfpnisysALGFLKGCLHMDPAERLTC-----EQLLQHPYFDSI 290
Cdd:cd05582   218 QFLS------PE---------------AQSLLRALFKRNPANRLGAgpdgvEEIKRHPFFATI 259
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
2-214 1.82e-15

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 75.16  E-value: 1.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQiVAIKrFLETEDDPVIKKIALrEIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd05148     6 EEFTLERKLGSGYFGEVWEGLWKNRVR-VAIK-ILKSDDLLKQQDFQK-EVQALKRLRHKHLISLFAVCSVGEPVYIITE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELDRYQRG--VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPgDYYT 159
Cdd:cd05148    83 LMEKGSLLAFLRSPEGqvLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARLIKED-VYLS 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 160 D--YVATRWyRSPELLvGDTQYGPPVDVWAIGCVFAELLS--GVPlWPGKSDVDQLYLI 214
Cdd:cd05148   162 SdkKIPYKW-TAPEAA-SHGTFSTKSDVWSFGILLYEMFTygQVP-YPGMNNHEVYDQI 217
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
10-290 2.03e-15

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 75.41  E-value: 2.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRfLETEDdpvIKK-----IALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFeycd 84
Cdd:cd05631     8 LGKGGFGEVCACQVRATGKMYACKK-LEKKR---IKKrkgeaMALNEKRILEKVNSRFVVSLAYAYETKDALCLVL---- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 hTVLHELDR----YQRGVPEplvKNITWQTLQAVNFC------HKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgP 154
Cdd:cd05631    80 -TIMNGGDLkfhiYNMGNPG---FDEQRAIFYAAELCcgledlQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIP-E 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 155 GDYYTDYVATRWYRSPElLVGDTQYGPPVDVWAIGCVFAELLSG-VPLWPGKSDVDQLYLIRKTlgdliprhqqvfsmnq 233
Cdd:cd05631   155 GETVRGRVGTVGYMAPE-VINNEKYTFSPDWWGLGCLIYEMIQGqSPFRKRKERVKREEVDRRV---------------- 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 234 yfsgvkipdPEDMETLELKFpniSYSALGFLKGCLHMDPAERLTCE-----QLLQHPYFDSI 290
Cdd:cd05631   218 ---------KEDQEEYSEKF---SEDAKSICRMLLTKNPKERLGCRgngaaGVKQHPIFKNI 267
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
18-289 2.08e-15

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 75.44  E-value: 2.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  18 VFKCRNRDTGQIVAI----KRFLETE---DDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRR-LHLVFE--YCD-HT 86
Cdd:cd14011    12 IYNGSKKSTKQEVSVfvfeKKQLEEYskrDREQILELLKRGVKQLTRLRHPRILTVQHPLEESREsLAFATEpvFASlAN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  87 VLHELDRYqrGVPEPLVKN-------IT---WQTLQAVNFCH-KHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPG 155
Cdd:cd14011    92 VLGERDNM--PSPPPELQDyklydveIKyglLQISEALSFLHnDVKLVHGNICPESVVINSNGEWKLAGFDFCISSEQAT 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 156 DYYTDYVATRW-----------YRSPELLVGDTqYGPPVDVWAIGCVFAELLS-GVPLWpgksDVDQLYLIRKtlgdlip 223
Cdd:cd14011   170 DQFPYFREYDPnlpplaqpnlnYLAPEYILSKT-CDPASDMFSLGVLIYAIYNkGKPLF----DCVNNLLSYK------- 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 224 RHQQVFSMNQYFSGVKIPDPedmetlelkfpniSYSalgFLKGCLHMDPAERLTCEQLLQHPYFDS 289
Cdd:cd14011   238 KNSNQLRQLSLSLLEKVPEE-------------LRD---HVKTLLNVTPEVRPDAEQLSKIPFFDD 287
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
10-225 2.17e-15

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 74.87  E-value: 2.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRdtGQIVAIKRF------LETEDDpvikkIALREIRMLKQLKHPNLVNLL-EVFRRKRRLHLVFEY 82
Cdd:cd14064     1 IGSGSFGKVYKGRCR--NKIVAIKRYrantycSKSDVD-----MFCREVSILCRLNHPCVIQFVgACLDDPSQFAIVTQY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHELDRYQRGVPEPLVK-NITWQTLQAVNFCHK--HNCIHRDVKPENILITKQSAIKLCDFGFARLLTG------ 153
Cdd:cd14064    74 VSGGSLFSLLHEQKRVIDLQSKlIIAVDVAKGMEYLHNltQPIIHRDLNSHNILLYEDGHAVVADFGESRFLQSldednm 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 154 ---PGDYytdyvatRWYrSPELLVGDTQYGPPVDVWAIGCVFAELLSG-VP---LWPGKSDVDQLY-LIRKTLGDLIPRH 225
Cdd:cd14064   154 tkqPGNL-------RWM-APEVFTQCTRYSIKADVFSYALCLWELLTGeIPfahLKPAAAAADMAYhHIRPPIGYSIPKP 225
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
1-282 2.40e-15

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 75.07  E-value: 2.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEKIGKIGEGSYGVVFK-----CRNRDTGQIVAIKRFLETEDDPVIKKIaLREIRMLKQLKHPNLVNLLEVFRRKRR 75
Cdd:cd05032     5 REKITLIRELGQGSFGMVYEglakgVVKGEPETRVAIKTVNENASMRERIEF-LNEASVMKEFNCHHVVRLLGVVSTGQP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  76 LHLVFEYCDHTVLHELDRYQR--------GVPEPLVKNITW--QTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDF 145
Cdd:cd05032    84 TLVVMELMAKGDLKSYLRSRRpeaennpgLGPPTLQKFIQMaaEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGDF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 146 GFARLLtgpgdYYTDY--------VATRWYrSPELLvGDTQYGPPVDVWAIGCVFAEL--LSGVPlWPGKSdvdqlylir 215
Cdd:cd05032   164 GMTRDI-----YETDYyrkggkglLPVRWM-APESL-KDGVFTTKSDVWSFGVVLWEMatLAEQP-YQGLS--------- 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039741915 216 ktlgdliprHQQVfsMNQYFSGVKIPDPEDMetlelkfPNISYSalgFLKGCLHMDPAERLTCEQLL 282
Cdd:cd05032   227 ---------NEEV--LKFVIDGGHLDLPENC-------PDKLLE---LMRMCWQYNPKMRPTFLEIV 272
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
10-198 2.58e-15

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 75.25  E-value: 2.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTgqIVAIKRFLETE--DDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTV 87
Cdd:cd14159     1 IGEGGFGCVYQAVMRNT--EYAVKRLKEDSelDWSVVKNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVYLPNGS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  88 LHelDRYQRGVPEPLVK-----NITWQTLQAVNFCHKHN--CIHRDVKPENILITKQSAIKLCDFGFARLLTGPGD---- 156
Cdd:cd14159    79 LE--DRLHCQVSCPCLSwsqrlHVLLGTARAIQYLHSDSpsLIHGDVKSSNILLDAALNPKLGDFGLARFSRRPKQpgms 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1039741915 157 ---YYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSG 198
Cdd:cd14159   157 stlARTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTG 201
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
10-290 2.61e-15

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 75.17  E-value: 2.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFleteDDPVIK-----KIALREIRMLKQLKH----PNLVNLLEVFRRKRRLHLVF 80
Cdd:cd05606     2 IGRGGFGEVYGCRKADTGKMYAMKCL----DKKRIKmkqgeTLALNERIMLSLVSTggdcPFIVCMTYAFQTPDKLCFIL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  81 EYCDHTVLHeldrY---QRGV-PEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFArlltgpgd 156
Cdd:cd05606    78 DLMNGGDLH----YhlsQHGVfSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLA-------- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 157 yyTDY--------VATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLgdliprhqqv 228
Cdd:cd05606   146 --CDFskkkphasVGTHGYMAPEVLQKGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKDKHEIDRMTL---------- 213
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039741915 229 fSMNqyfsgVKIPDpeDMeTLELKfpnisysalGFLKGCLHMDPAERLTC-----EQLLQHPYFDSI 290
Cdd:cd05606   214 -TMN-----VELPD--SF-SPELK---------SLLEGLLQRDVSKRLGClgrgaTEVKEHPFFKGV 262
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
10-286 2.72e-15

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 74.61  E-value: 2.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKrFLETEDDPviKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLH 89
Cdd:cd14115     1 IGRGRFSIVKKCLHKATRKDVAVK-FVSKKMKK--KEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  90 ELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQ---SAIKLCDFGFARLLTGpgdyytDYVATRW 166
Cdd:cd14115    78 DYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISG------HRHVHHL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 167 YRSPELLVGDTQYGPPV----DVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTlgdliprhqqVFSM-NQYFSGVkip 241
Cdd:cd14115   152 LGNPEFAAPEVIQGTPVslatDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRV----------DFSFpDEYFGDV--- 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1039741915 242 dpedmetlelkfpniSYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14115   219 ---------------SQAARDFINVILQEDPRRRPTAATCLQHPW 248
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
10-220 2.77e-15

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 74.84  E-value: 2.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRnRDTGQIVAIKRfLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLH 89
Cdd:cd14664     1 IGRGGAGTVYKGV-MPNGTLVAVKR-LKGEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGSLG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  90 EL--DRYQRGVP--EPLVKNITWQTLQAVNFCHkHNC----IHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDY 161
Cdd:cd14664    79 ELlhSRPESQPPldWETRQRIALGSARGLAYLH-HDCspliIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKDSHVMSS 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 162 VA-TRWYRSPElLVGDTQYGPPVDVWAIGCVFAELLSG---VPLWPGKSDVDQLYLIRKTLGD 220
Cdd:cd14664   158 VAgSYGYIAPE-YAYTGKVSEKSDVYSYGVVLLELITGkrpFDEAFLDDGVDIVDWVRGLLEE 219
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
10-282 2.91e-15

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 74.72  E-value: 2.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQ---IVAIKRfLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHT 86
Cdd:cd05033    12 IGGGEFGEVCSGSLKLPGKkeiDVAIKT-LKSGYSDKQRLDFLTEASIMGQFDHPNVIRLEGVVTKSRPVMIVTEYMENG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  87 VLHELDRYQRG--VPEPLVkNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDY--- 161
Cdd:cd05033    91 SLDKFLRENDGkfTVTQLV-GMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLEDSEATYTTKggk 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 162 VATRWyRSPElLVGDTQYGPPVDVWAIGCVFAELLS--GVPLWpgksDVDqlylirktlgdliprHQQVfsMNQYFSGVK 239
Cdd:cd05033   170 IPIRW-TAPE-AIAYRKFTSASDVWSFGIVMWEVMSygERPYW----DMS---------------NQDV--IKAVEDGYR 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1039741915 240 IPDPEDMetlelkfPNISYSalgFLKGCLHMDPAERLTCEQLL 282
Cdd:cd05033   227 LPPPMDC-------PSALYQ---LMLDCWQKDRNERPTFSQIV 259
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
1-197 2.98e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 76.66  E-value: 2.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIK---KIALR-------------EIRMLKQLKHPNLV 64
Cdd:PHA03210  147 LAHFRVIDDLPAGAFGKIFICALRASTEEAEARRGVNSTNQGKPKcerLIAKRvkagsraaiqlenEILALGRLNHENIL 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  65 NLLEVFRRKRRLHLV---FEYCDHTVLHELDRYQRGvpEPLVKN---ITWQTLQAVNFCHKHNCIHRDVKPENILITKQS 138
Cdd:PHA03210  227 KIEEILRSEANTYMItqkYDFDLYSFMYDEAFDWKD--RPLLKQtraIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDG 304
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 139 AIKLCDFGFARLLTGPG---DYytDYVATRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLS 197
Cdd:PHA03210  305 KIVLGDFGTAMPFEKEReafDY--GWVGTVATNSPEILAGDG-YCEITDIWSCGLILLDMLS 363
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
10-198 2.99e-15

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 74.96  E-value: 2.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRdtGQIVAIKRF-------------------LETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVF 70
Cdd:cd14000     2 LGDGGFGSVYRASYK--GEPVAVKIFnkhtssnfanvpadtmlrhLRATDAMKNFRLLRQELTVLSHLHHPSIVYLLGIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  71 RRKRRLhlVFEYCDHTVLHELDRYQRGVPEPL----VKNITWQTLQAVNFCHKHNCIHRDVKPENILI-----TKQSAIK 141
Cdd:cd14000    80 IHPLML--VLELAPLGSLDHLLQQDSRSFASLgrtlQQRIALQVADGLRYLHSAMIIYRDLKSHNVLVwtlypNSAIIIK 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039741915 142 LCDFGFARLLTGPGDYYTDyvATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSG 198
Cdd:cd14000   158 IADYGISRQCCRMGAKGSE--GTPGFRAPEIARGNVIYNEKVDVFSFGMLLYEILSG 212
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
13-198 3.10e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 76.19  E-value: 3.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  13 GSYGVVFKCRNRDTGQIVAIKRFLeteddpviKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVF-EYcdHTVLHEL 91
Cdd:PHA03212  103 GAEGFAFACIDNKTCEHVVIKAGQ--------RGGTATEAHILRAINHPSIIQLKGTFTYNKFTCLILpRY--KTDLYCY 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  92 DRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARlltgpgdYYTDYVATRWY---- 167
Cdd:PHA03212  173 LAAKRNIAICDILAIERSVLRAIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGAAC-------FPVDINANKYYgwag 245
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1039741915 168 ----RSPELLVGDTqYGPPVDVWAIGCVFAELLSG 198
Cdd:PHA03212  246 tiatNAPELLARDP-YGPAVDIWSAGIVLFEMATC 279
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
8-204 3.22e-15

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 75.21  E-value: 3.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   8 GKI-GEGSYGVV-----FKCRNRDTGQIVAIKRFLETEDDPViKKIALREIRMLKQL-KHPNLVNLLEVFRRKRRLHLVF 80
Cdd:cd05055    40 GKTlGAGAFGKVveataYGLSKSDAVMKVAVKMLKPTAHSSE-REALMSELKIMSHLgNHENIVNLLGACTIGGPILVIT 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  81 EYCDHTVLHELDRYQRGV---PEPLVkNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDY 157
Cdd:cd05055   119 EYCCYGDLLNFLRRKRESfltLEDLL-SFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLARDIMNDSNY 197
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 158 YTD---YVATRWYrSPELLVgDTQYGPPVDVWAIGCVFAELLS-GVPLWPG 204
Cdd:cd05055   198 VVKgnaRLPVKWM-APESIF-NCVYTFESDVWSYGILLWEIFSlGSNPYPG 246
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
9-197 3.82e-15

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 75.03  E-value: 3.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVAIKRFLET-EDDPVIKKIA--------------LREIRMLKQLKHPNLVNLLEVFRRK 73
Cdd:cd05095    12 KLGEGQFGEVHLCEAEGMEKFMDKDFALEVsENQPVLVAVKmlradanknarndfLKEIKIMSRLKDPNIIRLLAVCITD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  74 RRLHLVFEYCDHTVLHE-LDRYQrgVPEPLVKNITWQTLQAVNFCH---------KH----NCIHRDVKPENILITKQSA 139
Cdd:cd05095    92 DPLCMITEYMENGDLNQfLSRQQ--PEGQLALPSNALTVSYSDLRFmaaqiasgmKYlsslNFVHRDLATRNCLVGKNYT 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 140 IKLCDFGFARLLTGpGDYY----TDYVATRWYRSPELLVGdtQYGPPVDVWAIGCVFAELLS 197
Cdd:cd05095   170 IKIADFGMSRNLYS-GDYYriqgRAVLPIRWMSWESILLG--KFTTASDVWAFGVTLWETLT 228
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
10-199 4.37e-15

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 74.21  E-value: 4.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDpvIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLH 89
Cdd:cd14222     1 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEE--TQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  90 ELDRYQRGVPeplvknitWQtlQAVNFC----------HKHNCIHRDVKPENILITKQSAIKLCDFGFARLLT-----GP 154
Cdd:cd14222    79 DFLRADDPFP--------WQ--QKVSFAkgiasgmaylHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVeekkkPP 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 155 GDYYTD---------------YVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGV 199
Cdd:cd14222   149 PDKPTTkkrtlrkndrkkrytVVGNPYWMAPEMLNG-KSYDEKVDIFSFGIVLCEIIGQV 207
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
10-200 4.53e-15

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 74.25  E-value: 4.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLH 89
Cdd:cd14148     2 IGVGGFGKVYKGLWRGEEVAVKAARQDPDEDIAVTAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGALN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  90 ELDRYQRgVPEPLVKNITWQTLQAVNFCHKHN---CIHRDVKPENILITKQ--------SAIKLCDFGFAR------LLT 152
Cdd:cd14148    82 RALAGKK-VPPHVLVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILILEPienddlsgKTLKITDFGLARewhkttKMS 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1039741915 153 GPGDYYtdyvatrwYRSPElLVGDTQYGPPVDVWAIGCVFAELLSG-VP 200
Cdd:cd14148   161 AAGTYA--------WMAPE-VIRLSLFSKSSDVWSFGVLLWELLTGeVP 200
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
1-284 5.06e-15

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 73.86  E-value: 5.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEKIGKIGEGSYGVVFKCRNRdtGQIVAIKrfleteddpVIKKIA-----LREIRMLKQLKHPNLVNLLEVF-RRKR 74
Cdd:cd05082     5 MKELKLLQTIGKGEFGDVMLGDYR--GNKVAVK---------CIKNDAtaqafLAEASVMTQLRHSNLVQLLGVIvEEKG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  75 RLHLVFEYCDHTVLHELDRYQ-RGV--PEPLVKnITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLL 151
Cdd:cd05082    74 GLYIVTEYMAKGSLVDYLRSRgRSVlgGDCLLK-FSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 152 TGPGDyyTDYVATRWyRSPELLvGDTQYGPPVDVWAIGCVFAELLS--GVPlWPgksdvdqlyliRKTLGDLIPRHQQVF 229
Cdd:cd05082   153 SSTQD--TGKLPVKW-TAPEAL-REKKFSTKSDVWSFGILLWEIYSfgRVP-YP-----------RIPLKDVVPRVEKGY 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039741915 230 SMNQyfsgvkiPDpedmetlelKFPNISYSalgFLKGCLHMDPAERLTCEQL---LQH 284
Cdd:cd05082   217 KMDA-------PD---------GCPPAVYD---VMKNCWHLDAAMRPSFLQLreqLEH 255
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
9-197 7.22e-15

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 74.24  E-value: 7.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCR------------NRDTGQ--IVAIKRfLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKR 74
Cdd:cd05097    12 KLGEGQFGEVHLCEaeglaeflgegaPEFDGQpvLVAVKM-LRADVTKTARNDFLKEIKIMSRLKNPNIIRLLGVCVSDD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  75 RLHLVFEYCDHTVLHELdRYQR----------GVPEPLVKNITWQTLQ---AVNFCHKHNCIHRDVKPENILITKQSAIK 141
Cdd:cd05097    91 PLCMITEYMENGDLNQF-LSQReiestfthanNIPSVSIANLLYMAVQiasGMKYLASLNFVHRDLATRNCLVGNHYTIK 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 142 LCDFGFARLLTGpGDYY----TDYVATRWYRSPELLVGdtQYGPPVDVWAIGCVFAELLS 197
Cdd:cd05097   170 IADFGMSRNLYS-GDYYriqgRAVLPIRWMAWESILLG--KFTTASDVWAFGVTLWEMFT 226
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
10-293 8.78e-15

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 73.32  E-value: 8.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIkkiaLREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLH 89
Cdd:cd14156     1 IGSGFFSKVYKVTHGATGKVMVVKIYKNDVDQHKI----VREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  90 ELDRYQRgVPEPLVKNITWQT--LQAVNFCHKHNCIHRDVKPENILITKQSAIK---LCDFGFARLL----TGPGDYYTD 160
Cdd:cd14156    77 ELLAREE-LPLSWREKVELACdiSRGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLAREVgempANDPERKLS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 YVATRWYRSPELLVGDtQYGPPVDVWAIGCVFAELLSGVPLWPgksdvdqlylirktlgDLIPRHQQvFSMnqyfsgvki 240
Cdd:cd14156   156 LVGSAFWMAPEMLRGE-PYDRKVDVFSFGIVLCEILARIPADP----------------EVLPRTGD-FGL--------- 208
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 241 pdpeDMETLELKFPNISYSALGFLKGCLHMDPAERLTCEQLLQHpyFDSIREV 293
Cdd:cd14156   209 ----DVQAFKEMVPGCPEPFLDLAASCCRMDAFKRPSFAELLDE--LEDIAET 255
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
10-290 1.00e-14

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 73.97  E-value: 1.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIK---RFLETEDDPVikKIALREIRMLK-QLKHPNLVNLLEVFRRKRRLHLVFEYCDH 85
Cdd:cd05587     4 LGKGSFGKVMLAERKGTDELYAIKilkKDVIIQDDDV--ECTMVEKRVLAlSGKPPFLTQLHSCFQTMDRLYFVMEYVNG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 TVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYVATR 165
Cdd:cd05587    82 GDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGGKTTRTFCGTP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 166 WYRSPElLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGkSDVDQLYlirktlgdliprhQQVFSMNQYFsgvkipdPED 245
Cdd:cd05587   162 DYIAPE-IIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDG-EDEDELF-------------QSIMEHNVSY-------PKS 219
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039741915 246 MetlelkfpniSYSALGFLKGCLHMDPAERLTC-----EQLLQHPYFDSI 290
Cdd:cd05587   220 L----------SKEAVSICKGLLTKHPAKRLGCgptgeRDIKEHPFFRRI 259
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
60-287 1.02e-14

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 72.85  E-value: 1.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  60 HPNLVNLLEVFRRKRRLHLVFEYcDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPEN-ILITKQ- 137
Cdd:cd13976    44 HPNISGVHEVIAGETKAYVFFER-DHGDLHSYVRSRKRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKfVFADEEr 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 138 SAIKLCDFGFARLLTGPGDYYTDYVATRWYRSPELLVGDTQY-GPPVDVWAIGCVFAELLSG-VPLwpgkSDVDQLYLIR 215
Cdd:cd13976   123 TKLRLESLEDAVILEGEDDSLSDKHGCPAYVSPEILNSGATYsGKAADVWSLGVILYTMLVGrYPF----HDSEPASLFA 198
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 216 KtlgdlIPRHQqvfsmnqyfsgVKIPdpedmETLelkfpniSYSALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd13976   199 K-----IRRGQ-----------FAIP-----ETL-------SPRARCLIRSLLRREPSERLTAEDILLHPWL 242
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
6-284 1.36e-14

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 73.29  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   6 KIGK-IGEGSYGVV-----FKCRNRDTGQIVAIKrFLETEDDPVIKKIALREIRMLKQL-KHPNLVNLLEVFRRKRR-LH 77
Cdd:cd05054    10 KLGKpLGRGAFGKViqasaFGIDKSATCRTVAVK-MLKEGATASEHKALMTELKILIHIgHHLNVVNLLGACTKPGGpLM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  78 LVFEYCDHTVLHELDRYQRG--VPEPLVKNIT------------------------WQTLQAVNFCHKHNCIHRDVKPEN 131
Cdd:cd05054    89 VIVEFCKFGNLSNYLRSKREefVPYRDKGARDveeeedddelykepltledlicysFQVARGMEFLASRKCIHRDLAARN 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 132 ILITKQSAIKLCDFGFARLLTGPGDYYTDYVA---TRWYrSPELLVgDTQYGPPVDVWAIGCVFAELLS-GVPLWPGksd 207
Cdd:cd05054   169 ILLSENNVVKICDFGLARDIYKDPDYVRKGDArlpLKWM-APESIF-DKVYTTQSDVWSFGVLLWEIFSlGASPYPG--- 243
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039741915 208 vdqlylirktlgdliprhqqvFSMNQYFSGvKIPDPEDMETLELKFPNIsYSAlgfLKGCLHMDPAERLTCEQLLQH 284
Cdd:cd05054   244 ---------------------VQMDEEFCR-RLKEGTRMRAPEYTTPEI-YQI---MLDCWHGEPKERPTFSELVEK 294
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
6-285 1.39e-14

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1b subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 73.04  E-value: 1.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   6 KIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQL-KHPNLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:cd14139     4 ELEKIGVGEFGSVYKCIKRLDGCVYAIKRSMRPFAGSSNEQLALHEVYAHAVLgHHPHVVRYYSAWAEDDHMIIQNEYCN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 ----HTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAI-------------------- 140
Cdd:cd14139    84 ggslQDAISENTKSGNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFICHKMQSssgvgeevsneedeflsanv 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 141 --KLCDFGFARLLTGP----GDyytdyvatRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLwpgKSDVDQLYLI 214
Cdd:cd14139   164 vyKIGDLGHVTSINKPqveeGD--------SRFLANEILQEDYRHLPKADIFALGLTVALAAGAEPL---PTNGAAWHHI 232
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 215 RKtlGDLIPRHQQvfsmnqyfsgvkipdpedmetlelkfpnISYSALGFLKGCLHMDPAERLTCEQLLQHP 285
Cdd:cd14139   233 RK--GNFPDVPQE----------------------------LPESFSSLLKNMIQPDPEQRPSATALARHT 273
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
7-283 1.54e-14

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 73.12  E-value: 1.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   7 IGK-IGEGSYGVVFKCR---------NRDTGQIVAIKRFLETEDDpviKKIALREIRMLKQL-KHPNLVNLLEVFRRKRR 75
Cdd:cd05098    17 LGKpLGEGCFGQVVLAEaigldkdkpNRVTKVAVKMLKSDATEKD---LSDLISEMEMMKMIgKHKNIINLLGACTQDGP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  76 LHLVFEYCDHTVLHELDRYQR-----------GVPEPLVK-----NITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA 139
Cdd:cd05098    94 LYVIVEYASKGNLREYLQARRppgmeycynpsHNPEEQLSskdlvSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNV 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 140 IKLCDFGFARLLTGPgDYYTDYVATRW---YRSPELLVgDTQYGPPVDVWAIGCVFAEL--LSGVPlWPGKSdVDQLYLI 214
Cdd:cd05098   174 MKIADFGLARDIHHI-DYYKKTTNGRLpvkWMAPEALF-DRIYTHQSDVWSFGVLLWEIftLGGSP-YPGVP-VEELFKL 249
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 215 RKtlgdliprhqqvfsmnqyfSGVKIPDPEdmetlelkfpNISYSALGFLKGCLHMDPAERLTCEQLLQ 283
Cdd:cd05098   250 LK-------------------EGHRMDKPS----------NCTNELYMMMRDCWHAVPSQRPTFKQLVE 289
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
10-290 1.66e-14

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 73.19  E-value: 1.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIK---RFLETEDDPVikKIALREIRMLK-QLKHPNLVNLLEVFRRKRRLHLVFEYCDH 85
Cdd:cd05592     3 LGKGSFGKVMLAELKGTNQYFAIKalkKDVVLEDDDV--ECTMIERRVLAlASQHPFLTHLFCTFQTESHLFFVMEYLNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 TVL--H-------ELDRYQRGVPEPLVknitwqtlqAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGD 156
Cdd:cd05592    81 GDLmfHiqqsgrfDEDRARFYGAEIIC---------GLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYGEN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 157 YYTDYVATRWYRSPELLVGDtQYGPPVDVWAIGCVFAELLSGVPLWPGKsDVDQLYlirktlgDLIpRHQQVFsmnqyfs 236
Cdd:cd05592   152 KASTFCGTPDYIAPEILKGQ-KYNQSVDWWSFGVLLYEMLIGQSPFHGE-DEDELF-------WSI-CNDTPH------- 214
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 237 gvkipdpedmetlelkFPN-ISYSALGFLKGCLHMDPAERL-----TCEQLLQHPYFDSI 290
Cdd:cd05592   215 ----------------YPRwLTKEAASCLSLLLERNPEKRLgvpecPAGDIRDHPFFKTI 258
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
5-283 2.11e-14

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 72.65  E-value: 2.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   5 EKIGKIGEGSYGVVFKCR----NRDTGQIVAIKRFLETEDDPVIKKIAlREIRMLKQLKHPNLVNLLEVFRRK--RRLHL 78
Cdd:cd05079     7 KRIRDLGEGHFGKVELCRydpeGDNTGEQVAVKSLKPESGGNHIADLK-KEIEILRNLYHENIVKYKGICTEDggNGIKL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTVLHE-LDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDY 157
Cdd:cd05079    86 IMEFLPSGSLKEyLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEY 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 158 YT---DYVATRWYRSPELLVgDTQYGPPVDVWAIGCVFAELLSGVplwpgKSDVDQLYLIRKTLGdliPRHQQVFS---M 231
Cdd:cd05079   166 YTvkdDLDSPVFWYAPECLI-QSKFYIASDVWSFGVTLYELLTYC-----DSESSPMTLFLKMIG---PTHGQMTVtrlV 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 232 NQYFSGVKIPDPedmetlelkfPNISYSALGFLKGCLHMDPAERLTCEQLLQ 283
Cdd:cd05079   237 RVLEEGKRLPRP----------PNCPEEVYQLMRKCWEFQPSKRTTFQNLIE 278
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
10-201 2.28e-14

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 72.38  E-value: 2.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFkcRNRDTGQIVAIKRFLETEDDPVIKKI--ALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTV 87
Cdd:cd14145    14 IGIGGFGKVY--RAIWIGDEVAVKAARHDPDEDISQTIenVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFARGGP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  88 LHELDRYQRGVPEPLVkNITWQTLQAVNFCHKHN---CIHRDVKPENILITKQ--------SAIKLCDFGFAR------L 150
Cdd:cd14145    92 LNRVLSGKRIPPDILV-NWAVQIARGMNYLHCEAivpVIHRDLKSSNILILEKvengdlsnKILKITDFGLARewhrttK 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 151 LTGPGDYYtdyvatrwYRSPELLVGDTqYGPPVDVWAIGCVFAELLSG-VPL 201
Cdd:cd14145   171 MSAAGTYA--------WMAPEVIRSSM-FSKGSDVWSYGVLLWELLTGeVPF 213
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
9-288 2.36e-14

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 71.93  E-value: 2.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQiVAIKRFLETEDDPvikKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVL 88
Cdd:cd05034     2 KLGAGQFGEVWMGVWNGTTK-VAVKTLKPGTMSP---EAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSKGSL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  89 HELDRYQRG--VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgpGDYYTDYVATRW 166
Cdd:cd05034    78 LDYLRTGEGraLRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLIE--DDEYTAREGAKF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 167 ---YRSPELLVgDTQYGPPVDVWAIGCVFAELLS--GVPlWPGKSDvdqlyliRKTLgdliprhqqvfsmNQYFSGVKIP 241
Cdd:cd05034   156 pikWTAPEAAL-YGRFTIKSDVWSFGILLYEIVTygRVP-YPGMTN-------REVL-------------EQVERGYRMP 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1039741915 242 DPEDMetlelkfPNISYSalgFLKGCLHMDPAERLTCEQLlqHPYFD 288
Cdd:cd05034   214 KPPGC-------PDELYD---IMLQCWKKEPEERPTFEYL--QSFLE 248
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
10-215 2.53e-14

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 73.03  E-value: 2.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLET---EDDPVikKIALREIRMLK-QLKHPNLVNLLEVFRRKRRLHLVFEYCDH 85
Cdd:cd05619    13 LGKGSFGKVFLAELKGTNQFFAIKALKKDvvlMDDDV--ECTMVEKRVLSlAWEHPFLTHLFCTFQTKENLFFVMEYLNG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 TVL-------HELDRyqrgvpePLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFAR--LLtgpGD 156
Cdd:cd05619    91 GDLmfhiqscHKFDL-------PRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKenML---GD 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 157 YYTD-YVATRWYRSPELLVGDtQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIR 215
Cdd:cd05619   161 AKTStFCGTPDYIAPEILLGQ-KYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIR 219
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
4-204 3.23e-14

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 72.33  E-value: 3.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrfleteddpVIKK---IALREIRML---KQL-------KHPNLVNLLEVF 70
Cdd:cd05589     1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIK---------ALKKgdiIARDEVESLmceKRIfetvnsaRHPFLVNLFACF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  71 RRKRRLHLVFEYCD------HtvLHElDRYqrgvPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCD 144
Cdd:cd05589    72 QTPEHVCFVMEYAAggdlmmH--IHE-DVF----SEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIAD 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 145 FGFARLLTGPGDYYTDYVATRWYRSPELLVgDTQYGPPVDVWAIGCVFAELLSGVPLWPG 204
Cdd:cd05589   145 FGLCKEGMGFGDRTSTFCGTPEFLAPEVLT-DTSYTRAVDWWGLGVLIYEMLVGESPFPG 203
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
2-293 3.46e-14

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 72.96  E-value: 3.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEddpVIKKIALREIR----MLKQLKHPNLVNLLEVFRRKRRLH 77
Cdd:cd05629     1 EDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSE---MFKKDQLAHVKaerdVLAESDSPWVVSLYYSFQDAQYLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  78 LVFEYCD----HTVLHELDRYQrgvpEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFG------- 146
Cdd:cd05629    78 LIMEFLPggdlMTMLIKYDTFS----EDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGlstgfhk 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 147 ------FARLLTGPGD------------------------------------YYTdyVATRWYRSPELLVGDTqYGPPVD 184
Cdd:cd05629   154 qhdsayYQKLLQGKSNknridnrnsvavdsinltmsskdqiatwkknrrlmaYST--VGTPDYIAPEIFLQQG-YGQECD 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 185 VWAIGCVFAELLSGvplWPGKSDVDQLYLIRKTLGdliprhqqvFSMNQYFsgvkipdPEDMetlelkfpNISYSALGFL 264
Cdd:cd05629   231 WWSLGAIMFECLIG---WPPFCSENSHETYRKIIN---------WRETLYF-------PDDI--------HLSVEAEDLI 283
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1039741915 265 KGcLHMDPAERL---TCEQLLQHPYF-----DSIREV 293
Cdd:cd05629   284 RR-LITNAENRLgrgGAHEIKSHPFFrgvdwDTIRQI 319
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
4-284 3.60e-14

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 71.58  E-value: 3.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGK--IGEGSYGVVFKCRNRDTGQIVAIKRFleteddPViKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd13995     4 YRNIGSdfIPRGAFGKVYLAQDTKTKKRMACKLI------PV-EQFKPSDVEIQACFRHENIAELYGALLWEETVHLFME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDH-TVLHELDRYQrgvpePLVK-NITW---QTLQAVNFCHKHNCIHRDVKPENILITKQSAIkLCDFGFARLLTGPGD 156
Cdd:cd13995    77 AGEGgSVLEKLESCG-----PMREfEIIWvtkHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV-LVDFGLSVQMTEDVY 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 157 YYTDYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLW----PGKSDVDQLYLIrktlgdliprHQQVfsmn 232
Cdd:cd13995   151 VPKDLRGTEIYMSPEVILC-RGHNTKADIYSLGATIIHMQTGSPPWvrryPRSAYPSYLYII----------HKQA---- 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 233 qyfsgvkiPDPEDMETlelkfpNISYSALGFLKGCLHMDPAERLTCEQLLQH 284
Cdd:cd13995   216 --------PPLEDIAQ------DCSPAMRELLEAALERNPNHRSSAAELLKH 253
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
9-281 3.78e-14

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 71.67  E-value: 3.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCR-NRDTGqiVAIKRFLETEDDPvikKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTV 87
Cdd:cd05068    15 KLGSGQFGEVWEGLwNNTTP--VAVKTLKPGTMDP---EDFLREAQIMKKLRHPKLIQLYAVCTLEEPIYIITELMKHGS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  88 LHE-LDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPgDYYTDYVATRW 166
Cdd:cd05068    90 LLEyLQGKGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARVIKVE-DEYEAREGAKF 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 167 ---YRSPElLVGDTQYGPPVDVWAIGCVFAELLS-GVPLWPGKSDVDQLylirktlgdliprhQQVfsmnqyFSGVKIPD 242
Cdd:cd05068   169 pikWTAPE-AANYNRFSIKSDVWSFGILLTEIVTyGRIPYPGMTNAEVL--------------QQV------ERGYRMPC 227
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1039741915 243 PedmetlelkfPNISYSALGFLKGCLHMDPAERLTCEQL 281
Cdd:cd05068   228 P----------PNCPPQLYDIMLECWKADPMERPTFETL 256
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
9-211 4.25e-14

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 71.59  E-value: 4.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTgqiVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVnLLEVFRRKRRLHLVFEYCD---- 84
Cdd:cd14150     7 RIGTGSFGTVFRGKWHGD---VAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNIL-LFMGFMTRPNFAIITQWCEgssl 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 ----HTVLHELDRYQRgvpeplvKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARlltgpgdyytd 160
Cdd:cd14150    83 yrhlHVTETRFDTMQL-------IDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLAT----------- 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039741915 161 yVATRW--------------YRSPELL-VGDTQ-YGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQL 211
Cdd:cd14150   145 -VKTRWsgsqqveqpsgsilWMAPEVIrMQDTNpYSFQSDVYAYGVVLYELMSGTLPYSNINNRDQI 210
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
3-189 5.14e-14

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 71.52  E-value: 5.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIK-------------------RFLETEDDPVIKKIA-----LREIRMLKQL 58
Cdd:cd14200     1 QYKLQSEIGKGSYGVVKLAYNESDDKYYAMKvlskkkllkqygfprrpppRGSKAAQGEQAKPLAplervYQEIAILKKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  59 KHPNLVNLLEVFR--RKRRLHLVFEY----------CDHTVLHELDR-YQRGVpeplvknitwqtLQAVNFCHKHNCIHR 125
Cdd:cd14200    81 DHVNIVKLIEVLDdpAEDNLYMVFDLlrkgpvmevpSDKPFSEDQARlYFRDI------------VLGIEYLHYQKIVHR 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 126 DVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYVATRWYRSPELLVGDTQ--YGPPVDVWAIG 189
Cdd:cd14200   149 DIKPSNLLLGDDGHVKIADFGVSNQFEGNDALLSSTAGTPAFMAPETLSDSGQsfSGKALDVWAMG 214
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
8-197 5.22e-14

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 70.84  E-value: 5.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   8 GKIGEGSYGVVFK--CRNRDTGQI-VAIKrFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRrLHLVFEYCD 84
Cdd:cd05060     1 KELGHGNFGSVRKgvYLMKSGKEVeVAVK-TLKQEHEKAGKKEFLREASVMAQLDHPCIVRLIGVCKGEP-LMLVMELAP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLtGPG-DYYTDYVA 163
Cdd:cd05060    79 LGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRAL-GAGsDYYRATTA 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1039741915 164 TRW---YRSPELLvgdtQYG---PPVDVWAIGCVFAELLS 197
Cdd:cd05060   158 GRWplkWYAPECI----NYGkfsSKSDVWSYGVTLWEAFS 193
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
13-197 5.75e-14

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 71.20  E-value: 5.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  13 GSYGVVFKCRNRDtgQIVAIKRFLETEddpviKK--IALREIRMLKQLKHPNLVNLLEVfrRKRRLHLVFEYCDHTVLHE 90
Cdd:cd14053     6 GRFGAVWKAQYLN--RLVAVKIFPLQE-----KQswLTEREIYSLPGMKHENILQFIGA--EKHGESLEAEYWLITEFHE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  91 ldryqRGVPEPLVKN--ITWQTL--------QAVNFCH----------KHNCIHRDVKPENILITKQSAIKLCDFGFARL 150
Cdd:cd14053    77 -----RGSLCDYLKGnvISWNELckiaesmaRGLAYLHedipatngghKPSIAHRDFKSKNVLLKSDLTACIADFGLALK 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039741915 151 LT---GPGDYYtDYVATRWYRSPELLVGDTQYGPP----VDVWAIGCVFAELLS 197
Cdd:cd14053   152 FEpgkSCGDTH-GQVGTRRYMAPEVLEGAINFTRDaflrIDMYAMGLVLWELLS 204
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
2-224 6.66e-14

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 70.84  E-value: 6.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQiVAIKRFletEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd05072     7 ESIKLVKKLGAGQFGEVWMGYYNNSTK-VAVKTL---KPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELDRYQRGVPEPLVKNITW--QTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgpGDYYT 159
Cdd:cd05072    83 YMAKGSLLDFLKSDEGGKVLLPKLIDFsaQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIE--DNEYT 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 160 DYVATRW---YRSPELLvgdtQYGP---PVDVWAIGCVFAELLS-GVPLWPGKSDVDQLYLIRKtlGDLIPR 224
Cdd:cd05072   161 AREGAKFpikWTAPEAI----NFGSftiKSDVWSFGILLYEIVTyGKIPYPGMSNSDVMSALQR--GYRMPR 226
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
9-207 1.14e-13

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 70.30  E-value: 1.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQiVAIKRFLETEDDPvikKIALREIRMLKQLKHPNLVNLLEVFRRKRrLHLVFEYCDHTVL 88
Cdd:cd05067    14 RLGAGQFGEVWMGYYNGHTK-VAIKSLKQGSMSP---DAFLAEANLMKQLQHQRLVRLYAVVTQEP-IYIITEYMENGSL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  89 HELDRYQRGVPEPLVK--NITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGpgdyyTDYVA--- 163
Cdd:cd05067    89 VDFLKTPSGIKLTINKllDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIED-----NEYTAreg 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 164 ----TRWyRSPELLvgdtQYGP---PVDVWAIGCVFAELLS-GVPLWPGKSD 207
Cdd:cd05067   164 akfpIKW-TAPEAI----NYGTftiKSDVWSFGILLTEIVThGRIPYPGMTN 210
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
22-310 1.17e-13

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 71.59  E-value: 1.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  22 RNRDTGQIVAIK----------RFLETEDDPViKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLHEL 91
Cdd:PTZ00267   77 RNPTTAAFVATRgsdpkekvvaKFVMLNDERQ-AAYARSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQ 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  92 --DRYQRGVP--EPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPG--DYYTDYVATR 165
Cdd:PTZ00267  156 ikQRLKEHLPfqEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVslDVASSFCGTP 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 166 WYRSPELLvGDTQYGPPVDVWAIGCVFAELLSgvplwpgksdvdqlyLIRKTLGdliPRHQQVfsMNQYFSGVKIPdped 245
Cdd:PTZ00267  236 YYLAPELW-ERKRYSKKADMWSLGVILYELLT---------------LHRPFKG---PSQREI--MQQVLYGKYDP---- 290
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 246 metlelkFP-NISYSALGFLKGCLHMDPAERLTCEQLLQHPY-------FDSIREVGELTRQHDKpaRKTLRQ 310
Cdd:PTZ00267  291 -------FPcPVSSGMKALLDPLLSKNPALRPTTQQLLHTEFlkyvanlFQDIVRHSETISPHDR--EEILRQ 354
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
10-200 1.18e-13

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 70.07  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRdtGQIVAIK--RFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTV 87
Cdd:cd14146     2 IGVGGFGKVYRATWK--GQEVAVKaaRQDPDEDIKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  88 LHE---------LDRYQRGVPEPLVKNITWQTLQAVNFCHKHN---CIHRDVKPENILITKQ--------SAIKLCDFGF 147
Cdd:cd14146    80 LNRalaaanaapGPRRARRIPPHILVNWAVQIARGMLYLHEEAvvpILHRDLKSSNILLLEKiehddicnKTLKITDFGL 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 148 AR------LLTGPGDYYtdyvatrwYRSPElLVGDTQYGPPVDVWAIGCVFAELLSG-VP 200
Cdd:cd14146   160 ARewhrttKMSAAGTYA--------WMAPE-VIKSSLFSKGSDIWSYGVLLWELLTGeVP 210
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
5-207 1.31e-13

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 70.07  E-value: 1.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   5 EKIGKIGEGSYGVVFkcRNRDTGQiVAIkRFLE----TEDDPVIKKialREIRMLKQLKHPNLVNLLEVFRRKRRLHLVF 80
Cdd:cd14063     3 EIKEVIGKGRFGRVH--RGRWHGD-VAI-KLLNidylNEEQLEAFK---EEVAAYKNTRHDNLVLFMGACMDPPHLAIVT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  81 EYCDHTVLHELDRYQRG-VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIkLCDFGFARL--LTGPG-- 155
Cdd:cd14063    76 SLCKGRTLYSLIHERKEkFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLENGRVV-ITDFGLFSLsgLLQPGrr 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 156 -------DYYTDYVATRWYR--SPELLVGDT-QYGPPVDVWAIGCVFAELLSGVplWPGKSD 207
Cdd:cd14063   155 edtlvipNGWLCYLAPEIIRalSPDLDFEESlPFTKASDVYAFGTVWYELLAGR--WPFKEQ 214
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
7-283 1.32e-13

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 70.82  E-value: 1.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   7 IGK-IGEGSYGVVFKC------RNRDTGQI-VAIKRFletEDDPVIKKIA--LREIRMLKQL-KHPNLVNLLEVFRRKRR 75
Cdd:cd05100    16 LGKpLGEGCFGQVVMAeaigidKDKPNKPVtVAVKML---KDDATDKDLSdlVSEMEMMKMIgKHKNIINLLGACTQDGP 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  76 LHLVFEYCDHTVLHELDRYQR-----------GVPEPLVK-----NITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA 139
Cdd:cd05100    93 LYVLVEYASKGNLREYLRARRppgmdysfdtcKLPEEQLTfkdlvSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNV 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 140 IKLCDFGFARLLTGPgDYYTDYVATRW---YRSPELLVgDTQYGPPVDVWAIGCVFAEL--LSGVPlWPGKSdVDQLYLI 214
Cdd:cd05100   173 MKIADFGLARDVHNI-DYYKKTTNGRLpvkWMAPEALF-DRVYTHQSDVWSFGVLLWEIftLGGSP-YPGIP-VEELFKL 248
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 215 RKtlgdliprhqqvfsmnqyfSGVKIPDPedmetlelkfPNISYSALGFLKGCLHMDPAERLTCEQLLQ 283
Cdd:cd05100   249 LK-------------------EGHRMDKP----------ANCTHELYMIMRECWHAVPSQRPTFKQLVE 288
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
10-203 1.69e-13

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 69.43  E-value: 1.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIkkiaLREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLH 89
Cdd:cd14155     1 IGSGFFSEVYKVRHRTSGQVMALKMNTLSSNRANM----LREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNLE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  90 ELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQ----SAIkLCDFGFARLLTGPGDYYT--DYVA 163
Cdd:cd14155    77 QLLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDengyTAV-VGDFGLAEKIPDYSDGKEklAVVG 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1039741915 164 TRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLSGVPLWP 203
Cdd:cd14155   156 SPYWMAPEVLRGEP-YNEKADVFSYGIILCEIIARIQADP 194
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
3-215 1.78e-13

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 69.86  E-value: 1.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCR-------NRDTgqIVAIKrFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRR 75
Cdd:cd05050     6 NIEYVRDIGQGAFGRVFQARapgllpyEPFT--MVAVK-MLKEEASADMQADFQREAALMAEFDHPNIVKLLGVCAVGKP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  76 LHLVFEYCDHTVLHELDRY----------------QRGVPEPLVKNITWQTLQAVN------FCHKHNCIHRDVKPENIL 133
Cdd:cd05050    83 MCLLFEYMAYGDLNEFLRHrspraqcslshstssaRKCGLNPLPLSCTEQLCIAKQvaagmaYLSERKFVHRDLATRNCL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 134 ITKQSAIKLCDFGFARLLTGpGDYY----TDYVATRWYrSPELLVGDtQYGPPVDVWAIGCVFAELLS-GVPLWPGKSDV 208
Cdd:cd05050   163 VGENMVVKIADFGLSRNIYS-ADYYkaseNDAIPIRWM-PPESIFYN-RYTTESDVWAYGVVLWEIFSyGMQPYYGMAHE 239

                  ....*..
gi 1039741915 209 DQLYLIR 215
Cdd:cd05050   240 EVIYYVR 246
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
7-221 1.79e-13

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 69.80  E-value: 1.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   7 IGKIGEGSYGVVFKCRNR-----DTGQIVAIKRFLETEDDPVIKKIAlREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd05046    10 ITTLGRGEFGEVFLAKAKgieeeGGETLVLVKALQKTKDENLQSEFR-RELDMFRKLSHKNVVRLLGLCREAEPHYMILE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELDRYQRGVPEPLV-KNITwqTLQAVNFCH----------KHNCIHRDVKPENILITKQSAIKLcdfGFARL 150
Cdd:cd05046    89 YTDLGDLKQFLRATKSKDEKLKpPPLS--TKQKVALCTqialgmdhlsNARFVHRDLAARNCLVSSQREVKV---SLLSL 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039741915 151 LTGPgdYYTDY-------VATRWYrSPELLVGDtQYGPPVDVWAIGCVFAELLSGVPLwPGKSDVDQLYLIRKTLGDL 221
Cdd:cd05046   164 SKDV--YNSEYyklrnalIPLRWL-APEAVQED-DFSTKSDVWSFGVLMWEVFTQGEL-PFYGLSDEEVLNRLQAGKL 236
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
10-146 1.93e-13

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 66.70  E-value: 1.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRfleTEDDPVIKKIAL-REIRMLKQLK--HPNLVNLLEVFRRKRRLHLVFEYCDHT 86
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIGVAVKI---GDDVNNEEGEDLeSEMDILRRLKglELNIPKVLVTEDVDGPNILLMELVKGG 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039741915  87 vlhELDRYQRGV--PEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFG 146
Cdd:cd13968    78 ---TLIAYTQEEelDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
9-211 2.38e-13

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 69.32  E-value: 2.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTgqiVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVnLLEVFRRKRRLHLVFEYCDHTVL 88
Cdd:cd14151    15 RIGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSSL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  89 -HELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLT--GPGDYYTDYVATR 165
Cdd:cd14151    91 yHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSrwSGSHQFEQLSGSI 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1039741915 166 WYRSPEL--LVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQL 211
Cdd:cd14151   171 LWMAPEVirMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQI 218
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
5-197 2.91e-13

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 68.92  E-value: 2.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   5 EKIGKIGEGSYGVVFKCRNRdtGQIVAIKRFletEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:cd05039     9 KLGELIGKGEFGDVMLGDYR--GQKVAVKCL---KDDSTAAQAFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIVTEYMA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVLHELDRyQRG---VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARlltgPGDYYTD- 160
Cdd:cd05039    84 KGSLVDYLR-SRGravITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAK----EASSNQDg 158
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1039741915 161 -YVATRWyRSPELLvGDTQYGPPVDVWAIGCVFAELLS 197
Cdd:cd05039   159 gKLPIKW-TAPEAL-REKKFSTKSDVWSFGILLWEIYS 194
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
9-216 2.97e-13

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 69.27  E-value: 2.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCR----NRDTGQIVAIKRfLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:cd05090    12 ELGECAFGKIYKGHlylpGMDHAQLVAIKT-LKDYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFEFMN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVLHEL--------DRYQRGVPEPLVKN---------ITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGF 147
Cdd:cd05090    91 QGDLHEFlimrsphsDVGCSSDEDGTVKSsldhgdflhIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKISDLGL 170
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039741915 148 ARLLTGpGDYY----TDYVATRWYRSPELLVGdtQYGPPVDVWAIGCVFAELLS-GVPLWPGKSDVDQLYLIRK 216
Cdd:cd05090   171 SREIYS-SDYYrvqnKSLLPIRWMPPEAIMYG--KFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMVRK 241
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
1-200 2.99e-13

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 70.09  E-value: 2.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEddpVIKKIALREIR----MLKQLKHPNLVNLLEVFRRKRRL 76
Cdd:cd05627     1 LDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKAD---MLEKEQVAHIRaerdILVEADGAWVVKMFYSFQDKRNL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  77 HLVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFG---------- 146
Cdd:cd05627    78 YLIMEFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGlctglkkahr 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 147 --FARLLTG--PGDY----------------------YTDyVATRWYRSPELLVgDTQYGPPVDVWAIGCVFAELLSGVP 200
Cdd:cd05627   158 teFYRNLTHnpPSDFsfqnmnskrkaetwkknrrqlaYST-VGTPDYIAPEVFM-QTGYNKLCDWWSLGVIMYEMLIGYP 235
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
58-286 3.22e-13

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 68.37  E-value: 3.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  58 LKHPNLVNLLEVFRRKRRLHLVFEYcDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQ 137
Cdd:cd14024    42 GPHEGVCSVLEVVIGQDRAYAFFSR-HYGDMHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDE 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 138 SAIKLCDFGF--ARLLTGPGDYYTDYVATRWYRSPELLVGDTQY-GPPVDVWAIG-CVFAELLSGVPLwpgkSDVDQLYL 213
Cdd:cd14024   121 LRTKLVLVNLedSCPLNGDDDSLTDKHGCPAYVGPEILSSRRSYsGKAADVWSLGvCLYTMLLGRYPF----QDTEPAAL 196
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 214 IRKTlgdliprHQQVFSMnqyfsgvkipdPEdmetlelkfpNISYSALGFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:cd14024   197 FAKI-------RRGAFSL-----------PA----------WLSPGARCLVSCMLRRSPAERLKASEILLHPW 241
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
10-198 4.16e-13

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 68.52  E-value: 4.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRdtGQIVAIK--RFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTV 87
Cdd:cd14147    11 IGIGGFGKVYRGSWR--GELVAVKaaRQDPDEDISVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAGGP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  88 LHELDRYQRGVPEPLVkNITWQTLQAVNFCHKHN---CIHRDVKPENILIT--------KQSAIKLCDFGFARLLTGPGD 156
Cdd:cd14147    89 LSRALAGRRVPPHVLV-NWAVQIARGMHYLHCEAlvpVIHRDLKSNNILLLqpienddmEHKTLKITDFGLAREWHKTTQ 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1039741915 157 YYTdyVATRWYRSPELLVGDTqYGPPVDVWAIGCVFAELLSG 198
Cdd:cd14147   168 MSA--AGTYAWMAPEVIKAST-FSKGSDVWSFGVLLWELLTG 206
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
7-197 4.35e-13

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 68.65  E-value: 4.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   7 IGKIGEGSYGVVF--KCRNRDTGQ---IVAIKRfLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd05049    10 KRELGEGAFGKVFlgECYNLEPEQdkmLVAVKT-LKDASSPDARKDFEREAELLTNLQHENIVKFYGVCTEGDPLLMVFE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELDR----------YQRGVPEPLVKN----ITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGF 147
Cdd:cd05049    89 YMEHGDLNKFLRshgpdaaflaSEDSAPGELTLSqllhIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLVVKIGDFGM 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039741915 148 ARLLtgpgdYYTDY--------VATRWYrSPELLVGDTqYGPPVDVWAIGCVFAELLS 197
Cdd:cd05049   169 SRDI-----YSTDYyrvgghtmLPIRWM-PPESILYRK-FTTESDVWSFGVVLWEIFT 219
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
9-283 6.60e-13

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 67.75  E-value: 6.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCR-NRDTGQI--VAIKrFLETE--DDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRrLHLVFEYC 83
Cdd:cd05040     2 KLGDGSFGVVRRGEwTTPSGKViqVAVK-CLKSDvlSQPNAMDDFLKEVNAMHSLDHPNLIRLYGVVLSSP-LMMVTELA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 DHTVLheLDRYQRGVPEPLVKNITWQTLQAVN---FCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYT- 159
Cdd:cd05040    80 PLGSL--LDRLRKDQGHFLISTLCDYAVQIANgmaYLESKRFIHRDLAARNILLASKDKVKIGDFGLMRALPQNEDHYVm 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 160 ---DYVATRWYrSPELLvGDTQYGPPVDVWAIGCVFAELLS-GVPLWPGKSDVDQLYLIRKTlGDLIPRhqqvfsmnqyf 235
Cdd:cd05040   158 qehRKVPFAWC-APESL-KTRKFSHASDVWMFGVTLWEMFTyGEEPWLGLNGSQILEKIDKE-GERLER----------- 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039741915 236 sgvkiPD--PEDMETLELKfpnisysalgflkgCLHMDPAERLTCEQLLQ 283
Cdd:cd05040   224 -----PDdcPQDIYNVMLQ--------------CWAHKPADRPTFVALRD 254
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
10-204 7.34e-13

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 68.07  E-value: 7.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVV-----FKCRNRDTGQIVAIKrFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:cd05045     8 LGEGEFGKVvkataFRLKGRAGYTTVAVK-MLKENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLLIVEYAK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVLHELDRYQRGV--------------------PEPL----VKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAI 140
Cdd:cd05045    87 YGSLRSFLRESRKVgpsylgsdgnrnssyldnpdERALtmgdLISFAWQISRGMQYLAEMKLVHRDLAARNVLVAEGRKM 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 141 KLCDFGFARLLTGPGDYYT---DYVATRWYrSPELLVgDTQYGPPVDVWAIGCVFAEL--LSGVPlWPG 204
Cdd:cd05045   167 KISDFGLSRDVYEEDSYVKrskGRIPVKWM-AIESLF-DHIYTTQSDVWSFGVLLWEIvtLGGNP-YPG 232
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
7-197 8.35e-13

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 67.60  E-value: 8.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   7 IGKIGEGSYGVVFKCRNRdtGQI-VAIKRFLE---TEDDpvikkiALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEY 82
Cdd:cd05113     9 LKELGTGQFGVVKYGKWR--GQYdVAIKMIKEgsmSEDE------FIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  83 CDHTVLHELDRYQRGVPEPL-VKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgpGDYYTDY 161
Cdd:cd05113    81 MANGCLLNYLREMRKRFQTQqLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVL--DDEYTSS 158
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1039741915 162 VATRW---YRSPELLVGdTQYGPPVDVWAIGCVFAELLS 197
Cdd:cd05113   159 VGSKFpvrWSPPEVLMY-SKFSSKSDVWAFGVLMWEVYS 196
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
9-281 9.71e-13

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 67.45  E-value: 9.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFK---CRNRDTGQIVAIKRFlETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRrKRRLHLVFEYCDH 85
Cdd:cd05056    13 CIGEGQFGDVYQgvyMSPENEKIAVAVKTC-KNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVIT-ENPVWIVMELAPL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 TVLHE-LDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLtgpgDYYTDYVAT 164
Cdd:cd05056    91 GELRSyLQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYM----EDESYYKAS 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 165 R------WYrSPElLVGDTQYGPPVDVWAIG-CVFAELLSGVPLWPGKSDVDQLYLIRKtlgdliprhqqvfsmnqyfsG 237
Cdd:cd05056   167 KgklpikWM-APE-SINFRRFTSASDVWMFGvCMWEILMLGVKPFQGVKNNDVIGRIEN--------------------G 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1039741915 238 VKIPDPEdmetlelKFPNISYSalgFLKGCLHMDPAERLTCEQL 281
Cdd:cd05056   225 ERLPMPP-------NCPPTLYS---LMTKCWAYDPSKRPRFTEL 258
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
1-197 1.13e-12

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 67.75  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEKIGKIGEGSYGVVFKCR----------------NRDTGQIVAIKRfLETEDDPVIKKIALREIRMLKQLKHPNLV 64
Cdd:cd05051     4 REKLEFVEKLGEGQFGEVHLCEanglsdltsddfigndNKDEPVLVAVKM-LRPDASKNAREDFLKEVKIMSQLKDPNIV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  65 NLLEVFRRKRRLHLVFEYCDhtvLHELDRY-QRGVPE-PLVKNITWQTLQAVNFCH-------------KHNCIHRDVKP 129
Cdd:cd05051    83 RLLGVCTRDEPLCMIVEYME---NGDLNQFlQKHEAEtQGASATNSKTLSYGTLLYmatqiasgmkyleSLNFVHRDLAT 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 130 ENILITKQSAIKLCDFGFARLLTGpGDYY----TDYVATRWYRSPELLVGdtQYGPPVDVWAIGCVFAELLS 197
Cdd:cd05051   160 RNCLVGPNYTIKIADFGMSRNLYS-GDYYriegRAVLPIRWMAWESILLG--KFTTKSDVWAFGVTLWEILT 228
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
9-250 1.19e-12

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 67.36  E-value: 1.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCR-NRDTGqiVAIKRFletedDPVIKKIA--LREIRMLKQLKHPNLVNLLEVFRRKRrLHLVFEYCDH 85
Cdd:cd05073    18 KLGAGQFGEVWMATyNKHTK--VAVKTM-----KPGSMSVEafLAEANVMKTLQHDKLVKLHAVVTKEP-IYIITEFMAK 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 TVLHELDRYQRGVPEPLVKNITW--QTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGpgdyyTDYVA 163
Cdd:cd05073    90 GSLLDFLKSDEGSKQPLPKLIDFsaQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIED-----NEYTA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 164 -------TRWyRSPELLvgdtQYGP---PVDVWAIGCVFAELLS-GVPLWPGKSDVDQLYLIRKTLgdlipRHQQVFSMN 232
Cdd:cd05073   165 regakfpIKW-TAPEAI----NFGSftiKSDVWSFGILLMEIVTyGRIPYPGMSNPEVIRALERGY-----RMPRPENCP 234
                         250       260
                  ....*....|....*....|..
gi 1039741915 233 QYFSGVKI----PDPEDMETLE 250
Cdd:cd05073   235 EELYNIMMrcwkNRPEERPTFE 256
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
7-197 1.74e-12

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 66.42  E-value: 1.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   7 IGKIGEGSYGVVFKCRNRDTGQiVAIKRFLE---TEDDpvikkiALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYC 83
Cdd:cd05114     9 MKELGSGLFGVVRLGKWRAQYK-VAIKAIREgamSEED------FIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 DHTVLHELDRYQRGVPEP-LVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgpGDYYTDYV 162
Cdd:cd05114    82 ENGCLLNYLRQRRGKLSRdMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVL--DDQYTSSS 159
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1039741915 163 ATRW---YRSPELLvGDTQYGPPVDVWAIGCVFAELLS 197
Cdd:cd05114   160 GAKFpvkWSPPEVF-NYSKFSSKSDVWSFGVLMWEVFT 196
pknD PRK13184
serine/threonine-protein kinase PknD;
1-197 1.75e-12

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 68.64  E-value: 1.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   1 MEKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLET-EDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLV 79
Cdd:PRK13184    1 MQRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDlSENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  80 FEYCDHTVLHEL---DRYQRGVPEPLVKNITWQTL--------QAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFA 148
Cdd:PRK13184   81 MPYIEGYTLKSLlksVWQKESLSKELAEKTSVGAFlsifhkicATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAA 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 149 RL----------------------LTGPGdyytDYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLS 197
Cdd:PRK13184  161 IFkkleeedlldidvdernicyssMTIPG----KIVGTPDYMAPERLLG-VPASESTDIYALGVILYQMLT 226
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
10-198 2.13e-12

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 66.13  E-value: 2.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRdtGQIVAIKRFleteDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLhlVFEYCDHTVL- 88
Cdd:cd14068     2 LGDGGFGSVYRAVYR--GEDVAVKIF----NKHTSFRLLRQELVVLSHLHHPSLVALLAAGTAPRML--VMELAPKGSLd 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  89 HELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILI---TKQSAI--KLCDFGFARLLTGPGDYYTDyvA 163
Cdd:cd14068    74 ALLQQDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLftlYPNCAIiaKIADYGIAQYCCRMGIKTSE--G 151
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1039741915 164 TRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSG 198
Cdd:cd14068   152 TPGFRAPEVARGNVIYNQQADVYSFGLLLYDILTC 186
PTZ00284 PTZ00284
protein kinase; Provisional
106-286 2.33e-12

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 67.68  E-value: 2.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 106 ITWQTLQAVNFCHKH-NCIHRDVKPENILI-TKQSAI---------------KLCDFGfarlltGPGD---YYTDYVATR 165
Cdd:PTZ00284  236 IIFQTGVALDYFHTElHLMHTDLKPENILMeTSDTVVdpvtnralppdpcrvRICDLG------GCCDerhSRTAIVSTR 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 166 WYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDLiPRHQQVFSMNQ-----YFSGVKI 240
Cdd:PTZ00284  310 HYRSPEVVLG-LGWMYSTDMWSMGCIIYELYTGKLLYDTHDNLEHLHLMEKTLGRL-PSEWAGRCGTEearllYNSAGQL 387
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 241 ---PDPEDMETLELKFP---NISYSAL-GFLKGCLHMDPAERLTCEQLLQHPY 286
Cdd:PTZ00284  388 rpcTDPKHLARIARARPvreVIRDDLLcDLIYGLLHYDRQKRLNARQMTTHPY 440
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
9-198 2.54e-12

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 65.97  E-value: 2.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVAIKRFLETeDDPVIKKIALREIRMLKQLKHPNLVNLLEVFrrkrrlhLVFEYCDHT-- 86
Cdd:cd13975     7 ELGRGQYGVVYACDSWGGHFPCALKSVVPP-DDKHWNDLALEFHYTRSLPKHERIVSLHGSV-------IDYSYGGGSsi 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  87 -VLHELDRYQRGVPEPLVKNITWQT--------LQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFAR---LLTGp 154
Cdd:cd13975    79 aVLLIMERLHRDLYTGIKAGLSLEErlqialdvVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKpeaMMSG- 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1039741915 155 gdyytDYVATRWYRSPELLVGdtQYGPPVDVWAIGCVFAELLSG 198
Cdd:cd13975   158 -----SIVGTPIHMAPELFSG--KYDNSVDVYAFGILFWYLCAG 194
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
60-287 2.62e-12

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 65.83  E-value: 2.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  60 HPNLVNLLEVFRRKRRLHLVFEYcDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILIT--KQ 137
Cdd:cd14022    44 HSNINQITEIILGETKAYVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKdeER 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 138 SAIKLCDFGFARLLTGPGDYYTDYVATRWYRSPELLVGDTQY-GPPVDVWAIGCVFAELLSGvplwpgksdvdqlyliRK 216
Cdd:cd14022   123 TRVKLESLEDAYILRGHDDSLSDKHGCPAYVSPEILNTSGSYsGKAADVWSLGVMLYTMLVG----------------RY 186
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 217 TLGDLIPrhqqvfsmNQYFSGVKIPDPEDMETLELKfpnisysALGFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14022   187 PFHDIEP--------SSLFSKIRRGQFNIPETLSPK-------AKCLIRSILRREPSERLTSQEILDHPWF 242
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
18-292 2.71e-12

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. The STRAD-beta subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 66.82  E-value: 2.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  18 VFKCRNRDTGQIVAIKRF-LETEDDPVIKkIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLHELDR--Y 94
Cdd:cd08226    16 VYLARHTPTGTLVTVKITnLDNCSEEHLK-ALQNEVVLSHFFRHPNIMTHWTVFTEGSWLWVISPFMAYGSARGLLKtyF 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  95 QRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPG-------DYYTDYVATRWY 167
Cdd:cd08226    95 PEGMNEALIGNILYGAIKALNYLHQNGCIHRSVKASHILISGDGLVSLSGLSHLYSMVTNGqrskvvyDFPQFSTSVLPW 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 168 RSPELLVGDTQ-YGPPVDVWAIGCVFAELLSG-VPLwpgkSDVDQL-YLIRKTLG------DLIPRHQQVFSMNQYFSGV 238
Cdd:cd08226   175 LSPELLRQDLHgYNVKSDIYSVGITACELARGqVPF----QDMRRTqMLLQKLKGppysplDIFPFPELESRMKNSQSGM 250
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 239 KIPDPEDMETL---------ELKFP---NISYSALGFLKGCLHMDPAERLTCEQLLQHPYFDSIRE 292
Cdd:cd08226   251 DSGIGESVATSsmtrtmtseRLQTPsskTFSPAFHNLVELCLQQDPEKRPSASSLLSHSFFKQVKE 316
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
9-281 2.81e-12

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 66.07  E-value: 2.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCR-NRDTGQIVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDhtv 87
Cdd:cd05042     2 EIGNGWFGKVLLGEiYSGTSVAQVVVKELKASANPKEQDTFLKEGQPYRILQHPNILQCLGQCVEAIPYLLVMEFCD--- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  88 LHELDRYQRGVPEPLVKNITWQTLQ--------AVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARlltgpGDYYT 159
Cdd:cd05042    79 LGDLKAYLRSEREHERGDSDTRTLQrmacevaaGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLAH-----SRYKE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 160 DYVAT--------RWYrSPELL---------VGDTQYGppvDVWAIGCVFAELLS-GVPLWPGKSDVDQL-YLIRKtlgd 220
Cdd:cd05042   154 DYIETddklwfplRWT-APELVtefhdrllvVDQTKYS---NIWSLGVTLWELFEnGAQPYSNLSDLDVLaQVVRE---- 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 221 lipRHqqvfsmnqyfsgVKIPDPEdmetLELKFPNISYSALGFlkgCLhMDPAERLTCEQL 281
Cdd:cd05042   226 ---QD------------TKLPKPQ----LELPYSDRWYEVLQF---CW-LSPEQRPAAEDV 263
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
9-197 3.74e-12

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 65.74  E-value: 3.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVV----FKCRNRdtgQI-VAIKrFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRrLHLVFEYC 83
Cdd:cd05115    11 ELGSGNFGCVkkgvYKMRKK---QIdVAIK-VLKQGNEKAVRDEMMREAQIMHQLDNPYIVRMIGVCEAEA-LMLVMEMA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 DHTVLHE-LDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYV 162
Cdd:cd05115    86 SGGPLNKfLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKALGADDSYYKARS 165
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1039741915 163 ATRW---YRSPElLVGDTQYGPPVDVWAIGCVFAELLS 197
Cdd:cd05115   166 AGKWplkWYAPE-CINFRKFSSRSDVWSYGVTMWEAFS 202
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
10-290 4.97e-12

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 66.24  E-value: 4.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFleteDDPVIK-----KIALREIRMLKQLKH---PNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd05633    13 IGRGGFGEVYGCRKADTGKMYAMKCL----DKKRIKmkqgeTLALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLCFILD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHeLDRYQRGV-PEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTd 160
Cdd:cd05633    89 LMNGGDLH-YHLSQHGVfSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPHAS- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 yVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLgdliprhqqvfSMNqyfsgVKI 240
Cdd:cd05633   167 -VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTL-----------TVN-----VEL 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039741915 241 PDPEDMETLELkfpnisysalgfLKGCLHMDPAERLTC-----EQLLQHPYFDSI 290
Cdd:cd05633   230 PDSFSPELKSL------------LEGLLQRDVSKRLGChgrgaQEVKEHSFFKGI 272
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
2-250 5.32e-12

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 65.47  E-value: 5.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFK-CRNRDTGqiVAIKRFLETEDDPvikKIALREIRMLKQLKHPNLVNLLEVFRRkRRLHLVF 80
Cdd:cd05070     9 ESLQLIKRLGNGQFGEVWMgTWNGNTK--VAIKTLKPGTMSP---ESFLEEAQIMKKLKHDKLVQLYAVVSE-EPIYIVT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  81 EYCDHTVLHEL--DRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGpgdyy 158
Cdd:cd05070    83 EYMSKGSLLDFlkDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIED----- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 TDYVA-------TRWYRSPELLVGdtQYGPPVDVWAIGCVFAELLS-GVPLWPGKSDVDQLYLIRKtlGDLIPRHQQV-F 229
Cdd:cd05070   158 NEYTArqgakfpIKWTAPEAALYG--RFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVER--GYRMPCPQDCpI 233
                         250       260
                  ....*....|....*....|.
gi 1039741915 230 SMNQYFSGVKIPDPEDMETLE 250
Cdd:cd05070   234 SLHELMIHCWKKDPEERPTFE 254
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
5-197 5.45e-12

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 65.31  E-value: 5.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   5 EKIGKIGEGSYGVV----FKCRNRDTGQIVAIKRfLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRK--RRLHL 78
Cdd:cd05080     7 KKIRDLGEGHFGKVslycYDPTNDGTGEMVAVKA-LKADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQggKSLQL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCD-HTVLHELDRYQRGVPEPLVknITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDY 157
Cdd:cd05080    86 IMEYVPlGSLRDYLPKHSIGLAQLLL--FAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVPEGHEY 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1039741915 158 Y---TDYVATRWYRSPELLvGDTQYGPPVDVWAIGCVFAELLS 197
Cdd:cd05080   164 YrvrEDGDSPVFWYAPECL-KEYKFYYASDVWSFGVTLYELLT 205
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
51-197 5.86e-12

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 65.50  E-value: 5.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  51 EIRMLKQLKHPNLVNllevFR-----RKRRLHLVFEYCdHTVLHEL--DRYQRG---VPEPLVKNITWQTLQAVNFCHKH 120
Cdd:cd14001    55 EAKILKSLNHPNIVG----FRaftksEDGSLCLAMEYG-GKSLNDLieERYEAGlgpFPAATILKVALSIARALEYLHNE 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 121 NCI-HRDVKPENILITKQ-SAIKLCDFGFA----RLLTGPGDYYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAE 194
Cdd:cd14001   130 KKIlHGDIKSGNVLIKGDfESVKLCDFGVSlpltENLEVDSDPKAQYVGTEPWKAKEALEEGGVITDKADIFAYGLVLWE 209

                  ...
gi 1039741915 195 LLS 197
Cdd:cd14001   210 MMT 212
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
5-197 6.34e-12

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 65.13  E-value: 6.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   5 EKIGKIGEGSYGVVFK---CRNRDTGQI-VAIKRFLETEDDPVIKKIaLREIRMLKQLKHPNLVNLLEVFRRKRrLHLVF 80
Cdd:cd05057    10 EKGKVLGSGAFGTVYKgvwIPEGEKVKIpVAIKVLREETGPKANEEI-LDEAYVMASVDHPHLVRLLGICLSSQ-VQLIT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  81 EYCDHTVLHELDRYQRGVPEP-LVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYT 159
Cdd:cd05057    88 QLMPLGCLLDYVRNHRDNIGSqLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKLLDVDEKEYH 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1039741915 160 ---DYVATRWYRSPELLVGdtQYGPPVDVWAIGCVFAELLS 197
Cdd:cd05057   168 aegGKVPIKWMALESIQYR--IYTHKSDVWSYGVTVWELMT 206
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
49-287 6.65e-12

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 65.34  E-value: 6.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  49 LREIRMLKQLK-HPNLVNLLEVFRRKRRLH-----LVFEYCDHTVLHELDR-YQRGVPEPLVKNITWQTLQAVNFCHKHN 121
Cdd:cd14020    51 AKERAALEQLQgHRNIVTLYGVFTNHYSANvpsrcLLLELLDVSVSELLLRsSNQGCSMWMIQHCARDVLEALAFLHHEG 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 122 CIHRDVKPENILIT-KQSAIKLCDFGfarLLTGPGDYYTDYVATRWYRSPEL----------LVGDTQYGPPVDVWAIGC 190
Cdd:cd14020   131 YVHADLKPRNILWSaEDECFKLIDFG---LSFKEGNQDVKYIQTDGYRAPEAelqnclaqagLQSETECTSAVDLWSLGI 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 191 VFAELLSGVPLwpgKSDV-DQLYlirKTLGDLIPRHqqVFSMNQyfsgvkipdpedmetleLKFPNI-SYSALGFLKGCL 268
Cdd:cd14020   208 VLLEMFSGMKL---KHTVrSQEW---KDNSSAIIDH--IFASNA-----------------VVNPAIpAYHLRDLIKSML 262
                         250
                  ....*....|....*....
gi 1039741915 269 HMDPAERLTCEQLLQHPYF 287
Cdd:cd14020   263 HNDPGKRATAEAALCSPFF 281
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
10-290 7.40e-12

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 65.45  E-value: 7.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIVAIKRFleteDDPVIK-----KIALREIRMLKQLKH---PNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd14223     8 IGRGGFGEVYGCRKADTGKMYAMKCL----DKKRIKmkqgeTLALNERIMLSLVSTgdcPFIVCMSYAFHTPDKLSFILD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHeLDRYQRGV-PEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTd 160
Cdd:cd14223    84 LMNGGDLH-YHLSQHGVfSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDFSKKKPHAS- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 161 yVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGdliprhqqvfsmnqyfSGVKI 240
Cdd:cd14223   162 -VGTHGYMAPEVLQKGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLT----------------MAVEL 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039741915 241 PDPEDMETLELkfpnisysalgfLKGCLHMDPAERLTC-----EQLLQHPYFDSI 290
Cdd:cd14223   225 PDSFSPELRSL------------LEGLLQRDVNRRLGCmgrgaQEVKEEPFFRGL 267
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
10-277 8.31e-12

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 65.15  E-value: 8.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRdtGQIVAIKRFLETEDDPVIKKialREIRMLKQLKHPNLVNLLEVFRRKR----RLHLVFEYCDH 85
Cdd:cd13998     3 IGKGRFGEVWKASLK--NEPVAVKIFSSRDKQSWFRE---KEIYRTPMLKHENILQFIAADERDTalrtELWLVTAFHPN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 TVLHE-LDRYqrgvpeplvkNITWQTL------QAVNFCHKHNCI-----------HRDVKPENILITKQSAIKLCDFGF 147
Cdd:cd13998    78 GSL*DyLSLH----------TIDWVSLcrlalsVARGLAHLHSEIpgctqgkpaiaHRDLKSKNILVKNDGTCCIADFGL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 148 ARLLTgPGDYYTD-----YVATRWYRSPELLVGDTQYGPP-----VDVWAIGCVFAELLSGVPLWPGKSDVDQLylirkT 217
Cdd:cd13998   148 AVRLS-PSTGEEDnanngQVGTKRYMAPEVLEGAINLRDFesfkrVDIYAMGLVLWEMASRCTDLFGIVEEYKP-----P 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 218 LGDLIPRHQQVFSMNQYFSgvkipdpedMETLELKFPNISYSALGF------LKGCLHMDPAERLT 277
Cdd:cd13998   222 FYSEVPNHPSFEDMQEVVV---------RDKQRPNIPNRWLSHPGLqslaetIEECWDHDAEARLT 278
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
9-197 8.42e-12

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 64.51  E-value: 8.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKcrNRDTGQIVAIKRFleteDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRrKRRLHLVFEYCDHTVL 88
Cdd:cd05083    13 IIGEGEFGAVLQ--GEYMGQKVAVKNI----KCDVTAQAFLEETAVMTKLQHKNLVRLLGVIL-HNGLYIVMELMSKGNL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  89 HELDRyQRG---VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARllTGPGDYYTDYVATR 165
Cdd:cd05083    86 VNFLR-SRGralVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAK--VGSMGVDNSRLPVK 162
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1039741915 166 WyRSPELLvGDTQYGPPVDVWAIGCVFAELLS 197
Cdd:cd05083   163 W-TAPEAL-KNKKFSSKSDVWSYGVLLWEVFS 192
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
11-197 9.88e-12

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 64.21  E-value: 9.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  11 GEGSYGVVFKCRNRDTGQIVAIKRFLETEddpvikkialREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLHE 90
Cdd:cd14060     2 GGGSFGSVYRAIWVSQDKEVAVKKLLKIE----------KEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  91 LDRYQRGVPEPLVKNITWQT--LQAVNFCHKH---NCIHRDVKPENILITKQSAIKLCDFGFARLLTgpGDYYTDYVATR 165
Cdd:cd14060    72 YLNSNESEEMDMDQIMTWATdiAKGMHYLHMEapvKVIHRDLKSRNVVIAADGVLKICDFGASRFHS--HTTHMSLVGTF 149
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1039741915 166 WYRSPELLvgdtqYGPPV----DVWAIGCVFAELLS 197
Cdd:cd14060   150 PWMAPEVI-----QSLPVsetcDTYSYGVVLWEMLT 180
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
9-281 1.04e-11

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 64.17  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQiVAIKRFLETEDDPvikKIALREIRMLKQLKHPNLVNLLEVFRRKRrLHLVFEYCDHTVL 88
Cdd:cd14203     2 KLGQGCFGEVWMGTWNGTTK-VAIKTLKPGTMSP---EAFLEEAQIMKKLRHDKLVQLYAVVSEEP-IYIVTEFMSKGSL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  89 HEL--DRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTgpGDYYTDYVATRW 166
Cdd:cd14203    77 LDFlkDGEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIE--DNEYTARQGAKF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 167 ---YRSPE-LLVGdtQYGPPVDVWAIGCVFAELLSG--VPlWPGKSDvdqlyliRKTLgdliprhqqvfsmNQYFSGVKI 240
Cdd:cd14203   155 pikWTAPEaALYG--RFTIKSDVWSFGILLTELVTKgrVP-YPGMNN-------REVL-------------EQVERGYRM 211
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1039741915 241 PDPedmetlelkfPNISYSALGFLKGCLHMDPAERLTCEQL 281
Cdd:cd14203   212 PCP----------PGCPESLHELMCQCWRKDPEERPTFEYL 242
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
10-196 1.10e-11

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 64.60  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRdtGQIVAIKRFLETEDDPVIKKialREIRMLKQLKHPNLVNLLEVFRRKR----RLHLVFEYCDH 85
Cdd:cd14056     3 IGKGRYGEVWLGKYR--GEKVAVKIFSSRDEDSWFRE---TEIYQTVMLRHENILGFIAADIKSTgswtQLWLITEYHEH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 TVLHE-LDRYQRGVPEPLvkNITWQTlqAVNFCHKHNCI----------HRDVKPENILITKQSAIKLCDFGFA---RLL 151
Cdd:cd14056    78 GSLYDyLQRNTLDTEEAL--RLAYSA--ASGLAHLHTEIvgtqgkpaiaHRDLKSKNILVKRDGTCCIADLGLAvryDSD 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 152 TGPGDYYTDY-VATRWYRSPELLvgDTQYGPP-------VDVWAIGCVFAELL 196
Cdd:cd14056   154 TNTIDIPPNPrVGTKRYMAPEVL--DDSINPKsfesfkmADIYSFGLVLWEIA 204
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
105-204 1.21e-11

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 65.43  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 105 NITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTD---YVATRWYrSPELLVgDTQYGP 181
Cdd:cd05105   241 SFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKgstFLPVKWM-APESIF-DNLYTT 318
                          90       100
                  ....*....|....*....|....
gi 1039741915 182 PVDVWAIGCVFAELLS-GVPLWPG 204
Cdd:cd05105   319 LSDVWSYGILLWEIFSlGGTPYPG 342
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
9-197 1.30e-11

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 64.57  E-value: 1.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCR--------------NRDTGQ--IVAIKrFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRR 72
Cdd:cd05096    12 KLGEGQFGEVHLCEvvnpqdlptlqfpfNVRKGRplLVAVK-ILRPDANKNARNDFLKEVKILSRLKDPNIIRLLGVCVD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  73 KRRLHLVFEYCDHTVL-------HELDRYQRGVPE------------PLVKNITWQTLQAVNFCHKHNCIHRDVKPENIL 133
Cdd:cd05096    91 EDPLCMITEYMENGDLnqflsshHLDDKEENGNDAvppahclpaisySSLLHVALQIASGMKYLSSLNFVHRDLATRNCL 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039741915 134 ITKQSAIKLCDFGFARLLTGpGDYY----TDYVATRWYRSPELLVGdtQYGPPVDVWAIGCVFAELLS 197
Cdd:cd05096   171 VGENLTIKIADFGMSRNLYA-GDYYriqgRAVLPIRWMAWECILMG--KFTTASDVWAFGVTLWEILM 235
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
10-312 1.52e-11

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 64.58  E-value: 1.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQ---IVAIKRFLETEDDPVikKIALREIRMLK-QLKHPNLVNLLEVFRRKRRLHLVFEYCDH 85
Cdd:cd05620     3 LGKGSFGKVLLAELKGKGEyfaVKALKKDVVLIDDDV--ECTMVEKRVLAlAWENPFLTHLYCTFQTKEHLFFVMEFLNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  86 TVL----HELDRYQrgvpepLVKNITW--QTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYT 159
Cdd:cd05620    81 GDLmfhiQDKGRFD------LYRATFYaaEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVFGDNRAS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 160 DYVATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSGVPLWPGkSDVDQLylirktlgdliprhqqvfsmnqyFSGVK 239
Cdd:cd05620   155 TFCGTPDYIAPEILQG-LKYTFSVDWWSFGVLLYEMLIGQSPFHG-DDEDEL-----------------------FESIR 209
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039741915 240 IPDPEdmetlelkFPN-ISYSALGFLKGCLHMDPAERL-TCEQLLQHPYFDSIREVGELTRQHDKPARKTLRQSR 312
Cdd:cd05620   210 VDTPH--------YPRwITKESKDILEKLFERDPTRRLgVVGNIRGHPFFKTINWTALEKRELDPPFKPKVKSPS 276
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
10-200 1.88e-11

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 63.91  E-value: 1.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQIV--AIKRFLE--TEDDpviKKIALREIRMLKQL-KHPNLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:cd05047     3 IGEGNFGQVLKARIKKDGLRMdaAIKRMKEyaSKDD---HRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVLHELDRYQRGV---PEPLVKNITWQTLQAVNFCH-------------KHNCIHRDVKPENILITKQSAIKLCDFGFA 148
Cdd:cd05047    80 HGNLLDFLRKSRVLetdPAFAIANSTASTLSSQQLLHfaadvargmdylsQKQFIHRDLAARNILVGENYVAKIADFGLS 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039741915 149 RlltGPGDYYTDYVA---TRWYRSPELlvGDTQYGPPVDVWAIGCVFAELLS--GVP 200
Cdd:cd05047   160 R---GQEVYVKKTMGrlpVRWMAIESL--NYSVYTTNSDVWSYGVLLWEIVSlgGTP 211
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
10-277 2.50e-11

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 63.53  E-value: 2.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKcrNRDTGQIVAIKRFLETEDDpviKKIALREIRMLKQLKHPNLVNLLEVFRR-----KRRLHLVFEYCD 84
Cdd:cd14054     3 IGQGRYGTVWK--GSLDERPVAVKVFPARHRQ---NFQNEKDIYELPLMEHSNILRFIGADERptadgRMEYLLVLEYAP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVLHEldrYQRgvpeplVKNITWQTL--------QAVNFCH---------KHNCIHRDVKPENILITKQSAIKLCDFGF 147
Cdd:cd14054    78 KGSLCS---YLR------ENTLDWMSScrmalsltRGLAYLHtdlrrgdqyKPAIAHRDLNSRNVLVKADGSCVICDFGL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 148 ARLLTGPGDYYTDY----------VATRWYRSPELLVG-----DTQ-YGPPVDVWAIGCVFAELLSGVP-LWPGKSdvdq 210
Cdd:cd14054   149 AMVLRGSSLVRGRPgaaenasiseVGTLRYMAPEVLEGavnlrDCEsALKQVDVYALGLVLWEIAMRCSdLYPGES---- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 211 lylirktlgdlIPRHQQVFsmnQYFSGVKiPDPEDMETL------ELKFPNI---SYSALGFLK----GCLHMDPAERLT 277
Cdd:cd14054   225 -----------VPPYQMPY---EAELGNH-PTFEDMQLLvsrekaRPKFPDAwkeNSLAVRSLKetieDCWDQDAEARLT 289
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
107-284 3.46e-11

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 63.46  E-value: 3.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 107 TWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARlltgpgDYYT--DYV-------ATRWYrSPELLVgDT 177
Cdd:cd05103   185 SFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLAR------DIYKdpDYVrkgdarlPLKWM-APETIF-DR 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 178 QYGPPVDVWAIGCVFAELLS-GVPLWPGkSDVDQLYLIRKTLGdliprhqqvfsmnqyfSGVKIPD---PEDMETlelkf 253
Cdd:cd05103   257 VYTIQSDVWSFGVLLWEIFSlGASPYPG-VKIDEEFCRRLKEG----------------TRMRAPDyttPEMYQT----- 314
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1039741915 254 pnisysalgfLKGCLHMDPAERLTCEQLLQH 284
Cdd:cd05103   315 ----------MLDCWHGEPSQRPTFSELVEH 335
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
2-200 3.65e-11

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 63.90  E-value: 3.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   2 EKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKrFLETEDdpVIKKIALREIR----MLKQLKHPNLVNLLEVFRRKRRLH 77
Cdd:cd05628     1 EDFESLKVIGRGAFGEVRLVQKKDTGHVYAMK-ILRKAD--MLEKEQVGHIRaerdILVEADSLWVVKMFYSFQDKLNLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  78 LVFEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFG----------- 146
Cdd:cd05628    78 LIMEFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGlctglkkahrt 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039741915 147 -FARLLTG--PGDYY-----TDYVATRWYR----------------SPELLVgDTQYGPPVDVWAIGCVFAELLSGVP 200
Cdd:cd05628   158 eFYRNLNHslPSDFTfqnmnSKRKAETWKRnrrqlafstvgtpdyiAPEVFM-QTGYNKLCDWWSLGVIMYEMLIGYP 234
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
3-149 4.37e-11

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 62.66  E-value: 4.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   3 KYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKkialREIRMLKQLK-HPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd14017     1 RWKVVKKIGGGGFGEIYKVRDVVDGEEVAMKVESKSQPKQVLK----MEVAVLKKLQgKPHFCRLIGCGRTERYNYIVMT 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039741915  82 YCDHTvLHELDRYQ--RGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA----IKLCDFGFAR 149
Cdd:cd14017    77 LLGPN-LAELRRSQprGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGRGPSdertVYILDFGLAR 149
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
9-204 4.48e-11

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 62.78  E-value: 4.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQiVAIKRFLETEDDPvikKIALREIRMLKQLKHPNLVNLLEVFRRKRrLHLVFEYCDHTVL 88
Cdd:cd05071    16 KLGQGCFGEVWMGTWNGTTR-VAIKTLKPGTMSP---EAFLQEAQVMKKLRHEKLVQLYAVVSEEP-IYIVTEYMSKGSL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  89 HELDRYQRG--VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGpgdyyTDYVA--- 163
Cdd:cd05071    91 LDFLKGEMGkyLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIED-----NEYTArqg 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1039741915 164 ----TRWYRSPELLVGdtQYGPPVDVWAIGCVFAELLS-GVPLWPG 204
Cdd:cd05071   166 akfpIKWTAPEAALYG--RFTIKSDVWSFGILLTELTTkGRVPYPG 209
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
66-283 4.91e-11

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 63.07  E-value: 4.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  66 LLEVFRRKRRLHlvfEYCDHTVLHELDRYQRGVPEPLVKNI-------------TWQTLQAVNFCHKHNCIHRDVKPENI 132
Cdd:cd05102   127 MVEAVRADRRSR---QGSDRVASFTESTSSTNQPRQEVDDLwqspltmedlicySFQVARGMEFLASRKCIHRDLAARNI 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 133 LITKQSAIKLCDFGFARLLTGPGDYYTDYVAT---RWYrSPELLVgDTQYGPPVDVWAIGCVFAELLS-GVPLWPGksdv 208
Cdd:cd05102   204 LLSENNVVKICDFGLARDIYKDPDYVRKGSARlplKWM-APESIF-DKVYTTQSDVWSFGVLLWEIFSlGASPYPG---- 277
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039741915 209 dqlylirktlgdliprhqqvFSMNQYFSGvKIPDPEDMETLELKFPNIsysaLGFLKGCLHMDPAERLTCEQLLQ 283
Cdd:cd05102   278 --------------------VQINEEFCQ-RLKDGTRMRAPEYATPEI----YRIMLSCWHGDPKERPTFSDLVE 327
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
107-204 5.65e-11

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 63.10  E-value: 5.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 107 TWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARlltgpgDYYT--DYV-------ATRWYrSPELLVgDT 177
Cdd:cd14207   186 SFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLAR------DIYKnpDYVrkgdarlPLKWM-APESIF-DK 257
                          90       100
                  ....*....|....*....|....*...
gi 1039741915 178 QYGPPVDVWAIGCVFAELLS-GVPLWPG 204
Cdd:cd14207   258 IYSTKSDVWSYGVLLWEIFSlGASPYPG 285
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
4-200 6.30e-11

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 63.11  E-value: 6.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRfLETED----DPVIKKIALREIrmLKQLKHPNLVNLLEVFRRKRRLHLV 79
Cdd:cd05626     3 FVKIKTLGIGAFGEVCLACKVDTHALYAMKT-LRKKDvlnrNQVAHVKAERDI--LAEADNEWVVKLYYSFQDKDNLYFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  80 FEYCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGfarLLTG------ 153
Cdd:cd05626    80 MDYIPGGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFG---LCTGfrwthn 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 154 ----------------PGDYYTD----------------------------YVATRWYRSPELLV--GDTQYgppVDVWA 187
Cdd:cd05626   157 skyyqkgshirqdsmePSDLWDDvsncrcgdrlktleqratkqhqrclahsLVGTPNYIAPEVLLrkGYTQL---CDWWS 233
                         250
                  ....*....|...
gi 1039741915 188 IGCVFAELLSGVP 200
Cdd:cd05626   234 VGVILFEMLVGQP 246
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
9-214 7.37e-11

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 61.97  E-value: 7.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTgqiVAIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVnLLEVFRRKRRLHLVFEYCDHTVL 88
Cdd:cd14149    19 RIGSGSFGTVYKGKWHGD---VAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGSSL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  89 HE-LDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARlltgpgdyytdyVATRW- 166
Cdd:cd14149    95 YKhLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAT------------VKSRWs 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039741915 167 -------------YRSPEL--LVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLI 214
Cdd:cd14149   163 gsqqveqptgsilWMAPEVirMQDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFM 225
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
9-287 8.59e-11

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 61.63  E-value: 8.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVAikrFLETEDDPVIKKIALR---EIRMLKQLKHPNLVNLLEVF----RRKRRLHLVFE 81
Cdd:cd14032     8 ELGRGSFKTVYKGLDTETWVEVA---WCELQDRKLTKVERQRfkeEAEMLKGLQHPNIVRFYDFWescaKGKRCIVLVTE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHE-LDRYQRGVPEpLVKNITWQTLQAVNFCHKHN--CIHRDVKPENILITKQS-AIKLCDFGFARLLTgpGDY 157
Cdd:cd14032    85 LMTSGTLKTyLKRFKVMKPK-VLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGPTgSVKIGDLGLATLKR--ASF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 158 YTDYVATRWYRSPELLvgDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYliRKTLGDLIPRhqqvfsmnqyfSG 237
Cdd:cd14032   162 AKSVIGTPEFMAPEMY--EEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIY--RKVTCGIKPA-----------SF 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039741915 238 VKIPDPEDMEtlelkfpnisysalgFLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14032   227 EKVTDPEIKE---------------IIGECICKNKEERYEIKDLLSHAFF 261
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
9-287 9.62e-11

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 61.99  E-value: 9.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQIVAikrFLETEDDPVIKKIALR---EIRMLKQLKHPNLVNLLEVF----RRKRRLHLVFE 81
Cdd:cd14030    32 EIGRGSFKTVYKGLDTETTVEVA---WCELQDRKLSKSERQRfkeEAGMLKGLQHPNIVRFYDSWestvKGKKCIVLVTE 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHN--CIHRDVKPENILITKQS-AIKLCDFGFARLLTGpgDYY 158
Cdd:cd14030   109 LMTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTgSVKIGDLGLATLKRA--SFA 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 159 TDYVATRWYRSPELLvgDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYliRKTLGDLIPRHqqvfsmnqyFSGV 238
Cdd:cd14030   187 KSVIGTPEFMAPEMY--EEKYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIY--RRVTSGVKPAS---------FDKV 253
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1039741915 239 KIPDPEDMetlelkfpnisysalgfLKGCLHMDPAERLTCEQLLQHPYF 287
Cdd:cd14030   254 AIPEVKEI-----------------IEGCIRQNKDERYAIKDLLNHAFF 285
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
13-148 1.32e-10

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 60.98  E-value: 1.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  13 GSYGVVFKCRNRDTGQIVaIKRFLETEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDH-TVLHEL 91
Cdd:cd14027     4 GGFGKVSLCFHRTQGLVV-LKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKgNLMHVL 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915  92 DRyqrgVPEPL-VK-NITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFA 148
Cdd:cd14027    83 KK----VSVPLsVKgRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLA 137
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
9-202 1.96e-10

Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNT7 is a plant thylakoid-associated kinase that is essential in short- and long-term acclimation responses to cope with various light conditions in order to maintain photosynthetic redox poise for optimal photosynthetic performance. Short-term response involves state transitions over periods of minutes while the long-term response (LTR) occurs over hours to days and involves changing the relative amounts of photosystems I and II. SNT7 acts as a redox sensor and a signal transducer for both responses, which are triggered by the redox state of the plastoquinone (PQ) pool. It is positioned at the top of a phosphorylation cascade that induces state transitions by phosphorylating light-harvesting complex II (LHCII), and triggers the LTR through the phosphorylation of chloroplast proteins. The SNT7 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 61.30  E-value: 1.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKcrnrdtgqIVAIKRFLETEDDPVIKKIA----LREIRMLKQLK---------------HPNLVN---- 65
Cdd:cd14013     2 KLGEGGFGTVYK--------GSLLQKDPGGEKRRVVLKKAkeygEVEIWMNERVRracpsscaefvgaflDTTSKKftkp 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  66 ---LLEVFRRKRRLHLV-----FEYCDHTVLheLDRYQRGVPEP-----LVKNITWQTLQAVNFCHKHNCIHRDVKPENI 132
Cdd:cd14013    74 slwLVWKYEGDATLADLmqgkeFPYNLEPII--FGRVLIPPRGPkrenvIIKSIMRQILVALRKLHSTGIVHRDVKPQNI 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039741915 133 LITKQS-AIKLCDFGFAR-LLTG----PGDYYTDyvaTRwYRSPELLVGDTQY--GPPVDVwaigcvfAELLSGVpLW 202
Cdd:cd14013   152 IVSEGDgQFKIIDLGAAAdLRIGinyiPKEFLLD---PR-YAPPEQYIMSTQTpsAPPAPV-------AAALSPV-LW 217
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
13-197 2.34e-10

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2b (or ActRIIB) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 60.81  E-value: 2.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  13 GSYGVVFKCRNRDtgQIVAIKRFleteddPVIKKIAL---REIRMLKQLKHPNLVNLLEVfrRKRRLHLVFEYCDHTVLH 89
Cdd:cd14140     6 GRFGCVWKAQLMN--EYVAVKIF------PIQDKQSWqseREIFSTPGMKHENLLQFIAA--EKRGSNLEMELWLITAFH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  90 E---LDRYQRG----------VPEPLVKNITWQTlQAVNFC----HKHNCIHRDVKPENILITKQSAIKLCDFGFA-RLL 151
Cdd:cd14140    76 DkgsLTDYLKGnivswnelchIAETMARGLSYLH-EDVPRCkgegHKPAIAHRDFKSKNVLLKNDLTAVLADFGLAvRFE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 152 TG--PGDYYTDyVATRWYRSPELLVGDTQYGPP----VDVWAIGCVFAELLS 197
Cdd:cd14140   155 PGkpPGDTHGQ-VGTRRYMAPEVLEGAINFQRDsflrIDMYAMGLVLWELVS 205
STKc_CK1_fungal cd14127
Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; ...
6-204 2.35e-10

Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. This subfamily is composed of fungal CK1 homolog 1 proteins, also called Yck1 in Saccharomyces cerevisiae and Cki1 in Schizosaccharomyces pombe. Yck1 (or Yck1p) and Cki1 are plasma membrane-anchored proteins. Yck1 phosphorylates and regulates Khd1p, a RNA-binding protein that represses translation of bud-localized mRNA. Cki1 phosphorylates and regulates phosphatidylinositol (PI)-(4)P-5-kinase, which catalyzes the last step in the sythesis of PI(4,5)P2, which is involved in actin cytoskeleton remodeling and membrane traffic. The fungal CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271029 [Multi-domain]  Cd Length: 277  Bit Score: 60.58  E-value: 2.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   6 KIGK-IGEGSYGVVFKCRNRDTGQIVAIKRFLETEDDPVIKKialrEIRMLKQLKH-PNLVNLLEVFRRKRRLHLVFEYC 83
Cdd:cd14127     3 KVGKkIGEGSFGVIFEGTNLLNGQQVAIKFEPRKSDAPQLRD----EYRTYKLLAGcPGIPNVYYFGQEGLHNILVIDLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 DHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSA-----IKLCDFGFARlltgpgdYY 158
Cdd:cd14127    79 GPSLEDLFDLCGRKFSVKTVVMVAKQMLTRVQTIHEKNLIYRDIKPDNFLIGRPGTknanvIHVVDFGMAK-------QY 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741915 159 TDYVATRW--YRSPELLVGDTQY-----------GPPVDVWAIGCVFAELLSGVPLWPG 204
Cdd:cd14127   152 RDPKTKQHipYREKKSLSGTARYmsinthlgreqSRRDDLEALGHVFMYFLRGSLPWQG 210
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
105-204 2.74e-10

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 61.07  E-value: 2.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 105 NITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYVA---TRWYrSPELLVgDTQYGP 181
Cdd:cd05104   218 SFSYQVAKGMEFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIRNDSNYVVKGNArlpVKWM-APESIF-ECVYTF 295
                          90       100
                  ....*....|....*....|....
gi 1039741915 182 PVDVWAIGCVFAELLS-GVPLWPG 204
Cdd:cd05104   296 ESDVWSYGILLWEIFSlGSSPYPG 319
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
10-198 5.07e-10

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 59.59  E-value: 5.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKcRNRDTGQIVAIKRF--------LETEDDPVIKKI----ALR-------EIRMLKQLKHPNLVNLLEVf 70
Cdd:cd14067     1 LGQGGSGTVIY-RARYQGQPVAVKRFhikkckkrTDGSADTMLKHLraadAMKnfsefrqEASMLHSLQHPCIVYLIGI- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  71 rrkrRLH-LVFEY------CDHTVLHELDRYQRGVP--EPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILI-----TK 136
Cdd:cd14067    79 ----SIHpLCFALelaplgSLNTVLEENHKGSSFMPlgHMLTFKIAYQIAAGLAYLHKKNIIFCDLKSDNILVwsldvQE 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039741915 137 QSAIKLCDFGFARLLTGPGDYYTDyvATRWYRSPELLVGdTQYGPPVDVWAIGCVFAELLSG 198
Cdd:cd14067   155 HINIKLSDYGISRQSFHEGALGVE--GTPGYQAPEIRPR-IVYDEKVDMFSYGMVLYELLSG 213
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
10-197 5.83e-10

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 59.55  E-value: 5.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVV---FKCRNRDTGQIVAIKrFLETE--DDPVIKKIaLREIRMLKQLKHPNLVNLLEVFRRKR---RL---HL 78
Cdd:cd05074    17 LGKGEFGSVreaQLKSEDGSFQKVAVK-MLKADifSSSDIEEF-LREAACMKEFDHPNVIKLIGVSLRSRakgRLpipMV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  79 VFEYCDHTVLHELDRYQRGVPEPLvkNITWQTL--------QAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARL 150
Cdd:cd05074    95 ILPFMKHGDLHTFLLMSRIGEEPF--TLPLQTLvrfmidiaSGMEYLSSKNFIHRDLAARNCMLNENMTVCVADFGLSKK 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039741915 151 LTGpGDYYTDYVAT----RWYRSPELlvGDTQYGPPVDVWAIGCVFAELLS 197
Cdd:cd05074   173 IYS-GDYYRQGCASklpvKWLALESL--ADNVYTTHSDVWAFGVTMWEIMT 220
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
9-197 6.06e-10

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 59.21  E-value: 6.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVF--KCRNRDTGQ---IVAIKRFLETEDDPviKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYC 83
Cdd:cd05092    12 ELGEGAFGKVFlaECHNLLPEQdkmLVAVKALKEATESA--RQDFQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYM 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  84 DHTVL-----------HELDRYQRGVPEPL----VKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFA 148
Cdd:cd05092    90 RHGDLnrflrshgpdaKILDGGEGQAPGQLtlgqMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKIGDFGMS 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039741915 149 RLLtgpgdYYTDY--------VATRWYRSPELLVgdTQYGPPVDVWAIGCVFAELLS 197
Cdd:cd05092   170 RDI-----YSTDYyrvggrtmLPIRWMPPESILY--RKFTTESDIWSFGVVLWEIFT 219
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
109-283 6.65e-10

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 59.86  E-value: 6.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 109 QTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTDYVA---TRWYrSPELLVgDTQYGPPVDV 185
Cdd:cd05106   220 QVAQGMDFLASKNCIHRDVAARNVLLTDGRVAKICDFGLARDIMNDSNYVVKGNArlpVKWM-APESIF-DCVYTVQSDV 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 186 WAIGCVFAELLS-GVPLWPGKSDVDQLYLIRKtlgdliprhqqvfsmnqyfSGVKIPDPeDMETLELkfpnisYSalgFL 264
Cdd:cd05106   298 WSYGILLWEIFSlGKSPYPGILVNSKFYKMVK-------------------RGYQMSRP-DFAPPEI------YS---IM 348
                         170
                  ....*....|....*....
gi 1039741915 265 KGCLHMDPAERLTCEQLLQ 283
Cdd:cd05106   349 KMCWNLEPTERPTFSQISQ 367
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
9-204 1.23e-09

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 58.54  E-value: 1.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   9 KIGEGSYGVVFKCRNRDTGQiVAIKRFLETEDDPvikKIALREIRMLKQLKHPNLVNLLEVFRRKRrLHLVFEYCDHTVL 88
Cdd:cd05069    19 KLGQGCFGEVWMGTWNGTTK-VAIKTLKPGTMMP---EAFLQEAQIMKKLRHDKLVPLYAVVSEEP-IYIVTEFMGKGSL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  89 heLDRYQRG----VPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGpgdyyTDYVA- 163
Cdd:cd05069    94 --LDFLKEGdgkyLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIED-----NEYTAr 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1039741915 164 ------TRWYRSPELLVGdtQYGPPVDVWAIGCVFAELLS-GVPLWPG 204
Cdd:cd05069   167 qgakfpIKWTAPEAALYG--RFTIKSDVWSFGILLTELVTkGRVPYPG 212
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
10-202 1.28e-09

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 58.06  E-value: 1.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  10 IGEGSYGVVFKCRNRDTGQ---IVAIKRFLE--TEDDpviKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCD 84
Cdd:cd05063    13 IGAGEFGEVFRGILKMPGRkevAVAIKTLKPgyTEKQ---RQDFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYME 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  85 HTVLhelDRYQRGvpeplvKNITWQTLQAV----------NFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTG- 153
Cdd:cd05063    90 NGAL---DKYLRD------HDGEFSSYQLVgmlrgiaagmKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLEDd 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039741915 154 PGDYYTDY---VATRWyRSPElLVGDTQYGPPVDVWAIGCVFAELLS--GVPLW 202
Cdd:cd05063   161 PEGTYTTSggkIPIRW-TAPE-AIAYRKFTSASDVWSFGIVMWEVMSfgERPYW 212
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
4-215 1.67e-09

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 58.52  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915   4 YEKIGKIGEGSYGVVFKCRNRDTGQIVAIKRfLETEDDPVIKKIA--LREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFE 81
Cdd:cd05625     3 FVKIKTLGIGAFGEVCLARKVDTKALYATKT-LRKKDVLLRNQVAhvKAERDILAEADNEWVVRLYYSFQDKDNLYFVMD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  82 YCDHTVLHELDRYQRGVPEPLVKNITWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLL--TGPGDYYT 159
Cdd:cd05625    82 YIPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrwTHDSKYYQ 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 160 ---------------------------------------------DYVATRWYRSPELLVgDTQYGPPVDVWAIGCVFAE 194
Cdd:cd05625   162 sgdhlrqdsmdfsnewgdpencrcgdrlkplerraarqhqrclahSLVGTPNYIAPEVLL-RTGYTQLCDWWSVGVILFE 240
                         250       260
                  ....*....|....*....|..
gi 1039741915 195 LLSGVPLWPGKSDVD-QLYLIR 215
Cdd:cd05625   241 MLVGQPPFLAQTPLEtQMKVIN 262
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
69-284 1.81e-09

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 57.80  E-value: 1.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  69 VFRRKRRLHLVF------EYCD---------HTVLHELDRYQRgvpEPLVknITWQTLQAVNFCHKHNCIHRDVKPENIL 133
Cdd:cd13974    90 TGRVRKRLCLVLdclcahDFSDktadlinlqHYVIREKRLSER---EALV--IFYDVVRVVEALHKKNIVHRDLKLGNMV 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 134 ITKQS-AIKLCDFGFARLLTGPGDYYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSG-VPLWpgksdvdql 211
Cdd:cd13974   165 LNKRTrKITITNFCLGKHLVSEDDLLKDQRGSPAYISPDVLSGKPYLGKPSDMWALGVVLFTMLYGqFPFY--------- 235
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741915 212 ylirktlgDLIPrhQQVFSmnqyfsgvKIpdpedmETLELKFPN---ISYSALGFLKGCLHMDPAERLTCEQLLQH 284
Cdd:cd13974   236 --------DSIP--QELFR--------KI------KAAEYTIPEdgrVSENTVCLIRKLLVLNPQKRLTASEVLDS 287
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
107-200 2.03e-09

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 58.48  E-value: 2.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 107 TWQTLQAVNFCHKHNCIHRDVKPENILITKQSAIKLCDFGFARLLTGPGDYYTD---YVATRWYrSPELLVgDTQYGPPV 183
Cdd:cd05107   245 SYQVANGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISKgstFLPLKWM-APESIF-NNLYTTLS 322
                          90
                  ....*....|....*....
gi 1039741915 184 DVWAIGCVFAEL--LSGVP 200
Cdd:cd05107   323 DVWSFGILLWEIftLGGTP 341
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
49-281 3.25e-09

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 56.92  E-value: 3.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915  49 LREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDhtvLHELDRYQRG-------VPEPLV-KNITWQTLQAVNFCHKH 120
Cdd:cd05087    45 LEEAQPYRALQHTNLLQCLAQCAEVTPYLLVMEFCP---LGDLKGYLRScraaesmAPDPLTlQRMACEVACGLLHLHRN 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 121 NCIHRDVKPENILITKQSAIKLCDFGFARlLTGPGDYYTD----YVATRWYrSPELL---------VGDTQYGppvDVWA 187
Cdd:cd05087   122 NFVHSDLALRNCLLTADLTVKIGDYGLSH-CKYKEDYFVTadqlWVPLRWI-APELVdevhgnllvVDQTKQS---NVWS 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741915 188 IGCVFAEL--LSGVPlWPGKSDvdqlyliRKTLGDLIpRHQQvfsmnqyfsgVKIPDPEdmetLELKFPNISYSALGFlk 265
Cdd:cd05087   197 LGVTIWELfeLGNQP-YRHYSD-------RQVLTYTV-REQQ----------LKLPKPQ----LKLSLAERWYEVMQF-- 251
                         250
                  ....*....|....*.
gi 1039741915 266 gCLhMDPAERLTCEQL 281
Cdd:cd05087   252 -CW-LQPEQRPTAEEV 265
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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