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Conserved domains on  [gi|1370510836|ref|XP_024302663|]
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SRSF protein kinase 2 isoform X4 [Homo sapiens]

Protein Classification

protein kinase family protein( domain architecture ID 229378)

protein kinase family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to substrates such as serine/threonine and/or tyrosine residues on proteins, or may be a pseudokinase

CATH:  1.10.510.10
PubMed:  16244704
SCOP:  4003661

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
116-304 1.71e-137

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd14217:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 366  Bit Score: 409.42  E-value: 1.71e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 116 YHPVKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKDMVVQ 195
Cdd:cd14217     1 YHPVKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLRCVRESDPEDPNKDMVVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 196 LIDDFKISGMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDA 275
Cdd:cd14217    81 LIDDFKISGMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPIRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDA 160
                         170       180
                  ....*....|....*....|....*....
gi 1370510836 276 YVRRMAAEATEWQKAGAPPPSGSAVSTAP 304
Cdd:cd14217   161 YVRRMAAEATEWQKAGAPPPSGSAVSTAP 189
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
552-734 2.45e-124

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd14217:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 366  Bit Score: 375.52  E-value: 2.45e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 552 AKTRAADLLVNPLDPRNADKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYL 631
Cdd:cd14217   184 AVSTAPDLLVNPLDPRNADKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYL 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 632 FEPHSGEDYSRDEDHIALIIELLGKVPRKYAMLGKYSKEFFTRKGELRHITKLKPWSLFDVLVEKYGWPHEDAAQFTDFL 711
Cdd:cd14217   264 FEPHSGEDYSRDEDHIAHIIELLGCIPRHFALSGKYSREFFNRRGELRHITKLKPWSLFDVLVEKYGWPHEDAAQFTDFL 343
                         170       180
                  ....*....|....*....|...
gi 1370510836 712 IPMLEMVPEKRASAGECLRHPWL 734
Cdd:cd14217   344 IPMLEMVPEKRASAGECLRHPWL 366
2A1904 super family cl36772
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
389-431 7.65e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


The actual alignment was detected with superfamily member TIGR00927:

Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 39.59  E-value: 7.65e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1370510836  389 DNGEAEDQEEKEDAEKENIEKDEDDVDQELANIDPTWIESPKT 431
Cdd:TIGR00927  859 DGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLEWPET 901
 
Name Accession Description Interval E-value
STKc_SRPK2 cd14217
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs ...
116-304 1.71e-137

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: 409.42  E-value: 1.71e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 116 YHPVKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKDMVVQ 195
Cdd:cd14217     1 YHPVKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLRCVRESDPEDPNKDMVVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 196 LIDDFKISGMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDA 275
Cdd:cd14217    81 LIDDFKISGMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPIRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDA 160
                         170       180
                  ....*....|....*....|....*....
gi 1370510836 276 YVRRMAAEATEWQKAGAPPPSGSAVSTAP 304
Cdd:cd14217   161 YVRRMAAEATEWQKAGAPPPSGSAVSTAP 189
STKc_SRPK2 cd14217
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs ...
552-734 2.45e-124

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: 375.52  E-value: 2.45e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 552 AKTRAADLLVNPLDPRNADKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYL 631
Cdd:cd14217   184 AVSTAPDLLVNPLDPRNADKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYL 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 632 FEPHSGEDYSRDEDHIALIIELLGKVPRKYAMLGKYSKEFFTRKGELRHITKLKPWSLFDVLVEKYGWPHEDAAQFTDFL 711
Cdd:cd14217   264 FEPHSGEDYSRDEDHIAHIIELLGCIPRHFALSGKYSREFFNRRGELRHITKLKPWSLFDVLVEKYGWPHEDAAQFTDFL 343
                         170       180
                  ....*....|....*....|...
gi 1370510836 712 IPMLEMVPEKRASAGECLRHPWL 734
Cdd:cd14217   344 IPMLEMVPEKRASAGECLRHPWL 366
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
129-273 8.80e-31

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 121.48  E-value: 8.80e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836  129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVK--SAQHYTETALDEIKLLKCVREsdpsdPNkdmVVQLIDDFKisgmN 206
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKkkKIKKDRERILREIKILKKLKH-----PN---IVRLYDVFE----D 68
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510836  207 GIHVCMVFEVLGHHLLKWIIKSNyQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVD 273
Cdd:smart00220  69 EDKLYLVMEYCEGGDLFDLLKKR-GRLSEDEARFYLRQILSALEYLHSK-GIVHRDLKPENILLDED 133
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
123-273 9.04e-22

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 99.32  E-value: 9.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 123 DLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALD----EIKLLKCVResdpsDPNkdmVVQLID 198
Cdd:COG0515     3 ALLLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARErfrrEARALARLN-----HPN---IVRVYD 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510836 199 DFKISGmngiHVCMVFE-VLGHHLLKWIikSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVD 273
Cdd:COG0515    75 VGEEDG----RPYLVMEyVEGESLADLL--RRRGPLPPAEALRILAQLAEALAAAHAA-GIVHRDIKPANILLTPD 143
PTZ00284 PTZ00284
protein kinase; Provisional
123-285 5.33e-21

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 96.96  E-value: 5.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 123 DLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKDMVVQ--LIDDf 200
Cdd:PTZ00284  125 DVSTQRFKILSLLGEGTFGKVVEAWDRKRKEYCAVKIVRNVPKYTRDAKIEIQFMEKVRQADPADRFPLMKIQryFQNE- 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 201 kiSGmngiHVCMVFEVLGHHLLKWIIKsnYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDAYVRRM 280
Cdd:PTZ00284  204 --TG----HMCIVMPKYGPCLLDWIMK--HGPFSHRHLAQIIFQTGVALDYFHTELHLMHTDLKPENILMETSDTVVDPV 275

                  ....*
gi 1370510836 281 AAEAT 285
Cdd:PTZ00284  276 TNRAL 280
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
573-734 1.93e-18

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 85.66  E-value: 1.93e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836  573 RVKIADLGNACWVH--KHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEphsgedysrDEDHIALI 650
Cdd:smart00220 135 HVKLADFGLARQLDpgEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFP---------GDDQLLEL 205
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836  651 IELLGKvprkyamlGKYSKEFFtrkgelrhitklkpwslfdvlveKYGWPHEdaaqFTDFLIPMLEMVPEKRASAGECLR 730
Cdd:smart00220 206 FKKIGK--------PKPPFPPP-----------------------EWDISPE----AKDLIRKLLVKDPEKRLTAEEALQ 250

                   ....
gi 1370510836  731 HPWL 734
Cdd:smart00220 251 HPFF 254
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
121-270 1.93e-14

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 76.76  E-value: 1.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 121 IGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKsaqhyTETALDEIKLLKCVRE----SDPSDPNkdmVVQL 196
Cdd:NF033483    1 IGKLLGGRYEIGERIGRGGMAEVYLAKDTRLDRDVAVKVLR-----PDLARDPEFVARFRREaqsaASLSHPN---IVSV 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 197 IDdfkiSGMNGIHVCMVFE-VLGhHLLKWIIKSNYQgLPVRCVKSIIRQVLQGLDYLHsKCKIIHTDIKPENILM 270
Cdd:NF033483   73 YD----VGEDGGIPYIVMEyVDG-RTLKDYIREHGP-LSPEEAVEIMIQILSALEHAH-RNGIVHRDIKPQNILI 140
PTZ00284 PTZ00284
protein kinase; Provisional
557-734 1.11e-13

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 73.85  E-value: 1.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 557 ADLLVNPLDPRN--ADKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEP 634
Cdd:PTZ00284  268 SDTVVDPVTNRAlpPDPCRVRICDLGGCCDERHSRTAIVSTRHYRSPEVVLGLGWMYSTDMWSMGCIIYELYTGKLLYDT 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 635 HSgedysrDEDHIALIIELLGKVPRKYAML--GKYSKEFFTRKGELR------HITKL-KPWSLFDVLVEKYgwphedaa 705
Cdd:PTZ00284  348 HD------NLEHLHLMEKTLGRLPSEWAGRcgTEEARLLYNSAGQLRpctdpkHLARIaRARPVREVIRDDL-------- 413
                         170       180
                  ....*....|....*....|....*....
gi 1370510836 706 qFTDFLIPMLEMVPEKRASAGECLRHPWL 734
Cdd:PTZ00284  414 -LCDLIYGLLHYDRQKRLNARQMTTHPYV 441
Pkinase pfam00069
Protein kinase domain;
595-734 1.69e-11

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 64.19  E-value: 1.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 595 TRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSGedysrDEDHIALIIELLGKVPRKYAmlgkYSKEfftr 674
Cdd:pfam00069 123 TPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGING-----NEIYELIIDQPYAFPELPSN----LSEE---- 189
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 675 kgelrhitklkpwslfdvlvekygwphedaaqFTDFLIPMLEMVPEKRASAGECLRHPWL 734
Cdd:pfam00069 190 --------------------------------AKDLLKKLLKKDPSKRLTATQALQHPWF 217
Pkinase pfam00069
Protein kinase domain;
129-250 2.04e-11

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 64.19  E-value: 2.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQ---HYTETALDEIKLLKCVREsdpsdPNkdmVVQLIDDFkisgM 205
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKikkKKDKNILREIKILKKLNH-----PN---IVRLYDAF----E 68
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1370510836 206 NGIHVCMVFE-VLGHHLLKWIikSNYQGLPVRCVKSIIRQVLQGLD 250
Cdd:pfam00069  69 DKDNLYLVLEyVEGGSLFDLL--SEKGAFSEREAKFIMKQILEGLE 112
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
573-639 6.32e-05

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 46.16  E-value: 6.32e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510836 573 RVKIADLGNACWVHK-HFTED---IQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSGED 639
Cdd:COG0515   145 RVKLIDFGIARALGGaTLTQTgtvVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAE 215
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
389-431 7.65e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 39.59  E-value: 7.65e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1370510836  389 DNGEAEDQEEKEDAEKENIEKDEDDVDQELANIDPTWIESPKT 431
Cdd:TIGR00927  859 DGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLEWPET 901
 
Name Accession Description Interval E-value
STKc_SRPK2 cd14217
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs ...
116-304 1.71e-137

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: 409.42  E-value: 1.71e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 116 YHPVKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKDMVVQ 195
Cdd:cd14217     1 YHPVKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLRCVRESDPEDPNKDMVVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 196 LIDDFKISGMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDA 275
Cdd:cd14217    81 LIDDFKISGMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPIRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDA 160
                         170       180
                  ....*....|....*....|....*....
gi 1370510836 276 YVRRMAAEATEWQKAGAPPPSGSAVSTAP 304
Cdd:cd14217   161 YVRRMAAEATEWQKAGAPPPSGSAVSTAP 189
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
118-301 3.61e-134

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: 400.93  E-value: 3.61e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 118 PVKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKDMVVQLI 197
Cdd:cd14218     1 PVKIGDLFNGRYHVVRKLGWGHFSTVWLCWDIQRKRFVALKVVKSAVHYTETAVDEIKLLKCVRDSDPSDPKRETIVQLI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 198 DDFKISGMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDAYV 277
Cdd:cd14218    81 DDFKISGVNGVHVCMVLEVLGHQLLKWIIKSNYQGLPLPCVKSILRQVLQGLDYLHTKCKIIHTDIKPENILMCVDEGYV 160
                         170       180
                  ....*....|....*....|....
gi 1370510836 278 RRMAAEATEWQKAGAPPPSGSAVS 301
Cdd:cd14218   161 RRLAAEATIWQQAGAPPPSGSSVS 184
STKc_SRPK2 cd14217
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs ...
552-734 2.45e-124

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: 375.52  E-value: 2.45e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 552 AKTRAADLLVNPLDPRNADKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYL 631
Cdd:cd14217   184 AVSTAPDLLVNPLDPRNADKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYL 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 632 FEPHSGEDYSRDEDHIALIIELLGKVPRKYAMLGKYSKEFFTRKGELRHITKLKPWSLFDVLVEKYGWPHEDAAQFTDFL 711
Cdd:cd14217   264 FEPHSGEDYSRDEDHIAHIIELLGCIPRHFALSGKYSREFFNRRGELRHITKLKPWSLFDVLVEKYGWPHEDAAQFTDFL 343
                         170       180
                  ....*....|....*....|...
gi 1370510836 712 IPMLEMVPEKRASAGECLRHPWL 734
Cdd:cd14217   344 IPMLEMVPEKRASAGECLRHPWL 366
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
558-734 2.51e-121

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: 367.05  E-value: 2.51e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 558 DLLVNPLDPRNADKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSG 637
Cdd:cd14216   173 NFLVNPLEPKNAEKLKVKIADLGNACWVHKHFTEDIQTRQYRSLEVLIGSGYNTPADIWSTACMAFELATGDYLFEPHSG 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 638 EDYSRDEDHIALIIELLGKVPRKYAMLGKYSKEFFTRKGELRHITKLKPWSLFDVLVEKYGWPHEDAAQFTDFLIPMLEM 717
Cdd:cd14216   253 EDYSRDEDHIALIIELLGKVPRKLIVAGKYSKEFFTKKGDLKHITKLKPWGLFEVLVEKYEWSQEEAAGFTDFLLPMLEL 332
                         170
                  ....*....|....*..
gi 1370510836 718 VPEKRASAGECLRHPWL 734
Cdd:cd14216   333 IPEKRATAAECLRHPWL 349
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
556-734 1.19e-118

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: 360.87  E-value: 1.19e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 556 AADLLVNPLDPRNADKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPH 635
Cdd:cd14218   187 ASDFLVNPLEPQNADKIRVKIADLGNACWVHKHFTEDIQTRQYRALEVLIGAEYGTPADIWSTACMAFELATGDYLFEPH 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 636 SGEDYSRDEDHIALIIELLGKVPRKYAMLGKYSKEFFTRKGELRHITKLKPWSLFDVLVEKYGWPHEDAAQFTDFLIPML 715
Cdd:cd14218   267 SGEDYTRDEDHIAHIVELLGDIPPHFALSGRYSREYFNRRGELRHIKNLKHWGLYEVLVEKYEWPLEQAAQFTDFLLPMM 346
                         170
                  ....*....|....*....
gi 1370510836 716 EMVPEKRASAGECLRHPWL 734
Cdd:cd14218   347 EFLPEKRATAAQCLQHPWL 365
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
119-289 3.46e-118

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: 358.96  E-value: 3.46e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 119 VKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKDMVVQLID 198
Cdd:cd14216     2 VKIGDLFNGRYHVIRKLGWGHFSTVWLSWDIQGKRFVAMKVVKSAEHYTETALDEIKLLKSVRNSDPNDPNREMVVQLLD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 199 DFKISGMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDAYVR 278
Cdd:cd14216    82 DFKISGVNGTHICMVFEVLGHHLLKWIIKSNYQGLPLPCVKKIIRQVLQGLDYLHTKCRIIHTDIKPENILLSVNEQYIR 161
                         170
                  ....*....|.
gi 1370510836 279 RMAAEATEWQK 289
Cdd:cd14216   162 RLAAEATEWQR 172
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
564-734 3.67e-118

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: 357.66  E-value: 3.67e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 564 LDPRN----ADKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSGED 639
Cdd:cd14136   146 IKPENvllcISKIEVKIADLGNACWTDKHFTEDIQTRQYRSPEVILGAGYGTPADIWSTACMAFELATGDYLFDPHSGED 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 640 YSRDEDHIALIIELLGKVPRKYAMLGKYSKEFFTRKGELRHITKLKPWSLFDVLVEKYGWPHEDAAQFTDFLIPMLEMVP 719
Cdd:cd14136   226 YSRDEDHLALIIELLGRIPRSIILSGKYSREFFNRKGELRHISKLKPWPLEDVLVEKYKWSKEEAKEFASFLLPMLEYDP 305
                         170
                  ....*....|....*
gi 1370510836 720 EKRASAGECLRHPWL 734
Cdd:cd14136   306 EKRATAAQCLQHPWL 320
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
118-277 1.04e-114

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: 348.80  E-value: 1.04e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 118 PVKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKDMVVQLI 197
Cdd:cd14136     1 PVKIGEVYNGRYHVVRKLGWGHFSTVWLCWDLQNKRFVALKVVKSAQHYTEAALDEIKLLKCVREADPKDPGREHVVQLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 198 DDFKISGMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDAYV 277
Cdd:cd14136    81 DDFKHTGPNGTHVCMVFEVLGPNLLKLIKRYNYRGIPLPLVKKIARQVLQGLDYLHTKCGIIHTDIKPENVLLCISKIEV 160
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
119-278 3.99e-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: 167.36  E-value: 3.99e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 119 VKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSdpNKDMVVQLID 198
Cdd:cd14134     4 YKPGDLLTNRYKILRLLGEGTFGKVLECWDRKRKRYVAVKIIRNVEKYREAAKIEIDVLETLAEKDPN--GKSHCVQLRD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 199 DFKISGmngiHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHsKCKIIHTDIKPENILMcVDDAYVR 278
Cdd:cd14134    82 WFDYRG----HMCIVFELLGPSLYDFLKKNNYGPFPLEHVQHIAKQLLEAVAFLH-DLKLTHTDLKPENILL-VDSDYVK 155
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
129-271 9.88e-43

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: 155.09  E-value: 9.88e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVREsdpsDPNKDMVVQLIDDFKISGMNgi 208
Cdd:cd05118     1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKAALREIKLLKHLND----VEGHPNIVKLLDVFEHRGGN-- 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510836 209 HVCMVFEVLGHHLLKwIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILMC 271
Cdd:cd05118    75 HLCLVFELMGMNLYE-LIKDYPRGLPLDLIKSYLYQLLQALDFLHS-NGIIHRDLKPENILIN 135
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
115-271 8.10e-36

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: 137.68  E-value: 8.10e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 115 GYHPVKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDpnKDMVV 194
Cdd:cd14210     1 GDYKVVLGDHIAYRYEVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIRNKKRFHQQALVEVKILKHLNDNDPDD--KHNIV 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510836 195 QLIDDFKISGmngiHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMC 271
Cdd:cd14210    79 RYKDSFIFRG----HLCIVFELLSINLYELLKSNNFQGLSLSLIRKFAKQILQALQFLHKL-NIIHCDLKPENILLK 150
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
129-276 5.59e-34

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: 130.85  E-value: 5.59e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDpnKDMVVQLIDDFkisgMNGI 208
Cdd:cd14133     1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLDQSLDEIRLLELLNKKDKAD--KYHIVRLKDVF----YFKN 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510836 209 HVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILMCVDDAY 276
Cdd:cd14133    75 HLCIVFELLSQNLYEFLKQNKFQYLSLPRIRKIAQQILEALVFLHS-LGLIHCDLKPENILLASYSRC 141
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
559-734 2.18e-31

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: 124.96  E-value: 2.18e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 559 LLVNPldprnaDKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFephSGE 638
Cdd:cd14210   148 LLKQP------SKSSIKVIDFGSSCFEGEKVYTYIQSRFYRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLF---PGE 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 639 DysrDEDHIALIIELLGKVPRKYAMLGKYSKEFFTRKGELRHITklkpwslfdVLVEKYGWP---------HEDAAQFTD 709
Cdd:cd14210   219 N---EEEQLACIMEVLGVPPKSLIDKASRRKKFFDSNGKPRPTT---------NSKGKKRRPgskslaqvlKCDDPSFLD 286
                         170       180
                  ....*....|....*....|....*
gi 1370510836 710 FLIPMLEMVPEKRASAGECLRHPWL 734
Cdd:cd14210   287 FLKKCLRWDPSERMTPEEALQHPWI 311
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
129-273 8.80e-31

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 121.48  E-value: 8.80e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836  129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVK--SAQHYTETALDEIKLLKCVREsdpsdPNkdmVVQLIDDFKisgmN 206
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKkkKIKKDRERILREIKILKKLKH-----PN---IVRLYDVFE----D 68
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510836  207 GIHVCMVFEVLGHHLLKWIIKSNyQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVD 273
Cdd:smart00220  69 EDKLYLVMEYCEGGDLFDLLKKR-GRLSEDEARFYLRQILSALEYLHSK-GIVHRDLKPENILLDED 133
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
129-275 7.23e-29

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: 118.12  E-value: 7.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDpSDPNKDMVVQLIDDFkisgMNGI 208
Cdd:cd14212     1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVLKNKPAYFRQAMLEIAILTLLNTKY-DPEDKHHIVRLLDHF----MHHG 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510836 209 HVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHsKCKIIHTDIKPENILMCVDDA 275
Cdd:cd14212    76 HLCIVFELLGVNLYELLKQNQFRGLSLQLIRKFLQQLLDALSVLK-DARIIHCDLKPENILLVNLDS 141
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
119-271 5.51e-28

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: 115.49  E-value: 5.51e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 119 VKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKdmVVQLID 198
Cdd:cd14226     5 VKNGEKWMDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTENKYY--IVRLKR 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370510836 199 DFKISGmngiHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYL-HSKCKIIHTDIKPENILMC 271
Cdd:cd14226    83 HFMFRN----HLCLVFELLSYNLYDLLRNTNFRGVSLNLTRKFAQQLCTALLFLsTPELSIIHCDLKPENILLC 152
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
573-734 3.73e-27

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: 113.04  E-value: 3.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 573 RVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSgedysrDEDHIALIIE 652
Cdd:cd14134   172 DIKLIDFGSATFDDEYHSSIVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLFQTHD------NLEHLAMMER 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 653 LLGKVPRKYAMLGKY-SKEFFTRKGEL---------RHITKL-KPWSLFDVLVekygwpHEDAAQFTDFLIPMLEMVPEK 721
Cdd:cd14134   246 ILGPLPKRMIRRAKKgAKYFYFYHGRLdwpegsssgRSIKRVcKPLKRLMLLV------DPEHRLLFDLIRKMLEYDPSK 319
                         170
                  ....*....|...
gi 1370510836 722 RASAGECLRHPWL 734
Cdd:cd14134   320 RITAKEALKHPFF 332
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
568-734 1.02e-25

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: 106.55  E-value: 1.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 568 NADKIRVKIADLGNACWVHKHF-TEDIQTRQYRSIEVLIGA-GYSTPADIWSTACMAFELATGDYLFEPHSgedysrDED 645
Cdd:cd05118   135 NLELGQLKLADFGLARSFTSPPyTPYVATRWYRAPEVLLGAkPYGSSIDIWSLGCILAELLTGRPLFPGDS------EVD 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 646 HIALIIELLGKvprkyamlgkyskefftrkgelrhitklkpwslfdvlvekygwphedaAQFTDFLIPMLEMVPEKRASA 725
Cdd:cd05118   209 QLAKIVRLLGT------------------------------------------------PEALDLLSKMLKYDPAKRITA 240

                  ....*....
gi 1370510836 726 GECLRHPWL 734
Cdd:cd05118   241 SQALAHPYF 249
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
129-270 7.20e-25

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: 105.26  E-value: 7.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQH---YTETALDEIKLLKcvresDPSDPNkdmVVQLIDdfKISGM 205
Cdd:cd07829     1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDNEeegIPSTALREISLLK-----ELKHPN---IVKLLD--VIHTE 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 206 NGIHvcMVFEVLgHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd07829    71 NKLY--LVFEYC-DQDLKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSH-RILHRDLKPQNLLI 131
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
559-736 1.18e-24

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: 105.86  E-value: 1.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 559 LLVNPldPRNAdkirVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFephSGe 638
Cdd:cd14226   150 LLCNP--KRSA----IKIIDFGSSCQLGQRIYQYIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLF---SG- 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 639 dySRDEDHIALIIELLGKVPRKyaMLGKYSK--EFFTRKGE-----LRHITKLKPW-----SLFDVLVEKYGWP------ 700
Cdd:cd14226   220 --ANEVDQMNKIVEVLGMPPVH--MLDQAPKarKFFEKLPDgtyylKKTKDGKKYKppgsrKLHEILGVETGGPggrrag 295
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1370510836 701 ---H--EDAAQFTDFLIPMLEMVPEKRASAGECLRHPWLNS 736
Cdd:cd14226   296 epgHtvEDYLKFKDLILRMLDYDPKTRITPAEALQHSFFKR 336
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
559-734 1.91e-24

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: 103.50  E-value: 1.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 559 LLVNPldprnaDKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFePHSGE 638
Cdd:cd14133   134 LLASY------SRCQIKIIDFGSSCFLTQRLYSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLF-PGASE 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 639 dysrdEDHIALIIELLGKVPRKyaMLGKYSkefftrkgelrhitklkpwslfdvlvekygwphEDAAQFTDFLIPMLEMV 718
Cdd:cd14133   207 -----VDQLARIIGTIGIPPAH--MLDQGK---------------------------------ADDELFVDFLKKLLEID 246
                         170
                  ....*....|....*.
gi 1370510836 719 PEKRASAGECLRHPWL 734
Cdd:cd14133   247 PKERPTASQALSHPWL 262
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
115-269 9.69e-24

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: 103.17  E-value: 9.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 115 GYHPVKIGDLFNGRYHVIRKLGWGHFSTVWLCWDM-QGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSdpNKDMV 193
Cdd:cd14214     1 GHLVCRIGDWLQERYEIVGDLGEGTFGKVVECLDHaRGKSQVALKIIRNVGKYREAARLEINVLKKIKEKDKE--NKFLC 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510836 194 VQLIDDFKISGmngiHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:cd14214    79 VLMSDWFNFHG----HMCIAFELLGKNTFEFLKENNFQPYPLPHIRHMAYQLCHALKFLHEN-QLTHTDLKPENIL 149
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
120-278 2.24e-23

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: 102.02  E-value: 2.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 120 KIGDLFNGRYHVIRKLGWGHFSTVWLCWD-MQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSdpNKDMVVQLID 198
Cdd:cd14215     5 RSGDWLQERYEIVSTLGEGTFGRVVQCIDhRRGGARVALKIIKNVEKYKEAARLEINVLEKINEKDPE--NKNLCVQMFD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 199 DFKISGmngiHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVDDAYVR 278
Cdd:cd14215    83 WFDYHG----HMCISFELLGLSTFDFLKENNYLPYPIHQVRHMAFQVCQAVKFLHDN-KLTHTDLKPENILFVNSDYELT 157
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
135-270 2.67e-22

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: 95.80  E-value: 2.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKRFVAMKVVK--SAQHYTETALDEIKLLKCVResdpsDPNkdmVVQLIDDFKisgmNGIHVCM 212
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKKVAVKVIPkeKLKKLLEELLREIEILKKLN-----HPN---IVKLYDVFE----TENFLYL 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510836 213 VFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd00180    69 VMEYCEGGSLKDLLKENKGPLSEEEALSILRQLLSALEYLHSN-GIIHRDLKPENILL 125
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
128-269 2.84e-22

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: 98.45  E-value: 2.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQ-GKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDpnKDMVVQLIDDFKISGmn 206
Cdd:cd14135     1 RYRVYGYLGKGVFSNVVRARDLArGNQEVAIKIIRNNELMHKAGLKELEILKKLNDADPDD--KKHCIRLLRHFEHKN-- 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 207 giHVCMVFEVLgHHLLKWIIK--SNYQGLPVRCVKSIIRQVLQGLDYLhSKCKIIHTDIKPENIL 269
Cdd:cd14135    77 --HLCLVFESL-SMNLREVLKkyGKNVGLNIKAVRSYAQQLFLALKHL-KKCNILHADIKPDNIL 137
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
127-269 3.20e-22

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: 97.39  E-value: 3.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 127 GRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVK---SAQHYTETALDEIKLLKCVREsdpsdPNkdmVVQLIDDFKIS 203
Cdd:cd07833     1 NKYEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKeseDDEDVKKTALREVKVLRQLRH-----EN---IVNLKEAFRRK 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510836 204 GmngiHVCMVFEVLGHHLLKWIIKSNYqGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:cd07833    73 G----RLYLVFEYVERTLLELLEASPG-GLPPDAVRSYIWQLLQAIAYCHSH-NIIHRDIKPENIL 132
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
574-734 4.67e-22

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: 99.05  E-value: 4.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 574 VKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFephSGEDysrDEDHIALIIEL 653
Cdd:cd14224   209 IKVIDFGSSCYEHQRIYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGYPLF---PGED---EGDQLACMIEL 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 654 LGKVPRKYAMLGKYSKEFFTRKGELRHITKLkpwSLFDVLV----------EKYGWPHE----------DAAQFTDFLIP 713
Cdd:cd14224   283 LGMPPQKLLETSKRAKNFISSKGYPRYCTVT---TLPDGSVvlnggrsrrgKMRGPPGSkdwvtalkgcDDPLFLDFLKR 359
                         170       180
                  ....*....|....*....|.
gi 1370510836 714 MLEMVPEKRASAGECLRHPWL 734
Cdd:cd14224   360 CLEWDPAARMTPSQALRHPWL 380
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
99-270 7.43e-22

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: 97.47  E-value: 7.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836  99 GSDDEEqedpadyckGGYHPVkIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLK 178
Cdd:cd14225    25 GYDDEN---------GSYLKV-LHDHIAYRYEILEVIGKGSFGQVVKALDHKTNEHVAIKIIRNKKRFHHQALVEVKILD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 179 CVRESDPSdpNKDMVVQLIDDFKISGmngiHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHsKCKI 258
Cdd:cd14225    95 ALRRKDRD--NSHNVIHMKEYFYFRN----HLCITFELLGMNLYELIKKNNFQGFSLSLIRRFAISLLQCLRLLY-RERI 167
                         170
                  ....*....|..
gi 1370510836 259 IHTDIKPENILM 270
Cdd:cd14225   168 IHCDLKPENILL 179
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
123-273 9.04e-22

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 99.32  E-value: 9.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 123 DLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALD----EIKLLKCVResdpsDPNkdmVVQLID 198
Cdd:COG0515     3 ALLLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARErfrrEARALARLN-----HPN---IVRVYD 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510836 199 DFKISGmngiHVCMVFE-VLGHHLLKWIikSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVD 273
Cdd:COG0515    75 VGEEDG----RPYLVMEyVEGESLADLL--RRRGPLPPAEALRILAQLAEALAAAHAA-GIVHRDIKPANILLTPD 143
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
559-734 1.02e-21

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: 96.94  E-value: 1.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 559 LLVNPLDPRnadkirVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFePHSGE 638
Cdd:cd14212   135 LLVNLDSPE------IKLIDFGSACFENYTLYTYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAAELFLGLPLF-PGNSE 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 639 dYsrdeDHIALIIELLGKVPRKYAMLGKYSKEFFTRKG----------------ELRHITKLKP------WSLFDVLVEK 696
Cdd:cd14212   208 -Y----NQLSRIIEMLGMPPDWMLEKGKNTNKFFKKVAksggrstyrlktpeefEAENNCKLEPgkryfkYKTLEDIIMN 282
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1370510836 697 YGWPHEDAAQ----------FTDFLIPMLEMVPEKRASAGECLRHPWL 734
Cdd:cd14212   283 YPMKKSKKEQidkemetrlaFIDFLKGLLEYDPKKRWTPDQALNHPFI 330
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
128-276 2.19e-21

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: 94.47  E-value: 2.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVV---KSAQHYTETALDEIKLLKCVresdpSDPNkdmVVQLIDDFKisg 204
Cdd:cd05117     1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIdkkKLKSEDEEMLRREIEILKRL-----DHPN---IVKLYEVFE--- 69
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510836 205 mNGIHVCMVFEVL-GHHLLKWIIKSNYqgLPVRCVKSIIRQVLQGLDYLHSKCkIIHTDIKPENILMCVDDAY 276
Cdd:cd05117    70 -DDKNLYLVMELCtGGELFDRIVKKGS--FSEREAAKIMKQILSAVAYLHSQG-IVHRDLKPENILLASKDPD 138
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
122-277 2.43e-21

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: 95.69  E-value: 2.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 122 GDLFNGRYHVIRKLGWGHFSTVWLCWD--MQGKRfVAMKVVKSAQHYTETALDEIKLLKCVRESDPSdpNKDMVVQLIDD 199
Cdd:cd14213     7 GDVLRARYEIVDTLGEGAFGKVVECIDhkMGGMH-VAVKIVKNVDRYREAARSEIQVLEHLNTTDPN--STFRCVQMLEW 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510836 200 FKISGmngiHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMcVDDAYV 277
Cdd:cd14213    84 FDHHG----HVCIVFELLGLSTYDFIKENSFLPFPIDHIRNMAYQICKSVNFLHHN-KLTHTDLKPENILF-VQSDYV 155
PTZ00284 PTZ00284
protein kinase; Provisional
123-285 5.33e-21

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 96.96  E-value: 5.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 123 DLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKDMVVQ--LIDDf 200
Cdd:PTZ00284  125 DVSTQRFKILSLLGEGTFGKVVEAWDRKRKEYCAVKIVRNVPKYTRDAKIEIQFMEKVRQADPADRFPLMKIQryFQNE- 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 201 kiSGmngiHVCMVFEVLGHHLLKWIIKsnYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDAYVRRM 280
Cdd:PTZ00284  204 --TG----HMCIVMPKYGPCLLDWIMK--HGPFSHRHLAQIIFQTGVALDYFHTELHLMHTDLKPENILMETSDTVVDPV 275

                  ....*
gi 1370510836 281 AAEAT 285
Cdd:PTZ00284  276 TNRAL 280
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
574-734 6.83e-21

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: 94.69  E-value: 6.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 574 VKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSgedysrDEDHIALIIEL 653
Cdd:cd14214   175 IRVADFGSATFDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQTHE------NREHLVMMEKI 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 654 LGKVPRKyaMLGKYSKEFFTRKGEL---------RHITK----LKPWSLFDVLvekygwpheDAAQFTDFLIPMLEMVPE 720
Cdd:cd14214   249 LGPIPSH--MIHRTRKQKYFYKGSLvwdenssdgRYVSEnckpLMSYMLGDSL---------EHTQLFDLLRRMLEFDPA 317
                         170
                  ....*....|....
gi 1370510836 721 KRASAGECLRHPWL 734
Cdd:cd14214   318 LRITLKEALLHPFF 331
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
99-270 8.88e-21

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: 95.20  E-value: 8.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836  99 GSDDEEqedpadyckGGYHPVkIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLK 178
Cdd:cd14224    47 GYDDEQ---------GSYIHV-PHDHIAYRYEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNEKRFHRQAAEEIRILE 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 179 CVRESDPSdpNKDMVVQLIDDFKISGmngiHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHsKCKI 258
Cdd:cd14224   117 HLKKQDKD--NTMNVIHMLESFTFRN----HICMTFELLSMNLYELIKKNKFQGFSLQLVRKFAHSILQCLDALH-RNKI 189
                         170
                  ....*....|..
gi 1370510836 259 IHTDIKPENILM 270
Cdd:cd14224   190 IHCDLKPENILL 201
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
568-734 1.57e-20

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: 93.06  E-value: 1.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 568 NADKIRVKIADLGNACWVHKH-FTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSgedysrDEDH 646
Cdd:cd14135   139 NEKKNTLKLCDFGSASDIGENeITPYLVSRFYRAPEIILGLPYDYPIDMWSVGCTLYELYTGKILFPGKT------NNHM 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 647 IALIIELLGKVPRKyaML--GKYSKEFF--------------TRKGELRHITKLKP-WSLFDVLVEKYGWPHEDA---AQ 706
Cdd:cd14135   213 LKLMMDLKGKFPKK--MLrkGQFKDQHFdenlnfiyrevdkvTKKEVRRVMSDIKPtKDLKTLLIGKQRLPDEDRkklLQ 290
                         170       180
                  ....*....|....*....|....*...
gi 1370510836 707 FTDFLIPMLEMVPEKRASAGECLRHPWL 734
Cdd:cd14135   291 LKDLLDKCLMLDPEKRITPNEALQHPFI 318
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
129-269 3.33e-20

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: 91.44  E-value: 3.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTE--TALDEIKLLKCVresdPSDPNkdmVVQLIDDFKISGmn 206
Cdd:cd07830     1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKKKFYSWEecMNLREVKSLRKL----NEHPN---IVKLKEVFREND-- 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510836 207 giHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHsKCKIIHTDIKPENIL 269
Cdd:cd07830    72 --ELYFVFEYMEGNLYQLMKDRKGKPFSESVIRSIIYQILQGLAHIH-KHGFFHRDLKPENLL 131
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
565-734 5.18e-20

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: 92.00  E-value: 5.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 565 DPRNADKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSgedysrDE 644
Cdd:cd14215   165 DERSVKSTAIRVVDFGSATFDHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHD------NR 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 645 DHIALIIELLGKVPRKyaMLGKYSKEFFTRKGEL---------RHITK-LKPWSLFdVLVEKygwphEDAAQFTDFLIPM 714
Cdd:cd14215   239 EHLAMMERILGPIPSR--MIRKTRKQKYFYHGRLdwdentsagRYVREnCKPLRRY-LTSEA-----EEHHQLFDLIESM 310
                         170       180
                  ....*....|....*....|
gi 1370510836 715 LEMVPEKRASAGECLRHPWL 734
Cdd:cd14215   311 LEYEPSKRLTLAAALKHPFF 330
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
128-274 5.44e-20

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: 90.34  E-value: 5.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETA----LDEIKLLKCVresdpSDPNkdmVVQLIDdfkiS 203
Cdd:cd14014     1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFrerfLREARALARL-----SHPN---IVRVYD----V 68
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510836 204 GMNGIHVCMVFEVLGHHLLKWIIKSNyQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVDD 274
Cdd:cd14014    69 GEDDGRPYIVMEYVEGGSLADLLRER-GPLPPREALRILAQIADALAAAHRA-GIVHRDIKPANILLTEDG 137
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
574-734 1.30e-19

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: 90.92  E-value: 1.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 574 VKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFephSGEDysrDEDHIALIIEL 653
Cdd:cd14225   187 IKVIDFGSSCYEHQRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLF---PGEN---EVEQLACIMEV 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 654 LGKVPRKYAMLGKYSKEFFTRKGELRHIT-----KLKPWS--LFDVLvekygwpHEDAAQFTDFLIPMLEMVPEKRASAG 726
Cdd:cd14225   261 LGLPPPELIENAQRRRLFFDSKGNPRCITnskgkKRRPNSkdLASAL-------KTSDPLFLDFIRRCLEWDPSKRMTPD 333

                  ....*...
gi 1370510836 727 ECLRHPWL 734
Cdd:cd14225   334 EALQHEWI 341
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
573-734 1.93e-18

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 85.66  E-value: 1.93e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836  573 RVKIADLGNACWVH--KHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEphsgedysrDEDHIALI 650
Cdd:smart00220 135 HVKLADFGLARQLDpgEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFP---------GDDQLLEL 205
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836  651 IELLGKvprkyamlGKYSKEFFtrkgelrhitklkpwslfdvlveKYGWPHEdaaqFTDFLIPMLEMVPEKRASAGECLR 730
Cdd:smart00220 206 FKKIGK--------PKPPFPPP-----------------------EWDISPE----AKDLIRKLLVKDPEKRLTAEEALQ 250

                   ....
gi 1370510836  731 HPWL 734
Cdd:smart00220 251 HPFF 254
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
129-269 2.20e-18

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: 86.18  E-value: 2.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVK---SAQHYTETALDEIKLLKCVRESDpsDPNkdmVVQLIDDF-KISG 204
Cdd:cd07838     1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRvplSEEGIPLSTIREIALLKQLESFE--HPN---VVRLLDVChGPRT 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 205 MNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCkIIHTDIKPENIL 269
Cdd:cd07838    76 DRELKLTLVFEHVDQDLATYLDKCPKPGLPPETIKDLMRQLLRGLDFLHSHR-IVHRDLKPQNIL 139
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
135-270 3.51e-18

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: 85.30  E-value: 3.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKRFVAMKVV-----------KSAQHYTETALD----EIKLLKCVREsdpsdPNkdmVVQL--- 196
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQLYAIKIFnksrlrkrregKNDRGKIKNALDdvrrEIAIMKKLDH-----PN---IVRLyev 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 197 IDDfkiSGMNgiHVCMVFE-VLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd14008    73 IDD---PESD--KLYLVLEyCEGGPVMELDSGDRVPPLPEETARKYFRDLVLGLEYLHEN-GIVHRDIKPENLLL 141
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
129-273 4.45e-18

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: 85.96  E-value: 4.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNkdmVVQLIDDFKisgmNGI 208
Cdd:cd14211     1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILSRLSQENADEFN---FVRAYECFQ----HKN 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 209 HVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENIlMCVD 273
Cdd:cd14211    74 HTCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVLTALLKLKS-LGLIHADLKPENI-MLVD 136
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
128-270 1.87e-17

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: 83.78  E-value: 1.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTE------TALDEIKLLkcvRESdpSDPNkdmVVQLIDDFk 201
Cdd:cd07841     1 RYEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEAkdginfTALREIKLL---QEL--KHPN---IIGLLDVF- 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370510836 202 isgMNGIHVCMVFEVLGHHLLKwIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILM 270
Cdd:cd07841    72 ---GHKSNINLVFEFMETDLEK-VIKDKSIVLTPADIKSYMLMTLRGLEYLHS-NWILHRDLKPNNLLI 135
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
557-736 3.22e-17

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: 83.34  E-value: 3.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 557 ADLLVNpldpRNADkirVKIADLGNACWV-----HKHFTEDIQTRQYRSIEVLIGA-GYSTPADIWSTACMAFELATGDY 630
Cdd:cd07834   132 SNILVN----SNCD---LKICDFGLARGVdpdedKGFLTEYVVTRWYRAPELLLSSkKYTKAIDIWSVGCIFAELLTRKP 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 631 LFephSGEDYsrdEDHIALIIELLGKVPRKYAmlgkyskEFFTRKGELRHITKLKPwslfdvlVEKYGWPH---EDAAQF 707
Cdd:cd07834   205 LF---PGRDY---IDQLNLIVEVLGTPSEEDL-------KFISSEKARNYLKSLPK-------KPKKPLSEvfpGASPEA 264
                         170       180
                  ....*....|....*....|....*....
gi 1370510836 708 TDFLIPMLEMVPEKRASAGECLRHPWLNS 736
Cdd:cd07834   265 IDLLEKMLVFNPKKRITADEALAHPYLAQ 293
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
128-270 8.26e-17

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: 81.55  E-value: 8.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALD---EIKLLKCVRESDpsDPNkdmVVQLIDDFKISG 204
Cdd:cd07863     1 QYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVQTNEDGLPLStvrEVALLKRLEAFD--HPN---IVRLMDVCATSR 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510836 205 MN-GIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCkIIHTDIKPENILM 270
Cdd:cd07863    76 TDrETKVTLVFEHVDQDLRTYLDKVPPPGLPAETIKDLMRQFLRGLDFLHANC-IVHRDLKPENILV 141
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
574-734 1.02e-16

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: 80.99  E-value: 1.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 574 VKIADLGNACWVH---KHFTEDIQTRQYRSIEVLIGA-GYSTPADIWSTACMAFELATGDYLFephSGEDysrDEDHIAL 649
Cdd:cd07829   137 LKLADFGLARAFGiplRTYTHEVVTLWYRAPEILLGSkHYSTAVDIWSVGCIFAELITGKPLF---PGDS---EIDQLFK 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 650 IIELLG----KVPRKYAMLGKYSKEFFTRKGElrhitklkpwSLFDVLvekygwPHEDaAQFTDFLIPMLEMVPEKRASA 725
Cdd:cd07829   211 IFQILGtpteESWPGVTKLPDYKPTFPKWPKN----------DLEKVL------PRLD-PEGIDLLSKMLQYNPAKRISA 273

                  ....*....
gi 1370510836 726 GECLRHPWL 734
Cdd:cd07829   274 KEALKHPYF 282
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
128-271 1.76e-16

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: 80.44  E-value: 1.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKV----------VKsaQHYTETALDEIKLLKCVREsdpsdPNkdmVVQLI 197
Cdd:cd13990     1 RYLLLNLLGKGGFSEVYKAFDLVEQRYVACKIhqlnkdwseeKK--QNYIKHALREYEIHKSLDH-----PR---IVKLY 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 198 DDFKIsGMNGIhvCMVFEVLGHHLLKWIIKSNyQGLPVRCVKSIIRQVLQGLDYLHS-KCKIIHTDIKPENILMC 271
Cdd:cd13990    71 DVFEI-DTDSF--CTVLEYCDGNDLDFYLKQH-KSIPEREARSIIMQVVSALKYLNEiKPPIIHYDLKPGNILLH 141
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
570-733 1.96e-16

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: 80.39  E-value: 1.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 570 DKIRVKIADLGNACWVHKH--FTEDIQTRQYRSIEVLIGAGYSTPA-DIWSTACMAFELATGDYLFEphsGEDysrDEDH 646
Cdd:cd07831   134 KDDILKLADFGSCRGIYSKppYTEYISTRWYRAPECLLTDGYYGPKmDIWAVGCVFFEILSLFPLFP---GTN---ELDQ 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 647 IALIIELLG----KVPRKYAMLGKYSKEFFTRKGelRHITKLKPwslfdvlvekygwphEDAAQFTDFLIPMLEMVPEKR 722
Cdd:cd07831   208 IAKIHDVLGtpdaEVLKKFRKSRHMNYNFPSKKG--TGLRKLLP---------------NASAEGLDLLKKLLAYDPDER 270
                         170
                  ....*....|.
gi 1370510836 723 ASAGECLRHPW 733
Cdd:cd07831   271 ITAKQALRHPY 281
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
129-278 2.29e-16

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: 79.55  E-value: 2.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVK--SAQHYtETALDEIKLLKCVREsdpsdPNkdmVVQLIDDFKISGmn 206
Cdd:cd05122     2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKINleSKEKK-ESILNEIAILKKCKH-----PN---IVKYYGSYLKKD-- 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370510836 207 giHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMcVDDAYVR 278
Cdd:cd05122    71 --ELWIVMEFCSGGSLKDLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSH-GIIHRDIKAANILL-TSDGEVK 138
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
559-732 3.70e-16

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: 79.47  E-value: 3.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 559 LLVNPldprnaDKIRVKIADLGNAcwvhKHFTED------IQTRQYRSIEVLIGA-GYSTPADIWSTAC-MAfELATGDY 630
Cdd:cd14137   137 LLVDP------ETGVLKLCDFGSA----KRLVPGepnvsyICSRYYRAPELIFGAtDYTTAIDIWSAGCvLA-ELLLGQP 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 631 LFephSGEDysrDEDHIALIIELLGKVPRK--YAMLGKYSKEFFTrkgelrhITKLKPWSLfdVLvekygwPHEDAAQFT 708
Cdd:cd14137   206 LF---PGES---SVDQLVEIIKVLGTPTREqiKAMNPNYTEFKFP-------QIKPHPWEK--VF------PKRTPPDAI 264
                         170       180
                  ....*....|....*....|....
gi 1370510836 709 DFLIPMLEMVPEKRASAGECLRHP 732
Cdd:cd14137   265 DLLSKILVYNPSKRLTALEALAHP 288
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
565-734 9.05e-16

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: 79.12  E-value: 9.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 565 DPRNADKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSgedysrDE 644
Cdd:cd14213   165 DERTLKNPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQTHD------SK 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 645 DHIALIIELLGKVPRKyaMLGKYSKEFFTRKGEL-------------RHITKLKPWSLFDvlvekygwpHEDAAQFTDFL 711
Cdd:cd14213   239 EHLAMMERILGPLPKH--MIQKTRKRKYFHHDQLdwdehssagryvrRRCKPLKEFMLSQ---------DVDHEQLFDLI 307
                         170       180
                  ....*....|....*....|...
gi 1370510836 712 IPMLEMVPEKRASAGECLRHPWL 734
Cdd:cd14213   308 QKMLEYDPAKRITLDEALKHPFF 330
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
559-734 9.49e-16

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: 78.34  E-value: 9.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 559 LLVNPLDprnadkiRVKIADLGNAcwvhKH------FTEDIQTRQYRSIEVLIGAG-YSTPADIWSTACMAFELATGDYL 631
Cdd:cd07830   130 LLVSGPE-------VVKIADFGLA----REirsrppYTDYVSTRWYRAPEILLRSTsYSSPVDIWALGCIMAELYTLRPL 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 632 FEPHSgedysrDEDHIALIIELLGKV-----PRKYAMLGKYSKEFftrkgelrhiTKLKPWSLFDVLVEkygwPHEDAAq 706
Cdd:cd07830   199 FPGSS------EIDQLYKICSVLGTPtkqdwPEGYKLASKLGFRF----------PQFAPTSLHQLIPN----ASPEAI- 257
                         170       180
                  ....*....|....*....|....*...
gi 1370510836 707 ftDFLIPMLEMVPEKRASAGECLRHPWL 734
Cdd:cd07830   258 --DLIKDMLRWDPKKRPTASQALQHPYF 283
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
129-270 1.02e-15

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: 78.37  E-value: 1.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTE---TALDEIKLLKCVREsdpsdPNkdmVVQLIDDF--KIS 203
Cdd:cd07840     1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMENEKEGfpiTAIREIKLLQKLDH-----PN---VVRLKEIVtsKGS 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510836 204 GMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRcVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd07840    73 AKYKGSIYMVFEYMDHDLTGLLDNPEVKFTESQ-IKCYMKQLLEGLQYLHSN-GILHRDIKGSNILI 137
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
128-270 1.31e-15

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: 77.50  E-value: 1.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTeTALDEIKLLKCVResdpsdpNKDMVVQLIDdfkiSGMNG 207
Cdd:cd14016     1 RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDSKHP-QLEYEAKVYKLLQ-------GGPGIPRLYW----FGQEG 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510836 208 IHVCMVFEVLGHHLLKWIIKSNYQgLPVRCVKSIIRQVLQGLDYLHSKCkIIHTDIKPENILM 270
Cdd:cd14016    69 DYNVMVMDLLGPSLEDLFNKCGRK-FSLKTVLMLADQMISRLEYLHSKG-YIHRDIKPENFLM 129
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
135-273 5.62e-15

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: 75.34  E-value: 5.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKRFVAMKVVKSA-QHYTETALDEIKLLKCVREsdpsdPNkdmVVQLIDDFKISGMngihVCMV 213
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIKCRkAKDREDVRNEIEIMNQLRH-----PR---LLQLYDAFETPRE----MVLV 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510836 214 FE-VLGHHLLKWIIKSNYQGLPVRCVKsIIRQVLQGLDYLHSKcKIIHTDIKPENIlMCVD 273
Cdd:cd14103    69 MEyVAGGELFERVVDDDFELTERDCIL-FMRQICEGVQYMHKQ-GILHLDLKPENI-LCVS 126
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
128-271 1.02e-14

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: 74.48  E-value: 1.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETAL---DEIKLLKCVREsdpsdPNkdmVVQLIDDFKISG 204
Cdd:cd14003     1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEkikREIEIMKLLNH-----PN---IIKLYEVIETEN 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510836 205 mngiHVCMVFE-VLGHHLLKWIIKSNYqgLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMC 271
Cdd:cd14003    73 ----KIYLVMEyASGGELFDYIVNNGR--LSEDEARRFFQQLISAVDYCHSN-GIVHRDLKLENILLD 133
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
128-274 1.07e-14

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: 74.81  E-value: 1.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVK----SAQHyTETALDEIKLLKCVREsdpsdPNkdmVVQLIDDFKIS 203
Cdd:cd08215     1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDlsnmSEKE-REEALNEVKLLSKLKH-----PN---IVKYYESFEEN 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510836 204 GmngiHVCMVFEV-----LGHHLLKWiiKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVDD 274
Cdd:cd08215    72 G----KLCIVMEYadggdLAQKIKKQ--KKKGQPFPEEQILDWFVQICLALKYLHSR-KILHRDLKTQNIFLTKDG 140
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
129-269 1.66e-14

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: 74.62  E-value: 1.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTE--TALDEIKLLKCVresdPSDPNkdmVVQLID---DfKIS 203
Cdd:cd07831     1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKHFKSLEqvNNLREIQALRRL----SPHPN---ILRLIEvlfD-RKT 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510836 204 GmngiHVCMVFEVLGHHLLKwIIKSNYQGLPVRCVKSIIRQVLQGLDYLHsKCKIIHTDIKPENIL 269
Cdd:cd07831    73 G----RLALVFELMDMNLYE-LIKGRKRPLPEKRVKNYMYQLLKSLDHMH-RNGIFHRDIKPENIL 132
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
121-270 1.93e-14

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 76.76  E-value: 1.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 121 IGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKsaqhyTETALDEIKLLKCVRE----SDPSDPNkdmVVQL 196
Cdd:NF033483    1 IGKLLGGRYEIGERIGRGGMAEVYLAKDTRLDRDVAVKVLR-----PDLARDPEFVARFRREaqsaASLSHPN---IVSV 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 197 IDdfkiSGMNGIHVCMVFE-VLGhHLLKWIIKSNYQgLPVRCVKSIIRQVLQGLDYLHsKCKIIHTDIKPENILM 270
Cdd:NF033483   73 YD----VGEDGGIPYIVMEyVDG-RTLKDYIREHGP-LSPEEAVEIMIQILSALEHAH-RNGIVHRDIKPQNILI 140
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
128-281 2.90e-14

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: 73.66  E-value: 2.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMK-VVKSAQHYTETALD----EIKLLKCVREsdpsdPNkdmVVQLIDDFKi 202
Cdd:cd14098     1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKqIVKRKVAGNDKNLQlfqrEINILKSLEH-----PG---IVRLIDWYE- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 203 sgmNGIHVCMVFE-VLGHHLLKWIIksNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVDDAYVRRMA 281
Cdd:cd14098    72 ---DDQHIYLVMEyVEGGDLMDFIM--AWGAIPEQHARELTKQILEAMAYTHSM-GITHRDLKPENILITQDDPVIVKIS 145
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
128-270 4.81e-14

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: 73.17  E-value: 4.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMK-VVKSAQ--HYTETALDEIKLLKCVREsdpsdPNkdmVVQLIDDFKISg 204
Cdd:cd07847     2 KYEKLSKIGEGSYGVVFKCRNRETGQIVAIKkFVESEDdpVIKKIALREIRMLKQLKH-----PN---LVNLIEVFRRK- 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510836 205 mNGIHvcMVFEVLGHHLLKWIIKsNYQGLPVRCVKSIIRQVLQGLDYLHS-KCkiIHTDIKPENILM 270
Cdd:cd07847    73 -RKLH--LVFEYCDHTVLNELEK-NPRGVPEHLIKKIIWQTLQAVNFCHKhNC--IHRDVKPENILI 133
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
575-735 5.61e-14

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: 73.99  E-value: 5.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 575 KIADLGNACWVHKHF--TEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFephSGEDYSrdeDHIALIIE 652
Cdd:cd07850   142 KILDFGLARTAGTSFmmTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVLF---PGTDHI---DQWNKIIE 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 653 LLGKVPRKYAMLGKYSKEFFTR---KGELRHITKLKPWSLFDVLVEKYGwpHEDAAQFTDFLIPMLEMVPEKRASAGECL 729
Cdd:cd07850   216 QLGTPSDEFMSRLQPTVRNYVEnrpKYAGYSFEELFPDVLFPPDSEEHN--KLKASQARDLLSKMLVIDPEKRISVDDAL 293

                  ....*.
gi 1370510836 730 RHPWLN 735
Cdd:cd07850   294 QHPYIN 299
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
129-273 7.38e-14

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: 73.52  E-value: 7.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNkdmVVQLIDDFKISGmngi 208
Cdd:cd14229     2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQGQIEVGILARLSNENADEFN---FVRAYECFQHRN---- 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 209 HVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENIlMCVD 273
Cdd:cd14229    75 HTCLVFEMLEQNLYDFLKQNKFSPLPLKVIRPILQQVATALKKLKS-LGLIHADLKPENI-MLVD 137
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
128-273 8.25e-14

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: 72.17  E-value: 8.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETA---LDEIKLLKCVresdpSDPNkdmVVQLIDDFKISG 204
Cdd:cd06606     1 RWKKGELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELealEREIRILSSL-----KHPN---IVRYLGTERTEN 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510836 205 mngiHVCMVFE-VLG---HHLLKwiiksNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVD 273
Cdd:cd06606    73 ----TLNIFLEyVPGgslASLLK-----KFGKLPEPVVRKYTRQILEGLEYLHSN-GIVHRDIKGANILVDSD 135
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
128-269 8.63e-14

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: 72.94  E-value: 8.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVksaQHYTETALD------EIKLLKCVResdpsDPNkdmVVQLID--- 198
Cdd:cd07834     1 RYELLKPIGSGAYGVVCSAYDKRTGRKVAIKKI---SNVFDDLIDakrilrEIKILRHLK-----HEN---IIGLLDilr 69
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510836 199 DFKISGMNGIHVcmVFEVLGHHLLKwIIKSNyQGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENIL 269
Cdd:cd07834    70 PPSPEEFNDVYI--VTELMETDLHK-VIKSP-QPLTDDHIQYFLYQILRGLKYLHS-AGVIHRDLKPSNIL 135
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
131-270 8.67e-14

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: 72.24  E-value: 8.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 131 VIRKLGWGHFSTVWLCWDMQGKRFVAMKVVK--SAQHYTETALDEIK-LLKCvresdpsdpNKDMVVQLIDDFKISGMng 207
Cdd:cd06623     5 RVKVLGQGSSGVVYKVRHKPTGKIYALKKIHvdGDEEFRKQLLRELKtLRSC---------ESPYVVKCYGAFYKEGE-- 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510836 208 ihVCMVFEVLGHHLLKWIIKSnYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILM 270
Cdd:cd06623    74 --ISIVLEYMDGGSLADLLKK-VGKIPEPVLAYIARQILKGLDYLHTKRHIIHRDIKPSNLLI 133
PTZ00284 PTZ00284
protein kinase; Provisional
557-734 1.11e-13

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 73.85  E-value: 1.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 557 ADLLVNPLDPRN--ADKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEP 634
Cdd:PTZ00284  268 SDTVVDPVTNRAlpPDPCRVRICDLGGCCDERHSRTAIVSTRHYRSPEVVLGLGWMYSTDMWSMGCIIYELYTGKLLYDT 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 635 HSgedysrDEDHIALIIELLGKVPRKYAML--GKYSKEFFTRKGELR------HITKL-KPWSLFDVLVEKYgwphedaa 705
Cdd:PTZ00284  348 HD------NLEHLHLMEKTLGRLPSEWAGRcgTEEARLLYNSAGQLRpctdpkHLARIaRARPVREVIRDDL-------- 413
                         170       180
                  ....*....|....*....|....*....
gi 1370510836 706 qFTDFLIPMLEMVPEKRASAGECLRHPWL 734
Cdd:PTZ00284  414 -LCDLIYGLLHYDRQKRLNARQMTTHPYV 441
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
555-734 1.39e-13

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: 71.47  E-value: 1.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 555 RAADLLVNpldprnaDKIRVKIADLGNACWVHKHFTED--IQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYlf 632
Cdd:cd05122   125 KAANILLT-------SDGEVKLIDFGLSAQLSDGKTRNtfVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKP-- 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 633 ePHSgedysrdEDHialIIELLGKVPRKYAMlgkyskefftrkgELRHITKlkpWSlfdvlvekygwphedaAQFTDFLI 712
Cdd:cd05122   196 -PYS-------ELP---PMKALFLIATNGPP-------------GLRNPKK---WS----------------KEFKDFLK 232
                         170       180
                  ....*....|....*....|..
gi 1370510836 713 PMLEMVPEKRASAGECLRHPWL 734
Cdd:cd05122   233 KCLQKDPEKRPTAEQLLKHPFI 254
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
128-271 1.49e-13

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: 71.25  E-value: 1.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVV-KSAQHYTETALD-EIKLLKCVREsdpsdPNkdmVVQLIDDFKisgm 205
Cdd:cd14083     4 KYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIdKKALKGKEDSLEnEIAVLRKIKH-----PN---IVQLLDIYE---- 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510836 206 NGIHVCMVFE-VLGHHLLKWII-KSNYQGlpvRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILMC 271
Cdd:cd14083    72 SKSHLYLVMElVTGGELFDRIVeKGSYTE---KDASHLIRQVLEAVDYLHS-LGIVHRDLKPENLLYY 135
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
129-269 1.96e-13

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: 71.55  E-value: 1.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKsAQHYTE----TALDEIKLLKCVResdpsDPNkdmVVQLIDdfkisg 204
Cdd:cd07835     1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIR-LETEDEgvpsTAIREISLLKELN-----HPN---IVRLLD------ 65
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 205 mngIHVC-----MVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:cd07835    66 ---VVHSenklyLVFEFLDLDLKKYMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSH-RVLHRDLKPQNLL 131
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
135-270 2.36e-13

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: 70.37  E-value: 2.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVREsdpsdPNkdmVVQLIDDFKisgmNGIHVCMVF 214
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFAAKFIPKRDKKKEAVLREISILNQLQH-----PR---IIQLHEAYE----SPTELVLIL 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510836 215 EVL-GHHLLKWIIKSnyQGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILM 270
Cdd:cd14006    69 ELCsGGELLDRLAER--GSLSEEEVRTYMRQLLEGLQYLHN-HHILHLDLKPENILL 122
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
128-269 3.32e-13

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: 71.16  E-value: 3.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGK--RFVAMKVVKSAQHYTE----TALDEIKLLkcvRESdpSDPNkdmVVQLIDDFk 201
Cdd:cd07842     1 KYEIEGCIGRGTYGRVYKAKRKNGKdgKEYAIKKFKGDKEQYTgisqSACREIALL---REL--KHEN---VVSLVEVF- 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370510836 202 ISGMNGiHVCMVFEVLGHHLLkWIIKSNYQG----LPVRCVKSIIRQVLQGLDYLHSKCkIIHTDIKPENIL 269
Cdd:cd07842    72 LEHADK-SVYLLFDYAEHDLW-QIIKFHRQAkrvsIPPSMVKSLLWQILNGIHYLHSNW-VLHRDLKPANIL 140
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
128-269 3.63e-13

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: 70.44  E-value: 3.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKV-VKSAQHYTETALDEIKLLKCVresdPSDPNkdmVVQLIDDFKISGMN 206
Cdd:cd13985     1 RYQVTKQLGEGGFSYVYLAHDVNTGRRYALKRmYFNDEEQLRVAIKEIEIMKRL----CGHPN---IVQYYDSAILSSEG 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370510836 207 GIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHS-KCKIIHTDIKPENIL 269
Cdd:cd13985    74 RKEVLLLMEYCPGSLVDILEKSPPSPLSEEEVLRIFYQICQAVGHLHSqSPPIIHRDIKIENIL 137
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
128-270 5.23e-13

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: 70.06  E-value: 5.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQ-GKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSD-PNkdmVVQLIDDFKISGM 205
Cdd:cd07862     2 QYECVAEIGEGAYGKVFKARDLKnGGRFVALKRVRVQTGEEGMPLSTIREVAVLRHLETFEhPN---VVRLFDVCTVSRT 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510836 206 N-GIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd07862    79 DrETKLTLVFEHVDQDLTTYLDKVPEPGVPTETIKDMMFQLLRGLDFLHSH-RVVHRDLKPQNILV 143
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
128-274 6.49e-13

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: 69.84  E-value: 6.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCvresdpsdPNkdmVVQLIDDFKISGMNG 207
Cdd:cd14137     5 SYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQDKRYKNRELQIMRRLKH--------PN---IVKLKYFFYSSGEKK 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370510836 208 IHVC--MVFEVLG---HHLLKWIIKsNYQGLPVRCVKSIIRQVLQGLDYLHSKCkIIHTDIKPENILmcVDD 274
Cdd:cd14137    74 DEVYlnLVMEYMPetlYRVIRHYSK-NKQTIPIIYVKLYSYQLFRGLAYLHSLG-ICHRDIKPQNLL--VDP 141
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
129-270 6.67e-13

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: 70.89  E-value: 6.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNkdmVVQLIDDFKISGmngi 208
Cdd:cd14228    17 YEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSRLSSENADEYN---FVRSYECFQHKN---- 89
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370510836 209 HVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILM 270
Cdd:cd14228    90 HTCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKS-LGLIHADLKPENIML 150
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
135-270 6.78e-13

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: 69.17  E-value: 6.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKRFVAMKVVKSAQ---HYTETALDEIKLLKCVResdpsDPNkdmVVQLIDDFKISGmngiHVC 211
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKlnkKLQENLESEIAILKSIK-----HPN---IVRLYDVQKTED----FIY 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 212 MVFEVL-GHHLLKWIIKsnYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd14009    69 LVLEYCaGGDLSQYIRK--RGRLPEAVARHFMQQLASGLKFLRSK-NIIHRDLKPQNLLL 125
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
128-280 8.44e-13

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: 68.89  E-value: 8.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSA-----QHYTEtalDEIKLLKCVREsdpsdPNkdmVVQLIDDFKI 202
Cdd:cd14095     1 KYDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAkckgkEHMIE---NEVAILRRVKH-----PN---IVQLIEEYDT 69
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370510836 203 SGmngiHVCMVFE-VLGHHLLKWIIKSNyqGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVDDAYVRRM 280
Cdd:cd14095    70 DT----ELYLVMElVKGGDLFDAITSST--KFTERDASRMVTDLAQALKYLHSL-SIVHRDIKPENLLVVEHEDGSKSL 141
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
128-270 8.90e-13

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: 68.82  E-value: 8.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWlcwdmQGKR-----FVAMKVV-KSAQHYTETAL--DEIKLLKCVREsdpsdPNkdmVVQLIDD 199
Cdd:cd14002     2 NYHVLELIGEGSFGKVY-----KGRRkytgqVVALKFIpKRGKSEKELRNlrQEIEILRKLNH-----PN---IIEMLDS 68
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510836 200 FKISGmngiHVCMVFEVLGHHLLKwiIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd14002    69 FETKK----EFVVVTEYAQGELFQ--ILEDDGTLPEEEVRSIAKQLVSALHYLHSN-RIIHRDMKPQNILI 132
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
574-734 1.21e-12

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: 69.63  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 574 VKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAG-YSTPADIWSTACMAFELATGDYLFEphsGEDYSrdeDHIALIIE 652
Cdd:cd07851   157 LKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMhYNQTVDIWSVGCIMAELLTGKTLFP---GSDHI---DQLKRIMN 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 653 LLGKVPRKYamLGKYSKEffTRKGELRHITKLKPWSLFDVlvekYGWPHEDAaqfTDFLIPMLEMVPEKRASAGECLRHP 732
Cdd:cd07851   231 LVGTPDEEL--LKKISSE--SARNYIQSLPQMPKKDFKEV----FSGANPLA---IDLLEKMLVLDPDKRITAAEALAHP 299

                  ..
gi 1370510836 733 WL 734
Cdd:cd07851   300 YL 301
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
574-734 1.47e-12

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: 68.88  E-value: 1.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 574 VKIADLGNACWVH----KHFTEDIQTRQYRSIEVLIGAG-YSTPADIWSTACMAFELATGDYLFEPHSgedysrDEDHIA 648
Cdd:cd07833   139 LKLCDFGFARALTarpaSPLTDYVATRWYRAPELLVGDTnYGKPVDVWAIGCIMAELLDGEPLFPGDS------DIDQLY 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 649 LIIELLGKV-PRKYAMLgkYSKEFFTRkgeLRHITKLKPwslfDVLVEKYGWPHEDAAqfTDFLIPMLEMVPEKRASAGE 727
Cdd:cd07833   213 LIQKCLGPLpPSHQELF--SSNPRFAG---VAFPEPSQP----ESLERRYPGKVSSPA--LDFLKACLRMDPKERLTCDE 281

                  ....*..
gi 1370510836 728 CLRHPWL 734
Cdd:cd07833   282 LLQHPYF 288
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
556-735 1.91e-12

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: 68.97  E-value: 1.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 556 AADLLVNPLDPRN----ADkIRVKIADLGNACWVHK-------HFTEDIQTRQYRSIEVLIG-AGYSTPADIWSTACMAF 623
Cdd:cd07857   123 SANVLHRDLKPGNllvnAD-CELKICDFGLARGFSEnpgenagFMTEYVATRWYRAPEIMLSfQSYTKAIDVWSVGCILA 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 624 ELATGDYLFEphsGEDYSrdeDHIALIIELLGKVPrkyamlgkyskefftrKGELRHITKLKPWSLFDVL----VEKYGW 699
Cdd:cd07857   202 ELLGRKPVFK---GKDYV---DQLNQILQVLGTPD----------------EETLSRIGSPKAQNYIRSLpnipKKPFES 259
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1370510836 700 PHEDAA-QFTDFLIPMLEMVPEKRASAGECLRHPWLN 735
Cdd:cd07857   260 IFPNANpLALDLLEKLLAFDPTKRISVEEALEHPYLA 296
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
132-270 1.99e-12

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: 68.30  E-value: 1.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 132 IRKLGWGHFSTVWLCWDMQGKRFVAMKVVK---SAQHYTETALDEIKLLKcvresDPSDPNkdmVVQLIDdfKISGMNGI 208
Cdd:cd07860     5 VEKIGEGTYGVVYKARNKLTGEVVALKKIRldtETEGVPSTAIREISLLK-----ELNHPN---IVKLLD--VIHTENKL 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370510836 209 HvcMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd07860    75 Y--LVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSH-RVLHRDLKPQNLLI 133
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
559-734 2.42e-12

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: 68.87  E-value: 2.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 559 LLVNpldpRNADkirVKIADLG---NACWVHKH---FTEDIQTRQYRSIEV-LIGAGYSTPADIWSTACMAFELATGDYL 631
Cdd:cd07849   137 LLLN----TNCD---LKICDFGlarIADPEHDHtgfLTEYVATRWYRAPEImLNSKGYTKAIDIWSVGCILAEMLSNRPL 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 632 FephSGEDYsrdEDHIALIIELLGKvPRK---YAMLGKYSKEFFTrkgELRHITKLkPW-SLFdvlvekygwPHEDAAQF 707
Cdd:cd07849   210 F---PGKDY---LHQLNLILGILGT-PSQedlNCIISLKARNYIK---SLPFKPKV-PWnKLF---------PNADPKAL 269
                         170       180
                  ....*....|....*....|....*..
gi 1370510836 708 tDFLIPMLEMVPEKRASAGECLRHPWL 734
Cdd:cd07849   270 -DLLDKMLTFNPHKRITVEEALAHPYL 295
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
129-270 2.92e-12

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: 68.96  E-value: 2.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNkdmVVQLIDDFKISGmngi 208
Cdd:cd14227    17 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILARLSTESADDYN---FVRAYECFQHKN---- 89
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370510836 209 HVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILM 270
Cdd:cd14227    90 HTCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKS-LGLIHADLKPENIML 150
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
128-269 4.70e-12

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: 67.57  E-value: 4.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTetALDEIKLLKCVResdpSDPNkdmVVQLIDDFK--ISGm 205
Cdd:cd14132    19 DYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLKPVKKKK--IKREIKILQNLR----GGPN---IVKLLDVVKdpQSK- 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370510836 206 ngiHVCMVFEVLGHhlLKWiiKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:cd14132    89 ---TPSLIFEYVNN--TDF--KTLYPTLTDYDIRYYMYELLKALDYCHSK-GIMHRDVKPHNIM 144
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
129-270 6.15e-12

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: 66.47  E-value: 6.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKcvresDPSDPNkdmVVQLIDDFKISGmngi 208
Cdd:cd06614     2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQNKELIINEILIMK-----ECKHPN---IVDYYDSYLVGD---- 69
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370510836 209 HVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd06614    70 ELWVVMEYMDGGSLTDIITQNPVRMNESQIAYVCREVLQGLEYLHSQ-NVIHRDIKSDNILL 130
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
573-733 6.96e-12

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: 66.74  E-value: 6.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 573 RVKIADLGNA----CWVHKhFTEDIQTRQYRSIEVLIGA-GYSTPADIWSTACMAFELATGDYLFephSGEDysrDEDHI 647
Cdd:cd07836   138 ELKLADFGLArafgIPVNT-FSNEVVTLWYRAPDVLLGSrTYSTSIDIWSVGCIMAEMITGRPLF---PGTN---NEDQL 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 648 ALIIELLGkVPRKYAMLGkyskefFTRKGELRHITKLKPWSLFDVLVekygwPHEDAAQFtDFLIPMLEMVPEKRASAGE 727
Cdd:cd07836   211 LKIFRIMG-TPTESTWPG------ISQLPEYKPTFPRYPPQDLQQLF-----PHADPLGI-DLLHRLLQLNPELRISAHD 277

                  ....*.
gi 1370510836 728 CLRHPW 733
Cdd:cd07836   278 ALQHPW 283
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
129-274 8.44e-12

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: 65.96  E-value: 8.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQ---HYTETALD-EIKLLKCVREsdpsdPNkdmVVQLIDDFKisg 204
Cdd:cd14007     2 FEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQlqkSGLEHQLRrEIEIQSHLRH-----PN---ILRLYGYFE--- 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510836 205 mNGIHVCMVFEVLGH-HLLKWIIKSNYqgLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVDD 274
Cdd:cd14007    71 -DKKRIYLILEYAPNgELYKELKKQKR--FDEKEAAKYIYQLALALDYLHSK-NIIHRDIKPENILLGSNG 137
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
558-734 1.08e-11

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: 67.08  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 558 DLLVNpldprnaDKIRVKIADLGNA-CW---VHKHFTEDIQTRQYRSIEVLIGAG-YSTPADIWSTACMAFELATGDYLF 632
Cdd:cd07853   133 NLLVN-------SNCVLKICDFGLArVEepdESKHMTQEVVTQYYRAPEILMGSRhYTSAVDIWSVGCIFAELLGRRILF 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 633 EPHSgedysrDEDHIALIIELLGkVPRKYAMlgkyskeFFTRKGELRHI--TKLKPWSLfDVLvekYGWPHEDAAQFTDF 710
Cdd:cd07853   206 QAQS------PIQQLDLITDLLG-TPSLEAM-------RSACEGARAHIlrGPHKPPSL-PVL---YTLSSQATHEAVHL 267
                         170       180
                  ....*....|....*....|....
gi 1370510836 711 LIPMLEMVPEKRASAGECLRHPWL 734
Cdd:cd07853   268 LCRMLVFDPDKRISAADALAHPYL 291
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
128-269 1.40e-11

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: 65.92  E-value: 1.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGK-RFVAMKVVKSAQ---HYTETA-----LDEIKLLKCVresdpSDPNkdmVVQLID 198
Cdd:cd14096     2 NYRLINKIGEGAFSNVYKAVPLRNTgKPVAIKVVRKADlssDNLKGSsraniLKEVQIMKRL-----SHPN---IVKLLD 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370510836 199 DFKisgmNGIHVCMVFEVL-GHHLLKWIIKSNY--QGLPvrcvKSIIRQVLQGLDYLHSkCKIIHTDIKPENIL 269
Cdd:cd14096    74 FQE----SDEYYYIVLELAdGGEIFHQIVRLTYfsEDLS----RHVITQVASAVKYLHE-IGVVHRDIKPENLL 138
Pkinase pfam00069
Protein kinase domain;
595-734 1.69e-11

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 64.19  E-value: 1.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 595 TRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSGedysrDEDHIALIIELLGKVPRKYAmlgkYSKEfftr 674
Cdd:pfam00069 123 TPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGING-----NEIYELIIDQPYAFPELPSN----LSEE---- 189
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 675 kgelrhitklkpwslfdvlvekygwphedaaqFTDFLIPMLEMVPEKRASAGECLRHPWL 734
Cdd:pfam00069 190 --------------------------------AKDLLKKLLKKDPSKRLTATQALQHPWF 217
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
129-274 1.91e-11

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: 64.90  E-value: 1.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQG--KRFVAMKVV---KSAQHYTETALD-EIKLLKCVREsdpsdPNkdmVVQLIDDFKI 202
Cdd:cd14080     2 YRLGKTIGEGSYSKVKLAEYTKSglKEKVACKIIdkkKAPKDFLEKFLPrELEILRKLRH-----PN---IIQVYSIFER 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510836 203 SGMngihVCMVFEVLGH-HLLKWIIKsnYQGLPVRCVKSIIRQVLQGLDYLHSKCkIIHTDIKPENILMCVDD 274
Cdd:cd14080    74 GSK----VFIFMEYAEHgDLLEYIQK--RGALSESQARIWFRQLALAVQYLHSLD-IAHRDLKCENILLDSNN 139
Pkinase pfam00069
Protein kinase domain;
129-250 2.04e-11

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 64.19  E-value: 2.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQ---HYTETALDEIKLLKCVREsdpsdPNkdmVVQLIDDFkisgM 205
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKikkKKDKNILREIKILKKLNH-----PN---IVRLYDAF----E 68
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1370510836 206 NGIHVCMVFE-VLGHHLLKWIikSNYQGLPVRCVKSIIRQVLQGLD 250
Cdd:pfam00069  69 DKDNLYLVLEyVEGGSLFDLL--SEKGAFSEREAKFIMKQILEGLE 112
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
128-273 2.22e-11

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: 64.71  E-value: 2.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWD-MQGKRFvamkVVKSAQHYTETALDEIKLLKCVrESDPSDPNKDMVVQLIDdfkiSGMN 206
Cdd:cd13997     1 HFHELEQIGSGSFSEVFKVRSkVDGCLY----AVKKSKKPFRGPKERARALREV-EAHAALGQHPNIVRYYS----SWEE 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370510836 207 GIHVCMVFEVLGHHLLKWIIKSNYQG--LPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVD 273
Cdd:cd13997    72 GGHLYIQMELCENGSLQDALEELSPIskLSEAEVWDLLLQVALGLAFIHSK-GIVHLDIKPDNIFISNK 139
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
128-269 2.87e-11

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: 65.04  E-value: 2.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMK---VVKSAQHYTETALDEIKLLKCVRESdpsdPNkdmVVQLIDDFKisg 204
Cdd:cd07832     1 RYKILGRIGEGAHGIVFKAKDRETGETVALKkvaLRKLEGGIPNQALREIKALQACQGH----PY---VVKLRDVFP--- 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 205 mNGIHVCMVFEVLGHHLLKwIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:cd07832    71 -HGTGFVLVFEYMLSSLSE-VLRDEERPLTEAQVKRYMRMLLKGVAYMHAN-RIMHRDLKPANLL 132
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
128-290 3.44e-11

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: 64.75  E-value: 3.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTET---ALDEIKLLKCVREsdpsdpnkDMVVQLIDDFKisg 204
Cdd:cd07846     2 KYENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMVkkiAMREIKMLKQLRH--------ENLVNLIEVFR--- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 205 mNGIHVCMVFEVLGHHLLKWIikSNY-QGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENIL--------MCvDDA 275
Cdd:cd07846    71 -RKKRWYLVFEFVDHTVLDDL--EKYpNGLDESRVRKYLFQILRGIDFCHSH-NIIHRDIKPENILvsqsgvvkLC-DFG 145
                         170       180
                  ....*....|....*....|...
gi 1370510836 276 YVRRMAAE--------ATEWQKA 290
Cdd:cd07846   146 FARTLAAPgevytdyvATRWYRA 168
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
127-303 3.95e-11

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: 64.64  E-value: 3.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 127 GRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKvvKSAQHyTE------TALDEIKLLKCVREsdpsdPNkdmVVQLIDDF 200
Cdd:cd07866     8 RDYEILGKLGEGTFGEVYKARQIKTGRVVALK--KILMH-NEkdgfpiTALREIKILKKLKH-----PN---VVPLIDMA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 201 -----KISGMNGIhVCMVFEVLGHHLLKWIIKSNYQgLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILmcVDDA 275
Cdd:cd07866    77 verpdKSKRKRGS-VYMVTPYMDHDLSGLLENPSVK-LTESQIKCYMLQLLEGINYLHEN-HILHRDIKAANIL--IDNQ 151
                         170       180       190
                  ....*....|....*....|....*....|
gi 1370510836 276 YVRRMA--AEATEWQKAGAPPPSGSAVSTA 303
Cdd:cd07866   152 GILKIAdfGLARPYDGPPPNPKGGGGGGTR 181
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
133-269 4.07e-11

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: 63.91  E-value: 4.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 133 RKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTET-----ALD-EIKLLKCVREsdpsdpnkDMVVQLIDDFKISGmn 206
Cdd:cd06625     6 KLLGQGAFGQVYLCYDADTGRELAVKQVEIDPINTEAskevkALEcEIQLLKNLQH--------ERIVQYYGCLQDEK-- 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510836 207 giHVCMVFEVLGHHLLKWIIKsNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:cd06625    76 --SLSIFMEYMPGGSVKDEIK-AYGALTENVTRKYTRQILEGLAYLHSN-MIVHRDIKGANIL 134
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
553-733 4.33e-11

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: 64.55  E-value: 4.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 553 KTraADLLVNpldprnaDKIRVKIADLGNACWVH---KHFTEDIQTRQYRSIEVLIGAG-YSTPADIWSTACMAFELATG 628
Cdd:cd07843   133 KT--SNLLLN-------NRGILKICDFGLAREYGsplKPYTQLVVTLWYRAPELLLGAKeYSTAIDMWSVGCIFAELLTK 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 629 DYLFEPHSgedysrDEDHIALIIELLGKVPRK----YAMLGKYSKEFFTRKGELRHITKLKPWSLFDVLVekygwpheda 704
Cdd:cd07843   204 KPLFPGKS------EIDQLNKIFKLLGTPTEKiwpgFSELPGAKKKTFTKYPYNQLRKKFPALSLSDNGF---------- 267
                         170       180
                  ....*....|....*....|....*....
gi 1370510836 705 aqftDFLIPMLEMVPEKRASAGECLRHPW 733
Cdd:cd07843   268 ----DLLNRLLTYDPAKRISAEDALKHPY 292
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
574-735 4.34e-11

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: 65.05  E-value: 4.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 574 VKIADLGNACWVHKHF--TEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEphsGEDYSrdeDHIALII 651
Cdd:cd07876   162 LKILDFGLARTACTNFmmTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQ---GTDHI---DQWNKVI 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 652 ELLGkVPrkyamlgkySKEFFTRKGE-LRHITKLKPWS---LFDVLVEKYGWPHED------AAQFTDFLIPMLEMVPEK 721
Cdd:cd07876   236 EQLG-TP---------SAEFMNRLQPtVRNYVENRPQYpgiSFEELFPDWIFPSESerdklkTSQARDLLSKMLVIDPDK 305
                         170
                  ....*....|....
gi 1370510836 722 RASAGECLRHPWLN 735
Cdd:cd07876   306 RISVDEALRHPYIT 319
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
128-270 6.50e-11

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: 63.40  E-value: 6.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAqHYTETALD----EIKLLKCVREsdpsdPNkdmVVQLIDDFKIs 203
Cdd:cd06627     1 NYQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLE-KIPKSDLKsvmgEIDLLKKLNH-----PN---IVKYIGSVKT- 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510836 204 gmnGIHVCMVFE-VLGHHLLKwIIKsNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd06627    71 ---KDSLYIILEyVENGSLAS-IIK-KFGKFPESLVAVYIYQVLEGLAYLHEQ-GVIHRDIKGANILT 132
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
128-276 7.99e-11

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: 63.18  E-value: 7.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVK---SAQHYTETALDEIKLLKCVresdpSDPNkdmvvqlIDDFKISG 204
Cdd:cd08530     1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNlgsLSQKEREDSVNEIRLLASV-----NHPN-------IIRYKEAF 68
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 205 MNGIHVCMVFEVL-GHHLLKWIIKSNYQGLPVR--CVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILMCVDDAY 276
Cdd:cd08530    69 LDGNRLCIVMEYApFGDLSKLISKRKKKRRLFPedDIWRIFIQMLRGLKALHD-QKILHRDLKSANILLSAGDLV 142
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
564-735 8.21e-11

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: 63.70  E-value: 8.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 564 LDPRN--ADKIR--VKIADLG--NACWVH-KHFTEDIQTRQYRSIEVLIGAG-YSTPADIWSTACMAFELATGDYLFeph 635
Cdd:cd07837   135 LKPQNllVDKQKglLKIADLGlgRAFTIPiKSYTHEIVTLWYRAPEVLLGSThYSTPVDMWSVGCIFAEMSRKQPLF--- 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 636 SGEDYSRDEDHIaliiellgkvprkYAMLGKYSKEFFTrkgelrHITKLKPWSLFDvlvekyGWPHEDAAQF-------- 707
Cdd:cd07837   212 PGDSELQQLLHI-------------FRLLGTPNEEVWP------GVSKLRDWHEYP------QWKPQDLSRAvpdlepeg 266
                         170       180
                  ....*....|....*....|....*...
gi 1370510836 708 TDFLIPMLEMVPEKRASAGECLRHPWLN 735
Cdd:cd07837   267 VDLLTKMLAYDPAKRISAKAALQHPYFD 294
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
128-274 8.77e-11

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: 63.48  E-value: 8.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQH---YTETALDEIKLLKCVREsdpsdpnkDMVVQLIDDFKISG 204
Cdd:cd07848     2 KFEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEEneeVKETTLRELKMLRTLKQ--------ENIVELKEAFRRRG 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 205 mngiHVCMVFEVLGHHLLKwIIKSNYQGLPVRCVKSIIRQVLQGLDYLHsKCKIIHTDIKPENILMCVDD 274
Cdd:cd07848    74 ----KLYLVFEYVEKNMLE-LLEEMPNGVPPEKVRSYIYQLIKAIHWCH-KNDIVHRDIKPENLLISHND 137
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
129-273 1.03e-10

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: 62.71  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKS-AQHYTETALDEIKLLKCVRESDpsdpnkdmVVQLIDDFKisgmNG 207
Cdd:cd14191     4 YDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAySAKEKENIRQEISIMNCLHHPK--------LVQCVDAFE----EK 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510836 208 IHVCMVFEVL-GHHLLKWIIKSNYQGLPVRCVKsIIRQVLQGLDYLHSKcKIIHTDIKPENIlMCVD 273
Cdd:cd14191    72 ANIVMVLEMVsGGELFERIIDEDFELTERECIK-YMRQISEGVEYIHKQ-GIVHLDLKPENI-MCVN 135
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
132-269 1.04e-10

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: 62.95  E-value: 1.04e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836  132 IRKLGWGHFSTVWLC-WDMQG---KRFVAMKVVKSAQHYTETA--LDEIKLLKCVResdpsDPNkdmVVQLIddfkisgm 205
Cdd:smart00221   4 GKKLGEGAFGEVYKGtLKGKGdgkEVEVAVKTLKEDASEQQIEefLREARIMRKLD-----HPN---IVKLL-------- 67
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836  206 nGI-----HVCMVFEVLGH-HLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:smart00221  68 -GVcteeePLMIVMEYMPGgDLLDYLRKNRPKELSLSDLLSFALQIARGMEYLESK-NFIHRDLAARNCL 135
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
569-733 1.31e-10

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: 63.15  E-value: 1.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 569 ADKIRVKIADLGNACWVH---KHFTEDIQTRQYRSIEVLIGA-GYSTPADIWSTACMAFELATGDYLFePHSGEdysrdE 644
Cdd:cd07845   142 TDKGCLKIADFGLARTYGlpaKPMTPKVVTLWYRAPELLLGCtTYTTAIDMWAVGCILAELLAHKPLL-PGKSE-----I 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 645 DHIALIIELLGkVPRKYAMLGkYSKEFFTRKGELRHitklKPWSLfdvLVEKYGWPHEDAAQFTDFLipmLEMVPEKRAS 724
Cdd:cd07845   216 EQLDLIIQLLG-TPNESIWPG-FSDLPLVGKFTLPK----QPYNN---LKHKFPWLSEAGLRLLNFL---LMYDPKKRAT 283

                  ....*....
gi 1370510836 725 AGECLRHPW 733
Cdd:cd07845   284 AEEALESSY 292
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
128-270 1.45e-10

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: 62.62  E-value: 1.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDmQGKRFVAMKVVKSAQHYTETA---LDEIKLLKCVResdpsdpNKDMVVQLIDdFKISG 204
Cdd:cd14131     2 PYEILKQLGKGGSSKVYKVLN-PKKKIYALKRVDLEGADEQTLqsyKNEIELLKKLK-------GSDRIIQLYD-YEVTD 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510836 205 MNGiHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd14131    73 EDD-YLYMVMECGEIDLATILKKKRPKPIDPNFIRYYWKQMLEAVHTIHEE-GIVHSDLKPANFLL 136
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
564-734 1.47e-10

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: 62.78  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 564 LDPRN---ADKIRVKIADLGNA---CWVHKHFTEDIQTRQYRSIEVLIGA-GYSTPADIWSTACMAFELATGDYLFePHS 636
Cdd:cd07844   124 LKPQNlliSERGELKLADFGLArakSVPSKTYSNEVVTLWYRPPDVLLGStEYSTSLDMWGVGCIFYEMATGRPLF-PGS 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 637 gedySRDEDHIALIIELLG--------KVPRKYAMLgKYSKEFFTRKGELRHITKLkpwslfdvlvekygwphEDAAQFT 708
Cdd:cd07844   203 ----TDVEDQLHKIFRVLGtpteetwpGVSSNPEFK-PYSFPFYPPRPLINHAPRL-----------------DRIPHGE 260
                         170       180
                  ....*....|....*....|....*.
gi 1370510836 709 DFLIPMLEMVPEKRASAGECLRHPWL 734
Cdd:cd07844   261 ELALKFLQYEPKKRISAAEAMKHPYF 286
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
573-734 1.54e-10

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: 62.68  E-value: 1.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 573 RVKIADLGNA---CWvHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEphsGEDysrDEDHIAL 649
Cdd:cd07838   145 QVKLADFGLAriySF-EMALTSVVVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFR---GSS---EADQLGK 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 650 IIELLGKVPR----KYAMLGKYSKEFFTRkgelRHITKLKPwslfdvlvekygwphEDAAQFTDFLIPMLEMVPEKRASA 725
Cdd:cd07838   218 IFDVIGLPSEeewpRNSALPRSSFPSYTP----RPFKSFVP---------------EIDEEGLDLLKKMLTFNPHKRISA 278

                  ....*....
gi 1370510836 726 GECLRHPWL 734
Cdd:cd07838   279 FEALQHPYF 287
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
574-735 1.73e-10

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: 63.18  E-value: 1.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 574 VKIADLGNACWVHKHF--TEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFephSGEDYSrdeDHIALII 651
Cdd:cd07874   158 LKILDFGLARTAGTSFmmTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILF---PGRDYI---DQWNKVI 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 652 ELLGK-VPRKYAMLGKYSKEFFTRKGELRHIT--KLKPWSLFDVLVEKYGWpheDAAQFTDFLIPMLEMVPEKRASAGEC 728
Cdd:cd07874   232 EQLGTpCPEFMKKLQPTVRNYVENRPKYAGLTfpKLFPDSLFPADSEHNKL---KASQARDLLSKMLVIDPAKRISVDEA 308

                  ....*..
gi 1370510836 729 LRHPWLN 735
Cdd:cd07874   309 LQHPYIN 315
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
129-269 1.78e-10

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: 61.85  E-value: 1.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSA-QHYTETA-----LDEIKLLKCVResdpsdpNKDMVVQLIDDFKi 202
Cdd:cd14019     3 YRIIEKIGEGTFSSVYKAEDKLHDLYDRNKGRLVAlKHIYPTSspsriLNELECLERLG-------GSNNVSGLITAFR- 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510836 203 sgmNGIHVCMVFEVLGHHLLKWIIKSnyqgLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:cd14019    75 ---NEDQVVAVLPYIEHDDFRDFYRK----MSLTDIRIYLRNLFKALKHVHSF-GIIHRDVKPGNFL 133
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
128-278 2.85e-10

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: 61.60  E-value: 2.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMK-VVKSaqHYTETALDEIKLLKCVRESD-----PSDPNkdmVVQLIDDFK 201
Cdd:cd13993     1 RYQLISPIGEGAYGVVYLAVDLRTGRKYAIKcLYKS--GPNSKDGNDFQKLPQLREIDlhrrvSRHPN---IITLHDVFE 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370510836 202 ISgmNGIHVCMVFEVLGHhlLKWIIKSN--YQGLPVRcVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVDDAYVR 278
Cdd:cd13993    76 TE--VAIYIVLEYCPNGD--LFEAITENriYVGKTEL-IKNVFLQLIDAVKHCHSL-GIYHRDIKPENILLSQDEGTVK 148
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
125-276 3.63e-10

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: 61.25  E-value: 3.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 125 FNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVK-------SAQHYTETA--LDEIKLLKCVresdpSDPNkdmVVQ 195
Cdd:cd14084     4 LRKKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINkrkftigSRREINKPRniETEIEILKKL-----SHPC---IIK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 196 LIDDFKISGmngiHVCMVFEVL-GHHLLKWIIKSnyQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVDD 274
Cdd:cd14084    76 IEDFFDAED----DYYIVLELMeGGELFDRVVSN--KRLKEAICKLYFYQMLLAVKYLHSN-GIIHRDLKPENVLLSSQE 148

                  ..
gi 1370510836 275 AY 276
Cdd:cd14084   149 EE 150
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
123-270 3.69e-10

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: 61.14  E-value: 3.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 123 DLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESdpsdpnkdMVVQLIDDFKI 202
Cdd:cd14113     3 DNFDSFYSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQVTHELGVLQSLQHP--------QLVGLLDTFET 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370510836 203 SGmngiHVCMVFEVLGH-HLLKWIIKsnYQGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILM 270
Cdd:cd14113    75 PT----SYILVLEMADQgRLLDYVVR--WGNLTEEKIRFYLREILEALQYLHN-CRIAHLDLKPENILV 136
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
129-270 4.90e-10

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: 61.08  E-value: 4.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVReSDPSDPNkdmVVQLIDDFKISGmngi 208
Cdd:cd05581     3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIIKEKKVKYVTIEKEVL-SRLAHPG---IVKLYYTFQDES---- 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510836 209 hvCMVFeVLGH----HLLKWIIKsnYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd05581    75 --KLYF-VLEYapngDLLEYIRK--YGSLDEKCTRFYTAEIVLALEYLHSK-GIIHRDLKPENILL 134
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
135-277 5.05e-10

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: 60.63  E-value: 5.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLcwdmqGK---RFVAMKVVKSAQHYTETALD---EIKLLKCVResdpsDPNkdmVVQLIddfkisG--MN 206
Cdd:cd13999     1 IGSGSFGEVYK-----GKwrgTDVAIKKLKVEDDNDELLKEfrrEVSILSKLR-----HPN---IVQFI------GacLS 61
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510836 207 GIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILmcVDDAYV 277
Cdd:cd13999    62 PPPLCIVTEYMPGGSLYDLLHKKKIPLSWSLRLKIALDIARGMNYLHSP-PIIHRDLKSLNIL--LDENFT 129
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
573-734 8.36e-10

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: 60.36  E-value: 8.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 573 RVKIADLGNA----CwvHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSgedysrDEDHIA 648
Cdd:cd07863   146 QVKLADFGLAriysC--QMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNS------EADQLG 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 649 LIIELLG-----KVPRKYAMlgkySKEFFTRKGElRHITKLKPwslfdvlvekygwphEDAAQFTDFLIPMLEMVPEKRA 723
Cdd:cd07863   218 KIFDLIGlppedDWPRDVTL----PRGAFSPRGP-RPVQSVVP---------------EIEESGAQLLLEMLTFNPHKRI 277
                         170
                  ....*....|.
gi 1370510836 724 SAGECLRHPWL 734
Cdd:cd07863   278 SAFRALQHPFF 288
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
568-734 9.81e-10

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: 60.65  E-value: 9.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 568 NADkIRVKIADLGNACWVHKH--------FTEDIQTRQYRSIEVLIGA-GYSTPADIWSTACMAFELATGDYLFEPHSge 638
Cdd:cd07852   141 NSD-CRVKLADFGLARSLSQLeeddenpvLTDYVATRWYRAPEILLGStRYTKGVDMWSVGCILGEMLLGKPLFPGTS-- 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 639 dysrDEDHIALIIELLGKVPRK--------YA--MLgkyskefftrkgELRHITKLKPwslfdvLVEKYGWPHEDAAqft 708
Cdd:cd07852   218 ----TLNQLEKIIEVIGRPSAEdiesiqspFAatML------------ESLPPSRPKS------LDELFPKASPDAL--- 272
                         170       180
                  ....*....|....*....|....*.
gi 1370510836 709 DFLIPMLEMVPEKRASAGECLRHPWL 734
Cdd:cd07852   273 DLLKKLLVFNPNKRLTAEEALRHPYV 298
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
559-734 1.06e-09

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: 60.54  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 559 LLVNPLDPRnadkIRVKIADLGNACWVHKHFTED-IQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSG 637
Cdd:cd14211   133 MLVDPVRQP----YRVKVIDFGSASHVSKAVCSTyLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGSSE 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 638 ED--------------------------YSRDEDHIALIIELlgKVPRKY-AMLGKYSKE----FFTRKGELRHITKLKP 686
Cdd:cd14211   209 YDqiryisqtqglpaehllnaatktsrfFNRDPDSPYPLWRL--KTPEEHeAETGIKSKEarkyIFNCLDDMAQVNGPSD 286
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1370510836 687 WSLFDVLVEKYgwpheDAAQFTDFLIPMLEMVPEKRASAGECLRHPWL 734
Cdd:cd14211   287 LEGSELLAEKA-----DRREFIDLLKRMLTIDQERRITPGEALNHPFV 329
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
132-269 1.10e-09

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 59.85  E-value: 1.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836  132 IRKLGWGHFSTVWLC-WDMQG---KRFVAMKVVKSaqHYTETA----LDEIKLLKCVResdpsDPNkdmVVQLIddfkis 203
Cdd:smart00219   4 GKKLGEGAFGEVYKGkLKGKGgkkKVEVAVKTLKE--DASEQQieefLREARIMRKLD-----HPN---VVKLL------ 67
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510836  204 gmnGI-----HVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:smart00219  68 ---GVcteeePLYIVMEYMEGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESK-NFIHRDLAARNCL 134
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
135-274 1.19e-09

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: 59.86  E-value: 1.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKRFVAMKVV-------KSAQ---HYTETALDEIKLLKcvresDPSDPNkdmVVQLIDdfkiSG 204
Cdd:cd06628     8 IGSGSFGSVYLGMNASSGELMAVKQVelpsvsaENKDrkkSMLDALQREIALLR-----ELQHEN---IVQYLG----SS 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510836 205 MNGIHVCMVFE-VLGHHLLKWIikSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILmcVDD 274
Cdd:cd06628    76 SDANHLNIFLEyVPGGSVATLL--NNYGAFEESLVRNFVRQILKGLNYLHNR-GIIHRDIKGANIL--VDN 141
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
135-304 1.61e-09

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: 59.24  E-value: 1.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLC--WDMQGKRFVAMKVVK------SAQHYTETALDEIKLLKCVREsdpsdPNkdmVVQLIDDFKisgMN 206
Cdd:cd13994     1 IGKGATSVVRIVtkKNPRSGVLYAVKEYRrrddesKRKDYVKRLTSEYIISSKLHH-----PN---IVKVLDLCQ---DL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 207 GIHVCMVFE-VLGHHLLKWIIKSNyqGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVD------D---AY 276
Cdd:cd13994    70 HGKWCLVMEyCPGGDLFTLIEKAD--SLSLEEKDCFFKQILRGVAYLHSH-GIAHRDLKPENILLDEDgvlkltDfgtAE 146
                         170       180
                  ....*....|....*....|....*...
gi 1370510836 277 VRRMAAEATEWQKAGappPSGSAVSTAP 304
Cdd:cd13994   147 VFGMPAEKESPMSAG---LCGSEPYMAP 171
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
574-735 1.72e-09

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: 59.14  E-value: 1.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 574 VKIADLGnacwVHKHfTEDIQ--------TRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPhsgedysrded 645
Cdd:cd06623   139 VKIADFG----ISKV-LENTLdqcntfvgTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLP----------- 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 646 hialiiellGKVPRKYAMlgkyskefftrkgeLRHITKlkpwslfdvlVEKYGWPHEDA-AQFTDFLIPMLEMVPEKRAS 724
Cdd:cd06623   203 ---------PGQPSFFEL--------------MQAICD----------GPPPSLPAEEFsPEFRDFISACLQKDPKKRPS 249
                         170
                  ....*....|.
gi 1370510836 725 AGECLRHPWLN 735
Cdd:cd06623   250 AAELLQHPFIK 260
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
573-733 1.83e-09

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: 59.61  E-value: 1.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 573 RVKIADLGNACWVHKH----FTED--IQTRQYRSIEVLIGAGYSTPA-DIWSTACMAFELATGDYLF-----EPHSGEDY 640
Cdd:cd07842   150 VVKIGDLGLARLFNAPlkplADLDpvVVTIWYRAPELLLGARHYTKAiDIWAIGCIFAELLTLEPIFkgreaKIKKSNPF 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 641 SRDEdhIALIIELLG-----------KVPRKYAMLGKYSKEFFTRKGelrhitkLKPWslfdvlVEKYGWPhedAAQFTD 709
Cdd:cd07842   230 QRDQ--LERIFEVLGtptekdwpdikKMPEYDTLKSDTKASTYPNSL-------LAKW------MHKHKKP---DSQGFD 291
                         170       180
                  ....*....|....*....|....
gi 1370510836 710 FLIPMLEMVPEKRASAGECLRHPW 733
Cdd:cd07842   292 LLRKLLEYDPTKRITAEEALEHPY 315
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
574-733 2.06e-09

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: 59.03  E-value: 2.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 574 VKIADLGNAcwvhKHFTEDIQTRQ------YRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFephsgedYSRDEDhi 647
Cdd:cd05117   141 IKIIDFGLA----KIFEEGEKLKTvcgtpyYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPF-------YGETEQ-- 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 648 aliiELLGKVprkyaMLGKYSkefftrkgelrhitklkpwslFDvlvEKYGWPHEDAAQftDFLIPMLEMVPEKRASAGE 727
Cdd:cd05117   208 ----ELFEKI-----LKGKYS---------------------FD---SPEWKNVSEEAK--DLIKRLLVVDPKKRLTAAE 252

                  ....*.
gi 1370510836 728 CLRHPW 733
Cdd:cd05117   253 ALNHPW 258
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
128-269 2.66e-09

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: 59.30  E-value: 2.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETA---LDEIKLLKCVREsdpsdpnkDMVVQLIDDFKISG 204
Cdd:cd07855     6 RYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVTTAkrtLRELKILRHFKH--------DNIIAIRDILRPKV 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 205 M--NGIHVCMVFEVLG---HHllkwIIKSNyQGLPVRCVKSIIRQVLQGLDYLHSKCkIIHTDIKPENIL 269
Cdd:cd07855    78 PyaDFKDVYVVLDLMEsdlHH----IIHSD-QPLTLEHIRYFLYQLLRGLKYIHSAN-VIHRDLKPSNLL 141
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
126-278 2.92e-09

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: 58.84  E-value: 2.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 126 NGRY----HVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVK--SAQHYTETALDEIKLLKCVresdpSDPNkdmVVQLIDD 199
Cdd:cd13996     1 NSRYlndfEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRltEKSSASEKVLREVKALAKL-----NHPN---IVRYYTA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 200 FkiSGMNGIHVCMVFeVLGHHLLKWIIKSN---YQGLPVrcVKSIIRQVLQGLDYLHSKCkIIHTDIKPENILMCVDDAY 276
Cdd:cd13996    73 W--VEEPPLYIQMEL-CEGGTLRDWIDRRNsssKNDRKL--ALELFKQILKGVSYIHSKG-IVHRDLKPSNIFLDNDDLQ 146

                  ..
gi 1370510836 277 VR 278
Cdd:cd13996   147 VK 148
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
131-269 3.03e-09

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: 58.51  E-value: 3.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 131 VIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAqhyTETALDE--IKLLKCVRESDpsDPNkdmVVQLIDDFKISGmnGI 208
Cdd:cd06605     5 YLGELGEGNGGVVSKVRHRPSGQIMAVKVIRLE---IDEALQKqiLRELDVLHKCN--SPY---IVGFYGAFYSEG--DI 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510836 209 HVCMvfEVLGHHLLKWIIKSnYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENIL 269
Cdd:cd06605    75 SICM--EYMDGGSLDKILKE-VGRIPERILGKIAVAVVKGLIYLHEKHKIIHRDVKPSNIL 132
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
129-270 3.19e-09

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: 58.50  E-value: 3.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHyTETALDEIKLLKCVrESDPSDPNkdmVVQLIDdfkiSGMNGI 208
Cdd:cd14069     3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRA-PGDCPENIKKEVCI-QKMLSHKN---VVRFYG----HRREGE 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510836 209 HVCMVFE-VLGHHLLKWIIKSNyqGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILM 270
Cdd:cd14069    74 FQYLFLEyASGGELFDKIEPDV--GMPEDVAQFYFQQLMAGLKYLHS-CGITHRDIKPENLLL 133
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
135-269 3.25e-09

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: 58.18  E-value: 3.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKRFVAMKVV------KSAQHYTETALDEIKLLkcvreSDPSDPNkdmVVQLIDdfkiSGMNGI 208
Cdd:cd06632     8 LGSGSFGSVYEGFNGDTGDFFAVKEVslvdddKKSRESVKQLEQEIALL-----SKLRHPN---IVQYYG----TEREED 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370510836 209 HVCMVFE-VLGHHLLKwiIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:cd06632    76 NLYIFLEyVPGGSIHK--LLQRYGAFEEPVIRLYTRQILSGLAYLHSR-NTVHRDIKGANIL 134
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
556-736 4.01e-09

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: 58.81  E-value: 4.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 556 AADLLVNPLDPRNA---DKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIG-AGYSTPADIWSTACMAFELATGDYL 631
Cdd:cd07880   136 AAGIIHRDLKPGNLavnEDCELKILDFGLARQTDSEMTGYVVTRWYRAPEVILNwMHYTQTVDIWSVGCIMAEMLTGKPL 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 632 FEPHsgedysrdeDHIALIIELLgkvprkyAMLGKYSKEFFTR------KGELRHITKLKPWSLFDVLveKYGWPhedaa 705
Cdd:cd07880   216 FKGH---------DHLDQLMEIM-------KVTGTPSKEFVQKlqsedaKNYVKKLPRFRKKDFRSLL--PNANP----- 272
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1370510836 706 QFTDFLIPMLEMVPEKRASAGECLRHPWLNS 736
Cdd:cd07880   273 LAVNVLEKMLVLDAESRITAAEALAHPYFEE 303
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
128-270 4.43e-09

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: 57.95  E-value: 4.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSA----QHYTETALDEIKLLKCVREsdpsdPNkdmVVQLIDDFKIS 203
Cdd:cd14099     2 RYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSsltkPKQREKLKSEIKIHRSLKH-----PN---IVKFHDCFEDE 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510836 204 GmngiHVCMVFEVLGHHLLKWIIKSNyQGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILM 270
Cdd:cd14099    74 E----NVYILLELCSNGSLMELLKRR-KALTEPEVRYFMRQILSGVKYLHS-NRIIHRDLKLGNLFL 134
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
129-270 4.69e-09

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: 57.66  E-value: 4.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETaLDEIKLLKcvresdpsDPNKDMVVQliddFKISGMNGI 208
Cdd:cd06612     5 FDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQEI-IKEISILK--------QCDSPYIVK----YYGSYFKNT 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370510836 209 HVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd06612    72 DLWIVMEYCGAGSVSDIMKITNKTLTEEEIAAILYQTLKGLEYLHSN-KKIHRDIKAGNILL 132
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
135-276 4.94e-09

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: 57.81  E-value: 4.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKRFVAMKVVKSA--QHYTETAL-DEIKLLKCVRESDpsdpnkdmVVQLIDDFKISGmngiHVC 211
Cdd:cd14082    11 LGSGQFGIVYGGKHRKTGRDVAIKVIDKLrfPTKQESQLrNEVAILQQLSHPG--------VVNLECMFETPE----RVF 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 212 MVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVDDAY 276
Cdd:cd14082    79 VVMEKLHGDMLEMILSSEKGRLPERITKFLVTQILVALRYLHSK-NIVHCDLKPENVLLASAEPF 142
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
573-733 5.10e-09

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: 58.15  E-value: 5.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 573 RVKIADLGNACWVH---KHFTEDIQTRQYRSIEVLIG-AGYSTPADIWSTACMAFELATGDYLFEPHSgedysrDEDHIA 648
Cdd:cd07847   138 QIKLCDFGFARILTgpgDDYTDYVATRWYRAPELLVGdTQYGPPVDVWAIGCVFAELLTGQPLWPGKS------DVDQLY 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 649 LIIELLGK-VPRKYAMLGkySKEFFtrKG-ELRHITKLKPwslfdvLVEKYgwPHEDAAQFtDFLIPMLEMVPEKRASAG 726
Cdd:cd07847   212 LIRKTLGDlIPRHQQIFS--TNQFF--KGlSIPEPETREP------LESKF--PNISSPAL-SFLKGCLQMDPTERLSCE 278

                  ....*..
gi 1370510836 727 ECLRHPW 733
Cdd:cd07847   279 ELLEHPY 285
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
130-269 5.19e-09

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: 58.99  E-value: 5.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 130 HVIRKLGWGHFSTVWLCWDMQ-GKRFVAMKVVKSAQHYTET--ALDEIKLLKCVREsdpsdpnkDMVVQLIDDFKISGMN 206
Cdd:cd07853     3 EPDRPIGYGAFGVVWSVTDPRdGKRVALKKMPNVFQNLVSCkrVFRELKMLCFFKH--------DNVLSALDILQPPHID 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510836 207 GIHVCMVFEVLGHHLLKWIIKSNyQGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENIL 269
Cdd:cd07853    75 PFEEIYVVTELMQSDLHKIIVSP-QPLSSDHVKVFLYQILRGLKYLHS-AGILHRDIKPGNLL 135
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
127-270 5.70e-09

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: 58.15  E-value: 5.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 127 GRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVV---KSAQHYTETALDEIKLLKCVresdpsdpNKDMVVQLID--DFK 201
Cdd:cd07865    12 SKYEKLAKIGQGTFGEVFKARHRKTGQIVALKKVlmeNEKEGFPITALREIKILQLL--------KHENVVNLIEicRTK 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370510836 202 ISGMNGIH--VCMVFEVLGHHLLKWIIKSNYQ-GLPVrcVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd07865    84 ATPYNRYKgsIYLVFEFCEHDLAGLLSNKNVKfTLSE--IKKVMKMLLNGLYYIHRN-KILHRDMKAANILI 152
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
128-270 5.71e-09

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: 57.62  E-value: 5.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYH-VIRKLGWGHFSTVWLCWDMQGKRFVA---MKVVKSAQHYTETALDEIKLLKCVREsdpsdPNkdmVVQLIDdfkiS 203
Cdd:cd13983     1 RYLkFNEVLGRGSFKTVYRAFDTEEGIEVAwneIKLRKLPKAERQRFKQEIEILKSLKH-----PN---IIKFYD----S 68
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 204 GMNGIHVCMVF--EVLGHHLLKWIIKsNYQGLPVRCVKSIIRQVLQGLDYLHS-KCKIIHTDIKPENILM 270
Cdd:cd13983    69 WESKSKKEVIFitELMTSGTLKQYLK-RFKRLKLKVIKSWCRQILEGLNYLHTrDPPIIHRDLKCDNIFI 137
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
125-270 5.92e-09

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: 57.75  E-value: 5.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 125 FNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVV---------KSAQHYTETALDEIKLLKCVresdPSDPNkdmVVQ 195
Cdd:cd14093     1 FYAKYEPKEILGRGVSSTVRRCIEKETGQEFAVKIIditgeksseNEAEELREATRREIEILRQV----SGHPN---IIE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 196 LIDDFKISGMngihVCMVFEVLGH-----HLLKWIIKSNYQglpvrcVKSIIRQVLQGLDYLHSKCkIIHTDIKPENILM 270
Cdd:cd14093    74 LHDVFESPTF----IFLVFELCRKgelfdYLTEVVTLSEKK------TRRIMRQLFEAVEFLHSLN-IVHRDLKPENILL 142
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
128-290 6.22e-09

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: 58.46  E-value: 6.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVV----KSAQHYTETaLDEIKLLKCVREsdpsdpnkDMVVQLIDDF--K 201
Cdd:cd07851    16 RYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLsrpfQSAIHAKRT-YRELRLLKHMKH--------ENVIGLLDVFtpA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 202 ISGMNGIHVCMVFEVLGHHLLKwIIKSnyQGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENI-------LMCVDD 274
Cdd:cd07851    87 SSLEDFQDVYLVTHLMGADLNN-IVKC--QKLSDDHIQFLVYQILRGLKYIHS-AGIIHRDLKPSNLavnedceLKILDF 162
                         170       180
                  ....*....|....*....|.
gi 1370510836 275 AYVRRMAAE-----ATEWQKA 290
Cdd:cd07851   163 GLARHTDDEmtgyvATRWYRA 183
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
558-734 6.51e-09

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: 58.15  E-value: 6.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 558 DLLVNpldpRNADkirVKIADLGNACWV------HKHF-TEDIQTRQYRSIEVLIGAG-YSTPADIWSTACMAFELATGD 629
Cdd:cd07855   139 NLLVN----ENCE---LKIGDFGMARGLctspeeHKYFmTEYVATRWYRAPELMLSLPeYTQAIDMWSVGCIFAEMLGRR 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 630 YLFephSGEDYSrdeDHIALIIELLGKVPRKyaMLGKYSKEfFTRkgelRHITKL-----KPWSLFdvlvekYGWPHEDA 704
Cdd:cd07855   212 QLF---PGKNYV---HQLQLILTVLGTPSQA--VINAIGAD-RVR----RYIQNLpnkqpVPWETL------YPKADQQA 272
                         170       180       190
                  ....*....|....*....|....*....|
gi 1370510836 705 aqfTDFLIPMLEMVPEKRASAGECLRHPWL 734
Cdd:cd07855   273 ---LDLLSQMLRFDPSERITVAEALQHPFL 299
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
564-734 7.38e-09

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: 57.71  E-value: 7.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 564 LDPRNA---DKIRVKIADLGNA---CWVHKHFTEDIQTRQYRSIEVLIGAG-YSTPADIWSTACMAFELATGDYLFePHS 636
Cdd:cd07871   129 LKPQNLlinEKGELKLADFGLArakSVPTKTYSNEVVTLWYRPPDVLLGSTeYSTPIDMWGVGCILYEMATGRPMF-PGS 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 637 GedySRDEDHiaLIIELLGkVPRKYAMLGKYSKEFFTRKGelrhITKLKPWSLFDVLvekygwPHEDaAQFTDFLIPMLE 716
Cdd:cd07871   208 T---VKEELH--LIFRLLG-TPTEETWPGVTSNEEFRSYL----FPQYRAQPLINHA------PRLD-TDGIDLLSSLLL 270
                         170
                  ....*....|....*...
gi 1370510836 717 MVPEKRASAGECLRHPWL 734
Cdd:cd07871   271 YETKSRISAEAALRHSYF 288
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
135-271 7.99e-09

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: 57.14  E-value: 7.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKRFVAMKVVKSA----QHYTETALDEIKLLKCVresdpSDPNkdmVVQLIDDFKISGmngiHV 210
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKeiikRKEVEHTLNERNILERV-----NHPF---IVKLHYAFQTEE----KL 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370510836 211 CMVFE-VLGHHLLKWIikSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMC 271
Cdd:cd05123    69 YLVLDyVPGGELFSHL--SKEGRFPEERARFYAAEIVLALEYLHSL-GIIYRDLKPENILLD 127
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
128-273 8.65e-09

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: 57.28  E-value: 8.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVK----SAQHYTETALDEIKLLKCVREsdpsdPNkdmVVQLIDDFKIS 203
Cdd:cd08224     1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQifemMDAKARQDCLKEIDLLQQLNH-----PN---IIKYLASFIEN 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510836 204 GMNGIhvcmVFEVLGHHLLKWIIK---SNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVD 273
Cdd:cd08224    73 NELNI----VLELADAGDLSRLIKhfkKQKRLIPERTIWKYFVQLCSALEHMHSK-RIMHRDIKPANVFITAN 140
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
129-275 9.76e-09

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: 57.15  E-value: 9.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVK---SAQHYTETALDEIKLLKCVRESDpsdpnkdMVVQLIDDFKISGM 205
Cdd:cd07837     3 YEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRlemEEEGVPSTALREVSLLQMLSQSI-------YIVRLLDVEHVEEN 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510836 206 NGIHVCMVFEVLGHHLLKWII---KSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILmcVDDA 275
Cdd:cd07837    76 GKPLLYLVFEYLDTDLKKFIDsygRGPHNPLPAKTIQSFMYQLCKGVAHCHSH-GVMHRDLKPQNLL--VDKQ 145
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
134-270 1.08e-08

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: 57.38  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 134 KLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQH---YTETALDEIKLLKCVREsdpsdPNkdmVVQLIDDfkisgMNGIHV 210
Cdd:cd07845    14 RIGEGTYGIVYRARDTTSGEIVALKKVRMDNErdgIPISSLREITLLLNLRH-----PN---IVELKEV-----VVGKHL 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370510836 211 CMVFEVLGH--HLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCkIIHTDIKPENILM 270
Cdd:cd07845    81 DSIFLVMEYceQDLASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENF-IIHRDLKVSNLLL 141
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
138-269 1.15e-08

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: 56.84  E-value: 1.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 138 GHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLlkcvresdpsdpNKDMVVQLIDDFKI----SGMNGIHVCMV 213
Cdd:cd05579     4 GAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNQVDSVLA------------ERNILSQAQNPFVVklyySFQGKKNLYLV 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 214 FEVL--G--HHLLKwiiksNYQGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENIL 269
Cdd:cd05579    72 MEYLpgGdlYSLLE-----NVGALDEDVARIYIAEIVLALEYLHS-HGIIHRDLKPDNIL 125
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
128-270 1.21e-08

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: 56.66  E-value: 1.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKS------AQHYTETALDEIKLLkcvreSDPSDPNkdmVVQLIDDFk 201
Cdd:cd08222     1 RYRVVRKLGSGNFGTVYLVSDLKATADEELKVLKEisvgelQPDETVDANREAKLL-----SKLDHPA---IVKFHDSF- 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370510836 202 isgMNGIHVCMVFEVL-GHHLLKWI--IKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd08222    72 ---VEKESFCIVTEYCeGGDLDDKIseYKKSGTTIDENQILDWFIQLLLAVQYMHER-RILHRDLKAKNIFL 139
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
564-736 1.23e-08

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: 56.93  E-value: 1.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 564 LDPRNA---DKIRVKIADLGNA---CWVHKHFTEDIQTRQYRSIEVLIGAG-YSTPADIWSTACMAFELATGDYLFEPhs 636
Cdd:cd07873   126 LKPQNLlinERGELKLADFGLArakSIPTKTYSNEVVTLWYRPPDILLGSTdYSTQIDMWGVGCIFYEMSTGRPLFPG-- 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 637 gedySRDEDHIALIIELLGkVPRKYAMLGKYSKEFFTRkgelRHITKLKPwslfDVLVEKYGWPHEDAAqftDFLIPMLE 716
Cdd:cd07873   204 ----STVEEQLHFIFRILG-TPTEETWPGILSNEEFKS----YNYPKYRA----DALHNHAPRLDSDGA---DLLSKLLQ 267
                         170       180
                  ....*....|....*....|
gi 1370510836 717 MVPEKRASAGECLRHPWLNS 736
Cdd:cd07873   268 FEGRKRISAEEAMKHPYFHS 287
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
128-269 1.27e-08

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: 57.18  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSA-QHYTetalD------EIKLLKCVRESdpsdPNkdmVVQLIDDF 200
Cdd:cd07852     8 RYEILKKLGKGAYGIVWKAIDKKTGEVVALKKIFDAfRNAT----DaqrtfrEIMFLQELNDH----PN---IIKLLNVI 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510836 201 KisGMNGIHVCMVFE--------VLGHHLLKWIIKsnyqglpvrcvKSIIRQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:cd07852    77 R--AENDKDIYLVFEymetdlhaVIRANILEDIHK-----------QYIMYQLLKALKYLHSG-GVIHRDLKPSNIL 139
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
138-270 1.57e-08

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: 56.85  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 138 GHFSTVWLCWDMQGKRFVAMKVVKSAQH---YTETALDEIK-LLKCvresdpSDPN----KDMVVQliddfkiSGMNgiH 209
Cdd:cd07843    16 GTYGVVYRARDKKTGEIVALKKLKMEKEkegFPITSLREINiLLKL------QHPNivtvKEVVVG-------SNLD--K 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510836 210 VCMVFEVLGHHLlKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd07843    81 IYMVMEYVEHDL-KSLMETMKQPFLQSEVKCLMLQLLSGVAHLHDN-WILHRDLKTSNLLL 139
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
173-274 1.60e-08

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: 56.11  E-value: 1.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 173 EIKLLKCVREsdpsdPNkdmVVQLIDDFKISGMNGIHvcMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYL 252
Cdd:cd14119    44 EIQILRRLNH-----RN---VIKLVDVLYNEEKQKLY--MVMEYCVGGLQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYL 113
                          90       100
                  ....*....|....*....|..
gi 1370510836 253 HSkCKIIHTDIKPENILMCVDD 274
Cdd:cd14119   114 HS-QGIIHKDIKPGNLLLTTDG 134
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
132-271 1.68e-08

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: 56.66  E-value: 1.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 132 IRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQH--YTETALDEIKLLKcvresdpsDPNKDMVVQLIDDFKISGMNGIH 209
Cdd:cd06621     6 LSSLGEGAGGSVTKCRLRNTKTIFALKTITTDPNpdVQKQILRELEINK--------SCASPYIVKYYGAFLDEQDSSIG 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 210 VCMvfEVLGHHLLKWI---IKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMC 271
Cdd:cd06621    78 IAM--EYCEGGSLDSIykkVKKKGGRIGEKVLGKIAESVLKGLSYLHSR-KIIHRDIKPSNILLT 139
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
129-269 2.14e-08

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: 56.91  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQhytetaldeikLLK-----CVR-ESDP-SDPNKDMVVQLIDDFK 201
Cdd:cd05573     3 FEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSD-----------MLKreqiaHVRaERDIlADADSPWIVRLHYAFQ 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370510836 202 isgmNGIHVCMVFEVL-GHHLLKWIIKsnYQGLPVRCVKSIIRQVLQGLDYLHsKCKIIHTDIKPENIL 269
Cdd:cd05573    72 ----DEDHLYLVMEYMpGGDLMNLLIK--YDVFPEETARFYIAELVLALDSLH-KLGFIHRDIKPDNIL 133
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
564-736 2.78e-08

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: 56.15  E-value: 2.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 564 LDPRNA---DKIRVKIADLGNA---CWVHKHFTEDIQTRQYRSIEVLIGAG-YSTPADIWSTACMAFELATGDYLFEPhs 636
Cdd:cd07872   130 LKPQNLlinERGELKLADFGLArakSVPTKTYSNEVVTLWYRPPDVLLGSSeYSTQIDMWGVGCIFFEMASGRPLFPG-- 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 637 gedySRDEDHIALIIELLGkVPRKYAMLGKYSKEFFTRkgelRHITKLKPWSLFDvlvekyGWPHEDaAQFTDFLIPMLE 716
Cdd:cd07872   208 ----STVEDELHLIFRLLG-TPTEETWPGISSNDEFKN----YNFPKYKPQPLIN------HAPRLD-TEGIELLTKFLQ 271
                         170       180
                  ....*....|....*....|
gi 1370510836 717 MVPEKRASAGECLRHPWLNS 736
Cdd:cd07872   272 YESKKRISAEEAMKHAYFRS 291
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
135-269 3.20e-08

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: 55.77  E-value: 3.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALD-EIKLLKCVRESDpsdpnkdmVVQLIDDFKISgmngIHVCMV 213
Cdd:cd14166    11 LGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSSLEnEIAVLKRIKHEN--------IVTLEDIYEST----THYYLV 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510836 214 FE-VLGHHLLKWIIKsnyQGLPVRCVKS-IIRQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:cd14166    79 MQlVSGGELFDRILE---RGVYTEKDASrVINQVLSAVKYLHEN-GIVHRDLKPENLL 132
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
134-281 3.32e-08

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: 55.37  E-value: 3.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 134 KLGWGHFSTVWLCWDMQGKR-FVAMKVV------KSAqhyTETALDEIKLLKCVREsdpsdpnkDMVVQLIDdFKISGMN 206
Cdd:cd14121     2 KLGSGTYATVYKAYRKSGAReVVAVKCVsksslnKAS---TENLLTEIELLKKLKH--------PHIVELKD-FQWDEEH 69
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 207 gIHVCMVFeVLGHHLLKWIikSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVDDAYVRRMA 281
Cdd:cd14121    70 -IYLIMEY-CSGGDLSRFI--RSRRTLPESTVRRFLQQLASALQFLREH-NISHMDLKPQNLLLSSRYNPVLKLA 139
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
99-270 3.54e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 56.39  E-value: 3.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836  99 GSDDEEQEDPADYCKGGYHPVKIGD---LFNGRYHVIRKLGWGHFSTVWLC--WDMQGKRFVAMKVVKSAQhyteTALDE 173
Cdd:PHA03207   61 DADEESLSPQTDVCQEPCETTSSSDpasVVRMQYNILSSLTPGSEGEVFVCtkHGDEQRKKVIVKAVTGGK----TPGRE 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 174 IKLLKCVresdpsdpNKDMVVQLIDDFKisgmNGIHVCMVFEVLGHHLLKWIIKSnyQGLPVRCVKSIIRQVLQGLDYLH 253
Cdd:PHA03207  137 IDILKTI--------SHRAIINLIHAYR----WKSTVCMVMPKYKCDLFTYVDRS--GPLPLEQAITIQRRLLEALAYLH 202
                         170
                  ....*....|....*..
gi 1370510836 254 SKcKIIHTDIKPENILM 270
Cdd:PHA03207  203 GR-GIIHRDVKTENIFL 218
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
206-270 3.93e-08

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: 55.52  E-value: 3.93e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 206 NGIHVCMVFEVLGHhlLKWIIKSNYQgLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILM 270
Cdd:cd06620    77 NNIIICMEYMDCGS--LDKILKKKGP-FPEEVLGKIAVAVLEGLTYLYNVHRIIHRDIKPSNILV 138
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
128-277 4.56e-08

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: 55.25  E-value: 4.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDpsdpnkdmVVQLIDDFKISGmng 207
Cdd:cd14104     1 KYMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGADQVLVKKEISILNIARHRN--------ILRLHESFESHE--- 69
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510836 208 iHVCMVFEVL-GHHLLKWIIKSNYQGLPVRCVkSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVDDAYV 277
Cdd:cd14104    70 -ELVMIFEFIsGVDIFERITTARFELNEREIV-SYVRQVCEALEFLHSK-NIGHFDIRPENIIYCTRRGSY 137
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
570-734 5.88e-08

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: 55.19  E-value: 5.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 570 DKIRVKIADLGNACWVHKH----FTEDIQTRQYRSIEVLIGAGYSTPA-DIWSTACMAFELATGDYLFEPhsgedySRDE 644
Cdd:cd07864   151 NKGQIKLADFGLARLYNSEesrpYTNKVITLWYRPPELLLGEERYGPAiDVWSCGCILGELFTKKPIFQA------NQEL 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 645 DHIALIIELLGK-VPRKYAMLGKYSKeFFTRKGELRHITKLKpwslfdvlvEKYGWPHEDAaqfTDFLIPMLEMVPEKRA 723
Cdd:cd07864   225 AQLELISRLCGSpCPAVWPDVIKLPY-FNTMKPKKQYRRRLR---------EEFSFIPTPA---LDLLDHMLTLDPSKRC 291
                         170
                  ....*....|.
gi 1370510836 724 SAGECLRHPWL 734
Cdd:cd07864   292 TAEQALNSPWL 302
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
133-269 6.10e-08

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: 54.65  E-value: 6.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 133 RKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTET-----ALD-EIKLLKCVREsdpsdpnkDMVVQLIDDFKISGMN 206
Cdd:cd06653     8 KLLGRGAFGEVYLCYDADTGRELAVKQVPFDPDSQETskevnALEcEIQLLKNLRH--------DRIVQYYGCLRDPEEK 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510836 207 GIHVCMVFEVLGHhlLKWIIKSnYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:cd06653    80 KLSIFVEYMPGGS--VKDQLKA-YGALTENVTRRYTRQILQGVSYLHSN-MIVHRDIKGANIL 138
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
574-735 6.26e-08

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: 55.44  E-value: 6.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 574 VKIADLGNACWVHKHF--TEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFephSGEDYSrdeDHIALII 651
Cdd:cd07875   165 LKILDFGLARTAGTSFmmTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLF---PGTDHI---DQWNKVI 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 652 ELLGK-VPRKYAMLGKYSKEFFTRKGELR--HITKLKPWSLFDVLVEKYGWpheDAAQFTDFLIPMLEMVPEKRASAGEC 728
Cdd:cd07875   239 EQLGTpCPEFMKKLQPTVRTYVENRPKYAgySFEKLFPDVLFPADSEHNKL---KASQARDLLSKMLVIDASKRISVDEA 315

                  ....*..
gi 1370510836 729 LRHPWLN 735
Cdd:cd07875   316 LQHPYIN 322
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
128-270 6.66e-08

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: 54.56  E-value: 6.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKsaqhyTETALDEIKLLkcVRE----SDPSDPNkdmVVQLIDDFkis 203
Cdd:cd06609     2 LFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVID-----LEEAEDEIEDI--QQEiqflSQCDSPY---ITKYYGSF--- 68
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510836 204 gMNGIHVCMVFEVLG----HHLLKwiiksnYQGLPVRCVKSIIRQVLQGLDYLHSKCKiIHTDIKPENILM 270
Cdd:cd06609    69 -LKGSKLWIIMEYCGggsvLDLLK------PGPLDETYIAFILREVLLGLEYLHSEGK-IHRDIKAANILL 131
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
129-270 6.81e-08

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: 54.14  E-value: 6.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLkcvresdpSDPNKDMVVQLIDDFKISGMngi 208
Cdd:cd14108     4 YDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTSARRELALL--------AELDHKSIVRFHDAFEKRRV--- 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 209 hVCMVFEVLGHHLLKWIIKSnyqglPVRC---VKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd14108    73 -VIIVTELCHEELLERITKR-----PTVCeseVRSYMRQLLEGIEYLHQN-DVLHLDLKPENLLM 130
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
574-736 6.81e-08

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: 55.29  E-value: 6.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 574 VKIADLGNACWVHKHFTEDIQTRQYRSIEVLIG-AGYSTPADIWSTACMAFELATGDYLFEphsGEDYSrdeDHIALIIE 652
Cdd:cd07879   156 LKILDFGLARHADAEMTGYVVTRWYRAPEVILNwMHYNQTVDIWSVGCIMAEMLTGKTLFK---GKDYL---DQLTQILK 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 653 LLGkVPrkyamlgkySKEFFTR---KGELRHITKLK--PWSLFDVLVEKYgwphedAAQFTDFLIPMLEMVPEKRASAGE 727
Cdd:cd07879   230 VTG-VP---------GPEFVQKledKAAKSYIKSLPkyPRKDFSTLFPKA------SPQAVDLLEKMLELDVDKRLTATE 293

                  ....*....
gi 1370510836 728 CLRHPWLNS 736
Cdd:cd07879   294 ALEHPYFDS 302
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
128-290 7.65e-08

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: 55.06  E-value: 7.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVV----KSAQHYTETaLDEIKLLKCVRESDpsdpnkdmVVQLIDDF--K 201
Cdd:cd07878    16 RYQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLsrpfQSLIHARRT-YRELRLLKHMKHEN--------VIGLLDVFtpA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 202 ISGMNGIHVCMVFEVLGHHLLKwIIKsnYQGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENI-------LMCVDD 274
Cdd:cd07878    87 TSIENFNEVYLVTNLMGADLNN-IVK--CQKLSDEHVQFLIYQLLRGLKYIHS-AGIIHRDLKPSNVavnedceLRILDF 162
                         170       180
                  ....*....|....*....|.
gi 1370510836 275 AYVRRMAAE-----ATEWQKA 290
Cdd:cd07878   163 GLARQADDEmtgyvATRWYRA 183
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
135-303 9.61e-08

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: 53.88  E-value: 9.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKRFVAMKVV-KSAQHYTETALD-EIKLLKCVREsdpsdPNkdmVVQLIDDFKisgmNGIHVCM 212
Cdd:cd14167    11 LGTGAFSEVVLAEEKRTQKLVAIKCIaKKALEGKETSIEnEIAVLHKIKH-----PN---IVALDDIYE----SGGHLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 213 VFE-VLGHHLLKWIIKSNYqgLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILMCVDDAYVRRMAAEATEWQKAG 291
Cdd:cd14167    79 IMQlVSGGELFDRIVEKGF--YTERDASKLIFQILDAVKYLHD-MGIVHRDLKPENLLYYSLDEDSKIMISDFGLSKIEG 155
                         170
                  ....*....|..
gi 1370510836 292 apppSGSAVSTA 303
Cdd:cd14167   156 ----SGSVMSTA 163
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
128-270 1.08e-07

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: 53.85  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKsAQHYTETALDEIKllkcvRESdpsdpnkdMVVQLIDDFKISGMNG 207
Cdd:cd06626     1 RWQRGNKIGEGTFGKVYTAVNLDTGELMAMKEIR-FQDNDPKTIKEIA-----DEM--------KVLEGLDHPNLVRYYG 66
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510836 208 IHVcmvfevlghHLLKWIIKSNY-------------QGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILM 270
Cdd:cd06626    67 VEV---------HREEVYIFMEYcqegtleellrhgRILDEAVIRVYTLQLLEGLAYLHE-NGIVHRDIKPANIFL 132
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
129-270 1.09e-07

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: 53.96  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVK---SAQHYTETALDEIKLLKCVREsdpsdPNkdmVVQLIDDFkisgM 205
Cdd:cd07861     2 YTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRlesEEEGVPSTAIREISLLKELQH-----PN---IVCLEDVL----M 69
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510836 206 NGIHVCMVFEVLGHHLLKWI--IKSNyQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd07861    70 QENRLYLVFEFLSMDLKKYLdsLPKG-KYMDAELVKSYLYQILQGILFCHSR-RVLHRDLKPQNLLI 134
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
568-734 1.29e-07

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: 54.40  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 568 NADKIRVKIADLGNACWV-----HK-HFTEDIQTRQYRSIEVLIGA-GYSTPADIWSTACMAFELATGDYLFephSGedy 640
Cdd:cd07854   148 NTEDLVLKIGDFGLARIVdphysHKgYLSEGLVTKWYRSPRLLLSPnNYTKAIDMWAAGCIFAEMLTGKPLF---AG--- 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 641 SRDEDHIALIIEllgKVPrkyamlgkyskefFTRKGELRHITKLKPwslfdVLVEKYGW-PHEDAAQF--------TDFL 711
Cdd:cd07854   222 AHELEQMQLILE---SVP-------------VVREEDRNELLNVIP-----SFVRNDGGePRRPLRDLlpgvnpeaLDFL 280
                         170       180
                  ....*....|....*....|...
gi 1370510836 712 IPMLEMVPEKRASAGECLRHPWL 734
Cdd:cd07854   281 EQILTFNPMDRLTAEEALMHPYM 303
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
573-734 1.44e-07

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: 53.29  E-value: 1.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 573 RVKIADLGNAcwvhKHFTEDIQTRQYRSI---------EVLIGAGYSTPADIWSTACMAFELATGdylfEPhsgeDYSRD 643
Cdd:cd06606   137 VVKLADFGCA----KRLAEIATGEGTKSLrgtpywmapEVIRGEGYGRAADIWSLGCTVIEMATG----KP----PWSEL 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 644 EDHIALIIellgkvprKYAMlgkyskefftrkgelrhiTKLKPwslfdVLVEkygWPHEDAaqfTDFLIPMLEMVPEKRA 723
Cdd:cd06606   205 GNPVAALF--------KIGS------------------SGEPP-----PIPE---HLSEEA---KDFLRKCLQRDPKKRP 247
                         170
                  ....*....|.
gi 1370510836 724 SAGECLRHPWL 734
Cdd:cd06606   248 TADELLQHPFL 258
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
125-270 1.50e-07

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: 53.91  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 125 FNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKDMVVQLIDDFKisg 204
Cdd:cd14041     4 LNDRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFS--- 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510836 205 MNGIHVCMVFEVLGHHLLKWIIKsNYQGLPVRCVKSIIRQVLQGLDYLHS-KCKIIHTDIKPENILM 270
Cdd:cd14041    81 LDTDSFCTVLEYCEGNDLDFYLK-QHKLMSEKEARSIIMQIVNALKYLNEiKPPIIHYDLKPGNILL 146
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
130-269 1.55e-07

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: 53.27  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 130 HVIRKLGWGHFSTVWLC-WDMQG---KRFVAMKVVKsaQHYTETA----LDEIKLLKCVREsdpsdPNkdmVVQLIddfk 201
Cdd:pfam07714   2 TLGEKLGEGAFGEVYKGtLKGEGentKIKVAVKTLK--EGADEEEredfLEEASIMKKLDH-----PN---IVKLL---- 67
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 202 isG--MNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:pfam07714  68 --GvcTQGEPLYIVTEYMPGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESK-NFVHRDLAARNCL 134
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
562-733 1.60e-07

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: 53.41  E-value: 1.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 562 NPLDPRNADKIR-VKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGdylFEPHSGEDy 640
Cdd:cd14185   128 NLLVQHNPDKSTtLKLADFGLAKYVTGPIFTVCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCG---FPPFRSPE- 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 641 sRDEDHIALIIELlgkvprkyamlGKYskEFftrkgelrhitkLKPWslfdvlvekygWPH-EDAAQftDFLIPMLEMVP 719
Cdd:cd14185   204 -RDQEELFQIIQL-----------GHY--EF------------LPPY-----------WDNiSEAAK--DLISRLLVVDP 244
                         170
                  ....*....|....
gi 1370510836 720 EKRASAGECLRHPW 733
Cdd:cd14185   245 EKRYTAKQVLQHPW 258
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
127-270 1.70e-07

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: 53.03  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 127 GRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETAL----DEIKLLKCVREsdpsdPNkdmVVQLIDDFKI 202
Cdd:cd14081     1 GPYRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVLmkveREIAIMKLIEH-----PN---VLKLYDVYEN 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370510836 203 SGmngiHVCMVFE-VLGHHLLKWIIKSNyqGLPVRCVKSIIRQVLQGLDYLHSKCkIIHTDIKPENILM 270
Cdd:cd14081    73 KK----YLYLVLEyVSGGELFDYLVKKG--RLTEKEARKFFRQIISALDYCHSHS-ICHRDLKPENLLL 134
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
141-270 1.77e-07

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: 53.08  E-value: 1.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 141 STVWLCW-DMQGKRFVAMKvvksAQHYTEtaldEIKLLKCVREsdpsdPNkdmVVQLIDDFKiSGMNGiHVCMVF--EVL 217
Cdd:cd14033    25 TTVEVAWcELQTRKLSKGE----RQRFSE----EVEMLKGLQH-----PN---IVRFYDSWK-STVRG-HKCIILvtELM 86
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370510836 218 GHHLLKWIIKsNYQGLPVRCVKSIIRQVLQGLDYLHSKC-KIIHTDIKPENILM 270
Cdd:cd14033    87 TSGTLKTYLK-RFREMKLKLLQRWSRQILKGLHFLHSRCpPILHRDLKCDNIFI 139
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
128-273 1.92e-07

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: 53.56  E-value: 1.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKR--FVAMKVVK---SAQHYTETALDEIKLLKCVResdpsdpNKDMVVQLIDdFKI 202
Cdd:cd07857     1 RYELIKELGQGAYGIVCSARNAETSEeeTVAIKKITnvfSKKILAKRALRELKLLRHFR-------GHKNITCLYD-MDI 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370510836 203 ---SGMNGIHVcmvFEVLGHHLLKWIIKSNyQGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILMCVD 273
Cdd:cd07857    73 vfpGNFNELYL---YEELMEADLHQIIRSG-QPLTDAHFQSFIYQILCGLKYIHS-ANVLHRDLKPGNLLVNAD 141
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
128-270 2.06e-07

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: 52.81  E-value: 2.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTE---TALDEIKLLKCVresdpSDPNkdmVVQLIDDFKISg 204
Cdd:cd08220     1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEerqAALNEVKVLSML-----HHPN---IIEYYESFLED- 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510836 205 mNGIHVCMVFeVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd08220    72 -KALMIVMEY-APGGTLFEYIQQRKGSLLSEEEILHFFVQILLALHHVHSK-QILHRDLKTQNILL 134
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
568-733 2.19e-07

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: 52.86  E-value: 2.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 568 NADKIRVKIADLGNACWVHKH-FTED-IQTRQYRSIEVLIG------AGYSTPADIWSTACMAFELATGDYLFephsged 639
Cdd:cd14098   136 QDDPVIVKISDFGLAKVIHTGtFLVTfCGTMAYLAPEILMSkeqnlqGGYSNLVDMWSVGCLVYVMLTGALPF------- 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 640 ysrDEDHIALIIELLGKvprkyamlGKYSKEfftrkgelrhitklkPWSLFDVlvekygwphedAAQFTDFLIPMLEMVP 719
Cdd:cd14098   209 ---DGSSQLPVEKRIRK--------GRYTQP---------------PLVDFNI-----------SEEAIDFILRLLDVDP 251
                         170
                  ....*....|....
gi 1370510836 720 EKRASAGECLRHPW 733
Cdd:cd14098   252 EKRMTAAQALDHPW 265
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
135-276 2.32e-07

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: 52.61  E-value: 2.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKRFVAMKVVKS-AQHYTETALDEIKLLKCVRESDpsdpnkdmVVQLIDDFKisGMNGIhVCMV 213
Cdd:cd14193    12 LGGGRFGQVHKCEEKSSGLKLAAKIIKArSQKEKEEVKNEIEVMNQLNHAN--------LIQLYDAFE--SRNDI-VLVM 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510836 214 FEVLGHHLLKWIIKSNYQGLPVRCVkSIIRQVLQGLDYLHsKCKIIHTDIKPENILMCVDDAY 276
Cdd:cd14193    81 EYVDGGELFDRIIDENYNLTELDTI-LFIKQICEGIQYMH-QMYILHLDLKPENILCVSREAN 141
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
129-278 2.39e-07

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: 52.55  E-value: 2.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVK----SAQHYTETALDEIKLLKCVREsdpsdPNkdmVVQLIDDFKISG 204
Cdd:cd14164     2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDrrraSPDFVQKFLPRELSILRRVNH-----PN---IVQMFECIEVAN 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370510836 205 MNgihVCMVFEVLGHHLLKWIIKSNYqgLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVDDAYVR 278
Cdd:cd14164    74 GR---LYIVMEAAATDLLQKIQEVHH--IPKDLARDMFAQMVGAVNYLHDM-NIVHRDLKCENILLSADDRKIK 141
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
575-734 2.44e-07

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: 53.06  E-value: 2.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 575 KIADLGNACWVH---KHFTEDIQTRQYRSIEVLIGAG-YSTPADIWSTACMAFELATGDYLFEPHSgedysrDEDHIALI 650
Cdd:cd07835   139 KLADFGLARAFGvpvRTYTHEVVTLWYRAPEILLGSKhYSTPVDIWSVGCIFAEMVTRRPLFPGDS------EIDQLFRI 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 651 IELLGkVPRKYAMLG-----KYSKEF--FTRKGELRHITKLKPWSLfdvlvekygwphedaaqftDFLIPMLEMVPEKRA 723
Cdd:cd07835   213 FRTLG-TPDEDVWPGvtslpDYKPTFpkWARQDLSKVVPSLDEDGL-------------------DLLSQMLVYDPAKRI 272
                         170
                  ....*....|.
gi 1370510836 724 SAGECLRHPWL 734
Cdd:cd07835   273 SAKAALQHPYF 283
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
129-270 2.48e-07

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: 52.77  E-value: 2.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVkSAQHyTE----TALDEIKLLKCVRESDpsdpnkdmVVQLIDDfkisg 204
Cdd:cd07844     2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEI-RLEH-EEgapfTAIREASLLKDLKHAN--------IVTLHDI----- 66
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 205 mngIH----VCMVFEVLgHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd07844    67 ---IHtkktLTLVFEYL-DTDLKQYMDDCGGGLSMHNVRLFLFQLLRGLAYCHQR-RVLHRDLKPQNLLI 131
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
126-310 2.71e-07

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: 52.59  E-value: 2.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 126 NGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVV-KSAQHYTETALD-EIKLLKCVresdpSDPNkdmVVQLIDDFKis 203
Cdd:cd14169     2 NSVYELKEKLGEGAFSEVVLAQERGSQRLVALKCIpKKALRGKEAMVEnEIAVLRRI-----NHEN---IVSLEDIYE-- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 204 gmNGIHVCMVFEVL-GHHLLKWIIKSNYqgLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENIL---------MCVD 273
Cdd:cd14169    72 --SPTHLYLAMELVtGGELFDRIIERGS--YTEKDASQLIGQVLQAVKYLHQ-LGIVHRDLKPENLLyatpfedskIMIS 146
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1370510836 274 DAYVRRMAAEATEWQKAGAPppsGSAVSTAPQQKPIG 310
Cdd:cd14169   147 DFGLSKIEAQGMLSTACGTP---GYVAPELLEQKPYG 180
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
564-734 3.11e-07

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: 52.81  E-value: 3.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 564 LDPRNA---DKIRVKIAD--LGNACWVH-KHFTEDIQTRQYRSIEVLIGAG-YSTPADIWSTACMAFELATGDYLFEPHS 636
Cdd:cd07861   127 LKPQNLlidNKGVIKLADfgLARAFGIPvRVYTHEVVTLWYRAPEVLLGSPrYSTPVDIWSIGTIFAEMATKKPLFHGDS 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 637 gedysrDEDHIALIIELLG----KVPRKYAMLGKYSKEFftrkgelrhiTKLKPWSLFDVLvekygwPHEDAAQFtDFLI 712
Cdd:cd07861   207 ------EIDQLFRIFRILGtpteDIWPGVTSLPDYKNTF----------PKWKKGSLRTAV------KNLDEDGL-DLLE 263
                         170       180
                  ....*....|....*....|..
gi 1370510836 713 PMLEMVPEKRASAGECLRHPWL 734
Cdd:cd07861   264 KMLIYDPAKRISAKKALVHPYF 285
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
232-279 3.39e-07

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: 52.33  E-value: 3.39e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1370510836 232 GLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCvdDAYVRR 279
Cdd:cd13987    87 GLPEERVKRCAAQLASALDFMHSK-NLVHRDIKPENVLLF--DKDCRR 131
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
574-734 3.65e-07

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: 52.27  E-value: 3.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 574 VKIADLGNA---CWVHKHFTEDIQTRQYRSIEVLIGA-GYSTPADIWSTACMAFELATGDYLFephsgEDYSRDEDHIAL 649
Cdd:cd07870   137 LKLADFGLArakSIPSQTYSSEVVTLWYRPPDVLLGAtDYSSALDIWGAGCIFIEMLQGQPAF-----PGVSDVFEQLEK 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 650 IIELLGkVPRK-----YAMLGKYSKEFFtrkgelrhitKLKPWSLFDVLVEKYGWPH--EDAAQftdfliPMLEMVPEKR 722
Cdd:cd07870   212 IWTVLG-VPTEdtwpgVSKLPNYKPEWF----------LPCKPQQLRVVWKRLSRPPkaEDLAS------QMLMMFPKDR 274
                         170
                  ....*....|..
gi 1370510836 723 ASAGECLRHPWL 734
Cdd:cd07870   275 ISAQDALLHPYF 286
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
219-273 4.14e-07

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: 51.97  E-value: 4.14e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 219 HHLLKWIIKSNyqGLPVRCVKSIIRQVLQGLDYLHSKCKiIHTDIKPENILMCVD 273
Cdd:cd06610    87 LDIMKSSYPRG--GLDEAIIATVLKEVLKGLEYLHSNGQ-IHRDVKAGNILLGED 138
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
129-270 4.47e-07

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: 51.88  E-value: 4.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYT-------ETALDEIKLLKCVRESDpsdpnkdmVVQLIDDFK 201
Cdd:cd14196     7 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsrrgvsrEEIEREVSILRQVLHPN--------IITLHDVYE 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 202 isgmNGIHVCMVFE-VLGHHLLKWIIKSnyQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd14196    79 ----NRTDVVLILElVSGGELFDFLAQK--ESLSEEEATSFIKQILDGVNYLHTK-KIAHFDLKPENIML 141
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
127-274 4.73e-07

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: 52.47  E-value: 4.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 127 GRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMK-VVKSAQHYTETALDEIKLLK------CVRESDP-SDPNKDMVVQLID 198
Cdd:cd07854     5 SRYMDLRPLGCGSNGLVFSAVDSDCDKRVAVKkIVLTDPQSVKHALREIKIIRrldhdnIVKVYEVlGPSGSDLTEDVGS 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510836 199 DFKISGmngihVCMVFEVLGHHLLKWIiksNYQGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILMCVDD 274
Cdd:cd07854    85 LTELNS-----VYIVQEYMETDLANVL---EQGPLSEEHARLFMYQLLRGLKYIHS-ANVLHRDLKPANVFINTED 151
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
135-273 5.60e-07

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: 51.46  E-value: 5.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQ-GKRFVAMKVVKSAQHYTETALDEIKLLKCVresdpSDPNkdmVVQLIDDFKISgmNGIHVCMV 213
Cdd:cd14190    12 LGGGKFGKVHTCTEKRtGLKLAAKVINKQNSKDKEMVLLEIQVMNQL-----NHRN---LIQLYEAIETP--NEIVLFME 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 214 FeVLGHHLLKWIIKSNYQGLPVRCVkSIIRQVLQGLDYLHsKCKIIHTDIKPENILmCVD 273
Cdd:cd14190    82 Y-VEGGELFERIVDEDYHLTEVDAM-VFVRQICEGIQFMH-QMRVLHLDLKPENIL-CVN 137
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
559-734 5.63e-07

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: 52.34  E-value: 5.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 559 LLVNPLdprnADKIRVKIADLGNACWVHKHFTED-IQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFePHSG 637
Cdd:cd14229   134 MLVDPV----RQPYRVKVIDFGSASHVSKTVCSTyLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLY-PGAL 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 638 EdysrdEDHIALIIELLGKVPRKYAMLGKYSKEFFTRKG-----------------------------------ELRHIT 682
Cdd:cd14229   209 E-----YDQIRYISQTQGLPGEQLLNVGTKTSRFFCRETdapysswrlktleeheaetgmkskearkyifnsldDIAHVN 283
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370510836 683 KLKPWSLFDVLVEKygwphEDAAQFTDFLIPMLEMVPEKRASAGECLRHPWL 734
Cdd:cd14229   284 MVMDLEGSDLLAEK-----ADRREFVALLKKMLLIDADLRITPADTLSHPFV 330
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
555-733 5.78e-07

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: 51.93  E-value: 5.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 555 RAADLLVNpldprnaDKIRVKIADLGNAcwvhKHFTEDIQ------------------TRQYRSIEVLIGA-GYSTPADI 615
Cdd:cd07866   142 KAANILID-------NQGILKIADFGLA----RPYDGPPPnpkggggggtrkytnlvvTRWYRPPELLLGErRYTTAVDI 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 616 WSTACMAFELATGDYLFEPHSgedysrDEDHIALIIELLGkVPRKYAML------GKYSKEFFTrkgelRHITKLKpwsl 689
Cdd:cd07866   211 WGIGCVFAEMFTRRPILQGKS------DIDQLHLIFKLCG-TPTEETWPgwrslpGCEGVHSFT-----NYPRTLE---- 274
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1370510836 690 fdvlvEKYGWPHEDAAqftDFLIPMLEMVPEKRASAGECLRHPW 733
Cdd:cd07866   275 -----ERFGKLGPEGL---DLLSKLLSLDPYKRLTASDALEHPY 310
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
588-732 6.99e-07

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: 51.54  E-value: 6.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 588 HFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSgedysrDEDHIALIIELLGKVPRKYAMLgKY 667
Cdd:cd07848   157 NYTEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGES------EIDQLFTIQKVLGPLPAEQMKL-FY 229
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 668 SKEFFTrkgELRHITKLKPWSLfdvlveKYGWPHEDAAQFTDFLIPMLEMVPEKRASAGECLRHP 732
Cdd:cd07848   230 SNPRFH---GLRFPAVNHPQSL------ERRYLGILSGVLLDLMKNLLKLNPTDRYLTEQCLNHP 285
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
128-270 7.96e-07

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: 51.28  E-value: 7.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVK---SAQHYTETALDEIKLLKCVRESDpsdpnkdmVVQLID----DF 200
Cdd:cd07839     1 KYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRlddDDEGVPSSALREICLLKELKHKN--------IVRLYDvlhsDK 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510836 201 KISgmngihvcMVFEVLGHHLLKWIikSNYQGLPVR-CVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd07839    73 KLT--------LVFEYCDQDLKKYF--DSCNGDIDPeIVKSFMFQLLKGLAFCHSH-NVLHRDLKPQNLLI 132
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
135-269 8.81e-07

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: 51.18  E-value: 8.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKRFVAMKVV-KSAQHYTETALDEIK-LLKCvresdpsDPNKDmVVQLIDDFKisgmNGIHVCM 212
Cdd:cd14174    10 LGEGAYAKVQGCVSLQNGKEYAVKIIeKNAGHSRSRVFREVEtLYQC-------QGNKN-ILELIEFFE----DDTRFYL 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510836 213 VFEVL-GHHLLKWIIKSNYqgLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:cd14174    78 VFEKLrGGSILAHIQKRKH--FNEREASRVVRDIASALDFLHTK-GIAHRDLKPENIL 132
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
129-270 9.98e-07

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: 50.77  E-value: 9.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVK-SAQHYTETALDEIKLLKCVREsdpsdPNkdmVVQLIDDFKisGMNG 207
Cdd:cd06613     2 YELIQRIGSGTYGDVYKARNIATGELAAVKVIKlEPGDDFEIIQQEISMLKECRH-----PN---IVAYFGSYL--RRDK 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510836 208 IHVCM----------VFEVLGHhllkwiiksnyqgLPVRCVKSIIRQVLQGLDYLHSKCKiIHTDIKPENILM 270
Cdd:cd06613    72 LWIVMeycgggslqdIYQVTGP-------------LSELQIAYVCRETLKGLAYLHSTGK-IHRDIKGANILL 130
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
129-270 1.30e-06

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: 50.96  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVK---SAQHYTETALDEIKLLKCVRESDPSDPnKDMVVQLID--DFKIS 203
Cdd:cd07864     9 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRldnEKEGFPITAIREIKILRQLNHRSVVNL-KEIVTDKQDalDFKKD 87
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510836 204 GMNgihVCMVFEVLGHHLLKwIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd07864    88 KGA---FYLVFEYMDHDLMG-LLESGLVHFSEDHIKSFMKQLLEGLNYCHKK-NFLHRDIKCSNILL 149
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
238-269 1.37e-06

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 50.63  E-value: 1.37e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1370510836 238 VKSIIRQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:PHA03390  111 VKKIIRQLVEALNDLHKH-NIIHNDIKLENVL 141
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
129-270 1.53e-06

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: 50.18  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYT-------ETALDEIKLLKCVREsdpsdPNkdmVVQLIDDFK 201
Cdd:cd14105     7 YDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKAsrrgvsrEDIEREVSILRQVLH-----PN---IITLHDVFE 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 202 isgmNGIHVCMVFE-VLGHHLLKWIIKSnyQGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILM 270
Cdd:cd14105    79 ----NKTDVVLILElVAGGELFDFLAEK--ESLSEEEATEFLKQILDGVNYLHT-KNIAHFDLKPENIML 141
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
559-734 1.56e-06

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: 50.86  E-value: 1.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 559 LLVNPldprNADKIRVKIADLGNACWVHKHFTED-IQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSG 637
Cdd:cd14227   149 MLVDP----SRQPYRVKVIDFGSASHVSKAVCSTyLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASE 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 638 ED--------------------------YSRDEDHIALIIELlgKVPRKY-AMLGKYSKE----FFTRKGELRHITKLKP 686
Cdd:cd14227   225 YDqiryisqtqglpaeyllsagtkttrfFNRDTDSPYPLWRL--KTPEDHeAETGIKSKEarkyIFNCLDDMAQVNMTTD 302
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1370510836 687 WSLFDVLVEKygwphEDAAQFTDFLIPMLEMVPEKRASAGECLRHPWL 734
Cdd:cd14227   303 LEGSDMLVEK-----ADRREFIDLLKKMLTIDADKRITPIETLNHPFV 345
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
128-274 1.59e-06

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: 50.37  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVK--SAQHYTEtALDEIKLLKCVREsdpsdPNkdmVVQLIDDFKISGM 205
Cdd:cd13986     1 RYRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILchSKEDVKE-AMREIENYRLFNH-----PN---ILRLLDSQIVKEA 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510836 206 NGIH-VCMVFEV-----LGHHLLKWIIKSNYqgLPVRCVKSIIRQVLQGLDYLHSKCKI--IHTDIKPENILMCVDD 274
Cdd:cd13986    72 GGKKeVYLLLPYykrgsLQDEIERRLVKGTF--FPEDRILHIFLGICRGLKAMHEPELVpyAHRDIKPGNVLLSEDD 146
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
129-274 1.73e-06

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: 50.10  E-value: 1.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVV---KSAQHYTETALDEIKLLkcvresdpSDPNKDMVVQLIDDFkisgM 205
Cdd:cd08529     2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQIdisRMSRKMREEAIDEARVL--------SKLNSPYVIKYYDSF----V 69
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 206 NGIHVCMVFEVLGHHLLKWIIKSNY-QGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVDD 274
Cdd:cd08529    70 DKGKLNIVMEYAENGDLHSLIKSQRgRPLPEDQIWKFFIQTLLGLSHLHSK-KILHRDIKSMNIFLDKGD 138
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
126-273 1.73e-06

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: 50.42  E-value: 1.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 126 NGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKS-AQHYTETALDEIKLLKCVresdpsdpNKDMVVQLIDDFKISG 204
Cdd:cd06644    11 NEVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIETkSEEELEDYMVEIEILATC--------NHPYIVKLLGAFYWDG 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370510836 205 mngiHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVD 273
Cdd:cd06644    83 ----KLWIMIEFCPGGAVDAIMLELDRGLTEPQIQVICRQMLEALQYLHSM-KIIHRDLKAGNVLLTLD 146
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
125-270 1.73e-06

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: 50.44  E-value: 1.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 125 FNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKDMVVQLIDDFKisg 204
Cdd:cd14040     4 LNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFS--- 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510836 205 MNGIHVCMVFEVLGHHLLKWIIKsNYQGLPVRCVKSIIRQVLQGLDYLHS-KCKIIHTDIKPENILM 270
Cdd:cd14040    81 LDTDTFCTVLEYCEGNDLDFYLK-QHKLMSEKEARSIVMQIVNALRYLNEiKPPIIHYDLKPGNILL 146
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
131-273 1.80e-06

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: 50.27  E-value: 1.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 131 VIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSA----QHYTETALDEIKLLKCVREsdpsdPnkdMVVQLIDDFKisgmN 206
Cdd:cd05580     5 FLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAkiikLKQVEHVLNEKRILSEVRH-----P---FIVNLLGSFQ----D 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510836 207 GIHVCMVFE-VLGHHLLKWIIKSNYQGLPVRCVKSIirQVLQGLDYLHSKcKIIHTDIKPENILMCVD 273
Cdd:cd05580    73 DRNLYMVMEyVPGGELFSLLRRSGRFPNDVAKFYAA--EVVLALEYLHSL-DIVYRDLKPENLLLDSD 137
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
241-305 1.92e-06

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: 49.70  E-value: 1.92e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 241 IIRQVLQGLDYLHSKcKIIHTDIKPENILMcVDDAYVR----RMAAEATEWQKA-GAPPPSGSAVSTAPQ 305
Cdd:cd14062    94 IARQTAQGMDYLHAK-NIIHRDLKSNNIFL-HEDLTVKigdfGLATVKTRWSGSqQFEQPTGSILWMAPE 161
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
129-270 2.37e-06

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: 49.63  E-value: 2.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYT-------ETALDEIKLLKCVREsdpsdPNkdmVVQLIDDFK 201
Cdd:cd14194     7 YDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSsrrgvsrEDIEREVSILKEIQH-----PN---VITLHEVYE 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 202 isgmNGIHVCMVFE-VLGHHLLKWIIKSnyQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd14194    79 ----NKTDVILILElVAGGELFDFLAEK--ESLTEEEATEFLKQILNGVYYLHSL-QIAHFDLKPENIML 141
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
135-269 2.48e-06

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: 49.99  E-value: 2.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKRFVAMKVVkSAQHYTETaldEIKLLKCVResdpSDPNkdmVVQLIDDFKisgmNGIHVCMVF 214
Cdd:cd14092    14 LGDGSFSVCRKCVHKKTGQEFAVKIV-SRRLDTSR---EVQLLRLCQ----GHPN---IVKLHEVFQ----DELHTYLVM 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510836 215 EVL-GHHLLKWIIKSNYQGLPVRCvkSIIRQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:cd14092    79 ELLrGGELLERIRKKKRFTESEAS--RIMRQLVSAVSFMHSK-GVVHRDLKPENLL 131
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
135-270 2.64e-06

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: 49.76  E-value: 2.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKRFVAMKVVKSAQhyteTALDEIKLLKcvRESDpsdpnkdMVVQLIDDF--KISGM--NGIHV 210
Cdd:cd13978     1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSP----NCIEERKALL--KEAE-------KMERARHSYvlPLLGVcvERRSL 67
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510836 211 CMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCK-IIHTDIKPENILM 270
Cdd:cd13978    68 GLVMEYMENGSLKSLLEREIQDVPWSLRFRIIHEIALGMNFLHNMDPpLLHHDLKPENILL 128
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
128-269 2.65e-06

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: 49.45  E-value: 2.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDpsdpnkdmVVQLIDDFKISGmng 207
Cdd:cd14087     2 KYDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGREVCESELNVLRRVRHTN--------IIQLIEVFETKE--- 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370510836 208 iHVCMVFEVL-GHHLLKWII-KSNYQGlpvRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENIL 269
Cdd:cd14087    71 -RVYMVMELAtGGELFDRIIaKGSFTE---RDATRVLQMVLDGVKYLHG-LGITHRDLKPENLL 129
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
128-271 3.08e-06

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: 49.26  E-value: 3.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQ-GKRFvAMKVVKSA-----QHYTEtalDEIKLLKCVREsdpsdPNKDMVVQLIDdfk 201
Cdd:cd14184     2 KYKIGKVIGDGNFAVVKECVERStGKEF-ALKIIDKAkccgkEHLIE---NEVSILRRVKH-----PNIIMLIEEMD--- 69
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510836 202 isgmNGIHVCMVFE-VLGHHLLKWIIKSNyqGLPVRCVKSIIRQVLQGLDYLHSKCkIIHTDIKPENILMC 271
Cdd:cd14184    70 ----TPAELYLVMElVKGGDLFDAITSST--KYTERDASAMVYNLASALKYLHGLC-IVHRDIKPENLLVC 133
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
233-269 3.11e-06

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: 49.58  E-value: 3.11e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1370510836 233 LPVRCvkSIIRQVLQGLDYLHSKC--KIIHTDIKPENIL 269
Cdd:cd14066    92 WPQRL--KIAKGIARGLEYLHEECppPIIHGDIKSSNIL 128
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
135-268 3.12e-06

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 49.76  E-value: 3.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTE---------------TALDEIKLLKCVREsdpsdPNkdmVVQLIDD 199
Cdd:PTZ00024   17 LGEGTYGKVEKAYDTLTGKIVAIKKVKIIEISNDvtkdrqlvgmcgihfTTLRELKIMNEIKH-----EN---IMGLVDV 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370510836 200 FkisgMNGIHVCMVFEVLgHHLLKWIIKSNYQgLPVRCVKSIIRQVLQGLDYLHsKCKIIHTDIKPENI 268
Cdd:PTZ00024   89 Y----VEGDFINLVMDIM-ASDLKKVVDRKIR-LTESQVKCILLQILNGLNVLH-KWYFMHRDLSPANI 150
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
127-270 3.19e-06

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: 49.37  E-value: 3.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 127 GRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVREsDPSDPNKDMVVQLIDDFKISGMN 206
Cdd:cd14077     1 GNWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPRASNAGLKKEREKRLEKEISR-DIRTIREAALSSLLNHPHICRLR 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 207 GI-----HVCMVFE-VLGHHLLKWIIKSNyqGLPVRCVKSIIRQVLQGLDYLHsKCKIIHTDIKPENILM 270
Cdd:cd14077    80 DFlrtpnHYYMLFEyVDGGQLLDYIISHG--KLKEKQARKFARQIASALDYLH-RNSIVHRDLKIENILI 146
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
228-270 3.24e-06

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: 49.37  E-value: 3.24e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1370510836 228 SNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd13989    94 ENCCGLKESEVRTLLSDISSAISYLHEN-RIIHRDLKPENIVL 135
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
128-270 3.38e-06

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: 49.40  E-value: 3.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIrklGWGHFSTVWLCWDMQGKRFVAMKVVK--SAQHYTETALDEIKLLKCVRESDPSDpnkdmVVQliddFKISGM 205
Cdd:cd06917     5 RLELV---GRGSYGAVYRGYHVKTGRVVALKVLNldTDDDDVSDIQKEVALLSQLKLGQPKN-----IIK----YYGSYL 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 206 NGIHVCMVFEVLGHHLLKWIIKSnyQGLPVRCVKSIIRQVLQGLDYLHsKCKIIHTDIKPENILM 270
Cdd:cd06917    73 KGPSLWIIMDYCEGGSIRTLMRA--GPIAERYIAVIMREVLVALKFIH-KDGIIHRDIKAANILV 134
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
128-270 3.63e-06

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: 49.18  E-value: 3.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVvKSAQHYTETALDEIKLLKCVResdpsdpNKDMVVQLIDdfkiSGMNG 207
Cdd:cd14017     1 RWKVVKKIGGGGFGEIYKVRDVVDGEEVAMKV-ESKSQPKQVLKMEVAVLKKLQ-------GKPHFCRLIG----CGRTE 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510836 208 IHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILM 270
Cdd:cd14017    69 RYNYIVMTLLGPNLAELRRSQPRGKFSVSTTLRLGIQILKAIEDIHE-VGFLHRDVKPSNFAI 130
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
135-269 3.80e-06

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: 49.34  E-value: 3.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQ-GKRFvAMKVV-KSAQHYTETALDEIKLLKCVRESdpsdPNkdmVVQLIDDFKisgmNGIHVCM 212
Cdd:cd14090    10 LGEGAYASVQTCINLYtGKEY-AVKIIeKHPGHSRSRVFREVETLHQCQGH----PN---ILQLIEYFE----DDERFYL 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370510836 213 VFEVL-GHHLLKWIIKsnyQGLPVRCVKS-IIRQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:cd14090    78 VFEKMrGGPLLSHIEK---RVHFTEQEASlVVRDIASALDFLHDK-GIAHRDLKPENIL 132
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
238-275 4.02e-06

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: 49.05  E-value: 4.02e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1370510836 238 VKSIIRQVLQGLDYLHSkCKIIHTDIKPENILMCVDDA 275
Cdd:cd14111   101 VVGYLVQILQGLEYLHG-RRVLHLDIKPDNIMVTNLNA 137
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
129-273 4.02e-06

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: 49.36  E-value: 4.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVK-SAQHYTETALDEIKLLKCVREsdpsdPNkdmVVQLIDDFKISGmng 207
Cdd:cd06611     7 WEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQiESEEELEDFMVEIDILSECKH-----PN---IVGLYEAYFYEN--- 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510836 208 iHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVD 273
Cdd:cd06611    76 -KLWILIEFCDGGALDSIMLELERGLTEPQIRYVCRQMLEALNFLHSH-KVIHRDLKAGNILLTLD 139
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
128-270 4.57e-06

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: 48.92  E-value: 4.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKllkcvREsdpsdpnkdmvVQLIDdfKISGMNG 207
Cdd:cd14073     2 RYELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDMVRIR-----RE-----------IEIMS--SLNHPHI 63
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370510836 208 IHVCMVFE-----VL------GHHLLKWIikSNYQGLPVRCVKSIIRQVLQGLDYLHsKCKIIHTDIKPENILM 270
Cdd:cd14073    64 IRIYEVFEnkdkiVIvmeyasGGELYDYI--SERRRLPEREARRIFRQIVSAVHYCH-KNGVVHRDLKLENILL 134
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
558-733 4.98e-06

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: 48.97  E-value: 4.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 558 DLLVNpldpRNADkirVKIADLGNACWVH---KHFTEDIQTRQYRSIEVLIGA-GYSTPADIWSTACMAFELATGDYLFE 633
Cdd:cd07839   129 NLLIN----KNGE---LKLADFGLARAFGipvRCYSAEVVTLWYRPPDVLFGAkLYSTSIDMWSAGCIFAELANAGRPLF 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 634 PhsGEDYsrdEDHIALIIELLGkVPRKYAMLGkyskefftrkgeLRHITKLKPWSLFDVLVEkygWPHEDAAQFT---DF 710
Cdd:cd07839   202 P--GNDV---DDQLKRIFRLLG-TPTEESWPG------------VSKLPDYKPYPMYPATTS---LVNVVPKLNStgrDL 260
                         170       180
                  ....*....|....*....|...
gi 1370510836 711 LIPMLEMVPEKRASAGECLRHPW 733
Cdd:cd07839   261 LQNLLVCNPVQRISAEEALQHPY 283
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
129-270 5.10e-06

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: 48.79  E-value: 5.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVV-KSAQHYTETALD-EIKLLKCVresdpSDPNkdmVVQLIDDFKISgmn 206
Cdd:cd14185     2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIdKSKLKGKEDMIEsEILIIKSL-----SHPN---IVKLFEVYETE--- 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 207 gIHVCMVFE-VLGHHLLKWIIKSnyQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd14185    71 -KEIYLILEyVRGGDLFDAIIES--VKFTEHDAALMIIDLCEALVYIHSK-HIVHRDLKPENLLV 131
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
574-633 5.33e-06

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: 48.67  E-value: 5.33e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510836 574 VKIADLGNAcwvhKHFTEDIQ-------TRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFE 633
Cdd:cd05123   132 IKLTDFGLA----KELSSDGDrtytfcgTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFY 194
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
135-270 6.02e-06

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: 48.42  E-value: 6.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDpsdpnkdmVVQLIDDFKisgmNGIHVCMVF 214
Cdd:cd14115     1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQ--------YITLHDTYE----SPTSYILVL 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510836 215 EVLGH-HLLKWIIksNYQGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILM 270
Cdd:cd14115    69 ELMDDgRLLDYLM--NHDELMEEKVAFYIRDIMEALQYLHN-CRVAHLDIKPENLLI 122
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
128-270 6.14e-06

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 48.66  E-value: 6.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQH---YTETALDEIKLLKCVRESDpsdpnkdmVVQLIDDFKisg 204
Cdd:PLN00009    3 QYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEdegVPSTAIREISLLKEMQHGN--------IVRLQDVVH--- 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510836 205 mNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:PLN00009   72 -SEKRLYLVFEYLDLDLKKHMDSSPDFAKNPRLIKTYLYQILRGIAYCHSH-RVLHRDLKPQNLLI 135
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
128-290 6.85e-06

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: 48.88  E-value: 6.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVV----KSAQHYTETaLDEIKLLKCVRESDpsdpnkdmVVQLIDDF--- 200
Cdd:cd07877    18 RYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLsrpfQSIIHAKRT-YRELRLLKHMKHEN--------VIGLLDVFtpa 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 201 -KISGMNGIHvcMVFEVLGHHLLKwIIKSnyQGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENI-------LMCV 272
Cdd:cd07877    89 rSLEEFNDVY--LVTHLMGADLNN-IVKC--QKLTDDHVQFLIYQILRGLKYIHS-ADIIHRDLKPSNLavnedceLKIL 162
                         170       180
                  ....*....|....*....|...
gi 1370510836 273 DDAYVRRMAAE-----ATEWQKA 290
Cdd:cd07877   163 DFGLARHTDDEmtgyvATRWYRA 185
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
138-270 7.08e-06

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: 48.25  E-value: 7.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 138 GHFSTVWLCWDMQGKRFVAMKVVKSAQHyteTALDEIKLLKCVRESDPSDPNKDMVVQLIDDFKisgmNGIHVCMVFEVL 217
Cdd:cd05611     7 GAFGSVYLAKKRSTGDYFAIKVLKKSDM---IAKNQVTNVKAERAIMMIQGESPYVAKLYYSFQ----SKDYLYLVMEYL 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370510836 218 GHHLLKWIIKSnYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd05611    80 NGGDCASLIKT-LGGLPEDWAKQYIAEVVLGVEDLHQR-GIIHRDIKPENLLI 130
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
221-278 7.36e-06

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: 48.26  E-value: 7.36e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510836 221 LLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMcVDDAYVR 278
Cdd:cd14047   102 LESWIEKRNGEKLDKVLALEIFEQITKGVEYIHSK-KLIHRDLKPSNIFL-VDTGKVK 157
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
125-281 7.66e-06

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: 48.43  E-value: 7.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 125 FNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVK-SAQHYTETALDEIKLlKCVRESDPSD--PNKDMVVQLIDDFK 201
Cdd:cd14181     8 FYQKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEvTAERLSPEQLEEVRS-STLKEIHILRqvSGHPSIITLIDSYE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 202 ISGMngihVCMVFEVLGH-HLLKWIIKSnyQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMcvDDAYVRRM 280
Cdd:cd14181    87 SSTF----IFLVFDLMRRgELFDYLTEK--VTLSEKETRSIMRSLLEAVSYLHAN-NIVHRDLKPENILL--DDQLHIKL 157

                  .
gi 1370510836 281 A 281
Cdd:cd14181   158 S 158
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
129-270 7.67e-06

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: 48.54  E-value: 7.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTE--TALDEIKLLKCVRESDpsdpnkdmvVQLIDDFkisgmn 206
Cdd:cd07869     7 YEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTpfTAIREASLLKGLKHAN---------IVLLHDI------ 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510836 207 gIH----VCMVFEVLGHHLLKWIIKsNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd07869    72 -IHtketLTLVFEYVHTDLCQYMDK-HPGGLHPENVKLFLFQLLRGLSYIHQR-YILHRDLKPQNLLI 136
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
570-733 7.73e-06

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: 48.03  E-value: 7.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 570 DKIRVKIADLGNACWV--HKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYlfePHSGEDysrDEDHI 647
Cdd:cd14006   126 PSPQIKIIDFGLARKLnpGEELKEIFGTPEFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLS---PFLGED---DQETL 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 648 ALIIEllGKVprkyamlgKYSKEFFTrkgelrHITklkpwslfdvlvekygwphEDAaqfTDFLIPMLEMVPEKRASAGE 727
Cdd:cd14006   200 ANISA--CRV--------DFSEEYFS------SVS-------------------QEA---KDFIRKLLVKEPRKRPTAQE 241

                  ....*.
gi 1370510836 728 CLRHPW 733
Cdd:cd14006   242 ALQHPW 247
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
129-270 8.00e-06

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: 48.47  E-value: 8.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTE--TALDEIKLLKCVRESDpsdpnkdmVVQLIDDfkisgmn 206
Cdd:cd07871     7 YVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGApcTAIREVSLLKNLKHAN--------IVTLHDI------- 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510836 207 gIH----VCMVFEVLGHHLLKWIIKSNyQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd07871    72 -IHtercLTLVFEYLDSDLKQYLDNCG-NLMSMHNVKIFMFQLLRGLSYCHKR-KILHRDLKPQNLLI 136
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
129-270 8.30e-06

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: 48.15  E-value: 8.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALD---------EIKLLKCVRESdpSDPNkdmVVQLIDD 199
Cdd:cd14004     2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERILVDTWVRdrklgtvplEIHILDTLNKR--SHPN---IVKLLDF 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510836 200 FKisgmNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd14004    77 FE----DDEFYYLVMEKHGSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQ-GIVHRDIKDENVIL 142
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
574-732 8.55e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 48.72  E-value: 8.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 574 VKIADLGNACW--VHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFE-LATGDYLFE--PHSGEDYSRD-EDHI 647
Cdd:PHA03209  196 VCIGDLGAAQFpvVAPAFLGLAGTVETNAPEVLARDKYNSKADIWSAGIVLFEmLAYPSTIFEdpPSTPEEYVKScHSHL 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 648 ALIIELLGKVPRKYAML--GKYSKEFFTRKGELRhitklKPWSLFDVlVEKYGWPhEDAAqftdFLI-PMLEMVPEKRAS 724
Cdd:PHA03209  276 LKIISTLKVHPEEFPRDpgSRLVRGFIEYASLER-----QPYTRYPC-FQRVNLP-IDGE----FLVhKMLTFDAAMRPS 344

                  ....*...
gi 1370510836 725 AGECLRHP 732
Cdd:PHA03209  345 AEEILNYP 352
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
150-270 9.09e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 48.72  E-value: 9.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 150 QGKRFVAMK-------VVKSAQhyTETALDEIKLLKCVresdpsdpNKDMVVQLIDDFkisgMNGIHVCMVFEVLGHHLL 222
Cdd:PHA03209   79 EGRVFVATKpgqpdpvVLKIGQ--KGTTLIEAMLLQNV--------NHPSVIRMKDTL----VSGAITCMVLPHYSSDLY 144
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1370510836 223 KWIIKsNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:PHA03209  145 TYLTK-RSRPLPIDQALIIEKQILEGLRYLHAQ-RIIHRDVKTENIFI 190
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
129-270 9.19e-06

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: 48.03  E-value: 9.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVV--KSAQHYTETALDEIKLLKCVRESDpsdpnkdmvVQLIDDFkisgmn 206
Cdd:cd07870     2 YLNLEKLGEGSYATVYKGISRINGQLVALKVIsmKTEEGVPFTAIREASLLKGLKHAN---------IVLLHDI------ 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510836 207 gIH----VCMVFEVLGHHLLKWIIKsNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd07870    67 -IHtketLTFVFEYMHTDLAQYMIQ-HPGGLHPYNVRLFMFQLLRGLAYIHGQ-HILHRDLKPQNLLI 131
pknD PRK13184
serine/threonine-protein kinase PknD;
127-270 9.20e-06

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 49.38  E-value: 9.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 127 GRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAqhytetaLDEIKLLK--CVRE----SDPSDPNKDMVVQLIDDf 200
Cdd:PRK13184    2 QRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIRED-------LSENPLLKkrFLREakiaADLIHPGIVPVYSICSD- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 201 kisgMNGIHVCMVFeVLGHHLlKWIIKSNYQ----------GLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:PRK13184   74 ----GDPVYYTMPY-IEGYTL-KSLLKSVWQkeslskelaeKTSVGAFLSIFHKICATIEYVHSK-GVLHRDLKPDNILL 146
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
135-273 9.38e-06

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: 48.03  E-value: 9.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKRFVAMKV--VKSAQHYTETAlDEIKLLKCVresdpsdpNKDMVVQLIDDFKisGMNGIHVCM 212
Cdd:cd14192    12 LGGGRFGQVHKCTELSTGLTLAAKIikVKGAKEREEVK-NEINIMNQL--------NHVNLIQLYDAFE--SKTNLTLIM 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510836 213 VFeVLGHHLLKWIIKSNYQGLPVRCVkSIIRQVLQGLDYLHSKcKIIHTDIKPENILmCVD 273
Cdd:cd14192    81 EY-VDGGELFDRITDESYQLTELDAI-LFTRQICEGVHYLHQH-YILHLDLKPENIL-CVN 137
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
238-278 9.80e-06

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: 48.20  E-value: 9.80e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1370510836 238 VKSIIRQVLQGLDYLHSkCKIIHTDIKPENILMCVDDAYVR 278
Cdd:cd14013   122 IKSIMRQILVALRKLHS-TGIVHRDVKPQNIIVSEGDGQFK 161
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
128-270 1.06e-05

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: 47.78  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVV---KSAQH-YTETALDEIKLLKCVREsdpsdPNkdmVVQLiddFKIS 203
Cdd:cd14663     1 RYELGRTLGEGTFAKVKFARNTKTGESVAIKIIdkeQVAREgMVEQIKREIAIMKLLRH-----PN---IVEL---HEVM 69
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510836 204 GMNGiHVCMVFE-VLGHHLLKWIIKSNYqgLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd14663    70 ATKT-KIFFVMElVTGGELFSKIAKNGR--LKEDKARKYFQQLIDAVDYCHSR-GVFHRDLKPENLLL 133
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
130-270 1.06e-05

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: 47.87  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 130 HVIRKLGWGHFSTVWLCWDMQGKRFVAMKVV--KSAQHYTETALdEIKLLKcvresdpSDPNKDMVVQLID---DFKISG 204
Cdd:cd13975     3 KLGRELGRGQYGVVYACDSWGGHFPCALKSVvpPDDKHWNDLAL-EFHYTR-------SLPKHERIVSLHGsviDYSYGG 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510836 205 MNGIHVCMVFEVLgHHLLKWIIKSnyqGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd13975    75 GSSIAVLLIMERL-HRDLYTGIKA---GLSLEERLQIALDVVEGIRFLHSQ-GLVHRDIKLKNVLL 135
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
151-269 1.07e-05

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: 47.71  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 151 GKRFVAMKVVK-SAQHYTETALDEIKLLKCVREsdpsdPNkdmVVQLIDDFKISGMNGIHVCMVfevLGHHLLKWIIKSN 229
Cdd:cd14088    26 GKLYTCKKFLKrDGRKVRKAAKNEINILKMVKH-----PN---ILQLVDVFETRKEYFIFLELA---TGREVFDWILDQG 94
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1370510836 230 YQGlpVRCVKSIIRQVLQGLDYLHSKCkIIHTDIKPENIL 269
Cdd:cd14088    95 YYS--ERDTSNVIRQVLEAVAYLHSLK-IVHRNLKLENLV 131
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
573-735 1.11e-05

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: 47.59  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 573 RVKIADLGNACWVhkhfTEDIQTRqyRSI---------EVLIGAGYSTPADIWSTACMAFELATGD--YLFEPhsgedys 641
Cdd:cd06614   135 SVKLADFGFAAQL----TKEKSKR--NSVvgtpywmapEVIKRKDYGPKVDIWSLGIMCIEMAEGEppYLEEP------- 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 642 rdedhialiiellgkvPRKyAMlgkyskeFFTRKGELRHITKLKPWSlfdvlvekygwphedaAQFTDFLIPMLEMVPEK 721
Cdd:cd06614   202 ----------------PLR-AL-------FLITTKGIPPLKNPEKWS----------------PEFKDFLNKCLVKDPEK 241
                         170
                  ....*....|....
gi 1370510836 722 RASAGECLRHPWLN 735
Cdd:cd06614   242 RPSAEELLQHPFLK 255
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
135-270 1.12e-05

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: 47.61  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKRFVAMKVVKSAqHYTETALDE-IKLLKCVRESDpsdpNKDMVVQLIDDFKisgmNGIHVCMV 213
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTFALKCVKKR-HIVQTRQQEhIFSEKEILEEC----NSPFIVKLYRTFK----DKKYLYML 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510836 214 FE-VLGHHLlkWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd05572    72 MEyCLGGEL--WTILRDRGLFDEYTARFYTACVVLAFEYLHSR-GIIYRDLKPENLLL 126
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
555-734 1.15e-05

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: 47.62  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 555 RAADLLVNpldpRNADkirVKIADLGnacwVHKHFTEDIQTRQ-------YRSIEVLIGAGYSTPADIWSTACMAFELAT 627
Cdd:cd06609   125 KAANILLS----EEGD---VKLADFG----VSGQLTSTMSKRNtfvgtpfWMAPEVIKQSGYDEKADIWSLGITAIELAK 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 628 GDylfEPHSGEDysrdedhialiiellgkvPRKYAMLgkyskefftrkgelrhITKLKPWSLFDvlvEKYGWPhedaaqF 707
Cdd:cd06609   194 GE---PPLSDLH------------------PMRVLFL----------------IPKNNPPSLEG---NKFSKP------F 227
                         170       180
                  ....*....|....*....|....*..
gi 1370510836 708 TDFLIPMLEMVPEKRASAGECLRHPWL 734
Cdd:cd06609   228 KDFVELCLNKDPKERPSAKELLKHKFI 254
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
127-277 1.41e-05

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: 47.28  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 127 GRYHV--IRKLGWGHFSTVWLCWDMQ-GKRFVAMKVVKSAQHYTETALDEIKLLKCVResdpsdPNKDmVVQLIDDFKIS 203
Cdd:cd14037     1 GSHHVtiEKYLAEGGFAHVYLVKTSNgGNRAALKRVYVNDEHDLNVCKREIEIMKRLS------GHKN-IVGYIDSSANR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 204 GMNGihvcmVFEVL-------GHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSkCK--IIHTDIKPENILMCVDD 274
Cdd:cd14037    74 SGNG-----VYEVLllmeyckGGGVIDLMNQRLQTGLTESEILKIFCDVCEAVAAMHY-LKppLIHRDLKVENVLISDSG 147

                  ...
gi 1370510836 275 AYV 277
Cdd:cd14037   148 NYK 150
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
128-270 1.44e-05

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; 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. Mutations in TTBK2 is associated with the development of spinocerebellar ataxia type 11, belonging to a group of neurodegenerative disorders characterized by progressive incoordination, dysarthria and impairment of eye movements. Brain tissues of SCA11 patients show the presence of neurofibrillary tangles and tau deposition in the brain, similar to Alzheimer's disease (AD) patients. The TTBK2 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: 271031 [Multi-domain]  Cd Length: 262  Bit Score: 47.36  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVvKSAQHYTETALDEIKLLKCVResdpsdpNKDMVVQLIDdfkiSGMNG 207
Cdd:cd14129     1 RWKVLRKIGGGGFGEIYDALDLLTRENVALKV-ESAQQPKQVLKMEVAVLKKLQ-------GKDHVCRFIG----CGRND 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510836 208 IHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILM 270
Cdd:cd14129    69 RFNYVVMQLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHS-VGFLHRDIKPSNFAM 130
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
129-270 1.60e-05

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: 47.29  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVV---KSAQHYTETALD-EIKLLKCVREsdpsdPNKDMVVQLIDdfkisg 204
Cdd:cd14162     2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVskkKAPEDYLQKFLPrEIEVIKGLKH-----PNLICFYEAIE------ 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510836 205 mNGIHVCMVFEvLGHH--LLKWIIKSNYqgLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd14162    71 -TTSRVYIIME-LAENgdLLDYIRKNGA--LPEPQARRWFRQLVAGVEYCHSK-GVVHRDLKCENLLL 133
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
128-270 1.62e-05

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: 47.57  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMK-VVK--SAQHYTETALDEIKLLKCVRESDpsdpnkdmVVQLIDDFkISG 204
Cdd:cd07856    11 RYSDLQPVGMGAFGLVCSARDQLTGQNVAVKkIMKpfSTPVLAKRTYRELKLLKHLRHEN--------IISLSDIF-ISP 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370510836 205 MNGIHvcMVFEVLG---HHLLKwiiksnYQGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILM 270
Cdd:cd07856    82 LEDIY--FVTELLGtdlHRLLT------SRPLEKQFIQYFLYQILRGLKYVHS-AGVIHRDLKPSNILV 141
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
574-735 1.91e-05

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 47.12  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 574 VKIADLGNACWVH---KHFTEDIQTRQYRSIEVLIGA-GYSTPADIWSTACMAFELATGDYLFEPHSgedysrDEDHIAL 649
Cdd:PLN00009  142 LKLADFGLARAFGipvRTFTHEVVTLWYRAPEILLGSrHYSTPVDIWSVGCIFAEMVNQKPLFPGDS------EIDELFK 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 650 IIELLGkVPRKYAMLGKYS----KEFFTRkgelrhitklkpwslfdvlvekygWPHEDAAQFT--------DFLIPMLEM 717
Cdd:PLN00009  216 IFRILG-TPNEETWPGVTSlpdyKSAFPK------------------------WPPKDLATVVptlepagvDLLSKMLRL 270
                         170
                  ....*....|....*...
gi 1370510836 718 VPEKRASAGECLRHPWLN 735
Cdd:PLN00009  271 DPSKRITARAALEHEYFK 288
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
119-273 1.93e-05

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: 47.02  E-value: 1.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 119 VKIGDLfNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQH-YTETALDEIKLLKcvresDPSDPNkdmVVQLI 197
Cdd:cd06656    12 VSVGDP-KKKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQpKKELIINEILVMR-----ENKNPN---IVNYL 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510836 198 DDFKIsgmnGIHVCMVFEVLGHHLLKWIIKSNYqgLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVD 273
Cdd:cd06656    83 DSYLV----GDELWVVMEYLAGGSLTDVVTETC--MDEGQIAAVCRECLQALDFLHSN-QVIHRDIKSDNILLGMD 151
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
135-269 1.93e-05

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: 47.00  E-value: 1.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALD------EIKLLKCVREsdpsdpnkDMVVQLIDDFKISGMNGI 208
Cdd:cd06651    15 LGQGAFGRVYLCYDVDTGRELAAKQVQFDPESPETSKEvsalecEIQLLKNLQH--------ERIVQYYGCLRDRAEKTL 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510836 209 HVCMVFEVLGHhlLKWIIKSnYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:cd06651    87 TIFMEYMPGGS--VKDQLKA-YGALTESVTRKYTRQILEGMSYLHSN-MIVHRDIKGANIL 143
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
238-270 1.99e-05

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: 46.87  E-value: 1.99e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1370510836 238 VKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd05578   102 VKFYICEIVLALDYLHSK-NIIHRDIKPDNILL 133
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
128-269 2.16e-05

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: 47.08  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSA-QHYTETA--LDEIKLLKCVRESDPSDPNKDMVVQLIDDFKisg 204
Cdd:cd07859     1 RYKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINDVfEHVSDATriLREIKLLRLLRHPDIVEIKHIMLPPSRREFK--- 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 205 mngiHVCMVFEVLGHHLLKwIIKSNyQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:cd07859    78 ----DIYVVFELMESDLHQ-VIKAN-DDLTPEHHQFFLYQLLRALKYIHTA-NVFHRDLKPKNIL 135
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
135-278 2.35e-05

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: 46.58  E-value: 2.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKRFVAMKVV--------------------KSAQHYTETALD----EIKLLKCVresdpSDPNK 190
Cdd:cd14118     2 IGKGSYGIVKLAYNEEDNTLYAMKILskkkllkqagffrrppprrkPGALGKPLDPLDrvyrEIAILKKL-----DHPNV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 191 DMVVQLIDDfkisgMNGIHVCMVFEVLGHHLLKWIIKSNyqGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd14118    77 VKLVEVLDD-----PNEDNLYMVFELVDKGAVMEVPTDN--PLSEETARSYFRDIVLGIEYLHYQ-KIIHRDIKPSNLLL 148

                  ....*...
gi 1370510836 271 cVDDAYVR 278
Cdd:cd14118   149 -GDDGHVK 155
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
123-273 2.38e-05

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: 46.85  E-value: 2.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 123 DLFNGRYHVI--RKLGWGHFSTVWLCWDMQ-GKRFVA--MKVVKSAQHYTETALDEIKLLKCVRESDpsdpnkdMVVQLI 197
Cdd:cd14197     3 EPFQERYSLSpgRELGRGKFAVVRKCVEKDsGKEFAAkfMRKRRKGQDCRMEIIHEIAVLELAQANP-------WVINLH 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510836 198 DDFKISGmngiHVCMVFE-VLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVD 273
Cdd:cd14197    76 EVYETAS----EMILVLEyAAGGEIFNQCVADREEAFKEKDVKRLMKQILEGVSFLHNN-NVVHLDLKPQNILLTSE 147
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
208-270 2.39e-05

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: 46.42  E-value: 2.39e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510836 208 IHVCMVFEVLGHHLLKWIIKSnyqglpvRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd14107    77 LELCSSEELLDRLFLKGVVTE-------AEVKLYIQQVLEGIGYLHGM-NILHLDIKPDNILM 131
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
127-270 2.52e-05

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: 46.71  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 127 GRYHVIRKLGWGHFSTVWLCW-----DMQGKRFVAMKVVKSaqhytETALDEIKLLKCVRESDP----SDPNkdmVVQLI 197
Cdd:cd14076     1 GPYILGRTLGEGEFGKVKLGWplpkaNHRSGVQVAIKLIRR-----DTQQENCQTSKIMREINIlkglTHPN---IVRLL 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370510836 198 DDFKISGMNGIhvcmVFE-VLGHHLLKWIIKSNYQGLPVRCvkSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd14076    73 DVLKTKKYIGI----VLEfVSGGELFDYILARRRLKDSVAC--RLFAQLISGVAYLHKK-GVVHRDLKLENLLL 139
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
574-733 2.77e-05

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: 46.73  E-value: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 574 VKIADLGNACWVH---KHFTEDIQTRQYRSIEVLIGAG-YSTPADIWSTACMAFELATGDYLFEPHSgedysrDEDHIAL 649
Cdd:cd07860   139 IKLADFGLARAFGvpvRTYTHEVVTLWYRAPEILLGCKyYSTAVDIWSLGCIFAEMVTRRALFPGDS------EIDQLFR 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 650 IIELLG----KVPRKYAMLGKYSKEF--FTRKGelrhITKLKPwslfdvLVEKYGwphedaaqfTDFLIPMLEMVPEKRA 723
Cdd:cd07860   213 IFRTLGtpdeVVWPGVTSMPDYKPSFpkWARQD----FSKVVP------PLDEDG---------RDLLSQMLHYDPNKRI 273
                         170
                  ....*....|
gi 1370510836 724 SAGECLRHPW 733
Cdd:cd07860   274 SAKAALAHPF 283
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
238-269 3.55e-05

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: 46.22  E-value: 3.55e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1370510836 238 VKSIIRQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:cd06629   110 VRFFTRQILDGLAYLHSK-GILHRDLKADNIL 140
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
128-270 3.88e-05

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: 46.14  E-value: 3.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETAL--DEIKLLKCVREsdpsdPNkdmVVQLIDDFKISgm 205
Cdd:cd14183     7 RYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEHMiqNEVSILRRVKH-----PN---IVLLIEEMDMP-- 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 206 NGIHVCMVFeVLGHHLLKWIIKSNYqgLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILM 270
Cdd:cd14183    77 TELYLVMEL-VKGGDLFDAITSTNK--YTERDASGMLYNLASAIKYLHS-LNIVHRDIKPENLLV 137
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
241-270 4.11e-05

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: 45.77  E-value: 4.11e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1370510836 241 IIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd13995   101 VTKHVLKGLDFLHSK-NIIHHDIKPSNIVF 129
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
129-275 4.68e-05

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: 46.09  E-value: 4.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVV-KSAQHYTEtaldEIKLLkcVRESdpSDPNkdmVVQLIDDFKisgmNG 207
Cdd:cd14091     2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIdKSKRDPSE----EIEIL--LRYG--QHPN---IITLRDVYD----DG 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370510836 208 IHVCMVFEVL-GHHLLKWIIKSNYqgLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVDDA 275
Cdd:cd14091    67 NSVYLVTELLrGGELLDRILRQKF--FSEREASAVMKTLTKTVEYLHSQ-GVVHRDLKPSNILYADESG 132
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
239-275 5.21e-05

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: 45.73  E-value: 5.21e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1370510836 239 KSIIRQVLQGLDYLHSkCKIIHTDIKPENILMCVDDA 275
Cdd:cd13982   102 VRLLRQIASGLAHLHS-LNIVHRDLKPQNILISTPNA 137
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
121-275 6.06e-05

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: 45.30  E-value: 6.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 121 IGDLfNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVK-SAQHYTETALDEIKLLKcvresDPSDPNkdmVVQLIDD 199
Cdd:cd06647     2 VGDP-KKKYTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNlQQQPKKELIINEILVMR-----ENKNPN---IVNYLDS 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510836 200 FKIsgmnGIHVCMVFEVLGHHLLKWIIKSNYqgLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVDDA 275
Cdd:cd06647    73 YLV----GDELWVVMEYLAGGSLTDVVTETC--MDEGQIAAVCRECLQALEFLHSN-QVIHRDIKSDNILLGMDGS 141
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
128-270 6.07e-05

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: 45.49  E-value: 6.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQhytetaLDEIKLLKCVRESDP----SDPNkdmVVQLIDDFKIS 203
Cdd:cd14086     2 EYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKK------LSARDHQKLEREARIcrllKHPN---IVRLHDSISEE 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 204 GmngiHVCMVFE-VLGHHLLKWIIKSNY--QGLPVRCvksiIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd14086    73 G----FHYLVFDlVTGGELFEDIVAREFysEADASHC----IQQILESVNHCHQN-GIVHRDLKPENLLL 133
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
227-278 6.29e-05

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: 45.58  E-value: 6.29e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370510836 227 KSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVDDAYVR 278
Cdd:cd14049   111 SAPYTPVDVDVTTKILQQLLEGVTYIHSM-GIVHRDLKPRNIFLHGSDIHVR 161
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
573-639 6.32e-05

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 46.16  E-value: 6.32e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510836 573 RVKIADLGNACWVHK-HFTED---IQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSGED 639
Cdd:COG0515   145 RVKLIDFGIARALGGaTLTQTgtvVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAE 215
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
129-270 6.51e-05

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: 44.99  E-value: 6.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKS---AQHYTETALDEIKLLkcvrESDPSDPNkdmVVQLIDDFKISGM 205
Cdd:cd14050     3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSrfrGEKDRKRKLEEVERH----EKLGEHPN---CVRFIKAWEEKGI 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 206 NGIHVCMVFEVLGHHLLKWiiksnyQGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILM 270
Cdd:cd14050    76 LYIQTELCDTSLQQYCEET------HSLPESEVWNILLDLLKGLKHLHD-HGLIHLDIKPANIFL 133
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
559-678 6.98e-05

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: 45.85  E-value: 6.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 559 LLVNPLdprnADKIRVKIADLGNACWVHKHFTED-IQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFePHSG 637
Cdd:cd14228   149 MLVDPV----RQPYRVKVIDFGSASHVSKAVCSTyLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLY-PGAS 223
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1370510836 638 EdysrdEDHIALIIELLGkVPRKYAM-LGKYSKEFFTRKGEL 678
Cdd:cd14228   224 E-----YDQIRYISQTQG-LPAEYLLsAGTKTSRFFNRDPNL 259
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
129-270 7.14e-05

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: 45.38  E-value: 7.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTE--TALDEIKLLKCVRESDpsdpnkdmVVQLIDDfkisgmn 206
Cdd:cd07873     4 YIKLDKLGEGTYATVYKGRSKLTDNLVALKEIRLEHEEGApcTAIREVSLLKDLKHAN--------IVTLHDI------- 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510836 207 gIH----VCMVFEVLGHHLLKWIIKSNyQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd07873    69 -IHteksLTLVFEYLDKDLKQYLDDCG-NSINMHNVKLFLFQLLRGLAYCHRR-KVLHRDLKPQNLLI 133
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
574-633 7.31e-05

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: 44.99  E-value: 7.31e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510836 574 VKIADLGNACWVHKHFTEDIQ-------TRQYRSIEVLIGAGYS-TPADIWSTACMAFELATGDYLFE 633
Cdd:cd13994   137 LKLTDFGTAEVFGMPAEKESPmsaglcgSEPYMAPEVFTSGSYDgRAVDVWSCGIVLFALFTGRFPWR 204
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
128-270 8.43e-05

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: 45.37  E-value: 8.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQH--YTETALDEIKLLKCVRESDpsdpnkdmVVQLIDDFK---I 202
Cdd:cd07849     6 RYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISPFEHqtYCLRTLREIKILLRFKHEN--------IIGILDIQRpptF 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510836 203 SGMNGIHVcmVFEVLGHHLLKwIIKSnyQGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILM 270
Cdd:cd07849    78 ESFKDVYI--VQELMETDLYK-LIKT--QHLSNDHIQYFLYQILRGLKYIHS-ANVLHRDLKPSNLLL 139
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
123-270 8.47e-05

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: 44.91  E-value: 8.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 123 DLFNGRYHVIRK-LGWGHFSTVWLCWDMQ-GKRFVA--MKVVKSAQHYTETALDEIKLLKCVReSDPSDPNKDMVVQLID 198
Cdd:cd14198     3 DNFNNFYILTSKeLGRGKFAVVRQCISKStGQEYAAkfLKKRRRGQDCRAEILHEIAVLELAK-SNPRVVNLHEVYETTS 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370510836 199 DFkisgmngihVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd14198    82 EI---------ILILEYAAGGEIFNLCVPDLAEMVSENDIIRLIRQILEGVYYLHQN-NIVHLDLKPQNILL 143
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
239-271 8.58e-05

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: 45.09  E-value: 8.58e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1370510836 239 KSIIRQVLQGLDYLHSKcKIIHTDIKPENILMC 271
Cdd:cd14051   107 KDLLLQVAQGLKYIHSQ-NLVHMDIKPGNIFIS 138
PLN03224 PLN03224
probable serine/threonine protein kinase; Provisional
235-273 8.89e-05

probable serine/threonine protein kinase; Provisional


Pssm-ID: 178763 [Multi-domain]  Cd Length: 507  Bit Score: 45.83  E-value: 8.89e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1370510836 235 VRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILMCVD 273
Cdd:PLN03224  308 INVIKGVMRQVLTGLRKLHR-IGIVHRDIKPENLLVTVD 345
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
127-271 9.49e-05

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: 44.71  E-value: 9.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 127 GRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKsaqhytETALDEIkllkcvresdpsdpNKDMVVQLIDDFKIsgMN 206
Cdd:cd14074     3 GLYDLEETLGRGHFAVVKLARHVFTGEKVAVKVID------KTKLDDV--------------SKAHLFQEVRCMKL--VQ 60
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370510836 207 GIHVCMVFEVL--------------GHHLLKWIIKsNYQGLPVRCVKSIIRQVLQGLDYLHsKCKIIHTDIKPENILMC 271
Cdd:cd14074    61 HPNVVRLYEVIdtqtklylilelgdGGDMYDYIMK-HENGLNEDLARKYFRQIVSAISYCH-KLHVVHRDLKPENVVFF 137
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
238-270 9.70e-05

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: 44.65  E-value: 9.70e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1370510836 238 VKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd14106   110 VRRLMRQILEGVQYLHER-NIVHLDLKPQNILL 141
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
211-269 1.03e-04

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: 44.70  E-value: 1.03e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370510836 211 CMVFEVLGHHLLKWIIKSNYQGL---PVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENIL 269
Cdd:cd14001    82 CLAMEYGGKSLNDLIEERYEAGLgpfPAATILKVALSIARALEYLHNEKKILHGDIKSGNVL 143
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
128-271 1.11e-04

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: 44.50  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWD-MQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDpsdpnkdmVVQLIDDFKisgmN 206
Cdd:cd14114     3 HYDILEELGTGAFGVVHRCTErATGNNFAAKFIMTPHESDKETVRKEIQIMNQLHHPK--------LINLHDAFE----D 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510836 207 GIHVCMVFEVL-GHHLLKWIIKSNYQGLPVRCVkSIIRQVLQGLDYLHSKcKIIHTDIKPENIlMC 271
Cdd:cd14114    71 DNEMVLILEFLsGGELFERIAAEHYKMSEAEVI-NYMRQVCEGLCHMHEN-NIVHLDIKPENI-MC 133
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
211-275 1.12e-04

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: 44.41  E-value: 1.12e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 211 CMVFEVLGHHLLKWIIKSNYQGLPVRCVkSIIRQVLQGLDYLHSkCKIIHTDIKPENILMCVDDA 275
Cdd:cd14059    57 CILMEYCPYGQLYEVLRAGREITPSLLV-DWSKQIASGMNYLHL-HKIIHRDLKSPNVLVTYNDV 119
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
595-734 1.26e-04

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: 44.34  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 595 TRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSgedysrdedHIALIIELL-GKVPrkyAMLGKYSKefft 673
Cdd:cd08222   168 TPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQN---------LLSVMYKIVeGETP---SLPDKYSK---- 231
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510836 674 rkgELRHITKLkpwslfdvlvekygwphedaaqftdflipMLEMVPEKRASAGECLRHPWL 734
Cdd:cd08222   232 ---ELNAIYSR-----------------------------MLNKDPALRPSAAEILKIPFI 260
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
155-271 1.34e-04

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: 44.28  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 155 VAMKVV-KSAQHYTETALD-EIKLLKcvresdpsDPNKDMVVQLIDdFKISGMngiHVCMVFEVL-GHHLLKWIIKsnyQ 231
Cdd:cd14120    22 VAIKCItKKNLSKSQNLLGkEIKILK--------ELSHENVVALLD-CQETSS---SVYLVMEYCnGGDLADYLQA---K 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1370510836 232 G-LPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMC 271
Cdd:cd14120    87 GtLSEDTIRVFLQQIAAAMKALHSK-GIVHRDLKPQNILLS 126
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
138-270 1.36e-04

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: 44.14  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 138 GHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVREsdpsdPNkdmVVQLiddfKISGMNGIHVCMVFEV- 216
Cdd:cd14110    14 GRFSVVRQCEEKRSGQMLAAKIIPYKPEDKQLVLREYQVLRRLSH-----PR---IAQL----HSAYLSPRHLVLIEELc 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 217 LGHHLLKWIIKSN-YQGLPVRcvkSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd14110    82 SGPELLYNLAERNsYSEAEVT---DYLWQILSAVDYLHSR-RILHLDLRSENMII 132
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
119-273 1.40e-04

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: 44.33  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 119 VKIGDLfNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQH-YTETALDEIKLLKcvresDPSDPNkdmVVQLI 197
Cdd:cd06654    13 VSVGDP-KKKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQpKKELIINEILVMR-----ENKNPN---IVNYL 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510836 198 DDFKIsgmnGIHVCMVFEVLGHHLLKWIIKSNYqgLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVD 273
Cdd:cd06654    84 DSYLV----GDELWVVMEYLAGGSLTDVVTETC--MDEGQIAAVCRECLQALEFLHSN-QVIHRDIKSDNILLGMD 152
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
135-270 1.62e-04

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: 43.96  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKRFVAMKVVK------SAQHYT-ETALDEIKLLkcvreSDPSDPNkdmVVQLIDDFKisgmNG 207
Cdd:cd06630     8 LGTGAFSSCYQARDVKTGTLMAVKQVSfcrnssSEQEEVvEAIREEIRMM-----ARLNHPN---IVRMLGATQ----HK 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510836 208 IHVCMVFEVLG----HHLLkwiikSNYQGLPVRCVKSIIRQVLQGLDYLHSKCkIIHTDIKPENILM 270
Cdd:cd06630    76 SHFNIFVEWMAggsvASLL-----SKYGAFSENVIINYTLQILRGLAYLHDNQ-IIHRDLKGANLLV 136
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
131-305 1.71e-04

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: 43.85  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 131 VIRKLGWGHFSTVWlcwdmQGKRF--VAMKVVKSAQHYTETAL---DEIKLLKCVRESD-------PSDPNKDMVVQLID 198
Cdd:cd14150     4 MLKRIGTGSFGTVF-----RGKWHgdVAVKILKVTEPTPEQLQafkNEMQVLRKTRHVNillfmgfMTRPNFAIITQWCE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 199 DfkisgmngihvcmvfEVLGHHLlkWIIKSNYQglPVRCVkSIIRQVLQGLDYLHSKcKIIHTDIKPENILMcvDDAYVR 278
Cdd:cd14150    79 G---------------SSLYRHL--HVTETRFD--TMQLI-DVARQTAQGMDYLHAK-NIIHRDLKSNNIFL--HEGLTV 135
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1370510836 279 R-----MAAEATEWqkAGAPP---PSGSAVSTAPQ 305
Cdd:cd14150   136 KigdfgLATVKTRW--SGSQQveqPSGSILWMAPE 168
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
128-290 2.07e-04

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: 44.17  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVK---SAQHYTETALDEIKLLKCVREsdpsdpnkDMVVQLID----DF 200
Cdd:cd07880    16 RYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYrpfQSELFAKRAYRELRLLKHMKH--------ENVIGLLDvftpDL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 201 KISGMNGIHVCMVFevLGHHLLKwIIKsnYQGLPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENI-------LMCVD 273
Cdd:cd07880    88 SLDRFHDFYLVMPF--MGTDLGK-LMK--HEKLSEDRIQFLVYQMLKGLKYIHA-AGIIHRDLKPGNLavnedceLKILD 161
                         170       180
                  ....*....|....*....|..
gi 1370510836 274 DAYVRRMAAE-----ATEWQKA 290
Cdd:cd07880   162 FGLARQTDSEmtgyvVTRWYRA 183
PLN03225 PLN03225
Serine/threonine-protein kinase SNT7; Provisional
231-269 2.07e-04

Serine/threonine-protein kinase SNT7; Provisional


Pssm-ID: 215638 [Multi-domain]  Cd Length: 566  Bit Score: 44.78  E-value: 2.07e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1370510836 231 QGLP------VRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:PLN03225  244 QDLPkglereNKIIQTIMRQILFALDGLHST-GIVHRDVKPQNII 287
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
128-270 2.57e-04

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; 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. The delta and epsilon isoforms of CK1 play important roles in circadian rhythm and cell growth. They phosphorylate PERIOD proteins (PER1-3), which are circadian clock proteins that fulfill negative regulatory functions. PER phosphorylation leads to its degradation. However, CRY proteins form a complex with PER and CK1delta/epsilon that protects PER from degradation and leads to nuclear accummulation of the complex, which inhibits BMAL1-CLOCK dependent transcription activation. CK1delta/epsilon also phosphorylate the tumor suppressor p53 and the cellular oncogene Mdm2, which are key regulators of cell growth, genome integrity, and the development of cancer. This subfamily also includes the CK1 fungal proteins Saccharomyces cerevisiae HRR25 and Schizosaccharomyces pombe HHP1. These fungal proteins are involved in DNA repair. The CK1 delta/epsilon 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: 271027 [Multi-domain]  Cd Length: 275  Bit Score: 43.51  E-value: 2.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKvvksaqhytetaldeiklLKCVRESDPsdpnkdmvvQLIDDFKI----- 202
Cdd:cd14125     1 KYRLGRKIGSGSFGDIYLGTNIQTGEEVAIK------------------LESVKTKHP---------QLLYESKLykilq 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 203 ----------SGMNGIHVCMVFEVLGHHLLKWIiksNYQG--LPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd14125    54 ggvgipnvrwYGVEGDYNVMVMDLLGPSLEDLF---NFCSrkFSLKTVLMLADQMISRIEYVHSK-NFIHRDIKPDNFLM 129
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
132-270 2.70e-04

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: 43.51  E-value: 2.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 132 IRKLGWGHFSTVWLCWDMQGKRFVAMKVV--KSAQHYTETALDEIKLLkcvreSDPSDPnkdmvvqLIDDFKISGMNGIH 209
Cdd:cd06642     9 LERIGKGSFGEVYKGIDNRTKEVVAIKIIdlEEAEDEIEDIQQEITVL-----SQCDSP-------YITRYYGSYLKGTK 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510836 210 VCMVFEVLGHHLLKWIIKSNyqGLPVRCVKSIIRQVLQGLDYLHSKCKiIHTDIKPENILM 270
Cdd:cd06642    77 LWIIMEYLGGGSALDLLKPG--PLEETYIATILREILKGLDYLHSERK-IHRDIKAANVLL 134
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
242-274 2.75e-04

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: 43.51  E-value: 2.75e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1370510836 242 IRQVLQGLDYLHSKcKIIHTDIKPENILMCVDD 274
Cdd:cd14046   110 FRQILEGLAYIHSQ-GIIHRDLKPVNIFLDSNG 141
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
203-274 2.81e-04

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: 43.38  E-value: 2.81e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370510836 203 SGMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVDD 274
Cdd:cd14020    77 YSANVPSRCLLLELLDVSVSELLLRSSNQGCSMWMIQHCARDVLEALAFLHHE-GYVHADLKPRNILWSAED 147
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
128-270 2.85e-04

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: 43.21  E-value: 2.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVV----KSAQHYTETALDEIKLLKCVREsdpsdPNkdmvvqlIDDFKIS 203
Cdd:cd06607     2 IFEDLREIGHGSFGAVYYARNKRTSEVVAIKKMsysgKQSTEKWQDIIKEVKFLRQLRH-----PN-------TIEYKGC 69
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510836 204 GMNGIHVCMVFE-VLGHhlLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCKiIHTDIKPENILM 270
Cdd:cd06607    70 YLREHTAWLVMEyCLGS--ASDIVEVHKKPLQEVEIAAICHGALQGLAYLHSHNR-IHRDVKAGNILL 134
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
129-275 2.86e-04

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: 43.48  E-value: 2.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVV-KSAQHYTEtaldEIKLLKCVRESdpsdPNkdmVVQLIDDFKisgmNG 207
Cdd:cd14175     3 YVVKETIGVGSYSVCKRCVHKATNMEYAVKVIdKSKRDPSE----EIEILLRYGQH----PN---IITLKDVYD----DG 67
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370510836 208 IHVCMVFEVL-GHHLLKWIIKSNYqgLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMcVDDA 275
Cdd:cd14175    68 KHVYLVTELMrGGELLDKILRQKF--FSEREASSVLHTICKTVEYLHSQ-GVVHRDLKPSNILY-VDES 132
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
129-270 3.02e-04

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: 43.44  E-value: 3.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTE--TALDEIKLLKCVRESDpsdpnkdmVVQLIDDFKISGmn 206
Cdd:cd07872     8 YIKLEKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGApcTAIREVSLLKDLKHAN--------IVTLHDIVHTDK-- 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370510836 207 giHVCMVFEVLGHHLLKWIIKSNyQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd07872    78 --SLTLVFEYLDKDLKQYMDDCG-NIMSMHNVKIFLYQILRGLAYCHRR-KVLHRDLKPQNLLI 137
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
243-270 3.21e-04

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 43.66  E-value: 3.21e-04
                          10        20
                  ....*....|....*....|....*...
gi 1370510836 243 RQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:PLN00034  175 RQILSGIAYLHRR-HIVHRDIKPSNLLI 201
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
213-275 3.33e-04

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: 43.14  E-value: 3.33e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370510836 213 VFEVLGHHLLKWIIKSNYQGLPV-RCVKsIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVDDA 275
Cdd:cd13979    80 IMEYCGNGTLQQLIYEGSEPLPLaHRIL-ISLDIARALRFCHSH-GIVHLDVKPANILISEQGV 141
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
125-270 3.73e-04

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: 42.96  E-value: 3.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 125 FNGRY-HVIRKLGWGHFSTVWL-CWDMQGK---RFVAMKVVKS--AQHYTETALDEIKLLKCVRESDpsdpnkdmVVQLI 197
Cdd:cd05080     1 FHKRYlKKIRDLGEGHFGKVSLyCYDPTNDgtgEMVAVKALKAdcGPQHRSGWKQEIDILKTLYHEN--------IVKYK 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510836 198 DDFKISGMNGIHVCMVFEVLGHhLLKWIIKSNyqgLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd05080    73 GCCSEQGGKSLQLIMEYVPLGS-LRDYLPKHS---IGLAQLLLFAQQICEGMAYLHSQ-HYIHRDLAARNVLL 140
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
135-269 3.91e-04

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: 42.78  E-value: 3.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKRFVAMKVV--KSAQhYTETALDEIKLLKCVRESDpsdpnkdmVVQLIDDFKISGMngihvCM 212
Cdd:cd06624    16 LGKGTFGVVYAARDLSTQVRIAIKEIpeRDSR-EVQPLHEEIALHSRLSHKN--------IVQYLGSVSEDGF-----FK 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510836 213 VF--EVLG---HHLL--KWiiksnyqGlPVRCVKSII----RQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:cd06624    82 IFmeQVPGgslSALLrsKW-------G-PLKDNENTIgyytKQILEGLKYLHDN-KIVHRDIKGDNVL 140
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
126-270 4.02e-04

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: 43.06  E-value: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 126 NGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVvksaQHYTETALDEIKLLKCVRESDPSDPNkdmVVQLIDDFKISGM 205
Cdd:cd06608     5 AGIFELVEVIGEGTYGKVYKARHKKTGQLAAIKI----MDIIEDEEEEIKLEINILRKFSNHPN---IATFYGAFIKKDP 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510836 206 NGIH--VCMVFEVLGH----HLLKWIIKSNyQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd06608    78 PGGDdqLWLVMEYCGGgsvtDLVKGLRKKG-KRLKEEWIAYILRETLRGLAYLHEN-KVIHRDIKGQNILL 146
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
205-269 4.25e-04

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: 42.72  E-value: 4.25e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 205 MNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:cd14063    66 MDPPHLAIVTSLCKGRTLYSLIHERKEKFDFNKTVQIAQQICQGMGYLHAK-GIIHKDLKSKNIF 129
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
129-270 4.33e-04

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: 42.68  E-value: 4.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYT-------ETALDEIKLLKCVRESDpsdpnkdmVVQLIDDFK 201
Cdd:cd14195     7 YEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSsrrgvsrEEIEREVNILREIQHPN--------IITLHDIFE 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 202 isgmNGIHVCMVFE-VLGHHLLKWIIKSnyQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd14195    79 ----NKTDVVLILElVSGGELFDFLAEK--ESLTEEEATQFLKQILDGVHYLHSK-RIAHFDLKPENIML 141
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
127-270 4.41e-04

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: 42.64  E-value: 4.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 127 GRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVV-----KSAQHYTETAlDEIKLLKCVREsdpsdPNkdmVVQLIDdfK 201
Cdd:cd14079     2 GNYILGKTLGVGSFGKVKLAEHELTGHKVAVKILnrqkiKSLDMEEKIR-REIQILKLFRH-----PH---IIRLYE--V 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370510836 202 ISGMNGIHVCMVFeVLGHHLLKWIIKSNyqGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd14079    71 IETPTDIFMVMEY-VSGGELFDYIVQKG--RLSEDEARRFFQQIISGVEYCHRH-MVVHRDLKPENLLL 135
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
119-270 4.60e-04

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: 42.79  E-value: 4.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 119 VKIGDLfNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVK-SAQHYTETALDEIKLLKCVResdpsDPNkdmVVQLI 197
Cdd:cd06655    12 VSIGDP-KKKYTRYEKIGQGASGTVFTAIDVATGQEVAIKQINlQKQPKKELIINEILVMKELK-----NPN---IVNFL 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510836 198 DDFKIsgmnGIHVCMVFEVLGHHLLKWIIKSNYqgLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd06655    83 DSFLV----GDELFVVMEYLAGGSLTDVVTETC--MDEAQIAAVCRECLQALEFLHAN-QVIHRDIKSDNVLL 148
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
239-306 4.70e-04

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: 42.94  E-value: 4.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 239 KSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVDDAY------VRRMAAEATEWQKAGAPPPS--------GSAVSTAP 304
Cdd:cd14048   121 LNIFKQIASAVEYLHSK-GLIHRDLKPSNVFFSLDDVVkvgdfgLVTAMDQGEPEQTVLTPMPAyakhtgqvGTRLYMSP 199

                  ..
gi 1370510836 305 QQ 306
Cdd:cd14048   200 EQ 201
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
99-270 4.78e-04

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 43.10  E-value: 4.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836  99 GSDDEEQEDPADYCKGGYHPVKIGDLfngryhvirkLGWGHFSTVW--LCWDMQGKrfVAMKVVKSAQHYTETALDEIKL 176
Cdd:PTZ00036   48 EDEDEEKMIDNDINRSPNKSYKLGNI----------IGNGSFGVVYeaICIDTSEK--VAIKKVLQDPQYKNRELLIMKN 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 177 LkcvresdpsdpNKDMVVQLID-----DFKISGMNgIHVCMVFEVLG---HHLLKWIIKSNyQGLPVRCVKSIIRQVLQG 248
Cdd:PTZ00036  116 L-----------NHINIIFLKDyyyteCFKKNEKN-IFLNVVMEFIPqtvHKYMKHYARNN-HALPLFLVKLYSYQLCRA 182
                         170       180
                  ....*....|....*....|..
gi 1370510836 249 LDYLHSKCkIIHTDIKPENILM 270
Cdd:PTZ00036  183 LAYIHSKF-ICHRDLKPQNLLI 203
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
245-269 4.87e-04

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: 42.80  E-value: 4.87e-04
                          10        20
                  ....*....|....*....|....*
gi 1370510836 245 VLQGLDYLHSKCKIIHTDIKPENIL 269
Cdd:cd06617   112 IVKALEYLHSKLSVIHRDVKPSNVL 136
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
574-734 4.98e-04

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: 42.78  E-value: 4.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 574 VKIADLG--------NACwvHKHFTediQTRQYRSIEVLIGA--GYSTPADIWSTACMAFELATGDYLFephsgedysrd 643
Cdd:cd06624   148 VKISDFGtskrlagiNPC--TETFT---GTLQYMAPEVIDKGqrGYGPPADIWSLGCTIIEMATGKPPF----------- 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 644 edhialiIELLgkvPRKYAM--LGKYskefftrkgelrhitKLKPwslfDVlvekygwPHEDAAQFTDFLIPMLEMVPEK 721
Cdd:cd06624   212 -------IELG---EPQAAMfkVGMF---------------KIHP----EI-------PESLSEEAKSFILRCFEPDPDK 255
                         170
                  ....*....|...
gi 1370510836 722 RASAGECLRHPWL 734
Cdd:cd06624   256 RATASDLLQDPFL 268
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
134-273 5.60e-04

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: 42.43  E-value: 5.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 134 KLGWGHFSTVWLCWDMQGKRFVAMKVVK-SAQHYTETALDEIKLLKcvresDPSDPNkdmVVQLIDDFKIsgmnGIHVCM 212
Cdd:cd06648    14 KIGEGSTGIVCIATDKSTGRQVAVKKMDlRKQQRRELLFNEVVIMR-----DYQHPN---IVEMYSSYLV----GDELWV 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370510836 213 VFEVL-GHHLLKWIIKSNYQGLPVRCVksiIRQVLQGLDYLHSKcKIIHTDIKPENILMCVD 273
Cdd:cd06648    82 VMEFLeGGALTDIVTHTRMNEEQIATV---CRAVLKALSFLHSQ-GVIHRDIKSDSILLTSD 139
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
573-655 5.81e-04

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: 42.71  E-value: 5.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 573 RVKIADLGNA--CWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSgedysrDEDHIALI 650
Cdd:cd07862   148 QIKLADFGLAriYSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSS------DVDQLGKI 221

                  ....*
gi 1370510836 651 IELLG 655
Cdd:cd07862   222 LDVIG 226
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
592-735 5.96e-04

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: 42.33  E-value: 5.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 592 DIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSGEDYSrdedhiaLIIELLGKV-----PRKYAmlGK 666
Cdd:cd06605   158 FVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKPSM-------MIFELLSYIvdeppPLLPS--GK 228
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370510836 667 YSKEfftrkgelrhitklkpwslfdvlvekygwphedaaqFTDFLIPMLEMVPEKRASAGECLRHPWLN 735
Cdd:cd06605   229 FSPD------------------------------------FQDFVSQCLQKDPTERPSYKELMEHPFIK 261
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
566-625 6.37e-04

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: 41.87  E-value: 6.37e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510836 566 PRN---ADKIRVKIADLGNACWVHKHFTEDIQTRQ-----YRSIEVLIGAGYSTPADIWSTACMAFEL 625
Cdd:cd00180   120 PENillDSDGTVKLADFGLAKDLDSDDSLLKTTGGttppyYAPPELLGGRYYGPKVDIWSLGVILYEL 187
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
595-654 6.97e-04

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: 42.43  E-value: 6.97e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 595 TRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHsgEDYSRDEDHIALIIELL 654
Cdd:cd06620   166 TSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGS--NDDDDGYNGPMGILDLL 223
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
129-273 7.02e-04

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: 42.32  E-value: 7.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKS-AQHYTETALDEIKLLkcvreSDPSDPNkdmVVQLIDDFKISGmng 207
Cdd:cd06643     7 WEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTkSEEELEDYMVEIDIL-----ASCDHPN---IVKLLDAFYYEN--- 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510836 208 iHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVD 273
Cdd:cd06643    76 -NLWILIEFCAGGAVDAVMLELERPLTEPQIRVVCKQTLEALVYLHEN-KIIHRDLKAGNILFTLD 139
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
128-270 7.34e-04

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: 42.12  E-value: 7.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQhYTETALD----EIKLLKCVresdpSDPNKDMVVQLIDDFKIs 203
Cdd:cd14072     1 NYRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQ-LNPSSLQklfrEVRIMKIL-----NHPNIVKLFEVIETEKT- 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370510836 204 gmngIHVCM-------VFEVLGHHllkwiiksnyQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd14072    74 ----LYLVMeyasggeVFDYLVAH----------GRMKEKEARAKFRQIVSAVQYCHQK-RIVHRDLKAENLLL 132
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
132-270 7.36e-04

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: 41.86  E-value: 7.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 132 IRKLGWGHFSTVWL-CWdmQGKRFVAMKVVKSAQHYTETALDEIKLLkcVRESDPSdpnkdmVVQLiddFKISGMNGiHV 210
Cdd:cd05112     9 VQEIGSGQFGLVHLgYW--LNKDKVAIKTIREGAMSEEDFIEEAEVM--MKLSHPK------LVQL---YGVCLEQA-PI 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 211 CMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCkIIHTDIKPENILM 270
Cdd:cd05112    75 CLVFEFMEHGCLSDYLRTQRGLFSAETLLGMCLDVCEGMAYLEEAS-VIHRDLAARNCLV 133
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
206-273 7.97e-04

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: 42.28  E-value: 7.97e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370510836 206 NGIHVCMVFEVLGHHLLKWIIKSNY-QGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVD 273
Cdd:cd08216    70 VDNDLYVVTPLMAYGSCRDLLKTHFpEGLPELAIAFILRDVLNALEYIHSK-GYIHRSVKASHILISGD 137
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
574-661 8.18e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 42.29  E-value: 8.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 574 VKIADLGNACwvhkhFTEDIQTRQY---------RSIEVLIGAGYSTPADIWSTACMAFELATG-DYLFEpHSGEDYSRD 643
Cdd:PHA03212  221 VCLGDFGAAC-----FPVDINANKYygwagtiatNAPELLARDPYGPAVDIWSAGIVLFEMATChDSLFE-KDGLDGDCD 294
                          90
                  ....*....|....*....
gi 1370510836 644 ED-HIALIIELLGKVPRKY 661
Cdd:PHA03212  295 SDrQIKLIIRRSGTHPNEF 313
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
128-270 8.19e-04

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: 41.89  E-value: 8.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVREsdpsdPNkdmvvqlIDDFKISGMNG 207
Cdd:cd14665     1 RYELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKIDENVQREIINHRSLRH-----PN-------IVRFKEVILTP 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370510836 208 IHVCMVFE-VLGHHLLKWIikSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd14665    69 THLAIVMEyAAGGELFERI--CNAGRFSEDEARFFFQQLISGVSYCHSM-QICHRDLKLENTLL 129
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
558-734 8.28e-04

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: 41.77  E-value: 8.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 558 DLLVNPLDPRNADKIRVKIADLGNAcwVHK------HFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYL 631
Cdd:cd14097   130 NILVKSSIIDNNDKLNIKVTDFGLS--VQKyglgedMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPP 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 632 FephsgedYSRDEDHIALIIellgkvprkyamlgkyskefftRKGELRhitklkpwslFDVLVekygWPH-EDAAQftDF 710
Cdd:cd14097   208 F-------VAKSEEKLFEEI----------------------RKGDLT----------FTQSV----WQSvSDAAK--NV 242
                         170       180
                  ....*....|....*....|....
gi 1370510836 711 LIPMLEMVPEKRASAGECLRHPWL 734
Cdd:cd14097   243 LQQLLKVDPAHRMTASELLDNPWI 266
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
573-734 9.35e-04

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: 42.04  E-value: 9.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 573 RVKIADLGNACWV-HKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGdylFEPHSGEDysrdedhialiI 651
Cdd:cd14096   177 IVKLADFGLSKQVwDSNTKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCG---FPPFYDES-----------I 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 652 ELLG-KVPRkyamlGKYskefftrkgelrhiTKLKPWslfdvlvekygWpHEDAAQFTDFLIPMLEMVPEKRASAGECLR 730
Cdd:cd14096   243 ETLTeKISR-----GDY--------------TFLSPW-----------W-DEISKSAKDLISHLLTVDPAKRYDIDEFLA 291

                  ....
gi 1370510836 731 HPWL 734
Cdd:cd14096   292 HPWI 295
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
129-270 9.62e-04

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: 41.55  E-value: 9.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETA----LDEIKLLKCVresdpSDPNkdmVVQLIDDFkisg 204
Cdd:cd08228     4 FQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMMDAKArqdcVKEIDLLKQL-----NHPN---VIKYLDSF---- 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370510836 205 MNGIHVCMVFEVLGHHLLKWII---KSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd08228    72 IEDNELNIVLELADAGDLSQMIkyfKKQKRLIPERTVWKYFVQLCSAVEHMHSR-RVMHRDIKPANVFI 139
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
209-270 9.66e-04

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: 41.62  E-value: 9.66e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510836 209 HVCMVFE-VLG---HHLLKwiiksNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd05609    74 HLCMVMEyVEGgdcATLLK-----NIGPLPVDMARMYFAETVLALEYLHSY-GIVHRDLKPDNLLI 133
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
559-639 1.05e-03

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: 41.53  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 559 LLVNPLDPR-NADKIRVKIADLGNACWVHKHFTEDI--QTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPH 635
Cdd:cd14202   133 LLSYSGGRKsNPNNIRIKIADFGFARYLQNNMMAATlcGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQAS 212

                  ....
gi 1370510836 636 SGED 639
Cdd:cd14202   213 SPQD 216
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
125-274 1.08e-03

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: 41.76  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 125 FNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETAL--DEIKllkcvRESDPSDPNKD-MVVQLIDDFK 201
Cdd:cd14094     1 FEDVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSPGLstEDLK-----REASICHMLKHpHIVELLETYS 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510836 202 ISGMngihVCMVFEVL-GHHLLKWIIKSNYQGLPVR--CVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVDD 274
Cdd:cd14094    76 SDGM----LYMVFEFMdGADLCFEIVKRADAGFVYSeaVASHYMRQILEALRYCHDN-NIIHRDVKPHCVLLASKE 146
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
135-270 1.14e-03

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: 41.65  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKrFVAMKVV--------KSAQHYtETALDEIKLLKCVResdpsdpNKDMVVQL---IDDfkis 203
Cdd:cd06631     9 LGKGAYGTVYCGLTSTGQ-LIAVKQVeldtsdkeKAEKEY-EKLQEEVDLLKTLK-------HVNIVGYLgtcLED---- 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510836 204 gmNGIHVCMVFeVLGHHLLKwiIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCkIIHTDIKPENILM 270
Cdd:cd06631    76 --NVVSIFMEF-VPGGSIAS--ILARFGALEEPVFCRYTKQILEGVAYLHNNN-VIHRDIKGNNIML 136
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
574-628 1.18e-03

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: 41.27  E-value: 1.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510836 574 VKIADLGNA---CWVHKHFTediQTRQYRSI---------EVLIGAGYSTPADIWSTACMAFELATG 628
Cdd:cd06631   142 IKLIDFGCAkrlCINLSSGS---QSQLLKSMrgtpywmapEVINETGHGRKSDIWSIGCTVFEMATG 205
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
129-270 1.27e-03

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: 41.60  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVV--KSAQHYTETALDEIKLLkcvreSDPSDPnkdmvvqLIDDFKISGMN 206
Cdd:cd06641     6 FTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIdlEEAEDEIEDIQQEITVL-----SQCDSP-------YVTKYYGSYLK 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370510836 207 GIHVCMVFEVLGHHLLKWIIKSNyqGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd06641    74 DTKLWIIMEYLGGGSALDLLEPG--PLDETQIATILREILKGLDYLHSE-KKIHRDIKAANVLL 134
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
135-269 1.35e-03

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: 41.55  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKRFVAMKVV-KSAQHYTETALDEIKLL-KCVRESDpsdpnkdmVVQLIDDFKISGmngiHVCM 212
Cdd:cd14173    10 LGEGAYARVQTCINLITNKEYAVKIIeKRPGHSRSRVFREVEMLyQCQGHRN--------VLELIEFFEEED----KFYL 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510836 213 VFEVL-GHHLLKWIIKSnyQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:cd14173    78 VFEKMrGGSILSHIHRR--RHFNELEASVVVQDIASALDFLHNK-GIAHRDLKPENIL 132
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
129-269 1.37e-03

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: 41.35  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHyTETALDEIKLLKCVresdpSDPNkdmVVQLIDDFKisgmNGI 208
Cdd:cd14085     5 FEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKTVD-KKIVRTEIGVLLRL-----SHPN---IIKLKEIFE----TPT 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370510836 209 HVCMVFE-VLGHHLLKWIIKSNYQGlpVRCVKSIIRQVLQGLDYLHsKCKIIHTDIKPENIL 269
Cdd:cd14085    72 EISLVLElVTGGELFDRIVEKGYYS--ERDAADAVKQILEAVAYLH-ENGIVHRDLKPENLL 130
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
132-270 1.49e-03

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: 41.07  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 132 IRKLGWGHFSTVWLC-WDMQGKR---FVAMKVVK--SAQHYTETALDEIKLLKCVRESDpsdpnkdmVVQLIDDFKISGM 205
Cdd:cd05079     9 IRDLGEGHFGKVELCrYDPEGDNtgeQVAVKSLKpeSGGNHIADLKKEIEILRNLYHEN--------IVKYKGICTEDGG 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 206 NGIHVCMVFEVLGHhlLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd05079    81 NGIKLIMEFLPSGS--LKEYLPRNKNKINLKQQLKYAVQICKGMDYLGSR-QYVHRDLAARNVLV 142
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
245-269 1.58e-03

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: 41.27  E-value: 1.58e-03
                          10        20
                  ....*....|....*....|....*
gi 1370510836 245 VLQGLDYLHSKCKIIHTDIKPENIL 269
Cdd:cd06615   108 VLRGLTYLREKHKIMHRDVKPSNIL 132
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
133-270 1.80e-03

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: 40.67  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 133 RKLGWGHFSTVWL-CWDmqGKRFVAMKVVKSAQHYTETALDEIKLLKCVREsdpsdpnkDMVVQLiddFKISGMNGIHVc 211
Cdd:cd14203     1 VKLGQGCFGEVWMgTWN--GTTKVAIKTLKPGTMSPEAFLEEAQIMKKLRH--------DKLVQL---YAVVSEEPIYI- 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 212 mVFEVLGH-HLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHsKCKIIHTDIKPENILM 270
Cdd:cd14203    67 -VTEFMSKgSLLDFLKDGEGKYLKLPQLVDMAAQIASGMAYIE-RMNYIHRDLRAANILV 124
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
189-274 1.91e-03

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 41.13  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 189 NKDMVVQLIDDFKISGMNgihvCMVFEVLGHHLLKWIikSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENI 268
Cdd:PHA03212  141 NHPSIIQLKGTFTYNKFT----CLILPRYKTDLYCYL--AAKRNIAICDILAIERSVLRAIQYLHEN-RIIHRDIKAENI 213
                          90
                  ....*....|..
gi 1370510836 269 LM------CVDD 274
Cdd:PHA03212  214 FInhpgdvCLGD 225
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
573-628 1.94e-03

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: 40.85  E-value: 1.94e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370510836 573 RVKIADLGNAcwvhKHFTEDIQTRQYR------SIEVLI--GAGYSTPADIWSTACMAFELATG 628
Cdd:cd06632   140 VVKLADFGMA----KHVEAFSFAKSFKgspywmAPEVIMqkNSGYGLAVDIWSLGCTVLEMATG 199
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
166-307 2.13e-03

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: 40.42  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 166 YTETALDEiklLKCVREsdpsdPNkdmVVQLIDdFKISGM---NGIHVCMVFEvlghHLLKWII---KSNYQGLPVRCVK 239
Cdd:cd14012    44 LLEKELES---LKKLRH-----PN---LVSYLA-FSIERRgrsDGWKVYLLTE----YAPGGSLselLDSVGSVPLDTAR 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 240 SIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVDDA----------YVRRMAAE-----ATEWQKAGAPPPSGSAVSTAP 304
Cdd:cd14012   108 RWTLQLLEALEYLHRN-GVVHKSLHAGNVLLDRDAGtgivkltdysLGKTLLDMcsrgsLDEFKQTYWLPPELAQGSKSP 186

                  ...
gi 1370510836 305 QQK 307
Cdd:cd14012   187 TRK 189
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
574-734 2.26e-03

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: 40.69  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 574 VKIADLGNACWVH--KHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGdylFEPHSGEDYSRDEDHIAlii 651
Cdd:cd14197   153 IKIVDFGLSRILKnsEELREIMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTG---ISPFLGDDKQETFLNIS--- 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 652 ellgkvprkyAMLGKYSKEfftrkgELRHITklkpwslfdvlvekygwpheDAAqfTDFLIPMLEMVPEKRASAGECLRH 731
Cdd:cd14197   227 ----------QMNVSYSEE------EFEHLS--------------------ESA--IDFIKTLLIKKPENRATAEDCLKH 268

                  ...
gi 1370510836 732 PWL 734
Cdd:cd14197   269 PWL 271
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
135-269 2.28e-03

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: 38.96  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKRFVAMKVVKSAqhYTETALDEIKLLKCVRESDPSDPNkdmVVQLIDDFKIsgmNGIHVCMVF 214
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIGVAVKIGDDV--NNEEGEDLESEMDILRRLKGLELN---IPKVLVTEDV---DGPNILLME 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 215 EVLGHHLLKWIIKSNyqgLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:cd13968    73 LVKGGTLIAYTQEEE---LDEKDVESIMYQLAECMRLLHSF-HLIHRDLNNDNIL 123
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
128-278 2.33e-03

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: 40.70  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVV--------------------KSAQH------------YTETA----L 171
Cdd:cd14200     1 QYKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLskkkllkqygfprrppprgsKAAQGeqakplaplervYQEIAilkkL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 172 DEIKLLKCVRE-SDPSDPNKDMVVQLIDDFKisgmngihvcmVFEVLGHHLLkwiikSNYQGlpvrcvKSIIRQVLQGLD 250
Cdd:cd14200    81 DHVNIVKLIEVlDDPAEDNLYMVFDLLRKGP-----------VMEVPSDKPF-----SEDQA------RLYFRDIVLGIE 138
                         170       180
                  ....*....|....*....|....*...
gi 1370510836 251 YLHSKcKIIHTDIKPENILMCvDDAYVR 278
Cdd:cd14200   139 YLHYQ-KIVHRDIKPSNLLLG-DDGHVK 164
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
208-270 2.36e-03

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: 40.82  E-value: 2.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510836 208 IHVCMvfEVLGHHLLKWIIKSnYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILM 270
Cdd:cd06618    89 VFICM--ELMSTCLDKLLKRI-QGPIPEDILGKMTVSIVKALHYLKEKHGVIHRDVKPSNILL 148
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
135-269 2.50e-03

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: 40.80  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKRFVAMKVV-KSAQHYTETALD-EIKLLKCVRESDpsdpnkdmVVQLIDDFKISGmngiHVCM 212
Cdd:cd14168    18 LGTGAFSEVVLAEERATGKLFAVKCIpKKALKGKESSIEnEIAVLRKIKHEN--------IVALEDIYESPN----HLYL 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510836 213 VFEVL-GHHLLKWIIKSNYqgLPVRCVKSIIRQVLQGLDYLHsKCKIIHTDIKPENIL 269
Cdd:cd14168    86 VMQLVsGGELFDRIVEKGF--YTEKDASTLIRQVLDAVYYLH-RMGIVHRDLKPENLL 140
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
133-269 2.66e-03

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: 40.35  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 133 RKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQhytetaldeikllKCVRESD-----PSDPNkdmVVQLIDDFKISGMNG 207
Cdd:cd14089     7 QVLGLGINGKVLECFHKKTGEKFALKVLRDNP-------------KARREVElhwraSGCPH---IVRIIDVYENTYQGR 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510836 208 IHVCMVFEVL-GHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:cd14089    71 KCLLVVMECMeGGELFSRIQERADSAFTEREAAEIMRQIGSAVAHLHSM-NIAHRDLKPENLL 132
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
135-270 2.67e-03

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: 40.18  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 135 LGWGHFSTVWLCWDMQGKRFVAMKVVKSAQH--YTETALDEIKLLKCVREsdpsdpnkDMVVQL----IDDFKISgmngi 208
Cdd:cd14027     1 LDSGGFGKVSLCFHRTQGLVVLKTVYTGPNCieHNEALLEEGKMMNRLRH--------SRVVKLlgviLEEGKYS----- 67
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510836 209 hvcMVFEVLGH-HLLKWIIKSNyqgLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd14027    68 ---LVMEYMEKgNLMHVLKKVS---VPLSVKGRIILEIIEGMAYLHGK-GVIHKDLKPENILV 123
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
595-628 2.73e-03

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: 40.28  E-value: 2.73e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1370510836 595 TRQYRSIEVLIGAGYSTPADIWSTACMAFELATG 628
Cdd:cd05579   171 TPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVG 204
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
128-270 2.74e-03

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: 40.35  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWlcwdmQGKR-----FVAMKVVKSAQhytetaldEIKLLKCVRES-DPSDPNkdmVVQLIDDFK 201
Cdd:cd14010     1 NYVLYDEIGRGKHSVVY-----KGRRkgtieFVAIKCVDKSK--------RPEVLNEVRLThELKHPN---VLKFYEWYE 64
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370510836 202 ISGmngiHVCMVFEVLGHHLLKWIIKSNyQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd14010    65 TSN----HLWLVVEYCTGGDLETLLRQD-GNLPESSVRKFGRDLVRGLHYIHSK-GIIYCDLKPSNILL 127
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
133-278 2.78e-03

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: 40.42  E-value: 2.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 133 RKLGWGHFSTVWLCwdmQ----GKRFVAMKVVKS---AQHYTETALDEIKLLKCVresdpsdpNKDMVVQLIDDFKISGM 205
Cdd:cd05605     6 RVLGKGGFGEVCAC---QvratGKMYACKKLEKKrikKRKGEAMALNEKQILEKV--------NSRFVVSLAYAYETKDA 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 206 ngihVCMVFEVLGHHLLKWIIKS-NYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMcvDDA-YVR 278
Cdd:cd05605    75 ----LCLVLTIMNGGDLKFHIYNmGNPGFEEERAVFYAAEITCGLEHLHSE-RIVYRDLKPENILL--DDHgHVR 142
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
129-284 2.86e-03

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 41.26  E-value: 2.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836  129 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKS---AQHYTETALDEIKLLKCVRESDpsdpnkdmVVQLIDDFKISGM 205
Cdd:PTZ00266    15 YEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYrglKEREKSQLVIEVNVMRELKHKN--------IVRYIDRFLNKAN 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836  206 NGIHVCMVFEVLGHhlLKWIIKSNYQ---GLPVRCVKSIIRQVLQGLDYLHS------KCKIIHTDIKPENILMCVDDAY 276
Cdd:PTZ00266    87 QKLYILMEFCDAGD--LSRNIQKCYKmfgKIEEHAIVDITRQLLHALAYCHNlkdgpnGERVLHRDLKPQNIFLSTGIRH 164

                   ....*...
gi 1370510836  277 VRRMAAEA 284
Cdd:PTZ00266   165 IGKITAQA 172
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
244-278 2.88e-03

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: 40.25  E-value: 2.88e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1370510836 244 QVLQGLDYLHSKcKIIHTDIKPENILMcVDDAYVR 278
Cdd:cd05608   113 QIISGLEHLHQR-RIIYRDLKPENVLL-DDDGNVR 145
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
128-270 3.17e-03

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; 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. Genetic variations in TTBK1 are linked to Alzheimer's disease (AD). Hyperphosphorylated tau is a major component of paired helical filaments that accumulate in the brain of AD patients. Studies in transgenic mice show that TTBK1 is involved in the phosphorylation-dependent pathogenic aggregation of tau. The TTBK1 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: 271032 [Multi-domain]  Cd Length: 262  Bit Score: 40.01  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVvKSAQHYTETALDEIKLLKCVResdpsdpNKDMVVQLIDdfkiSGMNG 207
Cdd:cd14130     1 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKV-ESAQQPKQVLKMEVAVLKKLQ-------GKDHVCRFIG----CGRNE 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370510836 208 IHVCMVFEVLGHHLLKwIIKSNYQG-LPVRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILM 270
Cdd:cd14130    69 KFNYVVMQLQGRNLAD-LRRSQPRGtFTLSTTLRLGKQILESIEAIHS-VGFLHRDIKPSNFAM 130
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
570-673 3.24e-03

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: 40.12  E-value: 3.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 570 DKIRVKIADLGNACWVHKHF--TEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHS------GEDYS 641
Cdd:cd13989   140 GRVIYKLIDLGYAKELDQGSlcTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPFLPNWqpvqwhGKVKQ 219
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1370510836 642 RDEDHIALIIELLGKVprkyamlgKYSKEFFT 673
Cdd:cd13989   220 KKPEHICAYEDLTGEV--------KFSSELPS 243
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
574-639 3.32e-03

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: 40.11  E-value: 3.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510836 574 VKIADLGNACWVHKHFTE-DIQTRQYRSIEVLI-GAGYSTPADIWSTACMAFELATGDYLFEPHSGED 639
Cdd:cd05606   137 VRISDLGLACDFSKKKPHaSVGTHGYMAPEVLQkGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKD 204
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
245-270 3.46e-03

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: 40.04  E-value: 3.46e-03
                          10        20
                  ....*....|....*....|....*.
gi 1370510836 245 VLQGLDYLHSKCKIIHTDIKPENILM 270
Cdd:cd06616   118 TVKALNYLKEELKIIHRDVKPSNILL 143
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
244-273 3.60e-03

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: 39.80  E-value: 3.60e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1370510836 244 QVLQGLDYLHSKcKIIHTDIKPENILMCVD 273
Cdd:cd13991   106 QALEGLEYLHSR-KILHGDVKADNVLLSSD 134
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
128-270 3.72e-03

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: 39.94  E-value: 3.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 128 RYHVIRKLGWGHFSTVWLCWDMQGkRFVAMKVVKSaqhytETALDEIKLLKCVRESD-PSDPNKDMVVQLIDDFKISgmN 206
Cdd:cd14161     4 RYEFLETLGKGTYGRVKKARDSSG-RLVAIKSIRK-----DRIKDEQDLLHIRREIEiMSSLNHPHIISVYEVFENS--S 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370510836 207 GIHVCMVFEVLGHhLLKWIikSNYQGLPVRCVKSIIRQVLQGLDYLHsKCKIIHTDIKPENILM 270
Cdd:cd14161    76 KIVIVMEYASRGD-LYDYI--SERQRLSELEARHFFRQIVSAVHYCH-ANGIVHRDLKLENILL 135
K-ycf53 COG5752
Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 ...
242-269 4.07e-03

Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 porphyrin-binding domain [Signal transduction mechanisms];


Pssm-ID: 444462 [Multi-domain]  Cd Length: 466  Bit Score: 40.37  E-value: 4.07e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1370510836 242 IRQVLQG----LDYLHSKcKIIHTDIKPENIL 269
Cdd:COG5752   140 IWQLLKDllpvLQFIHSR-NVIHRDIKPANII 170
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
129-274 4.10e-03

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: 39.79  E-value: 4.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 129 YHVIRKLGWGHFSTVW-LCWDMQGKRFVAMKVV--------KSAQHYTETALDEIKLLKCVRESdPSDPNkdmVVQLIDD 199
Cdd:cd08528     2 YAVLELLGSGAFGCVYkVRKKSNGQTLLALKEInmtnpafgRTEQERDKSVGDIISEVNIIKEQ-LRHPN---IVRYYKT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 200 FkisgMNGIHVCMVFEV-----LGHHLLKwiIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDD 274
Cdd:cd08528    78 F----LENDRLYIVMELiegapLGEHFSS--LKEKNEHFTEDRIWNIFVQMVLALRYLHKEKQIVHRDLKPNNIMLGEDD 151
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
155-270 4.30e-03

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: 39.73  E-value: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 155 VAMKVVKSAQHyTETALDEIKLLkcvreSDPSDPNkdmVVQLIDdfkiSGMNGIHVCMVFEVLG----HHLLKWiiksnY 230
Cdd:cd14058    19 VAVKIIESESE-KKAFEVEVRQL-----SRVDHPN---IIKLYG----ACSNQKPVCLVMEYAEggslYNVLHG-----K 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1370510836 231 QGLPVRCVKSIIRQVLQ---GLDYLHSKC--KIIHTDIKPENILM 270
Cdd:cd14058    81 EPKPIYTAAHAMSWALQcakGVAYLHSMKpkALIHRDLKPPNLLL 125
STKc_VRK cd14015
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs ...
212-269 4.88e-03

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins (VRK1, VRK2, and VRK3) while invertebrates, specifically fruit flies and nematodes, seem to carry only a single ortholog. Mutations of VRK in Drosophila and Caenorhabditis elegans showed varying phenotypes ranging from embryonic lethality to mitotic and meiotic defects resulting in sterility. In vertebrates, VRK1 is implicated in cell cycle progression and proliferation, nuclear envelope assembly, and chromatin condensation. VRK2 is involved in modulating JNK signaling. VRK3 is an inactive pseudokinase that inhibits ERK signaling. The VRK 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: 270917 [Multi-domain]  Cd Length: 300  Bit Score: 39.57  E-value: 4.88e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510836 212 MVFEVLGHHLLKwIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENIL 269
Cdd:cd14015   104 LVMPRFGRDLQK-IFEKNGKRFPEKTVLQLALRILDVLEYIHEN-GYVHADIKASNLL 159
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
132-270 5.08e-03

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: 39.65  E-value: 5.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 132 IRKLGWGHFSTVWLCWDMQGKRFVAMKVV--KSAQHYTETALDEIKLLKcvrESDPSdpnkdmvvqLIDDFKISGMNGIH 209
Cdd:cd06640     9 LERIGKGSFGEVFKGIDNRTQQVVAIKIIdlEEAEDEIEDIQQEITVLS---QCDSP---------YVTKYYGSYLKGTK 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510836 210 VCMVFEVLGH----HLLKWIIKSNYQglpvrcVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:cd06640    77 LWIIMEYLGGgsalDLLRAGPFDEFQ------IATMLKEILKGLDYLHSE-KKIHRDIKAANVLL 134
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
244-268 5.52e-03

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: 39.61  E-value: 5.52e-03
                          10        20
                  ....*....|....*....|....*
gi 1370510836 244 QVLQGLDYLHSKCKIIHTDIKPENI 268
Cdd:cd14011   122 QISEALSFLHNDVKLVHGNICPESV 146
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
573-650 5.69e-03

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: 39.33  E-value: 5.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 573 RVKIADLGNACWVHKHFT-------EDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDylfEPHSGEDYSrdeD 645
Cdd:cd06630   142 RLRIADFGAAARLASKGTgagefqgQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAK---PPWNAEKIS---N 215

                  ....*
gi 1370510836 646 HIALI 650
Cdd:cd06630   216 HLALI 220
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
158-270 5.97e-03

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 39.88  E-value: 5.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 158 KVVKSAQHYTETAlDEIKLLKcvRESDPSdpnkdmVVQLIDDFKISGMNgihvCMVFEVLGHHLLKWI-IKSNYQGLPVr 236
Cdd:PHA03211  196 RVVVKAGWYASSV-HEARLLR--RLSHPA------VLALLDVRVVGGLT----CLVLPKYRSDLYTYLgARLRPLGLAQ- 261
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1370510836 237 cVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILM 270
Cdd:PHA03211  262 -VTAVARQLLSAIDYIHGE-GIIHRDIKTENVLV 293
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
228-274 6.22e-03

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: 39.40  E-value: 6.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1370510836 228 SNYQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVDD 274
Cdd:cd13988    88 SNAYGLPESEFLIVLRDVVAGMNHLREN-GIVHRDIKPGNIMRVIGE 133
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
595-734 6.27e-03

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: 39.45  E-value: 6.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 595 TRQYRSIEVLIGAGYSTPADIWSTACMAFELATGdYLfePHSGEDySRDEDHIaliiellgkvprkyaMLGKYSkefftr 674
Cdd:cd14094   175 TPHFMAPEVVKREPYGKPVDVWGCGVILFILLSG-CL--PFYGTK-ERLFEGI---------------IKGKYK------ 229
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 675 kgelrhitklkpwslfdvlVEKYGWPHeDAAQFTDFLIPMLEMVPEKRASAGECLRHPWL 734
Cdd:cd14094   230 -------------------MNPRQWSH-ISESAKDLVRRMLMLDPAERITVYEALNHPWI 269
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
558-644 6.47e-03

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: 39.12  E-value: 6.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 558 DLLVNPLDPRNA---DKIRVKIADLGNACWVH--KHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLF 632
Cdd:cd05607   124 KIVYRDMKPENVlldDNGNCRLSDLGLAVEVKegKPITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPF 203
                          90
                  ....*....|..
gi 1370510836 633 EPHSgEDYSRDE 644
Cdd:cd05607   204 RDHK-EKVSKEE 214
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
568-639 6.56e-03

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: 39.22  E-value: 6.56e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370510836 568 NADKIRVKIADLGNACWVHKHFTEDI--QTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSGED 639
Cdd:cd14201   147 SVSGIRIKIADFGFARYLQSNMMAATlcGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQD 220
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
574-633 6.88e-03

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: 39.07  E-value: 6.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370510836 574 VKIADLGNACWV----HKHFTEdIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFE 633
Cdd:cd14186   141 IKIADFGLATQLkmphEKHFTM-CGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFD 203
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
389-431 7.65e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 39.59  E-value: 7.65e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1370510836  389 DNGEAEDQEEKEDAEKENIEKDEDDVDQELANIDPTWIESPKT 431
Cdd:TIGR00927  859 DGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLEWPET 901
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
134-270 8.06e-03

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: 38.93  E-value: 8.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 134 KLGWGHFSTVWLCWDMQGKRFVA------MKVVKSAQHYTEtalDEIKLLKCVREsdpsdPNkdmVVQLIDDFKISGMNG 207
Cdd:cd14031    17 ELGRGAFKTVYKGLDTETWVEVAwcelqdRKLTKAEQQRFK---EEAEMLKGLQH-----PN---IVRFYDSWESVLKGK 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370510836 208 IHVCMVFEVLGHHLLKWIIKsNYQGLPVRCVKSIIRQVLQGLDYLHSKC-KIIHTDIKPENILM 270
Cdd:cd14031    86 KCIVLVTELMTSGTLKTYLK-RFKVMKPKVLRSWCRQILKGLQFLHTRTpPIIHRDLKCDNIFI 148
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
595-732 8.40e-03

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: 39.06  E-value: 8.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 595 TRQYRSIEVLIGAGYSTPA-DIWSTACMAFELATGDYLFEPhsGEDysrDEDHIALIIELLGKVPRkYAMLGKYSKEFFT 673
Cdd:cd14132   175 SRYYKGPELLVDYQYYDYSlDMWSLGCMLASMIFRKEPFFH--GHD---NYDQLVKIAKVLGTDDL-YAYLDKYGIELPP 248
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370510836 674 RKGELRHITKLKPWSLFdVLVEKYGWPHEDAaqfTDFLIPMLEMVPEKRASAGECLRHP 732
Cdd:cd14132   249 RLNDILGRHSKKPWERF-VNSENQHLVTPEA---LDLLDKLLRYDHQERITAKEAMQHP 303
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
688-734 8.78e-03

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: 38.72  E-value: 8.78e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370510836 688 SLFDVLVEKYGWPHEDAAQFT----DFLIPMLEMVPEKRASAGECLRHPWL 734
Cdd:cd14107   207 TLLNVAEGVVSWDTPEITHLSedakDFIKRVLQPDPEKRPSASECLSHEWF 257
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
236-273 9.06e-03

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: 38.65  E-value: 9.06e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1370510836 236 RCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVD 273
Cdd:cd14109    99 RQVAVFVRQLLLALKHMHDL-GIAHLDLRPEDILLQDD 135
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
564-644 9.08e-03

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: 38.66  E-value: 9.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 564 LDPRNA---DKIRVKIADLGNACWV--HKHFTEDIQTRQYRSIEVLI-GAGYSTPADIWSTACMAFELATGDYLFEPHsG 637
Cdd:cd05577   121 LKPENIlldDHGHVRISDLGLAVEFkgGKKIKGRVGTHGYMAPEVLQkEVAYDFSVDWFALGCMLYEMIAGRSPFRQR-K 199

                  ....*..
gi 1370510836 638 EDYSRDE 644
Cdd:cd05577   200 EKVDKEE 206
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
234-276 9.14e-03

putative serine/threonine kinase; Provisional


Pssm-ID: 165211 [Multi-domain]  Cd Length: 294  Bit Score: 38.78  E-value: 9.14e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1370510836 234 PVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILmcVDDAY 276
Cdd:PHA02882  124 NKKLIKNIMKDMLTTLEYIHEH-GISHGDIKPENIM--VDGNN 163
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
238-305 9.34e-03

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: 38.67  E-value: 9.34e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 238 VKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVDDAYVRRMA--AEATEWQKAGAPPPSGSAVSTAPQ 305
Cdd:cd14112   101 VATTVRQILDALHYLHFK-GIAHLDVQPDNIMFQSVRSWQVKLVdfGRAQKVSKLGKVPVDGDTDWASPE 169
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
125-274 9.39e-03

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: 38.74  E-value: 9.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 125 FNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVV----------KSAQHYTETALDEIKLLKCVresdPSDPNkdmVV 194
Cdd:cd14182     1 FYEKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIditgggsfspEEVQELREATLKEIDILRKV----SGHPN---II 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510836 195 QLIDDFKISGMngihVCMVFEVLGH-HLLKWIIKSnyQGLPVRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMcvD 273
Cdd:cd14182    74 QLKDTYETNTF----FFLVFDLMKKgELFDYLTEK--VTLSEKETRKIMRALLEVICALHKL-NIVHRDLKPENILL--D 144

                  .
gi 1370510836 274 D 274
Cdd:cd14182   145 D 145
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
238-284 9.49e-03

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: 38.76  E-value: 9.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1370510836 238 VKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCvddayvRRMAAEA 284
Cdd:cd14139   106 LKDILLQVSMGLKYIHNS-GLVHLDIKPSNIFIC------HKMQSSS 145
 
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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