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Conserved domains on  [gi|1331383559|ref|NP_001346852|]
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cyclin-G-associated kinase isoform 5 [Mus musculus]

Protein Classification

PTP_GAK and PTEN_C2 domain-containing protein( domain architecture ID 13135483)

protein containing domains Protein Kinases, catalytic domain, PTP_GAK, PTEN_C2, and PHA03247

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_GAK cd14564
protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated ...
 237-399 1.29e-117

protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated kinase (GAK), also called auxilin-2, contains an N-terminal protein kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of a protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN (a phosphoinositide 3-phosphatase), and a C-terminal region with clathrin-binding and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor.


:

Pssm-ID: 350412 [Multi-domain]  Cd Length: 163  Bit Score: 354.59  E-value: 1.29e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559 237 VANYAKGDLDISYITSRIAVMSFPAEGVESAIKNNIEDVRMFLDAKHPGHYAVYNLSPRIYRASKFHNRVTECGWAVRRA 316
Cdd:cd14564     1 VANYAKGDLDISYITSRIAVMSFPAEGVESAIKNNIEDVRLFLDSRHPGHYAVYNLSQRTYRPSRFHNRVSECGWPARRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559 317 PHLHSLYTLCRSMHAWLREDHRNVCVVHCMDGRAASAVAVCAFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEYV 396
Cdd:cd14564    81 PNLQNLYSICKNMHLWLKQDQKNICIVHCLDGRAASAVVVCSFLCFCRLFTTAEAAVYMFSMKRCPPGIWPSHKRYIEYM 160


                  ...
gi 1331383559 397 CDM 399
Cdd:cd14564   161 CDM 163
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
 1-159 9.67e-113

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 cd14036:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 282  Bit Score: 346.80  E-value: 9.67e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQKRAMVEEEITRNTTPMYRTPEIVDLYSNFPIG 80
Cdd:cd14036   124 MHKQSPPIIHRDLKIENLLIGNQGQIKLCDFGSATTEAHYPDYSWSAQKRSLVEDEITRNTTPMYRTPEMIDLYSNYPIG 203

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559  81 EKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQLQEIAAAR 159
Cdd:cd14036   204 EKQDIWALGCILYLLCFRKHPFEDGAKLRIINAKYTIPPNDTQYTVFHDLIRSTLKVNPEERLSITEIVEQLQELAAAR 282
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 407-545 2.27e-35

C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key form, of the PTEN protein, phosphatidyl-inositol triphosphate phosphatase, and it is the C-terminus. This domain may well include a CBR3 loop which means it plays a central role in membrane binding. This domain associates across an extensive interface with the N-terminal phosphatase domain DSPc (pfam00782) suggesting that the C2 domain productively positions the catalytic part of the protein onto the membrane.


:

Pssm-ID: 463081  Cd Length: 133  Bit Score: 130.86  E-value: 2.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559 407 PHSKPMLVKSVVMTPVPLFsKQRNGCRPFCEVYVGEERVTTTSQEYDRMKEFKIEDGKAVIPLGVTVQGDVLIIIYHARA 486
Cdd:pfam10409   1 PPPKPLTLHSIILHGIPNF-KSGGGCRPYIRIYQNKKKVFSTSGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEFYHKGS 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331383559 487 TLGGRlqakmasMKMFQIQFHTGFVPRNatTVKFAKYDLDACDIQ---EKYPDLFQVNLEVE 545
Cdd:pfam10409  80 DLLSE-------EKMFRFWFNTSFIEDN--TLTLPKNELDKADKDkkdKRFPKDFKVELLFS 132
 
Name Accession Description Interval E-value
PTP_GAK cd14564
protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated ...
 237-399 1.29e-117

protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated kinase (GAK), also called auxilin-2, contains an N-terminal protein kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of a protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN (a phosphoinositide 3-phosphatase), and a C-terminal region with clathrin-binding and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor.


Pssm-ID: 350412 [Multi-domain]  Cd Length: 163  Bit Score: 354.59  E-value: 1.29e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559 237 VANYAKGDLDISYITSRIAVMSFPAEGVESAIKNNIEDVRMFLDAKHPGHYAVYNLSPRIYRASKFHNRVTECGWAVRRA 316
Cdd:cd14564     1 VANYAKGDLDISYITSRIAVMSFPAEGVESAIKNNIEDVRLFLDSRHPGHYAVYNLSQRTYRPSRFHNRVSECGWPARRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559 317 PHLHSLYTLCRSMHAWLREDHRNVCVVHCMDGRAASAVAVCAFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEYV 396
Cdd:cd14564    81 PNLQNLYSICKNMHLWLKQDQKNICIVHCLDGRAASAVVVCSFLCFCRLFTTAEAAVYMFSMKRCPPGIWPSHKRYIEYM 160


                  ...
gi 1331383559 397 CDM 399
Cdd:cd14564   161 CDM 163
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
 1-159 9.67e-113

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


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 346.80  E-value: 9.67e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQKRAMVEEEITRNTTPMYRTPEIVDLYSNFPIG 80
Cdd:cd14036   124 MHKQSPPIIHRDLKIENLLIGNQGQIKLCDFGSATTEAHYPDYSWSAQKRSLVEDEITRNTTPMYRTPEMIDLYSNYPIG 203

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559  81 EKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQLQEIAAAR 159
Cdd:cd14036   204 EKQDIWALGCILYLLCFRKHPFEDGAKLRIINAKYTIPPNDTQYTVFHDLIRSTLKVNPEERLSITEIVEQLQELAAAR 282
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 407-545 2.27e-35

C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key form, of the PTEN protein, phosphatidyl-inositol triphosphate phosphatase, and it is the C-terminus. This domain may well include a CBR3 loop which means it plays a central role in membrane binding. This domain associates across an extensive interface with the N-terminal phosphatase domain DSPc (pfam00782) suggesting that the C2 domain productively positions the catalytic part of the protein onto the membrane.


Pssm-ID: 463081  Cd Length: 133  Bit Score: 130.86  E-value: 2.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559 407 PHSKPMLVKSVVMTPVPLFsKQRNGCRPFCEVYVGEERVTTTSQEYDRMKEFKIEDGKAVIPLGVTVQGDVLIIIYHARA 486
Cdd:pfam10409   1 PPPKPLTLHSIILHGIPNF-KSGGGCRPYIRIYQNKKKVFSTSGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEFYHKGS 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331383559 487 TLGGRlqakmasMKMFQIQFHTGFVPRNatTVKFAKYDLDACDIQ---EKYPDLFQVNLEVE 545
Cdd:pfam10409  80 DLLSE-------EKMFRFWFNTSFIEDN--TLTLPKNELDKADKDkkdKRFPKDFKVELLFS 132
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
 1-150 1.62e-32

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 126.88  E-value: 1.62e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559    1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSwsaqkramveeeiTRNTTPMYRTPEIVdlySNFPIG 80
Cdd:smart00220 113 LHSKG--IVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLT-------------TFVGTPEYMAPEVL---LGKGYG 174

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559   81 EKQDIWALGCILYLLCFRQHPFEDGAKL-----RIVNGKYSIPVNDTRYTV-FHDLIRAMLKVNPEERLSIAEVVR 150
Cdd:smart00220 175 KAVDIWSLGVILYELLTGKPPFPGDDQLlelfkKIGKPKPPFPPPEWDISPeAKDLIRKLLVKDPEKRLTAEEALQ 250
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
2-172 2.11e-18

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 89.30  E-value: 2.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQkpPIIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqkRAMVEEEITRNT----TPMYRTPEivdLYSNF 77
Cdd:COG0515   124 HAA--GIVHRDIKPANILLTPDGRVKLIDFGIA---------------RALGGATLTQTGtvvgTPGYMAPE---QARGE 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  78 PIGEKQDIWALGCILYLLCFRQHPFE---DGAKLRIVNGKYSIPVNDTRYTV---FHDLIRAMLKVNPEERL-SIAEVVR 150
Cdd:COG0515   184 PVDPRSDVYSLGVTLYELLTGRPPFDgdsPAELLRAHLREPPPPPSELRPDLppaLDAIVLRALAKDPEERYqSAAELAA 263

                         170       180
                  ....*....|....*....|..
gi 1331383559 151 QLQEIAAARNVNPKAPITELLE 172
Cdd:COG0515   264 ALRAVLRSLAAAAAAAAAAAAA 285
Pkinase pfam00069
Protein kinase domain;
62-150 2.18e-13

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 70.35  E-value: 2.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  62 TPMYRTPEIVdlySNFPIGEKQDIWALGCILYLLCFRQHPF----EDGAKLRIVNGKYSIPVNDTRYT-VFHDLIRAMLK 136
Cdd:pfam00069 123 TPWYMAPEVL---GGNPYGPKVDVWSLGCILYELLTGKPPFpginGNEIYELIIDQPYAFPELPSNLSeEAKDLLKKLLK 199

                          90
                  ....*....|....
gi 1331383559 137 VNPEERLSIAEVVR 150
Cdd:pfam00069 200 KDPSKRLTATQALQ 213
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
 8-143 2.90e-12

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 68.69  E-value: 2.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswsaqkramvEEEITRNTTPMYRTPEIVDLYSNfpiGEKQDIWA 87
Cdd:PTZ00263  139 IIYRDLKPENLLLDNKGHVKVTDFGFAKKVP---------------DRTFTLCGTPEYLAPEVIQSKGH---GKAVDWWT 200

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331383559  88 LGCILYLLCFRQHPFEDGAKLR----IVNGKYSIPV-NDTRYtvfHDLIRAMLKVNPEERL 143
Cdd:PTZ00263  201 MGVLLYEFIAGYPPFFDDTPFRiyekILAGRLKFPNwFDGRA---RDLVKGLLQTDHTKRL 258
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
2-103 2.44e-09

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 60.96  E-value: 2.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKppIIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqkRAMVEEEITRNTTPM----YRTPE-----IVD 72
Cdd:NF033483  124 HRNG--IVHRDIKPQNILITKDGRVKVTDFGIA---------------RALSSTTMTQTNSVLgtvhYLSPEqarggTVD 186

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1331383559  73 lysnfpigEKQDIWALGCILY-LLCFRQhPFE 103
Cdd:NF033483  187 --------ARSDIYSLGIVLYeMLTGRP-PFD 209
 
Name Accession Description Interval E-value
PTP_GAK cd14564
protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated ...
 237-399 1.29e-117

protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated kinase (GAK), also called auxilin-2, contains an N-terminal protein kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of a protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN (a phosphoinositide 3-phosphatase), and a C-terminal region with clathrin-binding and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor.


Pssm-ID: 350412 [Multi-domain]  Cd Length: 163  Bit Score: 354.59  E-value: 1.29e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559 237 VANYAKGDLDISYITSRIAVMSFPAEGVESAIKNNIEDVRMFLDAKHPGHYAVYNLSPRIYRASKFHNRVTECGWAVRRA 316
Cdd:cd14564     1 VANYAKGDLDISYITSRIAVMSFPAEGVESAIKNNIEDVRLFLDSRHPGHYAVYNLSQRTYRPSRFHNRVSECGWPARRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559 317 PHLHSLYTLCRSMHAWLREDHRNVCVVHCMDGRAASAVAVCAFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEYV 396
Cdd:cd14564    81 PNLQNLYSICKNMHLWLKQDQKNICIVHCLDGRAASAVVVCSFLCFCRLFTTAEAAVYMFSMKRCPPGIWPSHKRYIEYM 160


                  ...
gi 1331383559 397 CDM 399
Cdd:cd14564   161 CDM 163
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
 1-159 9.67e-113

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


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 346.80  E-value: 9.67e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQKRAMVEEEITRNTTPMYRTPEIVDLYSNFPIG 80
Cdd:cd14036   124 MHKQSPPIIHRDLKIENLLIGNQGQIKLCDFGSATTEAHYPDYSWSAQKRSLVEDEITRNTTPMYRTPEMIDLYSNYPIG 203

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559  81 EKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQLQEIAAAR 159
Cdd:cd14036   204 EKQDIWALGCILYLLCFRKHPFEDGAKLRIINAKYTIPPNDTQYTVFHDLIRSTLKVNPEERLSITEIVEQLQELAAAR 282
PTP_auxilin-like cd14511
protein tyrosine phosphatase-like domain of auxilin and similar proteins; This subfamily ...
 237-399 7.68e-101

protein tyrosine phosphatase-like domain of auxilin and similar proteins; This subfamily contains proteins similar to auxilin, characterized by also containing a J domain. It includes auxilin, also called auxilin-1, and cyclin-G-associated kinase (GAK), also called auxilin-2. Auxilin-1 and -2 facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, while auxilin-1 which is nerve-specific. Both proteins contain a protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN (a phosphoinositide 3-phosphatase), and a C-terminal region with clathrin-binding and J domains. In addition, GAK contains an N-terminal protein kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2.


Pssm-ID: 350361 [Multi-domain]  Cd Length: 164  Bit Score: 310.82  E-value: 7.68e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559 237 VANYAKGDLDISYITSRIAVMSFPAEGVESAI-KNNIEDVRMFLDAKHPGHYAVYNLSPRIYRASKFHNRVTECGWAVRR 315
Cdd:cd14511     1 QQSYARNDLDISYITSRIIVMPFPAEGIESTYrKNNIEDVRAFLDSRHPQKYSVYNLSPRSYPTLRLPSRVVECSWPYRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559 316 APHLHSLYTLCRSMHAWLREDHRNVCVVHCMDGRAASAVAVCAFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEY 395
Cdd:cd14511    81 APSLHALYALCRDIYQWLNKDPKNVIVIHCTDGKAASATVVCALLVYCGLFKTPEDALQMFAVKRCPPGLSPSELRYLYY 160


                  ....
gi 1331383559 396 VCDM 399
Cdd:cd14511   161 FSDI 164
PTP_auxilin_N cd14563
N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 ...
 237-399 1.20e-82

N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 or DnaJ homolog subfamily C member 6 (DNAJC6), is a J-domain containing protein that recruits the ATP-dependent chaperone Hsc70 to newly budded clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles, driving the clathrin assembly#disassembly cycle. Mutations in the DNAJC6 gene, encoding auxilin, are associated with early-onset Parkinson's disease. Auxilin contains an N-terminal protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN, a phosphoinositide 3-phosphatase, and a C-terminal region with clathrin-binding and J domains.


Pssm-ID: 350411 [Multi-domain]  Cd Length: 163  Bit Score: 262.89  E-value: 1.20e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559 237 VANYAKGDLDISYITSRIAVMSFPAEGVESAIKNNIEDVRMFLDAKHPGHYAVYNLSPRIYRASKFHNRVTECGWAVRRA 316
Cdd:cd14563     1 VASYTKGELDISYITSRIIVMSYPAEGVELGFRNHIEDVRSFLDSRHLDHYTVFNLSQKSYRSAKFHNRVSECSWPVRQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559 317 PHLHSLYTLCRSMHAWLREDHRNVCVVHCMDGRAASAVAVCAFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEYV 396
Cdd:cd14563    81 PSLHNLFAVCKNMHNWLQQNPKNVCVIHCMDGRAASAVLVSAMFCFCHLFSNPVPAMQLLNAKRPGIGLWPSHRRYIGYI 160


                  ...
gi 1331383559 397 CDM 399
Cdd:cd14563   161 CDL 163
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
 1-157 8.62e-81

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: 261.88  E-value: 8.62e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTIsHYPDYSWsaQKRAMVEEEITRNTTPMYRTPEIVDLYSNFPIG 80
Cdd:cd13985   119 LHSQSPPIIHRDIKIENILFSNTGRFKLCDFGSATTE-HYPLERA--EEVNIIEEEIQKNTTPMYRAPEMIDLYSKKPIG 195

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331383559  81 EKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQLQEIAA 157
Cdd:cd13985   196 EKADIWALGCLLYKLCFFKLPFDESSKLAIVAGKYSIPEQPRYSPELHDLIRHMLTPDPAERPDIFQVINIITKDTK 272
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
 1-156 6.32e-57

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: 197.12  E-value: 6.32e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDyswSAQKRAMVEEEITRNTTPMYRTPEIVDLYSNFPIG 80
Cdd:cd14037   124 MHYLKPPLIHRDLKVENVLISDSGNYKLCDFGSATTKILPPQ---TKQGVTYVEEDIKKYTTLQYRAPEMIDLYRGKPIT 200

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  81 EKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQLQEIA 156
Cdd:cd14037   201 EKSDIWALGCLLYKLCFYTTPFEESGQLAILNGNFTFPDNSRYSKRLHKLIRYMLEEDPEKRPNIYQVSYEAFELA 276
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 246-398 2.40e-53

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar proteins; Phosphatase and tensin homolog (PTEN) is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It dephosphorylates phosphoinositide trisphosphate. In addition to PTEN, this family includes tensins, voltage-sensitive phosphatases (VSPs), and auxilins. They all contain a protein tyrosine phosphatase-like domain although not all are active phosphatases. Tensins are intracellular proteins that act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility, and they may or may not have phosphatase activity. VSPs are phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. Auxilins are J domain-containing proteins that facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles, and they do not exhibit phosphatase activity.


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 182.78  E-value: 2.40e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559 246 DISYITSRIAVMSFPAEGV-ESAIKNNIEDVRMFLDAKHPGHYAVYNLSPRIYRA-SKFHNRVTECGWAVRRAPHLHSLY 323
Cdd:cd14497     1 DLSYITPRIIAMSFPATGYpESLYRNSIDDVANFLNTHHPDHYMIFNLSEEEYDDdSKFEGRVLHYGFPDHHPPPLGLLL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559 324 TLCRSMHAWLREDHRNVCVVHCMDGRAASAVAVCAFLCFCRLFSTAEAAVYMFSMKRCPPGIW----PSHKRYIEYVCD 398
Cdd:cd14497    81 EIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVICAYLLYYGQYSTADEALEYFAKKRFKEGLPgvtiPSQLRYLQYFER 159
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 246-395 2.41e-48

protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; Phosphatase and tensin homolog (PTEN), also phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN or mutated in multiple advanced cancers 1 (MMAC1), is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It is a critical endogenous inhibitor of phosphoinositide signaling. It dephosphorylates phosphoinositide trisphosphate, and therefore, has the function of negatively regulating Akt. The PTEN/PI3K/AKT pathway regulates the signaling of multiple biological processes such as apoptosis, metabolism, cell proliferation, and cell growth. PTEN contains an N-terminal PIP-binding domain, a protein tyrosine phosphatase (PTP)-like catalytic domain, a regulatory C2 domain responsible for its cellular location, a C-tail containing phosphorylation sites, and a C-terminal PDZ domain.


Pssm-ID: 350359 [Multi-domain]  Cd Length: 158  Bit Score: 168.54  E-value: 2.41e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559 246 DISYITSRIAVMSFPAEGVESAIKNNIEDVRMFLDAKHPGHYAVYNL-SPRIYRASKFHNRVTECGWAVRRAPHLHSLYT 324
Cdd:cd14509     1 DLTYITPNIIAMGFPAEGVEGVYRNPIDDVQRFLETKHKGHYKVYNLcSERSYDPSKFNGRVAEYPFDDHNPPPLELIKP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331383559 325 LCRSMHAWLREDHRNVCVVHCMDGRAASAVAVCAFLCFCRLFSTAEAAVYMFSMKRCPPG----IwPSHKRYIEY 395
Cdd:cd14509    81 FCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKFPSAKEALDFYGAKRTKNKkgvtI-PSQRRYVYY 154
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 244-399 1.35e-41

protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase/transmembrane phosphatase with tensin homology; Voltage-sensitive phosphatase (VSP) proteins comprise a family of phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. This family is conserved in deuterostomes; VSP was first identified as a sperm flagellar plasma membrane protein in Ciona intestinalis. Gene duplication events in primates resulted in the presence of paralogs, transmembrane phosphatase with tensin homology (TPTE) and TPTE2, that retain protein domain architecture but, in the case of TPTE, have lost catalytic activity. TPTE, also called cancer/testis antigen 44 (CT44), may play a role in the signal transduction pathways of the endocrine or spermatogenic function of the testis. TPTE2, also called TPTE and PTEN homologous inositol lipid phosphatase (TPIP), occurs in several differentially spliced forms; TPIP alpha displays phosphoinositide 3-phosphatase activity and is localized on the endoplasmic reticulum, while TPIP beta is cytosolic and lacks detectable phosphatase activity. VSP/TPTE proteins contain an N-terminal voltage sensor consisting of four transmembrane segments, a protein tyrosine phosphatase (PTP)-like phosphoinositide phosphatase catalytic domain, followed by a regulatory C2 domain.


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 150.21  E-value: 1.35e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559 244 DLDISYITSRIAVMSFPAEGVESAIKNNIEDVRMFLDAKHPGHYAVYNL-SPRIYRASKFHNRVTECGWAVRRAPHLHSL 322
Cdd:cd14510    13 DLDLTYVTDRVIAMSFPSSGKQAFYRNPIEEVVRFLDTKHPDHYKVYNLcSERGYDPKYFHNRVERVPIDDHNVPTLDEM 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559 323 YTLCRSMHAWLREDHRNVCVVHCMDGRAASAVAVCAFLCFCRLFSTAEAAVYMFSMKRCPPGIW--------PSHKRYIE 394
Cdd:cd14510    93 LSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAKEALEYFGERRTDKSVSskfqgvetPSQSRYVG 172


                  ....*
gi 1331383559 395 YVCDM 399
Cdd:cd14510   173 YFEKL 177
PTP_tensin cd14508
protein tyrosine phosphatase-like domain of tensins; The tensin family of intracellular ...
 246-395 1.23e-39

protein tyrosine phosphatase-like domain of tensins; The tensin family of intracellular proteins (tensin-1, -2, -3 and -4) act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Dysregulation of tensin expression has been implicated in human cancer. Tensin-1, -2, and -3 contain an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. In addition, tensin-2 contains a zinc finger N-terminal to its PTP domain. Tensin-4 is not included in this model as it does not contain a PTP-like domain.


Pssm-ID: 350358 [Multi-domain]  Cd Length: 159  Bit Score: 144.07  E-value: 1.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559 246 DISYITSRIAVMSFPAEGVESAIKNNIEDVRMFLDAKHPGHYAVYNLSPRIYRASKFHNRVTECGWAVRRAPHLHSLYTL 325
Cdd:cd14508     1 DLTYITERIIALSFPSTCSEQTYRHNLREAAHLLQSKHGDNYMVFNLSERRHDLRSLNPKVLDFGWPELHAPPLEKLCSI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331383559 326 CRSMHAWLREDHRNVCVVHCMDGRAASAVAVCAFLCFCRLFSTAEAAVYMFSMKR-----CPPGIWPSHKRYIEY 395
Cdd:cd14508    81 CKNMDSWLNADPQNVVVLHCKGGKGRLGVVVSAYMHYSKISATADQALDRFAMKRfyddkVGPLGQPSQKRYVGY 155
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 407-545 2.27e-35

C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key form, of the PTEN protein, phosphatidyl-inositol triphosphate phosphatase, and it is the C-terminus. This domain may well include a CBR3 loop which means it plays a central role in membrane binding. This domain associates across an extensive interface with the N-terminal phosphatase domain DSPc (pfam00782) suggesting that the C2 domain productively positions the catalytic part of the protein onto the membrane.


Pssm-ID: 463081  Cd Length: 133  Bit Score: 130.86  E-value: 2.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559 407 PHSKPMLVKSVVMTPVPLFsKQRNGCRPFCEVYVGEERVTTTSQEYDRMKEFKIEDGKAVIPLGVTVQGDVLIIIYHARA 486
Cdd:pfam10409   1 PPPKPLTLHSIILHGIPNF-KSGGGCRPYIRIYQNKKKVFSTSGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEFYHKGS 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331383559 487 TLGGRlqakmasMKMFQIQFHTGFVPRNatTVKFAKYDLDACDIQ---EKYPDLFQVNLEVE 545
Cdd:pfam10409  80 DLLSE-------EKMFRFWFNTSFIEDN--TLTLPKNELDKADKDkkdKRFPKDFKVELLFS 132
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
 1-150 1.62e-32

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 126.88  E-value: 1.62e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559    1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSwsaqkramveeeiTRNTTPMYRTPEIVdlySNFPIG 80
Cdd:smart00220 113 LHSKG--IVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLT-------------TFVGTPEYMAPEVL---LGKGYG 174

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559   81 EKQDIWALGCILYLLCFRQHPFEDGAKL-----RIVNGKYSIPVNDTRYTV-FHDLIRAMLKVNPEERLSIAEVVR 150
Cdd:smart00220 175 KAVDIWSLGVILYELLTGKPPFPGDDQLlelfkKIGKPKPPFPPPEWDISPeAKDLIRKLLVKDPEKRLTAEEALQ 250
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
 1-151 3.88e-31

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: 122.96  E-value: 3.88e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSwsaqkramveeeitrNT---TPMYRTPEIVdlySNF 77
Cdd:cd08215   119 LHSRK--ILHRDLKTQNIFLTKDGVVKLGDFGISKVLESTTDLA---------------KTvvgTPYYLSPELC---ENK 178

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559  78 PIGEKQDIWALGCILYLLCFRQHPFeDGAKL-----RIVNGKYSiPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQ 151
Cdd:cd08215   179 PYNYKSDIWALGCVLYELCTLKHPF-EANNLpalvyKIVKGQYP-PIPSQYSSELRDLVNSMLQKDPEKRPSANEILSS 255
PTP_tensin-1 cd14560
protein tyrosine phosphatase-like domain of tensin-1; Tensin-1 (TNS1) is part of the tensin ...
 246-395 1.18e-29

protein tyrosine phosphatase-like domain of tensin-1; Tensin-1 (TNS1) is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. It plays an essential role in TGF-beta-induced myofibroblast differentiation and myofibroblast-mediated formation of extracellular fibronectin and collagen matrix. It also positively regulates RhoA activity through its interaction with DLC1, a RhoGAP-containing tumor suppressor; the tensin-1-DLC1-RhoA signaling axis is critical in regulating cellular functions that lead to angiogenesis. Tensin-1 contains an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains.


Pssm-ID: 350408 [Multi-domain]  Cd Length: 159  Bit Score: 115.46  E-value: 1.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559 246 DISYITSRIAVMSFPAEGVESAIKNNIEDVRMFLDAKHPGHYAVYNLSPRIYRASKFHNRVTECGWAVRRAPHLHSLYTL 325
Cdd:cd14560     1 DLVYITERIISVSFPSTAEEPSFRSNLKEVAQMLKSKHGDNYLLFNLSERRHDISKLHPKVLDFGWPDLHAPALEKICSI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559 326 CRSMHAWLREDHRNVCVVHCMDGRAASAVAVCAFLCFCRLFSTAEAAVYMFSMKR------CPPGiWPSHKRYIEY 395
Cdd:cd14560    81 CKAMDTWLNADPHNVVVIHNKGNRGRTGVVIAAYMHYSNISASADQALDRFAMKRfyedkvVPVG-QPSQKRYVHY 155
PTP_tensin-3 cd14561
protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called ...
 246-396 1.30e-29

protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called tensin-like SH2 domain-containing protein 1 (TENS1) or tumor endothelial marker (TEM6). It is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Tensin-3 contributes to cell migration, anchorage-independent growth, tumorigenesis, and metastasis of cancer cells. It cooperates with Dock5, an exchange factor for the small GTPase Rac, for osteoclast activity to ensure the correct organization of podosomes. Tensin-3 contains an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains.


Pssm-ID: 350409 [Multi-domain]  Cd Length: 159  Bit Score: 115.43  E-value: 1.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559 246 DISYITSRIAVMSFPAEGVESAIKNNIEDVRMFLDAKHPGHYAVYNLSPRIYRASKFHNRVTECGWAVRRAPHLHSLYTL 325
Cdd:cd14561     1 DLTYITERIIAVSFPADCSEETYLHNLQDVTRMLKSKHGDNYLVLNLSEKRYELTKLNPKIMDVGWPDLHAPPLDKMCTI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559 326 CRSMHAWLREDHRNVCVVHCMDGRAASAVAVCAFLCFCRLFSTAEAAVYMFSMK-----RCPPGIWPSHKRYIEYV 396
Cdd:cd14561    81 CKAMESWLNSDPLHVVVIHCRGGKGRIGVVISSYMHFTNVSASADQALDRFAMKkfyddKVSALMQPSQKRYVQFL 156
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
 1-154 1.37e-29

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: 119.32  E-value: 1.37e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHR-QKPPIIHRDLKVENLLLSNQGTIKLCDFGSAT----TIShypdyswsAQKRAM-VEEEITRNTTPMYRTPEIVDLY 74
Cdd:cd13986   122 MHEpELVPYAHRDIKPGNVLLSEDDEPILMDLGSMNpariEIE--------GRREALaLQDWAAEHCTMPYRAPELFDVK 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  75 SNFPIGEKQDIWALGCILYLLCFRQHPFE------DGAKLRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEV 148
Cdd:cd13986   194 SHCTIDEKTDIWSLGCTLYALMYGESPFErifqkgDSLALAVLSGNYSFPDNSRYSEELHQLVKSMLVVNPAERPSIDDL 273


                  ....*.
gi 1331383559 149 VRQLQE 154
Cdd:cd13986   274 LSRVHD 279
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
 1-148 3.17e-27

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: 111.46  E-value: 3.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHypdyswsaQKRAMveeeiTRNTTPMYRTPEIVD--LYsnfp 78
Cdd:cd14003   115 CHSNG--IVHRDLKLENILLDKNGNLKIIDFGLSNEFRG--------GSLLK-----TFCGTPAYAAPEVLLgrKY---- 175

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331383559  79 IGEKQDIWALGCILYLLCFRQHPFEDG--AKLR--IVNGKYSIPvndtrYTV---FHDLIRAMLKVNPEERLSIAEV 148
Cdd:cd14003   176 DGPKADVWSLGVILYAMLTGYLPFDDDndSKLFrkILKGKYPIP-----SHLspdARDLIRRMLVVDPSKRITIEEI 247
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
 1-148 1.73e-26

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: 109.49  E-value: 1.73e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGsattishypdysWSAqkramVEEEITRNT---TPMYRTPEIVdlySNF 77
Cdd:cd14007   116 LHSKN--IIHRDIKPENILLGSNGELKLADFG------------WSV-----HAPSNRRKTfcgTLDYLPPEMV---EGK 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331383559  78 PIGEKQDIWALGCILYLLCFRQHPFEDG----AKLRIVNGKYSIPvnDTRYTVFHDLIRAMLKVNPEERLSIAEV 148
Cdd:cd14007   174 EYDYKVDIWSLGVLCYELLVGKPPFESKshqeTYKRIQNVDIKFP--SSVSPEAKDLISKLLQKDPSKRLSLEQV 246
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
 1-148 9.99e-26

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: 107.18  E-value: 9.99e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQ---GTIKLCDFGSATTIshypdyswsaqkramvEEEITRNT---TPMYRTPEIVDly 74
Cdd:cd05117   115 LHSQG--IVHRDLKPENILLASKdpdSPIKIIDFGLAKIF----------------EEGEKLKTvcgTPYYVAPEVLK-- 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  75 sNFPIGEKQDIWALGCILY-LLCFRqHPF--EDGAKL--RIVNGKYSIPvndtrYTVFH-------DLIRAMLKVNPEER 142
Cdd:cd05117   175 -GKGYGKKCDIWSLGVILYiLLCGY-PPFygETEQELfeKILKGKYSFD-----SPEWKnvseeakDLIKRLLVVDPKKR 247


                  ....*.
gi 1331383559 143 LSIAEV 148
Cdd:cd05117   248 LTAAEA 253
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
 1-150 2.42e-24

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: 103.40  E-value: 2.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHypdyswsaqkramvEEEiTRNT---TPMYRTPEIvdLYSNF 77
Cdd:cd14099   117 LHSNR--IIHRDLKLGNLFLDENMNVKIGDFGLAARLEY--------------DGE-RKKTlcgTPNYIAPEV--LEKKK 177

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331383559  78 PIGEKQDIWALGCILYLLCFRQHPFEDGAK----LRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVR 150
Cdd:cd14099   178 GHSFEVDIWSLGVILYTLLVGKPPFETSDVketyKRIKKNEYSFPSHLSISDEAKDLIRSMLQPDPTKRPSLDEILS 254
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
 1-152 2.57e-24

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: 101.96  E-value: 2.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWsaqkramveeeITRNTTPMYRTPEIVDlySNFPIG 80
Cdd:cd00180   108 LHSNG--IIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLK-----------TTGGTTPPYYAPPELL--GGRYYG 172

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331383559  81 EKQDIWALGCILYLLcfrqhpfedgaklrivngkysipvndtryTVFHDLIRAMLKVNPEERLSIAEVVRQL 152
Cdd:cd00180   173 PKVDIWSLGVILYEL-----------------------------EELKDLIRRMLQYDPKKRPSAKELLEHL 215
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 2-147 2.63e-24

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


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 103.39  E-value: 2.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHypdyswsAQKRAmveeeITRNTTPMYRTPEIVdlySNFPIGE 81
Cdd:cd08217   125 SVGGGKILHRDLKPANIFLDSDNNVKLGDFGLARVLSH-------DSSFA-----KTYVGTPYYMSPELL---NEQSYDE 189

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331383559  82 KQDIWALGCILYLLCFRQHPFE----DGAKLRIVNGKYS-IPvndTRYTvfHDL---IRAMLKVNPEERLSIAE 147
Cdd:cd08217   190 KSDIWSLGCLIYELCALHPPFQaanqLELAKKIKEGKFPrIP---SRYS--SELnevIKSMLNVDPDKRPSVEE 258
PTP_tensin-2 cd14562
protein tyrosine phosphatase-like domain of tensin-2; Tensin-2 (TNS2) is also called ...
 246-395 4.76e-24

protein tyrosine phosphatase-like domain of tensin-2; Tensin-2 (TNS2) is also called tensin-like C1 domain-containing phosphatase (TENC1) or C1 domain-containing phosphatase and tensin homolog (C1-TEN). It is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Tensin-2 is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It also modulates cell contractility and remodeling of collagen fibers through the DLC1, a RhoGAP that binds to tensins in focal adhesions. Tensin-2 may have phosphatase activity; it reduces AKT1 phosphorylation. It contains an N-terminal region with a zinc finger, a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains.


Pssm-ID: 350410 [Multi-domain]  Cd Length: 159  Bit Score: 99.25  E-value: 4.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559 246 DISYITSRIAVMSFPAEGVESAIKNNIEDVRMFLDAKHPGHYAVYNLSPRIYRASKFHNRVTECGWAVRRAPHLHSLYTL 325
Cdd:cd14562     1 DLTYITERIISVFFPPALEEQRYRGNLREVAQMLKSKHEDKYLLFNLSEKRHDITRLNPKVQDFGWPDLHAPPLDKICSI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331383559 326 CRSMHAWLREDHRNVCVVHCMDGRAASAVAVCAFLCFCRLFSTAEAAVYMFSMKR-C----PPGIWPSHKRYIEY 395
Cdd:cd14562    81 CKAMETWLNADPQHVVVLHCKGNKGKTGVIVAAYMHYSKISAGADQALSTLAMRKfCedkvATSLQPSQRRYISY 155
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
 1-148 1.18e-23

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: 101.18  E-value: 1.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDyswsaqkramvEEEITR-NTTPMYRTPEIVDLYSNFPi 79
Cdd:cd14119   113 LHSQG--IIHKDIKPGNLLLTTDGTLKISDFGVAEALDLFAE-----------DDTCTTsQGSPAFQPPEIANGQDSFS- 178

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331383559  80 GEKQDIWALGCILYLLCFRQHPFEDGAKLR----IVNGKYSIPvnDTRYTVFHDLIRAMLKVNPEERLSIAEV 148
Cdd:cd14119   179 GFKVDIWSAGVTLYNMTTGKYPFEGDNIYKlfenIGKGEYTIP--DDVDPDLQDLLRGMLEKDPEKRFTIEQI 249
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 2-144 2.71e-23

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


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 100.05  E-value: 2.71e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSwsaqkramveeeITRNTTPMYRTPEIvdlYSNFPIGE 81
Cdd:cd08219   115 HIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGAYA------------CTYVGTPYYVPPEI---WENMPYNN 179

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331383559  82 KQDIWALGCILYLLCFRQHPFEDGA----KLRIVNGKYSiPVNDTRYTVFHDLIRAMLKVNPEERLS 144
Cdd:cd08219   180 KSDIWSLGCILYELCTLKHPFQANSwknlILKVCQGSYK-PLPSHYSYELRSLIKQMFKRNPRSRPS 245
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 1-151 4.24e-23

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


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 99.50  E-value: 4.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswsaqkrAMVEEEITRNTTPMYRTPEIVDlysNFPIG 80
Cdd:cd08218   117 VHDRK--ILHRDIKSQNIFLTKDGIIKLGDFGIARVLN------------STVELARTCIGTPYYLSPEICE---NKPYN 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  81 EKQDIWALGCILYLLCFRQHPFEDGAK----LRIVNGKYsiPVNDTRYTV-FHDLIRAMLKVNPEERLSIAEVVRQ 151
Cdd:cd08218   180 NKSDIWALGCVLYEMCTLKHAFEAGNMknlvLKIIRGSY--PPVPSRYSYdLRSLVSQLFKRNPRDRPSINSILEK 253
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
 8-150 4.49e-23

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: 99.64  E-value: 4.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSAttishypdySWSaQKRAMVEeeiTRNTTPMYRTPEIV--DLYSnfpiGEKQDI 85
Cdd:cd14081   122 ICHRDLKPENLLLDEKNNIKIADFGMA---------SLQ-PEGSLLE---TSCGSPHYACPEVIkgEKYD----GRKADI 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331383559  86 WALGCILYLLCFRQHPFeDGAKLR-----IVNGKYSIPVN---DTRytvfhDLIRAMLKVNPEERLSIAEVVR 150
Cdd:cd14081   185 WSCGVILYALLVGALPF-DDDNLRqllekVKRGVFHIPHFispDAQ-----DLLRRMLEVNPEKRITIEEIKK 251
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
 1-148 2.72e-22

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: 97.67  E-value: 2.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShyPDYSWSAQKRAMVEEEITRNT-------TPMYRTPEIVdl 73
Cdd:cd05581   117 LHSKG--IIHRDLKPENILLDEDMHIKITDFGTAKVLG--PDSSPESTKGDADSQIAYNQAraasfvgTAEYVSPELL-- 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  74 ySNFPIGEKQDIWALGCILYLLCFRQHPFEDGA----KLRIVNGKYSIPVN---DTRytvfhDLIRAMLKVNPEERLSIA 146
Cdd:cd05581   191 -NEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNeyltFQKIVKLEYEFPENfppDAK-----DLIQKLLVLDPSKRLGVN 264


                  ..
gi 1331383559 147 EV 148
Cdd:cd05581   265 EN 266
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
 2-154 3.53e-22

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: 96.89  E-value: 3.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQkpPIIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqkRAMVEEEITRNT----TPMYRTPEIvdlYSNF 77
Cdd:cd14014   117 HRA--GIVHRDIKPANILLTEDGRVKLTDFGIA---------------RALGDSGLTQTGsvlgTPAYMAPEQ---ARGG 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  78 PIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYS------IPVNDTRYTVFHDLIRAMLKVNPEERL-SIAEVVR 150
Cdd:cd14014   177 PVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQeappppSPLNPDVPPALDAIILRALAKDPEERPqSAAELLA 256


                  ....
gi 1331383559 151 QLQE 154
Cdd:cd14014   257 ALRA 260
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
 1-148 9.61e-22

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: 96.13  E-value: 9.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFG-SATTISHYPDYSWSAQKRAMVEEEITRNT--TPMYRTPEIVdlySNF 77
Cdd:cd05579   109 LHSHG--IIHRDLKPDNILIDANGHLKLTDFGlSKVGLVRRQIKLSIQKKSNGAPEKEDRRIvgTPDYLAPEIL---LGQ 183

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331383559  78 PIGEKQDIWALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERL---SIAEV 148
Cdd:cd05579   184 GHGKTVDWWSLGVILYEFLVGIPPFhaETPEEIfqNILNGKIEWPEDPEVSDEAKDLISKLLTPDPEKRLgakGIEEI 261
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 1-151 1.41e-21

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: 95.65  E-value: 1.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKPpIIHRDLKVENLLLSNQGTIKLCDFGSATtishypdyswsaQKRAMVEEEITRNTTPMYRTPEIVdlySNFPIG 80
Cdd:cd08528   129 LHKEKQ-IVHRDLKPNNIMLGEDDKVTITDFGLAK------------QKGPESSKMTSVVGTILYSCPEIV---QNEPYG 192

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  81 EKQDIWALGCILYLLCFRQHPFEDGAKL----RIVNGKYSiPVNDTRYT-VFHDLIRAMLKVNPEERLSIAEVVRQ 151
Cdd:cd08528   193 EKADIWALGCILYQMCTLQPPFYSTNMLtlatKIVEAEYE-PLPEGMYSdDITFVIRSCLTPDPEARPDIVEVSSM 267
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
 1-148 1.44e-21

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: 95.31  E-value: 1.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATtishypdyswsaqkraMVEE--EITRNT--TPMYRTPEIVD---- 72
Cdd:cd14008   124 LHENG--IVHRDIKPENLLLTADGTVKISDFGVSE----------------MFEDgnDTLQKTagTPAFLAPELCDgdsk 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  73 LYSNFPIgekqDIWALGCILYLLCFRQHPFEDGAKL----RIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEV 148
Cdd:cd14008   186 TYSGKAA----DIWALGVTLYCLVFGRLPFNGDNILelyeAIQNQNDEFPIPPELSPELKDLLRRMLEKDPEKRITLKEI 261
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
 1-151 1.74e-21

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: 94.79  E-value: 1.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSwsaqkRAMVeeeitrnTTPMYRTPEivdLYSNFPIG 80
Cdd:cd08529   117 LHSKK--ILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTTNFA-----QTIV-------GTPYYLSPE---LCEDKPYN 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331383559  81 EKQDIWALGCILYLLCFRQHPFE---DGAK-LRIVNGKYSiPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQ 151
Cdd:cd08529   180 EKSDVWALGCVLYELCTGKHPFEaqnQGALiLKIVRGKYP-PISASYSQDLSQLIDSCLTKDYRQRPDTTELLRN 253
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 1-151 4.60e-21

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


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 93.87  E-value: 4.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTI-KLCDFGSATTISHYPDYSWsaqkramveeeiTRNTTPMYRTPEIVDlysNFPI 79
Cdd:cd08225   117 IHDRK--ILHRDIKSQNIFLSKNGMVaKLGDFGIARQLNDSMELAY------------TCVGTPYYLSPEICQ---NRPY 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  80 GEKQDIWALGCILYLLCFRQHPFEDGA----KLRIVNGKYSiPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQ 151
Cdd:cd08225   180 NNKTDIWSLGCVLYELCTLKHPFEGNNlhqlVLKICQGYFA-PISPNFSRDLRSLISQLFKVSPRDRPSITSILKR 254
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
 1-144 6.97e-21

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: 92.97  E-value: 6.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqkRAMVEEEITRNT---TPMYRTPEIVdlySNF 77
Cdd:cd05123   109 LHSLG--IIYRDLKPENILLDSDGHIKLTDFGLA---------------KELSSDGDRTYTfcgTPEYLAPEVL---LGK 168

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331383559  78 PIGEKQDIWALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSIPVNDTRytVFHDLIRAMLKVNPEERLS 144
Cdd:cd05123   169 GYGKAVDWWSLGVLLYEMLTGKPPFyaENRKEIyeKILKSPLKFPEYVSP--EAKSLISGLLQKDPTKRLG 237
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
 1-150 1.34e-20

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


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 92.40  E-value: 1.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTishypdyswsaqkramVEEEITRNT---TPMYRTPEIV--DLYs 75
Cdd:cd14075   117 MHENN--IIHRDLKAENVFYASNNCVKVGDFGFSTH----------------AKRGETLNTfcgSPPYAAPELFkdEHY- 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  76 nfpIGEKQDIWALGCILYLLCFRQHPF--EDGAKLR--IVNGKYSIP--VNDTrytvFHDLIRAMLKVNPEERLSIAEVV 149
Cdd:cd14075   178 ---IGIYVDIWALGVLLYFMVTGVMPFraETVAKLKkcILEGTYTIPsyVSEP----CQELIRGILQPVPSDRYSIDEIK 250


                  .
gi 1331383559 150 R 150
Cdd:cd14075   251 N 251
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
 1-150 3.08e-20

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: 91.14  E-value: 3.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQ-GTIKLCDFGSAttishypdySWSAQKrAMVEEEITRnttpMYRTPEIvdLYSNFPI 79
Cdd:cd05118   117 LHSNG--IIHRDLKPENILINLElGQLKLADFGLA---------RSFTSP-PYTPYVATR----WYRAPEV--LLGAKPY 178

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331383559  80 GEKQDIWALGCILYLLCFRQHPFEDG------AKLRIVNGKYSipvndtrytvFHDLIRAMLKVNPEERLSIAEVVR 150
Cdd:cd05118   179 GSSIDIWSLGCILAELLTGRPLFPGDsevdqlAKIVRLLGTPE----------ALDLLSKMLKYDPAKRITASQALA 245
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
 8-144 4.22e-20

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: 90.77  E-value: 4.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTISHypdyswsaqkRAMVEEEItrNTTPMYRTPEIVDlysNFPIGEKQDIWA 87
Cdd:cd14002   120 IIHRDMKPQNILIGKGGVVKLCDFGFARAMSC----------NTLVLTSI--KGTPLYMAPELVQ---EQPYDHTADLWS 184

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331383559  88 LGCILYLLCFRQHPF--EDGAKL--RIVNGKYSIPvnDTRYTVFHDLIRAMLKVNPEERLS 144
Cdd:cd14002   185 LGCILYELFVGQPPFytNSIYQLvqMIVKDPVKWP--SNMSPEFKSFLQGLLNKDPSKRLS 243
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
 1-148 5.36e-20

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: 90.88  E-value: 5.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaQKRAMVEEEITrNT--TPMYRTPEIVDLYSNFP 78
Cdd:cd14118   131 LHYQK--IIHRDIKPSNLLLGDDGHVKIADFGVS-------------NEFEGDDALLS-STagTPAFMAPEALSESRKKF 194

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331383559  79 IGEKQDIWALGCILYLLCFRQHPFEDGAKLR----IVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEV 148
Cdd:cd14118   195 SGKALDIWAMGVTLYCFVFGRCPFEDDHILGlhekIKTDPVVFPDDPVVSEQLKDLILRMLDKNPSERITLPEI 268
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
 1-151 7.53e-20

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: 90.14  E-value: 7.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATtishypdyswsAQKRAMVEEEItrnTTPMYRTPEIvdlYSNFPIG 80
Cdd:cd08530   119 LHDQK--ILHRDLKSANILLSAGDLVKIGDLGISK-----------VLKKNLAKTQI---GTPLYAAPEV---WKGRPYD 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331383559  81 EKQDIWALGCILYLLCFRQHPFE----DGAKLRIVNGKYSIPVNdtRYTvfHDL---IRAMLKVNPEERLSIAEVVRQ 151
Cdd:cd08530   180 YKSDIWSLGCLLYEMATFRPPFEartmQELRYKVCRGKFPPIPP--VYS--QDLqqiIRSLLQVNPKKRPSCDKLLQS 253
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 1-151 1.05e-19

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


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 89.80  E-value: 1.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSwsaqkramveeeITRNTTPMYRTPEivdLYSNFPIG 80
Cdd:cd08223   118 MHERN--ILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSDMA------------TTLIGTPYYMSPE---LFSNKPYN 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  81 EKQDIWALGCILYLLCFRQHPF--EDGAKL--RIVNGKysIPVNDTRY-TVFHDLIRAMLKVNPEERLSIAEVVRQ 151
Cdd:cd08223   181 HKSDVWALGCCVYEMATLKHAFnaKDMNSLvyKILEGK--LPPMPKQYsPELGELIKAMLHQDPEKRPSVKRILRQ 254
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
 2-148 1.51e-19

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: 89.58  E-value: 1.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKppIIHRDLKVENLLLSNqGTIKLCDFGSATTIshyPDYSWSaqkramveeeITRNT---TPMYRTPE-IVDL-YSN 76
Cdd:cd14131   120 HEEG--IVHSDLKPANFLLVK-GRLKLIDFGIAKAI---QNDTTS----------IVRDSqvgTLNYMSPEaIKDTsASG 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  77 FP-----IGEKQDIWALGCILYLLCFRQHPFED----GAKL-RIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIA 146
Cdd:cd14131   184 EGkpkskIGRPSDVWSLGCILYQMVYGKTPFQHitnpIAKLqAIIDPNHEIEFPDIPNPDLIDVMKRCLQRDPKKRPSIP 263


                  ..
gi 1331383559 147 EV 148
Cdd:cd14131   264 EL 265
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
 8-151 2.53e-19

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: 88.88  E-value: 2.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSN---QGTIKLCDFGSAttishypdyswsaqkramveEEITRNT-------TPMYRTPEIvdlysnf 77
Cdd:cd14089   121 IAHRDLKPENLLYSSkgpNAILKLTDFGFA--------------------KETTTKKslqtpcyTPYYVAPEV------- 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  78 pIGEKQ-----DIWALGCILY-LLC-----FRQH--PFEDGAKLRIVNGKYSIPvnDTRYT----VFHDLIRAMLKVNPE 140
Cdd:cd14089   174 -LGPEKydkscDMWSLGVIMYiLLCgyppfYSNHglAISPGMKKRIRNGQYEFP--NPEWSnvseEAKDLIRGLLKTDPS 250

                         170
                  ....*....|.
gi 1331383559 141 ERLSIAEVVRQ 151
Cdd:cd14089   251 ERLTIEEVMNH 261
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
 1-149 7.91e-19

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: 87.06  E-value: 7.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAqkramveeeitrntTPMYRTPEIvdLYSNFPIG 80
Cdd:cd14004   125 LHDQG--IVHRDIKDENVILDGNGTIKLIDFGSAAYIKSGPFDTFVG--------------TIDYAAPEV--LRGNPYGG 186

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559  81 EKQDIWALGCILYLLCFRQHPFEDgaKLRIVNGKYSIPVNDTRYTVfhDLIRAMLKVNPEERLSIAEVV 149
Cdd:cd14004   187 KEQDIWALGVLLYTLVFKENPFYN--IEEILEADLRIPYAVSEDLI--DLISRMLNRDVGDRPTIEELL 251
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
 2-147 1.23e-18

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: 86.49  E-value: 1.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHypdyswsaqkramveeEITRNT---TPMYRTPEIVdlySNFP 78
Cdd:cd05122   115 HSHG--IIHRDIKAANILLTSDGEVKLIDFGLSAQLSD----------------GKTRNTfvgTPYWMAPEVI---QGKP 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331383559  79 IGEKQDIWALGCILYLLCFRQHPFEDGAKLRI-----VNGKYSIPvNDTRYT-VFHDLIRAMLKVNPEERLSIAE 147
Cdd:cd05122   174 YGFKADIWSLGITAIEMAEGKPPYSELPPMKAlfliaTNGPPGLR-NPKKWSkEFKDFLKKCLQKDPEKRPTAEQ 247
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
2-172 2.11e-18

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 89.30  E-value: 2.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQkpPIIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqkRAMVEEEITRNT----TPMYRTPEivdLYSNF 77
Cdd:COG0515   124 HAA--GIVHRDIKPANILLTPDGRVKLIDFGIA---------------RALGGATLTQTGtvvgTPGYMAPE---QARGE 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  78 PIGEKQDIWALGCILYLLCFRQHPFE---DGAKLRIVNGKYSIPVNDTRYTV---FHDLIRAMLKVNPEERL-SIAEVVR 150
Cdd:COG0515   184 PVDPRSDVYSLGVTLYELLTGRPPFDgdsPAELLRAHLREPPPPPSELRPDLppaLDAIVLRALAKDPEERYqSAAELAA 263

                         170       180
                  ....*....|....*....|..
gi 1331383559 151 QLQEIAAARNVNPKAPITELLE 172
Cdd:COG0515   264 ALRAVLRSLAAAAAAAAAAAAA 285
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
 1-150 3.70e-18

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: 85.48  E-value: 3.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswsaqkramvEEEITRNT--TPMYRTPEI--VDLYSN 76
Cdd:cd14093   125 LHSLN--IVHRDLKPENILLDDNLNVKISDFGFATRLD---------------EGEKLRELcgTPGYLAPEVlkCSMYDN 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  77 FP-IGEKQDIWALGCILYLLCFRQHPFEDGAKL----RIVNGKYSI--PVNDTRYTVFHDLIRAMLKVNPEERLSIAEVV 149
Cdd:cd14093   188 APgYGKEVDMWACGVIMYTLLAGCPPFWHRKQMvmlrNIMEGKYEFgsPEWDDISDTAKDLISKLLVVDPKKRLTAEEAL 267


                  .
gi 1331383559 150 R 150
Cdd:cd14093   268 E 268
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
 8-148 4.25e-18

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: 84.75  E-value: 4.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSAttiSHYpdyswsaQKRAMVEeeiTRNTTPMYRTPEIVDlysNFP-IGEKQDIW 86
Cdd:cd14073   122 VVHRDLKLENILLDQNGNAKIADFGLS---NLY-------SKDKLLQ---TFCGSPLYASPEIVN---GTPyQGPEVDCW 185

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  87 ALGCILYLLCFRQHPFE--DGAKLR--IVNGKYSIPvndTRYTVFHDLIRAMLKVNPEERLSIAEV 148
Cdd:cd14073   186 SLGVLLYTLVYGTMPFDgsDFKRLVkqISSGDYREP---TQPSDASGLIRWMLTVNPKRRATIEDI 248
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
 8-150 5.85e-18

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: 85.14  E-value: 5.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGT---IKLCDFGsattishypdyswsaQKRAMVEEEI--TRNTTPMYRTPEIVDLYSNFPIGEK 82
Cdd:cd14084   132 IIHRDLKPENVLLSSQEEeclIKITDFG---------------LSKILGETSLmkTLCGTPTYLAPEVLRSFGTEGYTRA 196

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331383559  83 QDIWALGCILYLLCFRQHPFED-----GAKLRIVNGKYS-IPVNDTRYTV-FHDLIRAMLKVNPEERLSIAEVVR 150
Cdd:cd14084   197 VDCWSLGVILFICLSGYPPFSEeytqmSLKEQILSGKYTfIPKAWKNVSEeAKDLVKKMLVVDPSRRPSIEEALE 271
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
 8-150 6.99e-18

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


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 84.37  E-value: 6.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFG-SATTISHYPDYSWSAqkramveeeitrntTPMYRTPEIVD--LYSnfpiGEKQD 84
Cdd:cd14071   120 IVHRDLKAENLLLDANMNIKIADFGfSNFFKPGELLKTWCG--------------SPPYAAPEVFEgkEYE----GPQLD 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331383559  85 IWALGCILYLLCFRQHPFeDGAKL-----RIVNGKYSIPvndtrYTVFHD---LIRAMLKVNPEERLSIAEVVR 150
Cdd:cd14071   182 IWSLGVVLYVLVCGALPF-DGSTLqtlrdRVLSGRFRIP-----FFMSTDcehLIRRMLVLDPSKRLTIEQIKK 249
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
 1-147 1.51e-17

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: 83.34  E-value: 1.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShypDYSWSAQKRAMVeeeitrnTTPMYRTPEIVdlySNFPIG 80
Cdd:cd06606   115 LHSNG--IVHRDIKGANILVDSDGVVKLADFGCAKRLA---EIATGEGTKSLR-------GTPYWMAPEVI---RGEGYG 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331383559  81 EKQDIWALGCILYLLCFRQHPFED-----GAKLRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAE 147
Cdd:cd06606   180 RAADIWSLGCTVIEMATGKPPWSElgnpvAALFKIGSSGEPPPIPEHLSEEAKDFLRKCLQRDPKKRPTADE 251
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
 6-152 1.71e-17

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: 82.97  E-value: 1.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   6 PPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYpdyswsaqkramvEEEITRNT-TPMYRTPEIvdlYSNFPIGEKQD 84
Cdd:cd13999   110 PPIIHRDLKSLNILLDENFTVKIADFGLSRIKNST-------------TEKMTGVVgTPRWMAPEV---LRGEPYTEKAD 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331383559  85 IWALGCILYLLCFRQHPFEDGAKLRIVNGKYS------IPVN-DTRYTvfhDLIRAMLKVNPEERLSIAEVVRQL 152
Cdd:cd13999   174 VYSFGIVLWELLTGEVPFKELSPIQIAAAVVQkglrppIPPDcPPELS---KLIKRCWNEDPEKRPSFSEIVKRL 245
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
 8-149 3.72e-17

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: 82.22  E-value: 3.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIShYPDyswsaqkramvEEEITRNTTPMYRTPEIVdlySNFPIGEKQDIWA 87
Cdd:cd14186   123 ILHRDLTLSNLLLTRNMNIKIADFGLATQLK-MPH-----------EKHFTMCGTPNYISPEIA---TRSAHGLESDVWS 187

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  88 LGCILYLLCFRQHPFEDGAKLRIVN----GKYSIPVNDTRYTvfHDLIRAMLKVNPEERLSIAEVV 149
Cdd:cd14186   188 LGCMFYTLLVGRPPFDTDTVKNTLNkvvlADYEMPAFLSREA--QDLIHQLLRKNPADRLSLSSVL 251
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
 1-147 4.80e-17

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: 82.53  E-value: 4.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHypdyswsaQKRAMVEEEItrntTPMYRTPEIVdlysnfpIG 80
Cdd:cd07829   114 CHSHR--ILHRDLKPQNLLINRDGVLKLADFGLARAFGI--------PLRTYTHEVV----TLWYRAPEIL-------LG 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  81 EKQ-----DIWALGCILYLLCfRQHPF-----EDGAKLRI------------------VNGKYSIPV---NDTRyTVFH- 128
Cdd:cd07829   173 SKHystavDIWSVGCIFAELI-TGKPLfpgdsEIDQLFKIfqilgtpteeswpgvtklPDYKPTFPKwpkNDLE-KVLPr 250

                         170       180
                  ....*....|....*....|....*
gi 1331383559 129 ------DLIRAMLKVNPEERLSIAE 147
Cdd:cd07829   251 ldpegiDLLSKMLQYNPAKRISAKE 275
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
 1-154 7.41e-17

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: 81.55  E-value: 7.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCD------FGSATTISHypdyswsaqkrAMVeeeitrnTTPMYRTPEIV--D 72
Cdd:cd08224   120 MHSKR--IMHRDIKPANVFITANGVVKLGDlglgrfFSSKTTAAH-----------SLV-------GTPYYMSPERIreQ 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  73 LYsNFpigeKQDIWALGCILYLLCFRQHPFE-DGAKL-----RIVNGKYSiPVNDTRYTV-FHDLIRAMLKVNPEERLSI 145
Cdd:cd08224   180 GY-DF----KSDIWSLGCLLYEMAALQSPFYgEKMNLyslckKIEKCEYP-PLPADLYSQeLRDLVAACIQPDPEKRPDI 253


                  ....*....
gi 1331383559 146 AEVVRQLQE 154
Cdd:cd08224   254 SYVLDVAKR 262
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 8-147 9.04e-17

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: 81.70  E-value: 9.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQ---GTIKLCDFGSATTIS-HYPDYSWSAqkramveeeitrnTTPMYRTPEIVdlySNFPIGEKQ 83
Cdd:cd14086   121 IVHRDLKPENLLLASKskgAAVKLADFGLAIEVQgDQQAWFGFA-------------GTPGYLSPEVL---RKDPYGKPV 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  84 DIWALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSIPVN--DTRYTVFHDLIRAMLKVNPEERLSIAE 147
Cdd:cd14086   185 DIWACGVILYILLVGYPPFwdEDQHRLyaQIKAGAYDYPSPewDTVTPEAKDLINQMLTVNPAKRITAAE 254
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
 1-148 1.28e-16

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: 80.69  E-value: 1.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYpdyswsaqkramvEEEITRNT---TPMYRTPEIvdLYSNF 77
Cdd:cd14080   118 LHSLD--IAHRDLKCENILLDSNNNVKLSDFGFARLCPDD-------------DGDVLSKTfcgSAAYAAPEI--LQGIP 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  78 PIGEKQDIWALGCILYLLCFRQHPFEDG--AKL--RIVNGKYSIPVNDTRYTV-FHDLIRAMLKVNPEERLSIAEV 148
Cdd:cd14080   181 YDPKKYDIWSLGVILYIMLCGSMPFDDSniKKMlkDQQNRKVRFPSSVKKLSPeCKDLIDQLLEPDPTKRATIEEI 256
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 2-151 1.70e-16

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: 80.16  E-value: 1.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPPIIHRDLKVENLLLSNQGTI-KLCDFGSATTIShypdyswSAQKRAMVEeeitrnTTPMYRTPEIVDlysNFPIG 80
Cdd:cd08220   116 HVHSKQILHRDLKTQNILLNKKRTVvKIGDFGISKILS-------SKSKAYTVV------GTPCYISPELCE---GKPYN 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  81 EKQDIWALGCILYLLCFRQHPFEdGAKL-----RIVNGKYSiPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQ 151
Cdd:cd08220   180 QKSDIWALGCVLYELASLKRAFE-AANLpalvlKIMRGTFA-PISDRYSEELRHLILSMLHLDPNKRPTLSEIMAQ 253
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
 1-155 1.71e-16

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: 80.17  E-value: 1.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKP-PIIHRDLKVENLLLSNQGT-IKLCDFGSATTISHYpdyswsaqkramveeeITRNT-TPMYRTPEIVD--LYS 75
Cdd:cd14058   105 LHSMKPkALIHRDLKPPNLLLTNGGTvLKICDFGTACDISTH----------------MTNNKgSAAWMAPEVFEgsKYS 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  76 nfpigEKQDIWALGCILYLLCFRQHPFED--GAKLRIV----NGKySIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVV 149
Cdd:cd14058   169 -----EKCDVFSWGIILWEVITRRKPFDHigGPAFRIMwavhNGE-RPPLIKNCPKPIESLMTRCWSKDPEKRPSMKEIV 242


                  ....*.
gi 1331383559 150 RQLQEI 155
Cdd:cd14058   243 KIMSHL 248
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
 2-148 2.01e-16

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: 80.00  E-value: 2.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKppIIHRDLKVENLLLSNQGTIKLCDFGsattISHYpdyswsaqkraMVEEEITRNT--TPMYRTPEIVD--LYSnf 77
Cdd:cd14079   119 HRHM--VVHRDLKPENLLLDSNMNVKIADFG----LSNI-----------MRDGEFLKTScgSPNYAAPEVISgkLYA-- 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  78 piGEKQDIWALGCILY-LLCFRQhPFEDG--AKL--RIVNGKYSIPVNDTRYTVfhDLIRAMLKVNPEERLSIAEV 148
Cdd:cd14079   180 --GPEVDVWSCGVILYaLLCGSL-PFDDEhiPNLfkKIKSGIYTIPSHLSPGAR--DLIKRMLVVDPLKRITIPEI 250
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
 9-149 2.55e-16

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


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 79.73  E-value: 2.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswSAQKRAMVEEEITRNTTPMYRTPEIV--DLYsnfpIGEKQDIW 86
Cdd:cd14078   123 AHRDLKPENLLLDEDQNLKLIDFGLC-----------AKPKGGMDHHLETCCGSPAYAAPELIqgKPY----IGSEADVW 187

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559  87 ALGCILY-LLC-FRqhPFEDG--AKL--RIVNGKYSIPVNDTRYTVFhdLIRAMLKVNPEERLSIAEVV 149
Cdd:cd14078   188 SMGVLLYaLLCgFL--PFDDDnvMALyrKIQSGKYEEPEWLSPSSKL--LLDQMLQVDPKKRITVKELL 252
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
 1-149 3.41e-16

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


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 79.59  E-value: 3.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIshypDYSWSAQKramveeeiTRNTTPMYRTPEIVDLYS-NFPI 79
Cdd:cd14187   123 LHRNR--VIHRDLKLGNLFLNDDMEVKIGDFGLATKV----EYDGERKK--------TLCGTPNYIAPEVLSKKGhSFEV 188

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  80 gekqDIWALGCILYLLCFRQHPFEDG----AKLRIVNGKYSIP--VNdtryTVFHDLIRAMLKVNPEERLSIAEVV 149
Cdd:cd14187   189 ----DIWSIGCIMYTLLVGKPPFETSclkeTYLRIKKNEYSIPkhIN----PVAASLIQKMLQTDPTARPTINELL 256
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 1-150 6.15e-16

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: 78.62  E-value: 6.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNqGTIKLCDFGSATTISHYPDyswsaqkramveEEITRNTTPMYRTPEIVDL--YSNfp 78
Cdd:cd08222   122 MHERR--ILHRDLKAKNIFLKN-NVIKVGDFGISRILMGTSD------------LATTFTGTPYYMSPEVLKHegYNS-- 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331383559  79 igeKQDIWALGCILYLLCFRQHPFeDGAKL-----RIVNGKY-SIPvnDTRYTVFHDLIRAMLKVNPEERLSIAEVVR 150
Cdd:cd08222   185 ---KSDIWSLGCILYEMCCLKHAF-DGQNLlsvmyKIVEGETpSLP--DKYSKELNAIYSRMLNKDPALRPSAAEILK 256
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
 1-150 6.70e-16

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: 78.60  E-value: 6.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGsattISHYPDyswSAQKRAMVEeeiTRNTTPMYRTPEIvdLYSNFPIG 80
Cdd:cd14663   116 CHSRG--VFHRDLKPENLLLDEDGNLKISDFG----LSALSE---QFRQDGLLH---TTCGTPNYVAPEV--LARRGYDG 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  81 EKQDIWALGCILYLLCFRQHPFEDG--AKL--RIVNGKYSIPvndtRY--TVFHDLIRAMLKVNPEERLSIAEVVR 150
Cdd:cd14663   182 AKADIWSCGVILFVLLAGYLPFDDEnlMALyrKIMKGEFEYP----RWfsPGAKSLIKRILDPNPSTRITVEQIMA 253
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
 8-149 8.02e-16

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


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 79.04  E-value: 8.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLL---SNQGTIKLCDFGSAT------TISHYPDYSWS-----AQKRAMVEeeitRNTTPMYRTPEIVDl 73
Cdd:cd14171   130 IAHRDLKPENLLLkdnSEDAPIKLCDFGFAKvdqgdlMTPQFTPYYVApqvleAQRRHRKE----RSGIPTSPTPYTYD- 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  74 ysnfpigEKQDIWALGCILY-LLC-----FRQHP---FEDGAKLRIVNGKYSIPVNDTRYT--VFHDLIRAMLKVNPEER 142
Cdd:cd14171   205 -------KSCDMWSLGVIIYiMLCgyppfYSEHPsrtITKDMKRKIMTGSYEFPEEEWSQIseMAKDIVRKLLCVDPEER 277


                  ....*..
gi 1331383559 143 LSIAEVV 149
Cdd:cd14171   278 MTIEEVL 284
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
 1-143 1.10e-15

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: 78.04  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswSAQKramveeEITRNTTPMYRTPEIVdlySNFPIG 80
Cdd:cd05572   109 LHSRG--IIYRDLKPENLLLDSNGYVKLVDFGFAKKLG-------SGRK------TWTFCGTPEYVAPEII---LNKGYD 170

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331383559  81 EKQDIWALGCILY-LLCFRQhPF----EDGAKL--RIVNGKYSI--PVNDTRytVFHDLIRAMLKVNPEERL 143
Cdd:cd05572   171 FSVDYWSLGILLYeLLTGRP-PFggddEDPMKIynIILKGIDKIefPKYIDK--NAKNLIKQLLRRNPEERL 239
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
 8-148 1.19e-15

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: 77.69  E-value: 1.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGsATTISHYPDYSWsaqkramveeeiTRNTTPMYRTPEIVDlysNFP-IGEKQDIW 86
Cdd:cd14161   123 IVHRDLKLENILLDANGNIKIADFG-LSNLYNQDKFLQ------------TYCGSPLYASPEIVN---GRPyIGPEVDSW 186

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  87 ALGCILYLLCFRQHPFE--DGAKL--RIVNGKYSIPvndTRYTVFHDLIRAMLKVNPEERLSIAEV 148
Cdd:cd14161   187 SLGVLLYILVHGTMPFDghDYKILvkQISSGAYREP---TKPSDACGLIRWLLMVNPERRATLEDV 249
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
 8-148 2.51e-15

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: 76.98  E-value: 2.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLL----SNQGTIKLCDFGSATtishypdyswsaqkraMVEEEI-TRNTTPMYRTPEIVdlySNFPIGEK 82
Cdd:cd14095   119 IVHRDIKPENLLVveheDGSKSLKLADFGLAT----------------EVKEPLfTVCGTPTYVAPEIL---AETGYGLK 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331383559  83 QDIWALGCILY-LLC----FRQhPFEDGAKL--RIVNGKYSI--PVNDTRYTVFHDLIRAMLKVNPEERLSIAEV 148
Cdd:cd14095   180 VDIWAAGVITYiLLCgfppFRS-PDRDQEELfdLILAGEFEFlsPYWDNISDSAKDLISRMLVVDPEKRYSAGQV 253
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
 1-150 2.96e-15

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: 76.96  E-value: 2.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATtishypDYSWSAQKRAMVEEEItRNTTPmYRTPEIvdLYSNFPIG 80
Cdd:cd13994   114 LHSHG--IAHRDLKPENILLDEDGVLKLTDFGTAE------VFGMPAEKESPMSAGL-CGSEP-YMAPEV--FTSGSYDG 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  81 EKQDIWALGCILYLLCFRQHPFEDGAK-----------LRIVNGKYSIPVNDTRYTVfHDLIRAMLKVNPEERLSIAEVV 149
Cdd:cd13994   182 RAVDVWSCGIVLFALFTGRFPWRSAKKsdsaykayeksGDFTNGPYEPIENLLPSEC-RRLIYRMLHPDPEKRITIDEAL 260


                  .
gi 1331383559 150 R 150
Cdd:cd13994   261 N 261
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
 8-147 6.92e-15

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: 75.77  E-value: 6.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQG--TIKLCDFGSAttiSHYPDYSWS-AQKRAmveeeitrnttpmYRTPEIVdlySNFPIGEKQD 84
Cdd:cd14133   123 LIHCDLKPENILLASYSrcQIKIIDFGSS---CFLTQRLYSyIQSRY-------------YRAPEVI---LGLPYDEKID 183

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331383559  85 IWALGCILYLLCFRqHPFEDGAKL-----RIVNGKYSIPV-----NDTRYTVFHDLIRAMLKVNPEERLSIAE 147
Cdd:cd14133   184 MWSLGCILAELYTG-EPLFPGASEvdqlaRIIGTIGIPPAhmldqGKADDELFVDFLKKLLEIDPKERPTASQ 255
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
 1-151 7.14e-15

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: 76.03  E-value: 7.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSwsaqkrAMVEeeiTRnttpMYRTPEIV--DLYSNFP 78
Cdd:cd07830   115 IHKHG--FFHRDLKPENLLVSGPEVVKIADFGLAREIRSRPPYT------DYVS---TR----WYRAPEILlrSTSYSSP 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  79 IgekqDIWALGCI-------------------LYLLC-----FRQHPFEDGAKL-RIVNGKY----SIPVND---TRYTV 126
Cdd:cd07830   180 V----DIWALGCImaelytlrplfpgsseidqLYKICsvlgtPTKQDWPEGYKLaSKLGFRFpqfaPTSLHQlipNASPE 255

                         170       180
                  ....*....|....*....|....*
gi 1331383559 127 FHDLIRAMLKVNPEERLSIAEVVRQ 151
Cdd:cd07830   256 AIDLIKDMLRWDPKKRPTASQALQH 280
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
 8-149 1.02e-14

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: 75.14  E-value: 1.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLS-NQGTIKLCDFGsattishypdYSWSAQKRAMVEeeiTRNTTPMYRTPEIV--DLYSnfpiGEKQD 84
Cdd:cd14074   124 VVHRDLKPENVVFFeKQGLVKLTDFG----------FSNKFQPGEKLE---TSCGSLAYSAPEILlgDEYD----APAVD 186

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331383559  85 IWALGCILYLLCFRQHPFEDGAK----LRIVNGKYSIP--VNDTrytvFHDLIRAMLKVNPEERLSIAEVV 149
Cdd:cd14074   187 IWSLGVILYMLVCGQPPFQEANDsetlTMIMDCKYTVPahVSPE----CKDLIRRMLIRDPKKRASLEEIE 253
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
 2-152 1.04e-14

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: 75.41  E-value: 1.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKppIIHRDLKVENLLLSNQ-GTIKLCDFGSATTISHYPDYSWSAQKRAM--VEEEITRNTTPMYRTPEivdLYSNFP 78
Cdd:cd13996   124 HSKG--IVHRDLKPSNIFLDNDdLQVKIGDFGLATSIGNQKRELNNLNNNNNgnTSNNSVGIGTPLYASPE---QLDGEN 198

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331383559  79 IGEKQDIWALGCILY-LLCFRQHPFEdgaKLRIVNG--KYSIPVN-DTRYTVFHDLIRAMLKVNPEERLSIAEVVRQL 152
Cdd:cd13996   199 YNEKADIYSLGIILFeMLHPFKTAME---RSTILTDlrNGILPESfKAKHPKEADLIQSLLSKNPEERPSAEQLLRSL 273
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
 8-150 1.38e-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: 74.82  E-value: 1.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGT--IKLCDFGSATTIshypdyswsaQKRAMVEeeiTRNTTPMYRTPEIV--------DLYSNf 77
Cdd:cd14098   122 ITHRDLKPENILITQDDPviVKISDFGLAKVI----------HTGTFLV---TFCGTMAYLAPEILmskeqnlqGGYSN- 187

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559  78 pigeKQDIWALGCILYLLCFRQHPFEDGAKL----RIVNGKYSI-PVNDTRYT-VFHDLIRAMLKVNPEERLSIAEVVR 150
Cdd:cd14098   188 ----LVDMWSVGCLVYVMLTGALPFDGSSQLpvekRIRKGRYTQpPLVDFNISeEAIDFILRLLDVDPEKRMTAAQALD 262
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 2-151 1.56e-14

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


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 74.39  E-value: 1.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswsaQKRAMVEEEItrnTTPMYRTPEIVdlySNFPIGE 81
Cdd:cd08221   116 HIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLD---------SESSMAESIV---GTPYYMSPELV---QGVKYNF 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331383559  82 KQDIWALGCILYLLCFRQHPFEDGAKLR----IVNGKYSipVNDTRYTV-FHDLIRAMLKVNPEERLSIAEVVRQ 151
Cdd:cd08221   181 KSDIWAVGCVLYELLTLKRTFDATNPLRlavkIVQGEYE--DIDEQYSEeIIQLVHDCLHQDPEDRPTAEELLER 253
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
 9-151 1.73e-14

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: 75.78  E-value: 1.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSAT------TISHYPDYSWSAQKRAMVEEEITRNT-----------TPMYRTPEIv 71
Cdd:cd05573   123 IHRDIKPDNILLDADGHIKLADFGLCTkmnksgDRESYLNDSVNTLFQDNVLARRRPHKqrrvraysavgTPDYIAPEV- 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  72 dLYSNfPIGEKQDIWALGCILYLLCFRQHPFED----GAKLRIVNGKYS--IPVNDTRYTVFHDLIRAMLKvNPEERLSI 145
Cdd:cd05573   202 -LRGT-GYGPECDWWSLGVILYEMLYGFPPFYSdslvETYSKIMNWKESlvFPDDPDVSPEAIDLIRRLLC-DPEDRLGS 278


                  ....*.
gi 1331383559 146 AEVVRQ 151
Cdd:cd05573   279 AEEIKA 284
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
 1-148 1.73e-14

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


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 75.00  E-value: 1.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHypdyswsaqkramvEEEITRNT--TPMYRTPEIVDLYSNFP 78
Cdd:cd14199   142 LHYQK--IIHRDVKPSNLLVGEDGHIKIADFGVSNEFEG--------------SDALLTNTvgTPAFMAPETLSETRKIF 205

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331383559  79 IGEKQDIWALGCILYLLCFRQHPFEDGAKL----RIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEV 148
Cdd:cd14199   206 SGKALDVWAMGVTLYCFVFGQCPFMDERILslhsKIKTQPLEFPDQPDISDDLKDLLFRMLDKNPESRISVPEI 279
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
 2-92 3.76e-14

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: 73.89  E-value: 3.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDyswsaqkRAMVEEEITRnttpMYRTPEIvdLYSNFPIGE 81
Cdd:cd07833   117 HSHN--IIHRDIKPENILVSESGVLKLCDFGFARALTARPA-------SPLTDYVATR----WYRAPEL--LVGDTNYGK 181

                          90
                  ....*....|.
gi 1331383559  82 KQDIWALGCIL 92
Cdd:cd07833   182 PVDVWAIGCIM 192
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
 8-144 3.90e-14

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: 73.85  E-value: 3.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIShyPDyswsaqkramveeEITRNT--TPMYRTPEIV--DLYSNFP-IGEK 82
Cdd:cd14181   137 IVHRDLKPENILLDDQLHIKLSDFGFSCHLE--PG-------------EKLRELcgTPGYLAPEILkcSMDETHPgYGKE 201

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331383559  83 QDIWALGCILYLLCFRQHPFEDGAKL----RIVNGKY--SIPVNDTRYTVFHDLIRAMLKVNPEERLS 144
Cdd:cd14181   202 VDLWACGVILFTLLAGSPPFWHRRQMlmlrMIMEGRYqfSSPEWDDRSSTVKDLISRLLVVDPEIRLT 269
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
 8-147 4.03e-14

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: 73.54  E-value: 4.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQ-GTIKLCDFGSATTISHYPDYSWSAQKramveeeitrnttpmYRTPEIVDlySNFPIGE----- 81
Cdd:cd13993   128 IYHRDIKPENILLSQDeGTVKLCDFGLATTEKISMDFGVGSEF---------------YMAPECFD--EVGRSLKgypca 190

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331383559  82 KQDIWALGCILYLLCFRQHPF------EDGAKLRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAE 147
Cdd:cd13993   191 AGDIWSLGIILLNLTFGRNPWkiasesDPIFYDYYLNSPNLFDVILPMSDDFYNLLRQIFTVNPNNRILLPE 262
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
 8-147 4.45e-14

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: 73.03  E-value: 4.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLS---NQGTIKLCDFGSATTIshypdyswsaQKRAMVEeeiTRNTTPMYRTPEIVdLYSNFpiGEKQD 84
Cdd:cd14009   113 IIHRDLKPQNLLLStsgDDPVLKIADFGFARSL----------QPASMAE---TLCGSPLYMAPEIL-QFQKY--DAKAD 176

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559  85 IWALGCILYLLCFRQHPFEDGAKL----RIVNGKYSIPVNDTRYTVFH--DLIRAMLKVNPEERLSIAE 147
Cdd:cd14009   177 LWSVGAILFEMLVGKPPFRGSNHVqllrNIERSDAVIPFPIAAQLSPDckDLLRRLLRRDPAERISFEE 245
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
 8-150 5.14e-14

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: 72.94  E-value: 5.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswSAQKRAmveeeiTRNTTPMYRTPEIVD--LYSnfpiGEKQDI 85
Cdd:cd14072   120 IVHRDLKAENLLLDADMNIKIADFGFSNEFT-------PGNKLD------TFCGSPPYAAPELFQgkKYD----GPEVDV 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  86 WALGCILYLLCFRQHPFeDGAKL-----RIVNGKYSIPVNDTryTVFHDLIRAMLKVNPEERLSIAEVVR 150
Cdd:cd14072   183 WSLGVILYTLVSGSLPF-DGQNLkelreRVLRGKYRIPFYMS--TDCENLLKKFLVLNPSKRGTLEQIMK 249
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
 8-150 6.21e-14

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: 72.95  E-value: 6.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGT---IKLCDFGSATTishypdyswsaqkRAMVEEEITRNT--TPMYRTPEIVdlySNFPIGEK 82
Cdd:cd14087   118 ITHRDLKPENLLYYHPGPdskIMITDFGLAST-------------RKKGPNCLMKTTcgTPEYIAPEIL---LRKPYTQS 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331383559  83 QDIWALGCILYLLCFRQHPFEDGAKLR----IVNGKYSI---PVNDTRyTVFHDLIRAMLKVNPEERLSIAEVVR 150
Cdd:cd14087   182 VDMWAVGVIAYILLSGTMPFDDDNRTRlyrqILRAKYSYsgePWPSVS-NLAKDFIDRLLTVNPGERLSATQALK 255
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
 8-173 1.04e-13

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: 72.51  E-value: 1.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTISHypdyswSAQKRamveeeITRNTTPMYRTPEIV---DLYSnfpigEKQD 84
Cdd:cd06917   122 IIHRDIKAANILVTNTGNVKLCDFGVAASLNQ------NSSKR------STFVGTPYWMAPEVItegKYYD-----TKAD 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  85 IWALGCILYLLCFRQHPFEDGAKLRIVN--GKYSIP-VNDTRY-TVFHDLIRAMLKVNPEERLSIAEVVRqLQEIAAARN 160
Cdd:cd06917   185 IWSLGITTYEMATGNPPYSDVDALRAVMliPKSKPPrLEGNGYsPLLKEFVAACLDEEPKDRLSADELLK-SKWIKQHSK 263

                         170
                  ....*....|...
gi 1331383559 161 VnPKAPITELLEQ 173
Cdd:cd06917   264 T-PTSVLKELISR 275
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
 8-149 1.09e-13

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: 72.96  E-value: 1.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLS---NQGTIKLCDFGSATTIshyPDYSWSAQKRAmveeeitrnTTPMYRTPEIVdlySNFPIGEKQD 84
Cdd:cd14094   130 IIHRDVKPHCVLLAskeNSAPVKLGGFGVAIQL---GESGLVAGGRV---------GTPHFMAPEVV---KREPYGKPVD 194

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331383559  85 IWALGCILYLLCFRQHPFEdGAKLR----IVNGKYSI--PVNDTRYTVFHDLIRAMLKVNPEERLSIAEVV 149
Cdd:cd14094   195 VWGCGVILFILLSGCLPFY-GTKERlfegIIKGKYKMnpRQWSHISESAKDLVRRMLMLDPAERITVYEAL 264
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
 1-173 1.25e-13

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: 72.28  E-value: 1.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKPpiIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswSAQKRamveeeitRNT---TPMYRTPEIVdlySNF 77
Cdd:cd06609   114 LHSEGK--IHRDIKAANILLSEEGDVKLADFGVSGQLT-------STMSK--------RNTfvgTPFWMAPEVI---KQS 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  78 PIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVngkYSIPVN------DTRYT-VFHDLIRAMLKVNPEERLSiAEVVR 150
Cdd:cd06609   174 GYDEKADIWSLGITAIELAKGEPPLSDLHPMRVL---FLIPKNnppsleGNKFSkPFKDFVELCLNKDPKERPS-AKELL 249

                         170       180
                  ....*....|....*....|...
gi 1331383559 151 QLQEIAAARnvnPKAPITELLEQ 173
Cdd:cd06609   250 KHKFIKKAK---KTSYLTLLIER 269
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
 8-147 1.49e-13

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: 71.56  E-value: 1.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIshypdyswSAQKRAMVEEEITRNT-TPMYRTPEIVDLYSNFPIGEKQDIW 86
Cdd:cd06626   120 IVHRDIKPANIFLDSNGLIKLGDFGSAVKL--------KNNTTTMAPGEVNSLVgTPAYMAPEVITGNKGEGHGRAADIW 191

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331383559  87 ALGCILYLLCFRQHP-----------FEDGAKlrivnGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAE 147
Cdd:cd06626   192 SLGCVVLEMATGKRPwseldnewaimYHVGMG-----HKPPIPDSLQLSPEGKDFLSRCLESDPKKRPTASE 258
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
 8-149 1.51e-13

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: 71.87  E-value: 1.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswSAQKRamveEEITrnTTPMYRTPEIVD--LYSNFP-IGEKQD 84
Cdd:cd14182   131 IVHRDLKPENILLDDDMNIKLTDFGFSCQLD-------PGEKL----REVC--GTPGYLAPEIIEcsMDDNHPgYGKEVD 197

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331383559  85 IWALGCILYLLCFRQHPF---EDGAKLR-IVNGKYSI--PVNDTRYTVFHDLIRAMLKVNPEERLSIAEVV 149
Cdd:cd14182   198 MWSTGVIMYTLLAGSPPFwhrKQMLMLRmIMSGNYQFgsPEWDDRSDTVKDLISRFLVVQPQKRYTAEEAL 268
Pkinase pfam00069
Protein kinase domain;
62-150 2.18e-13

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 70.35  E-value: 2.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  62 TPMYRTPEIVdlySNFPIGEKQDIWALGCILYLLCFRQHPF----EDGAKLRIVNGKYSIPVNDTRYT-VFHDLIRAMLK 136
Cdd:pfam00069 123 TPWYMAPEVL---GGNPYGPKVDVWSLGCILYELLTGKPPFpginGNEIYELIIDQPYAFPELPSNLSeEAKDLLKKLLK 199

                          90
                  ....*....|....
gi 1331383559 137 VNPEERLSIAEVVR 150
Cdd:pfam00069 200 KDPSKRLTATQALQ 213
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
 8-143 2.40e-13

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


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 71.86  E-value: 2.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGsattishypdyswsaqkraMVEEEI----TRNT---TPMYRTPEIV--DLYsNFP 78
Cdd:cd05570   117 IIYRDLKLDNVLLDAEGHIKIADFG-------------------MCKEGIwggnTTSTfcgTPDYIAPEILreQDY-GFS 176

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559  79 IgekqDIWALGCILYLLCFRQHPF----EDGAKLRIVNGKYSIPVNDTRYTVfhDLIRAMLKVNPEERL 143
Cdd:cd05570   177 V----DWWALGVLLYEMLAGQSPFegddEDELFEAILNDEVLYPRWLSREAV--SILKGLLTKDPARRL 239
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
 8-150 2.40e-13

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


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 70.97  E-value: 2.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTISHypdyswSAQKRAMVEEeiTRNTTPMYRTPEIVDLYSNFPigEKQDIWA 87
Cdd:cd14165   123 IVHRDLKCENLLLDKDFNIKLTDFGFSKRCLR------DENGRIVLSK--TFCGSAAYAAPEVLQGIPYDP--RIYDIWS 192

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331383559  88 LGCILYLLCFRQHPFEDG---AKLRI-VNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVR 150
Cdd:cd14165   193 LGVILYIMVCGSMPYDDSnvkKMLKIqKEHRVRFPRSKNLTSECKDLIYRLLQPDVSQRLCIDEVLS 259
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
 1-148 2.89e-13

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 71.13  E-value: 2.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSattishypdyswSAQKRAMVEEEITRNTTPMYRTPE-IVDLYSNFPi 79
Cdd:cd14200   140 LHYQK--IVHRDIKPSNLLLGDDGHVKIADFGV------------SNQFEGNDALLSSTAGTPAFMAPEtLSDSGQSFS- 204

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331383559  80 GEKQDIWALGCILYLLCFRQHPFEDGAKL----RIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEV 148
Cdd:cd14200   205 GKALDVWAMGVTLYCFVYGKCPFIDEFILalhnKIKNKPVEFPEEPEISEELKDLILKMLDKNPETRITVPEI 277
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
 1-151 2.90e-13

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


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 70.81  E-value: 2.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsAQKRAMVEEEITRNTTPMYRTPEIVDLYSNfpiG 80
Cdd:cd14188   117 LHEQE--ILHRDLKLGNFFINENMELKVGDFGLA------------ARLEPLEHRRRTICGTPNYLSPEVLNKQGH---G 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  81 EKQDIWALGCILYLLCFRQHPFEDgAKLR-----IVNGKYSIPvnDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQ 151
Cdd:cd14188   180 CESDIWALGCVMYTMLLGRPPFET-TNLKetyrcIREARYSLP--SSLLAPAKHLIASMLSKNPEDRPSLDEIIRH 252
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
 1-173 3.02e-13

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: 71.22  E-value: 3.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSattishypdyswSAQKRAMVEEEITRNTTPMYRTPEIV--DLYSNFP 78
Cdd:cd06644   126 LHSMK--IIHRDLKAGNVLLTLDGDIKLADFGV------------SAKNVKTLQRRDSFIGTPYWMAPEVVmcETMKDTP 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  79 IGEKQDIWALGCILYLLCFRQHPFEDGAKLRIV--NGKYSIPVNDT--RYTV-FHDLIRAMLKVNPEERLSIAevvrQLQ 153
Cdd:cd06644   192 YDYKADIWSLGITLIEMAQIEPPHHELNPMRVLlkIAKSEPPTLSQpsKWSMeFRDFLKTALDKHPETRPSAA----QLL 267

                         170       180
                  ....*....|....*....|
gi 1331383559 154 EIAAARNVNPKAPITELLEQ 173
Cdd:cd06644   268 EHPFVSSVTSNRPLRELVAE 287
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
 8-149 3.21e-13

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: 70.94  E-value: 3.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGsattISHYpdYSWSAQKRamveeeiTRNTTPMYRTPEIVDlySNFPIGEKQDIWA 87
Cdd:cd14077   134 IVHRDLKIENILISKSGNIKIIDFG----LSNL--YDPRRLLR-------TFCGSLYFAAPELLQ--AQPYTGPEVDVWS 198

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  88 LGCILYLLCFRQHPFED----GAKLRIVNGKYSIPVNDTRYTVfhDLIRAMLKVNPEERLSIAEVV 149
Cdd:cd14077   199 FGVVLYVLVCGKVPFDDenmpALHAKIKKGKVEYPSYLSSECK--SLISRMLVVDPKKRATLEQVL 262
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
 1-150 3.69e-13

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: 70.51  E-value: 3.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShYPDYSWSAQKramveeeitrntTPMYRTPEIVDlYSNFPIG 80
Cdd:cd06632   118 LHSRN--TVHRDIKGANILVDTNGVVKLADFGMAKHVE-AFSFAKSFKG------------SPYWMAPEVIM-QKNSGYG 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331383559  81 EKQDIWALGCILYLLCFRQHPFED----GAKLRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVR 150
Cdd:cd06632   182 LAVDIWSLGCTVLEMATGKPPWSQyegvAAIFKIGNSGELPPIPDHLSPDAKDFIRLCLQRDPEDRPTASQLLE 255
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
 8-147 5.39e-13

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: 70.07  E-value: 5.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLS---NQGTIKLCDFGSATTISHypdyswSAQKRAMVeeeitrnTTPMYRTPEIVdlySNFPIGEKQD 84
Cdd:cd14106   129 IVHLDLKPQNILLTsefPLGDIKLCDFGISRVIGE------GEEIREIL-------GTPDYVAPEIL---SYEPISLATD 192

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331383559  85 IWALGCILYLLCFRQHPFEDGAK----LRIVNGKYSIPVNdtrytVFH-------DLIRAMLKVNPEERLSIAE 147
Cdd:cd14106   193 MWSIGVLTYVLLTGHSPFGGDDKqetfLNISQCNLDFPEE-----LFKdvsplaiDFIKRLLVKDPEKRLTAKE 261
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
 8-143 5.40e-13

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: 70.69  E-value: 5.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIshyPDYSWsaqkramveeeiTRNTTPMYRTPEIVdlySNFPIGEKQDIWA 87
Cdd:cd05580   122 IVYRDLKPENLLLDSDGHIKITDFGFAKRV---KDRTY------------TLCGTPEYLAPEII---LSKGHGKAVDWWA 183

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  88 LGCILYLLCFRQHPFEDGAKL----RIVNGKYSIPVNdtRYTVFHDLIRAMLKVNPEERL 143
Cdd:cd05580   184 LGILIYEMLAGYPPFFDENPMkiyeKILEGKIRFPSF--FDPDAKDLIKRLLVVDLTKRL 241
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
 8-162 6.92e-13

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: 69.82  E-value: 6.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTI---SHYPDYSwsaqkramveeeitrnTTPMYRTPEIVDlysNFPIGEKQD 84
Cdd:cd05611   118 IIHRDIKPENLLIDQTGHLKLTDFGLSRNGlekRHNKKFV----------------GTPDYLAPETIL---GVGDDKMSD 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  85 IWALGCILYLLCFRQHPFE----DGAKLRIVNGKYSIP--VNDTRYTVFHDLIRAMLKVNPEERLSiAEVVRQLQEIAAA 158
Cdd:cd05611   179 WWSLGCVIFEFLFGYPPFHaetpDAVFDNILSRRINWPeeVKEFCSPEAVDLINRLLCMDPAKRLG-ANGYQEIKSHPFF 257


                  ....
gi 1331383559 159 RNVN 162
Cdd:cd05611   258 KSIN 261
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
 1-147 7.53e-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: 69.22  E-value: 7.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQG--TIKLCDFGSATTISHypdyswsaqkramveEEITRN--TTPMYRTPEIVDLYsn 76
Cdd:cd14006   105 LHNHH--ILHLDLKPENILLADRPspQIKIIDFGLARKLNP---------------GEELKEifGTPEFVAPEIVNGE-- 165

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331383559  77 fPIGEKQDIWALGCILYLLCFRQHPF-EDGA---KLRIVNGKYSIPvNDTRYTVFH---DLIRAMLKVNPEERLSIAE 147
Cdd:cd14006   166 -PVSLATDMWSIGVLTYVLLSGLSPFlGEDDqetLANISACRVDFS-EEYFSSVSQeakDFIRKLLVKEPRKRPTAQE 241
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
 8-150 9.49e-13

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: 69.24  E-value: 9.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSA---TTISHYPDYSWSAQKRAMVEEEITR-NTTPMYRTPEivdLYSNFPIGEKQ 83
Cdd:cd14010   115 IIYCDLKPSNILLDGNGTLKLSDFGLArreGEILKELFGQFSDEGNVNKVSKKQAkRGTPYYMAPE---LFQGGVHSFAS 191

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331383559  84 DIWALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSIPVNDTRY---TVFHDLIRAMLKVNPEERLSIAEVVR 150
Cdd:cd14010   192 DLWALGCVLYEMFTGKPPFvaESFTELveKILNEDPPPPPPKVSSkpsPDFKSLLKGLLEKDPAKRLSWDELVK 265
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
 1-147 1.09e-12

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: 68.79  E-value: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswsaqkramvEEEITRNT---TPMYRTPEIVDLYsnf 77
Cdd:cd06627   115 LHEQG--VIHRDIKGANILTTKDGLVKLADFGVATKLN---------------EVEKDENSvvgTPYWMAPEVIEMS--- 174

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331383559  78 PIGEKQDIWALGCILYLLCFRQHPFED----GAKLRIVNGKYS-IPVNDTryTVFHDLIRAMLKVNPEERLSIAE 147
Cdd:cd06627   175 GVTTASDIWSVGCTVIELLTGNPPYYDlqpmAALFRIVQDDHPpLPENIS--PELRDFLLQCFQKDPTLRPSAKE 247
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
 1-149 1.29e-12

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: 68.56  E-value: 1.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswsaqKRAMVEEEITRnttpmYRTPEIvdLYSNFPIG 80
Cdd:cd13997   119 IHSKG--IVHLDIKPDNIFISNKGTCKIGDFGLATRLE----------TSGDVEEGDSR-----YLAPEL--LNENYTHL 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331383559  81 EKQDIWALGCILYLLCfRQHPFEDGAKL--RIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVV 149
Cdd:cd13997   180 PKADIFSLGVTVYEAA-TGEPLPRNGQQwqQLRQGKLPLPPGLVLSQELTRLLKVMLDPDPTRRPTADQLL 249
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
 8-148 1.79e-12

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: 68.47  E-value: 1.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLL--SNQGTIKLCDFG-SATTISHypdyswsAQKRAMVeeeitrnTTPMYRTPEIVdLYSNFPiGEKQD 84
Cdd:cd14665   117 ICHRDLKLENTLLdgSPAPRLKICDFGySKSSVLH-------SQPKSTV-------GTPAYIAPEVL-LKKEYD-GKIAD 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331383559  85 IWALGCILYLLCFRQHPFEDGAK--------LRIVNGKYSIPvNDTRYTV-FHDLIRAMLKVNPEERLSIAEV 148
Cdd:cd14665   181 VWSCGVTLYVMLVGAYPFEDPEEprnfrktiQRILSVQYSIP-DYVHISPeCRHLISRIFVADPATRITIPEI 252
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
 8-147 1.99e-12

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: 68.75  E-value: 1.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIShYPDyswsaqkRAMVEEEITRnttpMYRTPEIvdLYsnfpiGEKQ---- 83
Cdd:cd07841   123 ILHRDLKPNNLLIASDGVLKLADFGLARSFG-SPN-------RKMTHQVVTR----WYRAPEL--LF-----GARHygvg 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  84 -DIWALGCILYLLCFRQhPFEDG-------AKLRIVNG-------------KYSIPVNDTRYTVFH-----------DLI 131
Cdd:cd07841   184 vDMWSVGCIFAELLLRV-PFLPGdsdidqlGKIFEALGtpteenwpgvtslPDYVEFKPFPPTPLKqifpaasddalDLL 262

                         170
                  ....*....|....*.
gi 1331383559 132 RAMLKVNPEERLSIAE 147
Cdd:cd07841   263 QRLLTLNPNKRITARQ 278
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
 1-149 2.44e-12

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: 68.36  E-value: 2.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIS--HYPDYSwsaqkramveeeiTRNTTPMYRTPEIVdlysnfp 78
Cdd:cd07840   120 LHSNG--ILHRDIKGSNILINNDGVLKLADFGLARPYTkeNNADYT-------------NRVITLWYRPPELL------- 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  79 IGEKQ-----DIWALGCIL----------------------YLLC----------FRQHPFEDGAKL-----RIVNGKYS 116
Cdd:cd07840   178 LGATRygpevDMWSVGCILaelftgkpifqgkteleqlekiFELCgspteenwpgVSDLPWFENLKPkkpykRRLREVFK 257

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1331383559 117 IPVNdtryTVFHDLIRAMLKVNPEERLSIAEVV 149
Cdd:cd07840   258 NVID----PSALDLLDKLLTLDPKKRISADQAL 286
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
 8-143 2.90e-12

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 68.69  E-value: 2.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswsaqkramvEEEITRNTTPMYRTPEIVDLYSNfpiGEKQDIWA 87
Cdd:PTZ00263  139 IIYRDLKPENLLLDNKGHVKVTDFGFAKKVP---------------DRTFTLCGTPEYLAPEVIQSKGH---GKAVDWWT 200

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331383559  88 LGCILYLLCFRQHPFEDGAKLR----IVNGKYSIPV-NDTRYtvfHDLIRAMLKVNPEERL 143
Cdd:PTZ00263  201 MGVLLYEFIAGYPPFFDDTPFRiyekILAGRLKFPNwFDGRA---RDLVKGLLQTDHTKRL 258
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
 5-153 3.29e-12

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 68.20  E-value: 3.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   5 KPPIIHRDLKVENLLLsNQGTIKLcdfgsatTISHYpdyswSAQKRAMVEEEITRNT--TPMYRTPeivDLYSNFP-IGE 81
Cdd:cd13974   150 KKNIVHRDLKLGNMVL-NKRTRKI-------TITNF-----CLGKHLVSEDDLLKDQrgSPAYISP---DVLSGKPyLGK 213

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559  82 KQDIWALGCILYLLCFRQHPFEDGA--KL--RIVNGKYSIPvNDTRY---TVfhDLIRAMLKVNPEERLSIAEVVRQLQ 153
Cdd:cd13974   214 PSDMWALGVVLFTMLYGQFPFYDSIpqELfrKIKAAEYTIP-EDGRVsenTV--CLIRKLLVLNPQKRLTASEVLDSLE 289
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
 8-144 3.68e-12

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: 67.28  E-value: 3.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTishypdysWSAQKRAmveeeITRNTTPMYRTPEIVDL-YSNFPIgekqDIW 86
Cdd:cd05578   121 IIHRDIKPDNILLDEQGHVHITDFNIATK--------LTDGTLA-----TSTSGTKPYMAPEVFMRaGYSFAV----DWW 183

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331383559  87 ALGCILYLLCFRQHPFE-------DGAKLRIVNGKYSIPVNDTRYTVfhDLIRAMLKVNPEERLS 144
Cdd:cd05578   184 SLGVTAYEMLRGKRPYEihsrtsiEEIRAKFETASVLYPAGWSEEAI--DLINKLLERDPQKRLG 246
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
 2-163 4.10e-12

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


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 67.58  E-value: 4.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATtisHYPdyswSAQKRAMVeeeitrnTTPMYRTPEIVDLYSNfpiGE 81
Cdd:cd14117   123 HEKK--VIHRDIKPENLLMGYKGELKIADFGWSV---HAP----SLRRRTMC-------GTLDYLPPEMIEGRTH---DE 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  82 KQDIWALGCILYLLCFRQHPFEDGAKL----RIVNGKYSIPVNDTRYTvfHDLIRAMLKVNPEERLSIAEVVRQLQEIAA 157
Cdd:cd14117   184 KVDLWCIGVLCYELLVGMPPFESASHTetyrRIVKVDLKFPPFLSDGS--RDLISKLLRYHPSERLPLKGVMEHPWVKAN 261


                  ....*.
gi 1331383559 158 ARNVNP 163
Cdd:cd14117   262 SRRVLP 267
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
 8-151 4.60e-12

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: 67.26  E-value: 4.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIShyPDYSwsaQKRAMVeeeitrnTTPMYRTPEIVdlySNFPIGEKQDIWA 87
Cdd:cd06647   124 VIHRDIKSDNILLGMDGSVKLTDFGFCAQIT--PEQS---KRSTMV-------GTPYWMAPEVV---TRKAYGPKVDIWS 188

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559  88 LGCILYLLCFRQHPFEDGAKLRIV-----NGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQ 151
Cdd:cd06647   189 LGIMAIEMVEGEPPYLNENPLRALyliatNGTPELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQH 257
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
 8-151 4.95e-12

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


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 66.87  E-value: 4.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsAQKRAMVEEEITRNTTPMYRTPEIVDLYSNfpiGEKQDIWA 87
Cdd:cd14189   122 ILHRDLKLGNFFINENMELKVGDFGLA------------ARLEPPEQRKKTICGTPNYLAPEVLLRQGH---GPESDVWS 186

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559  88 LGCILYLLCFRQHPFEDgAKLR-----IVNGKYSIPVNDTryTVFHDLIRAMLKVNPEERLSIAEVVRQ 151
Cdd:cd14189   187 LGCVMYTLLCGNPPFET-LDLKetyrcIKQVKYTLPASLS--LPARHLLAGILKRNPGDRLTLDQILEH 252
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
 1-171 5.16e-12

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: 67.46  E-value: 5.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFG-SATTIShypdyswSAQKRAmveeeiTRNTTPMYRTPEIV--DLYSNF 77
Cdd:cd06611   119 LHSHK--VIHRDLKAGNILLTLDGDVKLADFGvSAKNKS-------TLQKRD------TFIGTPYWMAPEVVacETFKDN 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  78 PIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVngkYSIPVND-------TRYTV-FHDLIRAMLKVNPEERLSiaevV 149
Cdd:cd06611   184 PYDYKADIWSLGITLIELAQMEPPHHELNPMRVL---LKILKSEpptldqpSKWSSsFNDFLKSCLVKDPDDRPT----A 256

                         170       180
                  ....*....|....*....|..
gi 1331383559 150 RQLQEIAAARNVNPKAPITELL 171
Cdd:cd06611   257 AELLKHPFVSDQSDNKAIKDLL 278
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
 1-147 5.16e-12

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: 66.95  E-value: 5.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHypdyswSAQKramveeeitRNT---TPMYRTPEIVDLYSNF 77
Cdd:cd06613   113 LHSTG--KIHRDIKGANILLTEDGDVKLADFGVSAQLTA------TIAK---------RKSfigTPYWMAPEVAAVERKG 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  78 PIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVngkYSIPVND---------TRYT-VFHDLIRAMLKVNPEERLSIAE 147
Cdd:cd06613   176 GYDGKCDIWALGITAIELAELQPPMFDLHPMRAL---FLIPKSNfdppklkdkEKWSpDFHDFIKKCLTKNPKKRPTATK 252
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
 1-92 5.95e-12

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: 67.94  E-value: 5.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDyswsaqKRAMVEEEITRnttpMYRTPEIVDLYSNF--P 78
Cdd:cd07834   119 LHSAG--VIHRDLKPSNILVNSNCDLKICDFGLARGVDPDED------KGFLTEYVVTR----WYRAPELLLSSKKYtkA 186

                          90
                  ....*....|....
gi 1331383559  79 IgekqDIWALGCIL 92
Cdd:cd07834   187 I----DIWSVGCIF 196
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
 2-147 6.38e-12

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: 66.85  E-value: 6.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPpIIHRDLKVENLLLSNQGTIKLCDFGSATTISH--YPDYSWSAqkramveeeitrntTPMYRTPEIVD--LYSNf 77
Cdd:cd06623   116 HTKRH-IIHRDIKPSNLLINSKGEVKIADFGISKVLENtlDQCNTFVG--------------TVTYMSPERIQgeSYSY- 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331383559  78 pigeKQDIWALGCILYLLCFRQHPFEDGAK------LRIVNGKYSIPVNDTRYTV-FHDLIRAMLKVNPEERLSIAE 147
Cdd:cd06623   180 ----AADIWSLGLTLLECALGKFPFLPPGQpsffelMQAICDGPPPSLPAEEFSPeFRDFISACLQKDPKKRPSAAE 252
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
 1-149 6.76e-12

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: 67.01  E-value: 6.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATT----ISHYP---DYSWSAQKRAmvEEEITRNT-TPMYRTPEIVd 72
Cdd:cd14046   120 IHSQG--IIHRDLKPVNIFLDSNGNVKIGDFGLATSnklnVELATqdiNKSTSAALGS--SGDLTGNVgTALYVAPEVQ- 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  73 lySNFP--IGEKQDIWALGCILYLLCfrqHPFEDGA-------KLRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERL 143
Cdd:cd14046   195 --SGTKstYNEKVDMYSLGIIFFEMC---YPFSTGMervqiltALRSVSIEFPPDFDDNKHSKQAKLIRWLLNHDPAKRP 269


                  ....*.
gi 1331383559 144 SIAEVV 149
Cdd:cd14046   270 SAQELL 275
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
 1-150 7.61e-12

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: 66.89  E-value: 7.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQG----TIKLCDFGSATtishypdyswsaQKRA-----MveeeitrntTPMYR----T 67
Cdd:cd14091   110 LHSQG--VVHRDLKPSNILYADESgdpeSLRICDFGFAK------------QLRAengllM---------TPCYTanfvA 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  68 PEIVdlysnfpigEKQ------DIWALGCILYLLCFRQHPF----EDGAK---LRIVNGKYSI--PVNDTRYTVFHDLIR 132
Cdd:cd14091   167 PEVL---------KKQgydaacDIWSLGVLLYTMLAGYTPFasgpNDTPEvilARIGSGKIDLsgGNWDHVSDSAKDLVR 237

                         170
                  ....*....|....*...
gi 1331383559 133 AMLKVNPEERLSIAEVVR 150
Cdd:cd14091   238 KMLHVDPSQRPTAAQVLQ 255
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
 8-150 8.48e-12

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: 66.74  E-value: 8.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSaqkramveeeiTRNTTPMYRTPEIVDLYSNFPiGEKQDIWA 87
Cdd:cd14076   127 VVHRDLKLENLLLDKNRNLVITDFGFANTFDHFNGDLMS-----------TSCGSPCYAAPELVVSDSMYA-GRKADIWS 194

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331383559  88 LGCILYLLCFRQHPFED-------GAKLRIVNGKYSIPVNDTRYTVFH--DLIRAMLKVNPEERLSIAEVVR 150
Cdd:cd14076   195 CGVILYAMLAGYLPFDDdphnpngDNVPRLYRYICNTPLIFPEYVTPKarDLLRRILVPNPRKRIRLSAIMR 266
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
 2-147 9.35e-12

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: 66.63  E-value: 9.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYswsaqkraMVEEEITRnttpMYRTPEIV--DLYSNFPI 79
Cdd:cd07847   117 HKHN--CIHRDVKPENILITKQGQIKLCDFGFARILTGPGDD--------YTDYVATR----WYRAPELLvgDTQYGPPV 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  80 gekqDIWALGCI-------------------LYL-------LCFR-QHPFEDGAKLRivngKYSIPVNDTR------YTV 126
Cdd:cd07847   183 ----DVWAIGCVfaelltgqplwpgksdvdqLYLirktlgdLIPRhQQIFSTNQFFK----GLSIPEPETRepleskFPN 254

                         170       180
                  ....*....|....*....|....*
gi 1331383559 127 FH----DLIRAMLKVNPEERLSIAE 147
Cdd:cd07847   255 ISspalSFLKGCLQMDPTERLSCEE 279
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
 1-150 1.02e-11

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: 66.53  E-value: 1.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLsNQGTIKLCDFGSATTISHYPDYSwsaqkramveEEItrnTTPMYRTPEIvdLYSNFPIG 80
Cdd:cd07831   116 MHRNG--IFHRDIKPENILI-KDDILKLADFGSCRGIYSKPPYT----------EYI---STRWYRAPEC--LLTDGYYG 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  81 EKQDIWALGCILY-------------------------------LLCFRQH--------PFEDGAKLRivngkYSIPvND 121
Cdd:cd07831   178 PKMDIWAVGCVFFeilslfplfpgtneldqiakihdvlgtpdaeVLKKFRKsrhmnynfPSKKGTGLR-----KLLP-NA 251

                         170       180
                  ....*....|....*....|....*....
gi 1331383559 122 TRYTVfhDLIRAMLKVNPEERLSIAEVVR 150
Cdd:cd07831   252 SAEGL--DLLKKLLAYDPDERITAKQALR 278
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
 8-148 1.07e-11

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: 66.14  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLS-----NQGTIKLCDFGSATTIShYPDYSWSAqkramveeeitRNTTP---MYRTPEIVDLYSNFPI 79
Cdd:cd13982   120 IVHRDLKPQNILIStpnahGNVRAMISDFGLCKKLD-VGRSSFSR-----------RSGVAgtsGWIAPEMLSGSTKRRQ 187

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331383559  80 GEKQDIWALGCIL-YLLCFRQHPFedGAKLR----IVNGKYSIPVND---TRYTVFHDLIRAMLKVNPEERLSIAEV 148
Cdd:cd13982   188 TRAVDIFSLGCVFyYVLSGGSHPF--GDKLEreanILKGKYSLDKLLslgEHGPEAQDLIERMIDFDPEKRPSAEEV 262
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
 8-150 1.16e-11

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: 66.04  E-value: 1.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQG-TIKLCDFGSATTISHYPDYSwsaqkramveeeITRNTTPMYRTPEIVDLYSNFPigEKQDIW 86
Cdd:cd14164   121 IVHRDLKCENILLSADDrKIKIADFGFARFVEDYPELS------------TTFCGSRAYTPPEVILGTPYDP--KKYDVW 186

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331383559  87 ALGCILYLLCFRQHPFEDGAKLRIVNGKYsiPVNDTRYTVFHD----LIRAMLKVNPEERLSIAEVVR 150
Cdd:cd14164   187 SLGVVLYVMVTGTMPFDETNVRRLRLQQR--GVLYPSGVALEEpcraLIRTLLQFNPSTRPSIQQVAG 252
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
 2-101 1.17e-11

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: 66.53  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRqkppIIHRDLKVENLLLSNQGTIKLCDFGSATTishypdYSWSAQKRAMVeeeitrnTTPMYRTPEI-VDLYSNFPIg 80
Cdd:cd07838   126 HR----IVHRDLKPQNILVTSDGQVKLADFGLARI------YSFEMALTSVV-------VTLWYRAPEVlLQSSYATPV- 187

                          90       100
                  ....*....|....*....|.
gi 1331383559  81 ekqDIWALGCILYLLcFRQHP 101
Cdd:cd07838   188 ---DMWSVGCIFAEL-FNRRP 204
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
 1-150 1.44e-11

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: 65.78  E-value: 1.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqKRAMVEEEITRNTTPM------YRTPEIV--D 72
Cdd:cd14162   116 CHSKG--VVHRDLKCENLLLDKNNNLKITDFGFA--------------RGVMKTKDGKPKLSETycgsyaYASPEILrgI 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  73 LYSNFpigeKQDIWALGCILYLLCFRQHPFEDG---AKLRIVNGKYSIPVNDTRYTVFHDLIRAMLkVNPEERLSIAEVV 149
Cdd:cd14162   180 PYDPF----LSDIWSMGVVLYTMVYGRLPFDDSnlkVLLKQVQRRVVFPKNPTVSEECKDLILRML-SPVKKRITIEEIK 254


                  .
gi 1331383559 150 R 150
Cdd:cd14162   255 R 255
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
 8-92 1.58e-11

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: 66.24  E-value: 1.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTISHyPDYSWSAQkraMVeeeitrntTPMYRTPEIVdlysnfpIGEKQ---- 83
Cdd:cd07845   129 IIHRDLKVSNLLLTDKGCLKIADFGLARTYGL-PAKPMTPK---VV--------TLWYRAPELL-------LGCTTytta 189

                          90
                  ....*....|
gi 1331383559  84 -DIWALGCIL 92
Cdd:cd07845   190 iDMWAVGCIL 199
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
 1-92 1.62e-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: 66.18  E-value: 1.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSAttiSHYPDyswSAQKRAMVEEEITRNTTPM-----YRTPEIVdlys 75
Cdd:cd07866   131 LHENH--ILHRDIKAANILIDNQGILKIADFGLA---RPYDG---PPPNPKGGGGGGTRKYTNLvvtrwYRPPELL---- 198

                          90       100
                  ....*....|....*....|..
gi 1331383559  76 nfpIGEKQ-----DIWALGCIL 92
Cdd:cd07866   199 ---LGERRyttavDIWGIGCVF 217
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
 1-150 1.68e-11

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: 65.31  E-value: 1.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswsaqkramvEEEITRNT---TPMYRTPEIVdlySNF 77
Cdd:cd06614   113 LHSQN--VIHRDIKSDNILLSKDGSVKLADFGFAAQLT---------------KEKSKRNSvvgTPYWMAPEVI---KRK 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  78 PIGEKQDIWALGCILYLLC------FRQHPFEdgAKLRIV-NGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVR 150
Cdd:cd06614   173 DYGPKVDIWSLGIMCIEMAegeppyLEEPPLR--ALFLITtKGIPPLKNPEKWSPEFKDFLNKCLVKDPEKRPSAEELLQ 250
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
 8-92 1.73e-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: 65.91  E-value: 1.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTISH----YPDYSwsaqkramveeeitrnTTPMYRTPEIvdLYSNFPIGEKQ 83
Cdd:cd07846   121 IIHRDIKPENILVSQSGVVKLCDFGFARTLAApgevYTDYV----------------ATRWYRAPEL--LVGDTKYGKAV 182


                  ....*....
gi 1331383559  84 DIWALGCIL 92
Cdd:cd07846   183 DVWAVGCLV 191
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 1-148 2.06e-11

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: 66.17  E-value: 2.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQG---TIKLCDFGSAttishypdyswsaqkRAMVEEEitRNTTPM----YRTPEIVDL 73
Cdd:cd14092   115 MHSKG--VVHRDLKPENLLFTDEDddaEIKIVDFGFA---------------RLKPENQ--PLKTPCftlpYAAPEVLKQ 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  74 YSNFP-IGEKQDIWALGCILYLLCFRQHPFEDGAKL--------RIVNGKYSI------PVNDTRytvfHDLIRAMLKVN 138
Cdd:cd14092   176 ALSTQgYDESCDLWSLGVILYTMLSGQVPFQSPSRNesaaeimkRIKSGDFSFdgeewkNVSSEA----KSLIQGLLTVD 251

                         170
                  ....*....|
gi 1331383559 139 PEERLSIAEV 148
Cdd:cd14092   252 PSKRLTMSEL 261
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
 8-154 2.13e-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: 66.69  E-value: 2.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTisHYPDYSwsaqkRAMVEEEITRnttpMYRTPEIvdLYSNFPIGEKQDIWA 87
Cdd:cd07853   124 ILHRDIKPGNLLVNSNCVLKICDFGLARV--EEPDES-----KHMTQEVVTQ----YYRAPEI--LMGSRHYTSAVDIWS 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  88 LGCILYLLCFRQHPFE---------------------------DGAKLRIVNGKYSIPVNDTRYTV--------FHDLIR 132
Cdd:cd07853   191 VGCIFAELLGRRILFQaqspiqqldlitdllgtpsleamrsacEGARAHILRGPHKPPSLPVLYTLssqatheaVHLLCR 270

                         170       180
                  ....*....|....*....|....
gi 1331383559 133 aMLKVNPEERLSIAEVVRQ--LQE 154
Cdd:cd07853   271 -MLVFDPDKRISAADALAHpyLDE 293
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
 1-91 2.31e-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: 65.71  E-value: 2.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATtishypdySWSAQKRAMveeeiTRN-TTPMYRTPEIVdlysnfpI 79
Cdd:cd07843   122 LHDNW--ILHRDLKTSNLLLNNRGILKICDFGLAR--------EYGSPLKPY-----TQLvVTLWYRAPELL-------L 179

                          90
                  ....*....|....*..
gi 1331383559  80 GEKQ-----DIWALGCI 91
Cdd:cd07843   180 GAKEystaiDMWSVGCI 196
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
 8-149 2.72e-11

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: 65.05  E-value: 2.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSN--QGT--IKLCDFGSATTISHyPDYswsaqkramveeeiTRNTTPMYRTPEIVdlySNFPIGEKQ 83
Cdd:cd14184   120 IVHRDIKPENLLVCEypDGTksLKLGDFGLATVVEG-PLY--------------TVCGTPTYVAPEII---AETGYGLKV 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331383559  84 DIWALGCILYLLCFRQHPFEDGAKL------RIVNGKYSIPVN--DTRYTVFHDLIRAMLKVNPEERLSIAEVV 149
Cdd:cd14184   182 DIWAAGVITYILLCGFPPFRSENNLqedlfdQILLGKLEFPSPywDNITDSAKELISHMLQVNVEARYTAEQIL 255
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
 8-143 2.94e-11

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 65.49  E-value: 2.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqKRAMVEEEITRN--TTPMYRTPEIVdLYSnfPIGEKQDI 85
Cdd:cd05587   118 IIYRDLKLDNVMLDAEGHIKIADFGMC--------------KEGIFGGKTTRTfcGTPDYIAPEII-AYQ--PYGKSVDW 180

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331383559  86 WALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSIPVNDTRYTVfhDLIRAMLKVNPEERL 143
Cdd:cd05587   181 WAYGVLLYEMLAGQPPFdgEDEDELfqSIMEHNVSYPKSLSKEAV--SICKGLLTKHPAKRL 240
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
 2-143 4.25e-11

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


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 65.12  E-value: 4.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqkRAMVEEEITRNT---TPMYRTPEIVDLYSNfp 78
Cdd:cd05584   115 HLHSLGIIYRDLKPENILLDAQGHVKLTDFGLC---------------KESIHDGTVTHTfcgTIEYMAPEILTRSGH-- 177

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331383559  79 iGEKQDIWALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSIP---VNDTRytvfhDLIRAMLKVNPEERL 143
Cdd:cd05584   178 -GKAVDWWSLGALMYDMLTGAPPFtaENRKKTidKILKGKLNLPpylTNEAR-----DLLKKLLKRNVSSRL 243
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
 8-146 4.92e-11

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: 64.17  E-value: 4.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSN---QGTIKLCDFGSATTISHypdyswSAQKRAMVeeeitrnTTPMYRTPEIVDlYSnfPIGEKQD 84
Cdd:cd14198   131 IVHLDLKPQNILLSSiypLGDIKIVDFGMSRKIGH------ACELREIM-------GTPEYLAPEILN-YD--PITTATD 194

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331383559  85 IWALGCILYLLCFRQHPF--EDGAK--LRI--VNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIA 146
Cdd:cd14198   195 MWNIGVIAYMLLTHESPFvgEDNQEtfLNIsqVNVDYSEETFSSVSQLATDFIQKLLVKNPEKRPTAE 262
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
 8-149 5.66e-11

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


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 63.82  E-value: 5.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGsattishypdysWSAQkrAMVEEEITRNTTPMYRTPEIVDLYSNfpiGEKQDIWA 87
Cdd:cd14116   126 VIHRDIKPENLLLGSAGELKIADFG------------WSVH--APSSRRTTLCGTLDYLPPEMIEGRMH---DEKVDLWS 188

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  88 LGCILYLLCFRQHPFEDGAK----LRIVNGKYSIPVNDTRYTvfHDLIRAMLKVNPEERLSIAEVV 149
Cdd:cd14116   189 LGVLCYEFLVGKPPFEANTYqetyKRISRVEFTFPDFVTEGA--RDLISRLLKHNPSQRPMLREVL 252
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
 8-150 7.67e-11

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: 63.61  E-value: 7.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIshypdyswSAQKRAMVEEEITRNT--TPMYRTPEIVDLYSNfpiGEKQDI 85
Cdd:cd06631   124 VIHRDIKGNNIMLMPNGVIKLIDFGCAKRL--------CINLSSGSQSQLLKSMrgTPYWMAPEVINETGH---GRKSDI 192

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  86 WALGCILYLLCFRQHPFEDGAKLR----IVNGKYSIPVNDTRYTV-FHDLIRAMLKVNPEERLSIAEVVR 150
Cdd:cd06631   193 WSIGCTVFEMATGKPPWADMNPMAaifaIGSGRKPVPRLPDKFSPeARDFVHACLTRDQDERPSAEQLLK 262
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
 8-150 7.83e-11

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: 63.50  E-value: 7.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTISHypdyswSAQKRAMVEEeitRNTTPmYRTPEIvdLYSNFPIGEKQDIWA 87
Cdd:cd14069   121 ITHRDIKPENLLLDENDNLKISDFGLATVFRY------KGKERLLNKM---CGTLP-YVAPEL--LAKKKYRAEPVDVWS 188

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331383559  88 LGCILYLLCFRQHPFEDGAKlriVNGKYSIPVNDTRY---------TVFHDLIRAMLKVNPEERLSIAEVVR 150
Cdd:cd14069   189 CGIVLFAMLAGELPWDQPSD---SCQEYSDWKENKKTyltpwkkidTAALSLLRKILTENPNKRITIEDIKK 257
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
 4-142 9.39e-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: 63.86  E-value: 9.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   4 QKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSaqkramvEEEITRnttpMYRTPEivdLYSNFPIGEKQ 83
Cdd:cd07848   117 HKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGSNANYT-------EYVATR----WYRSPE---LLLGAPYGKAV 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  84 DIWALGCILYLLC--------------------------------FRQHPFEDGAKLRIVNGKYSIpvnDTRY-----TV 126
Cdd:cd07848   183 DMWSVGCILGELSdgqplfpgeseidqlftiqkvlgplpaeqmklFYSNPRFHGLRFPAVNHPQSL---ERRYlgilsGV 259

                         170
                  ....*....|....*.
gi 1331383559 127 FHDLIRAMLKVNPEER 142
Cdd:cd07848   260 LLDLMKNLLKLNPTDR 275
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
 2-144 9.91e-11

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 65.28  E-value: 9.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPPIIHRDLKVENLLLSNQGTIKLCDFGsattishypdysWSAQKRAMVEEEITRN--TTPMYRTPEIvdlYSNFPI 79
Cdd:PTZ00283  158 HVHSKHMIHRDIKSANILLCSNGLVKLGDFG------------FSKMYAATVSDDVGRTfcGTPYYVAPEI---WRRKPY 222

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  80 GEKQDIWALGCILYLLCFRQHPFeDGAKLRIV-----NGKYSiPVNDTRYTVFHDLIRAMLKVNPEERLS 144
Cdd:PTZ00283  223 SKKADMFSLGVLLYELLTLKRPF-DGENMEEVmhktlAGRYD-PLPPSISPEMQEIVTALLSSDPKRRPS 290
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
 8-92 1.10e-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: 64.12  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAqkrAMVEEEITRnttpMYRTPEIVdlysnfpIGEKQ---- 83
Cdd:cd07852   128 VIHRDLKPSNILLNSDCRVKLADFGLARSLSQLEEDDENP---VLTDYVATR----WYRAPEIL-------LGSTRytkg 193

                          90
                  ....*....|
gi 1331383559  84 -DIWALGCIL 92
Cdd:cd07852   194 vDMWSVGCIL 203
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
 8-147 1.12e-10

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 63.94  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGsattishypdyswsaqkraMVEEEITRNT-------TPMYRTPEIVDlysnfpiG 80
Cdd:cd05592   117 IIYRDLKLDNVLLDREGHIKIADFG-------------------MCKENIYGENkastfcgTPDYIAPEILK-------G 170

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331383559  81 EKQ----DIWALGCILYLLCFRQHPF----EDGAKLRIVNGKYSIPVNDTRYTvfHDLIRAMLKVNPEERLSIAE 147
Cdd:cd05592   171 QKYnqsvDWWSFGVLLYEMLIGQSPFhgedEDELFWSICNDTPHYPRWLTKEA--ASCLSLLLERNPEKRLGVPE 243
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
 1-148 1.16e-10

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


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 63.02  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLS-NQGTIKLCDFGSATTI--SHYPDYSwsaqkramveeeitrnTTPMYRTPEIV--DLYS 75
Cdd:cd14005   123 CHQRG--VLHRDIKDENLLINlRTGEVKLIDFGCGALLkdSVYTDFD----------------GTRVYSPPEWIrhGRYH 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331383559  76 nfpiGEKQDIWALGCILYLLCFRQHPFEDgaKLRIVNGKYSIPVNDTRYTvfHDLIRAMLKVNPEERLSIAEV 148
Cdd:cd14005   185 ----GRPATVWSLGILLYDMLCGDIPFEN--DEQILRGNVLFRPRLSKEC--CDLISRCLQFDPSKRPSLEQI 249
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
 8-151 1.39e-10

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: 62.66  E-value: 1.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQG----TIKLCDFGSAttishypdyswsaqkRAMVEEEITRNTTPMYRTPEIVdlySNFPIGEKQ 83
Cdd:cd14185   119 IVHRDLKPENLLVQHNPdkstTLKLADFGLA---------------KYVTGPIFTVCGTPTYVAPEIL---SEKGYGLEV 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  84 DIWALGCILY-LLC----FRQHPFEDGAKLRIVN-GKYSI--PVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQ 151
Cdd:cd14185   181 DMWAAGVILYiLLCgfppFRSPERDQEELFQIIQlGHYEFlpPYWDNISEAAKDLISRLLVVDPEKRYTAKQVLQH 256
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
 8-147 1.61e-10

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: 63.22  E-value: 1.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLS---------------------------------NQGTIKLCDFGSATTIshypdysWSAQKRamve 54
Cdd:cd14096   127 VVHRDIKPENLLFEpipfipsivklrkadddetkvdegefipgvgggGIGIVKLADFGLSKQV-------WDSNTK---- 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  55 eeiTRNTTPMYRTPEIV--DLYSnfpigEKQDIWALGCILY-LLC-FRqhPFEDGAK----LRIVNGKYSI--PVNDTRY 124
Cdd:cd14096   196 ---TPCGTVGYTAPEVVkdERYS-----KKVDMWALGCVLYtLLCgFP--PFYDESIetltEKISRGDYTFlsPWWDEIS 265

                         170       180
                  ....*....|....*....|...
gi 1331383559 125 TVFHDLIRAMLKVNPEERLSIAE 147
Cdd:cd14096   266 KSAKDLISHLLTVDPAKRYDIDE 288
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
 1-150 1.85e-10

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: 62.95  E-value: 1.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGT--IKLCDFGSATTiSHYPDYSWsAQKRamveeeitrnttpMYRTPEIVdlySNFP 78
Cdd:cd14210   132 LHKLN--IIHCDLKPENILLKQPSKssIKVIDFGSSCF-EGEKVYTY-IQSR-------------FYRAPEVI---LGLP 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  79 IGEKQDIWALGCI---LY-------------LLC------------------FRQHPFEDGAKLRIVN---GKYSIP--- 118
Cdd:cd14210   192 YDTAIDMWSLGCIlaeLYtgyplfpgeneeeQLAcimevlgvppkslidkasRRKKFFDSNGKPRPTTnskGKKRRPgsk 271

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1331383559 119 ----VNDTRYTVFHDLIRAMLKVNPEERLSIAEVVR 150
Cdd:cd14210   272 slaqVLKCDDPSFLDFLKKCLRWDPSERMTPEEALQ 307
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
 9-144 1.87e-10

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


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 63.48  E-value: 1.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTIshypdyswSAQKRAMVEEEItrnTTPMYRTPEI---VDLYSNFPIGEKQDI 85
Cdd:cd05601   124 VHRDIKPENILIDRTGHIKLADFGSAAKL--------SSDKTVTSKMPV---GTPDYIAPEVltsMNGGSKGTYGVECDW 192

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331383559  86 WALGCILYLLCFRQHPFEDGAKL----RIVNGK--YSIPVNDTRYTVFHDLIRAMLkVNPEERLS 144
Cdd:cd05601   193 WSLGIVAYEMLYGKTPFTEDTVIktysNIMNFKkfLKFPEDPKVSESAVDLIKGLL-TDAKERLG 256
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
 8-152 1.92e-10

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: 62.51  E-value: 1.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTISHYpdyswsaqkramveEEITRNT-TPMYRTPEIVDLYSnfpIGEKQDIW 86
Cdd:cd14047   138 LIHRDLKPSNIFLVDTGKVKIGDFGLVTSLKND--------------GKRTKSKgTLSYMSPEQISSQD---YGKEVDIY 200

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331383559  87 ALGCILYLLCfrqHPFEDG-------AKLRivNGKYSiPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQL 152
Cdd:cd14047   201 ALGLILFELL---HVCDSAfekskfwTDLR--NGILP-DIFDKRYKIEKTIIKKMLSKKPEDRPNASEILRTL 267
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
 8-147 1.95e-10

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


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 62.31  E-value: 1.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQ---GTIKLCDFGSAttishypdyswsaqKRAMVEEEI-TRNTTPMYRTPEIV--DLYSnfpigE 81
Cdd:cd14172   124 IAHRDVKPENLLYTSKekdAVLKLTDFGFA--------------KETTVQNALqTPCYTPYYVAPEVLgpEKYD-----K 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331383559  82 KQDIWALGCILYLLCFRQHPF--------EDGAKLRIVNGKYSIPvNDTRYTVFHD---LIRAMLKVNPEERLSIAE 147
Cdd:cd14172   185 SCDMWSLGVIMYILLCGFPPFysntgqaiSPGMKRRIRMGQYGFP-NPEWAEVSEEakqLIRHLLKTDPTERMTITQ 260
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
 8-183 1.96e-10

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 64.27  E-value: 1.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGsattishypdysWSAQKRAMVEEEITRN--TTPMYRTPEivdLYSNFPIGEKQDI 85
Cdd:PTZ00267  190 MMHRDLKSANIFLMPTGIIKLGDFG------------FSKQYSDSVSLDVASSfcGTPYYLAPE---LWERKRYSKKADM 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  86 WALGCILYLLCFRQHPFEDGAKLRIVN----GKYS---IPVNDTrytvFHDLIRAMLKVNPEERLSIAE---------VV 149
Cdd:PTZ00267  255 WSLGVILYELLTLHRPFKGPSQREIMQqvlyGKYDpfpCPVSSG----MKALLDPLLSKNPALRPTTQQllhteflkyVA 330

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1331383559 150 RQLQEIAAARNVNPKAPITELLEQNGGYGNSGPS 183
Cdd:PTZ00267  331 NLFQDIVRHSETISPHDREEILRQLQESGERAPP 364
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
 9-174 2.43e-10

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: 62.38  E-value: 2.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswsaqkramvEEEITRNT---TPMYRTPEIVDLYS-NFpigeKQD 84
Cdd:cd06642   123 IHRDIKAANVLLSEQGDVKLADFGVAGQLT---------------DTQIKRNTfvgTPFWMAPEVIKQSAyDF----KAD 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  85 IWALGCILYLLCFRQHPFEDGAKLRIVN--GKYSIPVNDTRYTV-FHDLIRAMLKVNPEERLSIAEVvrqLQEIAAARNV 161
Cdd:cd06642   184 IWSLGITAIELAKGEPPNSDLHPMRVLFliPKNSPPTLEGQHSKpFKEFVEACLNKDPRFRPTAKEL---LKHKFITRYT 260

                         170
                  ....*....|...
gi 1331383559 162 NPKAPITELLEQN 174
Cdd:cd06642   261 KKTSFLTELIDRY 273
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
 1-92 2.48e-10

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: 62.35  E-value: 2.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQKramveeeitrnTTPMYRTPEIvdLYSNFPIG 80
Cdd:cd07832   116 MHANR--IMHRDLKPANLLISSTGVLKIADFGLARLFSEEDPRLYSHQV-----------ATRWYRAPEL--LYGSRKYD 180

                          90
                  ....*....|..
gi 1331383559  81 EKQDIWALGCIL 92
Cdd:cd07832   181 EGVDLWAVGCIF 192
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
 8-148 2.58e-10

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


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 62.09  E-value: 2.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLL--SNQGTIKLCDFG-SATTISHypdyswsAQKRAMVeeeitrnTTPMYRTPEIvdLYSNFPIGEKQD 84
Cdd:cd14662   117 ICHRDLKLENTLLdgSPAPRLKICDFGySKSSVLH-------SQPKSTV-------GTPAYIAPEV--LSRKEYDGKVAD 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331383559  85 IWALGCILYLLCFRQHPFEDGAK--------LRIVNGKYSIP-----VNDTRYtvfhdLIRAMLKVNPEERLSIAEV 148
Cdd:cd14662   181 VWSCGVTLYVMLVGAYPFEDPDDpknfrktiQRIMSVQYKIPdyvrvSQDCRH-----LLSRIFVANPAKRITIPEI 252
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
 8-102 2.89e-10

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


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 62.77  E-value: 2.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYswsaqkraMVEEEITRnttpMYRTPEIVDLYSNFpiGEKQDIWA 87
Cdd:cd07858   129 VLHRDLKPSNLLLNANCDLKICDFGLARTTSEKGDF--------MTEYVVTR----WYRAPELLLNCSEY--TTAIDVWS 194

                          90
                  ....*....|....*
gi 1331383559  88 LGCILYLLCFRQHPF 102
Cdd:cd07858   195 VGCIFAELLGRKPLF 209
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
 1-151 2.89e-10

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: 62.35  E-value: 2.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLL----SNQGTIKLCDFGSATtishypdyswsaQKRAMVEEEITRNTTPMYRTPEIVDLYSn 76
Cdd:cd14175   111 LHSQG--VVHRDLKPSNILYvdesGNPESLRICDFGFAK------------QLRAENGLLMTPCYTANFVAPEVLKRQG- 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  77 fpIGEKQDIWALGCILYLLCFRQHPFEDGAK-------LRIVNGKYSIPVN--DTRYTVFHDLIRAMLKVNPEERLSIAE 147
Cdd:cd14175   176 --YDEGCDIWSLGILLYTMLAGYTPFANGPSdtpeeilTRIGSGKFTLSGGnwNTVSDAAKDLVSKMLHVDPHQRLTAKQ 253


                  ....
gi 1331383559 148 VVRQ 151
Cdd:cd14175   254 VLQH 257
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
 1-156 3.02e-10

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: 61.36  E-value: 3.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATtishypdySWSAQKRAMveeeiTRNTTPMYRTPEIVdlySNFPIG 80
Cdd:cd14059    97 LHLHK--IIHRDLKSPNVLVTYNDVLKISDFGTSK--------ELSEKSTKM-----SFAGTVAWMAPEVI---RNEPCS 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  81 EKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYS----IPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQLqEIA 156
Cdd:cd14059   159 EKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSnslqLPVPSTCPDGFKLLMKQCWNSKPRNRPSFRQILMHL-DIA 237
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
 8-143 3.31e-10

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


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 62.07  E-value: 3.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIShypDYSWsaqkramveeeiTRNTTPMYRTPEIVDLYSNfpiGEKQDIWA 87
Cdd:cd05612   122 IVYRDLKPENILLDKEGHIKLTDFGFAKKLR---DRTW------------TLCGTPEYLAPEVIQSKGH---NKAVDWWA 183

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331383559  88 LGCILYLLCFRQHPFED----GAKLRIVNGKYSIPvndtRYTVFH--DLIRAMLKVNPEERL 143
Cdd:cd05612   184 LGILIYEMLVGYPPFFDdnpfGIYEKILAGKLEFP----RHLDLYakDLIKKLLVVDRTRRL 241
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
 5-149 3.38e-10

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: 61.80  E-value: 3.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   5 KPPIIHRDLKVENLLLSN-------QGTIKLCDFGsattishypdysWSAQKRAMVEEEITRNT-TPMYRTPEIVdlySN 76
Cdd:cd14097   118 KNDIVHRDLKLENILVKSsiidnndKLNIKVTDFG------------LSVQKYGLGEDMLQETCgTPIYMAPEVI---SA 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559  77 FPIGEKQDIWALGCILYLLCFRQHPF----EDGAKLRIVNG--KYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVV 149
Cdd:cd14097   183 HGYSQQCDIWSIGVIMYMLLCGEPPFvaksEEKLFEEIRKGdlTFTQSVWQSVSDAAKNVLQQLLKVDPAHRMTASELL 261
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
 8-150 3.69e-10

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: 61.63  E-value: 3.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGsattISHYPDYSWSAQkramveEEITRNTTPMYRTPEIVDLYSNfPIGEKQDIWA 87
Cdd:cd06629   129 ILHRDLKADNILVDLEGICKISDFG----ISKKSDDIYGNN------GATSMQGSVFWMAPEVIHSQGQ-GYSAKVDIWS 197

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559  88 LGCILYLLCFRQHPFED----GAKLRIVNGKYSIPV-NDTRYT-VFHDLIRAMLKVNPEERLSIAEVVR 150
Cdd:cd06629   198 LGCVVLEMLAGRRPWSDdeaiAAMFKLGNKRSAPPVpEDVNLSpEALDFLNACFAIDPRDRPTAAELLS 266
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
 8-147 4.21e-10

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: 61.44  E-value: 4.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLL--SNQGTIKLCDFGSAttishypdyswsaQKRAMVEEEITRNTTPMYRTPEIVdlySNFPIGEKQDI 85
Cdd:cd14107   119 ILHLDIKPDNILMvsPTREDIKICDFGFA-------------QEITPSEHQFSKYGSPEFVAPEIV---HQEPVSAATDI 182

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331383559  86 WALGCILYLLCFRQHPF----EDGAKLRIVNGK--YSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAE 147
Cdd:cd14107   183 WALGVIAYLSLTCHSPFagenDRATLLNVAEGVvsWDTPEITHLSEDAKDFIKRVLQPDPEKRPSASE 250
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
 1-150 4.52e-10

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: 62.20  E-value: 4.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSN-------------------QGTIKLCDFGSATTISHYpdyswsaqKRAMVeeeitrnT 61
Cdd:cd14134   131 LHDLK--LTHTDLKPENILLVDsdyvkvynpkkkrqirvpkSTDIKLIDFGSATFDDEY--------HSSIV-------S 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  62 TPMYRTPEIV-DLYSNFPIgekqDIWALGCILYLLC-----FRQH--------------PF------------------- 102
Cdd:cd14134   194 TRHYRAPEVIlGLGWSYPC----DVWSIGCILVELYtgellFQTHdnlehlammerilgPLpkrmirrakkgakyfyfyh 269

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559 103 ---------EDGAKLRIV--NGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVR 150
Cdd:cd14134   270 grldwpegsSSGRSIKRVckPLKRLMLLVDPEHRLLFDLIRKMLEYDPSKRITAKEALK 328
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
 1-156 4.72e-10

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 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: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 61.47  E-value: 4.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGsattISHYPDYSWSAQKRAMVEEEitrNTTPMYRTPEIVDLYSNFPIG 80
Cdd:cd14026   116 LHNMSPPLLHHDLKTQNILLDGEFHVKIADFG----LSKWRQLSISQSRSSKSAPE---GGTIIYMPPEEYEPSQKRRAS 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  81 EKQDIWALGCILYLLCFRQHPFEDGAK-----------LRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLS----- 144
Cdd:cd14026   189 VKHDIYSYAIIMWEVLSRKIPFEEVTNplqimysvsqgHRPDTGEDSLPVDIPHRATLINLIESGWAQNPDERPSflkcl 268

                         170
                  ....*....|....
gi 1331383559 145 --IAEVVRQLQEIA 156
Cdd:cd14026   269 ieLEPVLRTFDEID 282
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
 2-162 4.83e-10

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


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 62.20  E-value: 4.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqkRAMVEEEITRNT---TPMYRTPEIvdLYSNFP 78
Cdd:cd05586   111 HLHKNDIVYRDLKPENILLDANGHIALCDFGLS---------------KADLTDNKTTNTfcgTTEYLAPEV--LLDEKG 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  79 IGEKQDIWALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSIPvNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQLQE 154
Cdd:cd05586   174 YTKMVDFWSLGVLVFEMCCGWSPFyaEDTQQMyrNIAFGKVRFP-KDVLSDEGRSFVKGLLNRNPKHRLGAHDDAVELKE 252


                  ....*...
gi 1331383559 155 IAAARNVN 162
Cdd:cd05586   253 HPFFADID 260
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
 1-173 5.35e-10

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: 61.58  E-value: 5.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSattishypdyswSAQKRAMVEEEITRNTTPMYRTPEIV--DLYSNFP 78
Cdd:cd06643   119 LHENK--IIHRDLKAGNILFTLDGDIKLADFGV------------SAKNTRTLQRRDSFIGTPYWMAPEVVmcETSKDRP 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  79 IGEKQDIWALGCILYLLCFRQHPFEDGAKLRIV--NGKYSIP--VNDTRYTV-FHDLIRAMLKVNPEERLSIAEVVRQlq 153
Cdd:cd06643   185 YDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLlkIAKSEPPtlAQPSRWSPeFKDFLRKCLEKNVDARWTTSQLLQH-- 262

                         170       180
                  ....*....|....*....|
gi 1331383559 154 eiAAARNVNPKAPITELLEQ 173
Cdd:cd06643   263 --PFVSVLVSNKPLRELIAE 280
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
 1-155 6.96e-10

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


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 60.48  E-value: 6.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKP-PIIHRDLKVENLLLSN--------QGTIKLCDFGSA------TTISHYPDYSWsaqkraMVEEEITRNTtpmy 65
Cdd:cd14061   108 LHNEAPvPIIHRDLKSSNILILEaienedleNKTLKITDFGLArewhktTRMSAAGTYAW------MAPEVIKSST---- 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  66 rtpeivdlYSNFpigekQDIWALGCILYLLCFRQHPFEDGAKLRIVNG----KYSIPVNDTRYTVFHDLIRAMLKVNPEE 141
Cdd:cd14061   178 --------FSKA-----SDVWSYGVLLWELLTGEVPYKGIDGLAVAYGvavnKLTLPIPSTCPEPFAQLMKDCWQPDPHD 244

                         170
                  ....*....|....
gi 1331383559 142 RLSIAEVVRQLQEI 155
Cdd:cd14061   245 RPSFADILKQLENI 258
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
 1-151 7.54e-10

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


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 61.57  E-value: 7.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLL----SNQGTIKLCDFGsattishypdysWSAQKRAMVEEEITRNTTPMYRTPEIVdlysn 76
Cdd:cd14176   129 LHAQG--VVHRDLKPSNILYvdesGNPESIRICDFG------------FAKQLRAENGLLMTPCYTANFVAPEVL----- 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  77 fpigEKQ------DIWALGCILYLLCFRQHPFEDGAK-------LRIVNGKYSI------PVNDTRytvfHDLIRAMLKV 137
Cdd:cd14176   190 ----ERQgydaacDIWSLGVLLYTMLTGYTPFANGPDdtpeeilARIGSGKFSLsggywnSVSDTA----KDLVSKMLHV 261

                         170
                  ....*....|....
gi 1331383559 138 NPEERLSIAEVVRQ 151
Cdd:cd14176   262 DPHQRLTAALVLRH 275
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
 1-151 7.96e-10

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


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 61.18  E-value: 7.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQG----TIKLCDFGSATtishypdyswsaQKRAMVEEEITRNTTPMYRTPEIVdlysn 76
Cdd:cd14178   113 LHSQG--VVHRDLKPSNILYMDESgnpeSIRICDFGFAK------------QLRAENGLLMTPCYTANFVAPEVL----- 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  77 fpigEKQ------DIWALGCILYLLCFRQHPFEDGAK-------LRIVNGKYSIPVN--DTRYTVFHDLIRAMLKVNPEE 141
Cdd:cd14178   174 ----KRQgydaacDIWSLGILLYTMLAGFTPFANGPDdtpeeilARIGSGKYALSGGnwDSISDAAKDIVSKMLHVDPHQ 249

                         170
                  ....*....|
gi 1331383559 142 RLSIAEVVRQ 151
Cdd:cd14178   250 RLTAPQVLRH 259
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
 8-150 8.26e-10

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: 60.89  E-value: 8.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTI---KLCDFGSATTISHYPDYSWSAQKRAMveeeitrnTTPM----YRTPEIVDLYsnfpIG 80
Cdd:cd14090   121 IAHRDLKPENILCESMDKVspvKICDFDLGSGIKLSSTSMTPVTTPEL--------LTPVgsaeYMAPEVVDAF----VG 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  81 E------KQDIWALGCILYLLCFRQHPF-------------------EDGAKLRIVNGKYSIPVNDTRYTVFH--DLIRA 133
Cdd:cd14090   189 EalsydkRCDLWSLGVILYIMLCGYPPFygrcgedcgwdrgeacqdcQELLFHSIQEGEYEFPEKEWSHISAEakDLISH 268

                         170
                  ....*....|....*..
gi 1331383559 134 MLKVNPEERLSIAEVVR 150
Cdd:cd14090   269 LLVRDASQRYTAEQVLQ 285
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
 1-155 9.03e-10

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 59.97  E-value: 9.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKP-PIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAqkramveeeitrnTTPmYRTPEIVdlySNFPI 79
Cdd:cd14060   100 LHMEAPvKVIHRDLKSRNVVIAADGVLKICDFGASRFHSHTTHMSLVG-------------TFP-WMAPEVI---QSLPV 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  80 GEKQDIWALGCILYLLCFRQHPFEDGAKLRIVngkYSIPVNDTRYTV-------FHDLIRAMLKVNPEERLSIAEVVRQL 152
Cdd:cd14060   163 SETCDTYSYGVVLWEMLTREVPFKGLEGLQVA---WLVVEKNERPTIpsscprsFAELMRRCWEADVKERPSFKQIIGIL 239


                  ...
gi 1331383559 153 QEI 155
Cdd:cd14060   240 ESM 242
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
 2-95 9.30e-10

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: 61.08  E-value: 9.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPPIIHRDLKVENLLLS-NQGTIKLCDFGSATTIShypdyswsaqkramvEEEIT-----RnttpMYRTPEIV-DLY 74
Cdd:cd14135   120 HLKKCNILHADIKPDNILVNeKKNTLKLCDFGSASDIG---------------ENEITpylvsR----FYRAPEIIlGLP 180

                          90       100
                  ....*....|....*....|.
gi 1331383559  75 SNFPIgekqDIWALGCILYLL 95
Cdd:cd14135   181 YDYPI----DMWSVGCTLYEL 197
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
 1-150 1.02e-09

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: 60.39  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSattishypdyswSAQKRAMVEEeitRNT---TPMYRTPEIV--DLYS 75
Cdd:cd06608   129 LHENK--VIHRDIKGQNILLTEEAEVKLVDFGV------------SAQLDSTLGR---RNTfigTPYWMAPEVIacDQQP 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  76 NFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVngkYSIPVND-------TRYT-VFHDLIRAMLKVNPEERLSIAE 147
Cdd:cd06608   192 DASYDARCDVWSLGITAIELADGKPPLCDMHPMRAL---FKIPRNPpptlkspEKWSkEFNDFISECLIKNYEQRPFTEE 268


                  ...
gi 1331383559 148 VVR 150
Cdd:cd06608   269 LLE 271
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
 7-92 1.05e-09

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: 61.18  E-value: 1.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   7 PIIHRDLKVENLLL--SNQGTIKLCDFGSATTISH--YPdYswsAQKRamveeeitrnttpMYRTPEIVdLYsnFPIGEK 82
Cdd:cd14226   138 SIIHCDLKPENILLcnPKRSAIKIIDFGSSCQLGQriYQ-Y---IQSR-------------FYRSPEVL-LG--LPYDLA 197

                          90
                  ....*....|
gi 1331383559  83 QDIWALGCIL 92
Cdd:cd14226   198 IDMWSLGCIL 207
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
 8-92 1.06e-09

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: 60.88  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIShyPDYSWSAQKraMVEEEITRnttpMYRTPEIvdLYSNFPIGEKQDIWA 87
Cdd:cd07857   126 VLHRDLKPGNLLVNADCELKICDFGLARGFS--ENPGENAGF--MTEYVATR----WYRAPEI--MLSFQSYTKAIDVWS 195


                  ....*
gi 1331383559  88 LGCIL 92
Cdd:cd07857   196 VGCIL 200
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
 3-155 1.06e-09

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 60.53  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   3 RQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswsaQKRAMVE-EEITRNTTPMYRTPEIVDLYSNFPIGE 81
Cdd:cd13998   117 QGKPAIAHRDLKSKNILVKNDGTCCIADFGLAVRLS---------PSTGEEDnANNGQVGTKRYMAPEVLEGAINLRDFE 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  82 ---KQDIWALGCIL----------------YLLCF----RQHP-FEDGAKLRIV-NGKYSIP---VNDTRYTVFHDLIRA 133
Cdd:cd13998   188 sfkRVDIYAMGLVLwemasrctdlfgiveeYKPPFysevPNHPsFEDMQEVVVRdKQRPNIPnrwLSHPGLQSLAETIEE 267

                         170       180
                  ....*....|....*....|..
gi 1331383559 134 MLKVNPEERLSIAEVVRQLQEI 155
Cdd:cd13998   268 CWDHDAEARLTAQCIEERLSEF 289
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
 2-102 1.08e-09

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: 60.38  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRqkppIIHRDLKVENLLLSNQGTIKLCDFGSATtishypdySWSAQKRAMVEEEITRnttpMYRTPEIVdlysnfpIGE 81
Cdd:cd07835   118 HR----VLHRDLKPQNLLIDTEGALKLADFGLAR--------AFGVPVRTYTHEVVTL----WYRAPEIL-------LGS 174

                          90       100
                  ....*....|....*....|....*.
gi 1331383559  82 KQ-----DIWALGCILYLLCFRQHPF 102
Cdd:cd07835   175 KHystpvDIWSVGCIFAEMVTRRPLF 200
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
 8-145 1.13e-09

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: 60.22  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTishYPDYSWSAQKRamveeeitRNTTPMYRTPEIVdlySNFPIGEKQDIWA 87
Cdd:cd14111   120 VLHLDIKPDNIMVTNLNAIKIVDFGSAQS---FNPLSLRQLGR--------RTGTLEYMAPEMV---KGEPVGPPADIWS 185

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  88 LGCILYLLCFRQHPFEDG----AKLRIVNGKYS----IPVNDTRYTVFhdlIRAMLKVNPEERLSI 145
Cdd:cd14111   186 IGVLTYIMLSGRSPFEDQdpqeTEAKILVAKFDafklYPNVSQSASLF---LKKVLSSYPWSRPTT 248
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
 1-143 1.26e-09

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


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 60.79  E-value: 1.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqKRAMVEEEITRN--TTPMYRTPEIVdlySNFP 78
Cdd:cd05575   112 LHSLN--IIYRDLKPENILLDSQGHVVLTDFGLC--------------KEGIEPSDTTSTfcGTPEYLAPEVL---RKQP 172

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559  79 IGEKQDIWALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSIPVNDTryTVFHDLIRAMLKVNPEERL 143
Cdd:cd05575   173 YDRTVDWWCLGAVLYEMLYGLPPFysRDTAEMydNILHKPLRLRTNVS--PSARDLLEGLLQKDRTKRL 239
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
 8-151 1.27e-09

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


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 60.44  E-value: 1.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIShyPDYSWSAqkramveeeitrntTPMYRTPEIVDLYSNFPIGEKQDIWA 87
Cdd:cd06633   142 MIHRDIKAGNILLTEPGQVKLADFGSASIAS--PANSFVG--------------TPYWMAPEVILAMDEGQYDGKVDIWS 205

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331383559  88 LGCILYLLCFRQHPFEDgakLRIVNGKYSIPVNDT------RYT-VFHDLIRAMLKVNPEERLSIAEVVRQ 151
Cdd:cd06633   206 LGITCIELAERKPPLFN---MNAMSALYHIAQNDSptlqsnEWTdSFRGFVDYCLQKIPQERPSSAELLRH 273
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
 8-143 1.31e-09

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


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 60.11  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIShypDYSWsaqkramveeeiTRNTTPMYRTPEIVdlySNFPIGEKQDIWA 87
Cdd:cd14209   122 LIYRDLKPENLLIDQQGYIKVTDFGFAKRVK---GRTW------------TLCGTPEYLAPEII---LSKGYNKAVDWWA 183

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331383559  88 LGCILYLLCFRQHPFEDGAKL----RIVNGKYSIPV---NDTRytvfhDLIRAMLKVNPEERL 143
Cdd:cd14209   184 LGVLIYEMAAGYPPFFADQPIqiyeKIVSGKVRFPShfsSDLK-----DLLRNLLQVDLTKRF 241
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
 8-147 1.41e-09

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


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 60.43  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQ---GTIKLCDFGSAttishypdyswsaqkramvEEEITRNT------TPMYRTPEIV--DLYSn 76
Cdd:cd14170   122 IAHRDVKPENLLYTSKrpnAILKLTDFGFA-------------------KETTSHNSlttpcyTPYYVAPEVLgpEKYD- 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  77 fpigEKQDIWALGCILYLLCFRQHPF--------EDGAKLRIVNGKYSIPvnDTRYTVFHD----LIRAMLKVNPEERLS 144
Cdd:cd14170   182 ----KSCDMWSLGVIMYILLCGYPPFysnhglaiSPGMKTRIRMGQYEFP--NPEWSEVSEevkmLIRNLLKTEPTQRMT 255


                  ...
gi 1331383559 145 IAE 147
Cdd:cd14170   256 ITE 258
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
 4-147 1.45e-09

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: 60.03  E-value: 1.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   4 QKPPIIHRDLKVENLLL---SNQGTIKLCDFGSATTI--SHYPDYSwsaqkraMveeEITRN--TTPMYRTPEIVDLYSN 76
Cdd:cd13990   124 IKPPIIHYDLKPGNILLhsgNVSGEIKITDFGLSKIMddESYNSDG-------M---ELTSQgaGTYWYLPPECFVVGKT 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  77 FP-IGEKQDIWALGCILYLLCFRQHPF-EDGAKLRIVngKYSIPVNDTRYTVF---------HDLIRAMLKVNPEERLSI 145
Cdd:cd13990   194 PPkISSKVDVWSVGVIFYQMLYGRKPFgHNQSQEAIL--EENTILKATEVEFPskpvvsseaKDFIRRCLTYRKEDRPDV 271


                  ..
gi 1331383559 146 AE 147
Cdd:cd13990   272 LQ 273
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
 8-167 1.46e-09

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: 60.12  E-value: 1.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIShyPDYSwsaQKRAMVeeeitrnTTPMYRTPEIVdlySNFPIGEKQDIWA 87
Cdd:cd06654   137 VIHRDIKSDNILLGMDGSVKLTDFGFCAQIT--PEQS---KRSTMV-------GTPYWMAPEVV---TRKAYGPKVDIWS 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  88 LGCILYLLCFRQHPFEDGAKLRIV-----NGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVrQLQEIAAARNVN 162
Cdd:cd06654   202 LGIMAIEMIEGEPPYLNENPLRALyliatNGTPELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELL-QHQFLKIAKPLS 280


                  ....*
gi 1331383559 163 PKAPI 167
Cdd:cd06654   281 SLTPL 285
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
 2-150 1.63e-09

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


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 59.45  E-value: 1.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTiSHYPDYSwsaqkramvEEEITRNTTPMYRTPEivdLYSNFPIGE 81
Cdd:cd14070   118 HLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNC-AGILGYS---------DPFSTQCGSPAYAAPE---LLARKKYGP 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331383559  82 KQDIWALGCILYL-----LCFRQHPFEDGA-KLRIVNGKYSiPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVR 150
Cdd:cd14070   185 KVDVWSIGVNMYAmltgtLPFTVEPFSLRAlHQKMVDKEMN-PLPTDLSPGAISFLRSLLEPDPLKRPNIKQALA 258
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
 8-148 1.72e-09

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: 59.82  E-value: 1.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQ-GTIKLCDFGSAttishypdyswsaqKRaMVEEE-----I-TRNttpmYRTPE-IVD--LYSNf 77
Cdd:cd14137   127 ICHRDIKPQNLLVDPEtGVLKLCDFGSA--------------KR-LVPGEpnvsyIcSRY----YRAPElIFGatDYTT- 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  78 PIgekqDIWALGCILYLLcFRQHPF---EDGAK--LRIV--------------NGKYSIPVNDTRY-----TVFH----- 128
Cdd:cd14137   187 AI----DIWSAGCVLAEL-LLGQPLfpgESSVDqlVEIIkvlgtptreqikamNPNYTEFKFPQIKphpweKVFPkrtpp 261

                         170       180
                  ....*....|....*....|...
gi 1331383559 129 ---DLIRAMLKVNPEERLSIAEV 148
Cdd:cd14137   262 daiDLLSKILVYNPSKRLTALEA 284
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
 9-150 1.97e-09

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: 59.39  E-value: 1.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTIShyPDYSWSAqkramveeeitrntTPMYRTPEIVDLYSNFPIGEKQDIWAL 88
Cdd:cd06607   123 IHRDVKAGNILLTEPGTVKLADFGSASLVC--PANSFVG--------------TPYWMAPEVILAMDEGQYDGKVDVWSL 186

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559  89 GCILYLLCFRQHPFEDgakLRIVNGKYSIPVNDTRY-------TVFHDLIRAMLKVNPEERLSIAEVVR 150
Cdd:cd06607   187 GITCIELAERKPPLFN---MNAMSALYHIAQNDSPTlssgewsDDFRNFVDSCLQKIPQDRPSAEDLLK 252
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
 8-151 2.28e-09

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: 59.74  E-value: 2.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIShyPDYSwsaQKRAMVeeeitrnTTPMYRTPEIVdlySNFPIGEKQDIWA 87
Cdd:cd06655   136 VIHRDIKSDNVLLGMDGSVKLTDFGFCAQIT--PEQS---KRSTMV-------GTPYWMAPEVV---TRKAYGPKVDIWS 200

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559  88 LGCILYLLCFRQHPFEDGAKLRIV-----NGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQ 151
Cdd:cd06655   201 LGIMAIEMVEGEPPYLNENPLRALyliatNGTPELQNPEKLSPIFRDFLNRCLEMDVEKRGSAKELLQH 269
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
 1-89 2.38e-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: 59.20  E-value: 2.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHypdyswsaqkrAMVEeeitRNT---TPMYRTPEIVdlySNF 77
Cdd:cd06612   115 LHSNK--KIHRDIKAGNILLNEEGQAKLADFGVSGQLTD-----------TMAK----RNTvigTPFWMAPEVI---QEI 174

                          90
                  ....*....|..
gi 1331383559  78 PIGEKQDIWALG 89
Cdd:cd06612   175 GYNNKADIWSLG 186
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
 8-147 2.38e-09

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: 58.84  E-value: 2.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGT--IKLCDFGsattishypdyswSAQKRAMVEEEITRNTTPMYRTPEIV--DLYSNfpigeKQ 83
Cdd:cd14121   116 ISHMDLKPQNLLLSSRYNpvLKLADFG-------------FAQHLKPNDEAHSLRGSPLYMAPEMIlkKKYDA-----RV 177

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  84 DIWALGCILYLLCFRQHPF------EDGAKLRiVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAE 147
Cdd:cd14121   178 DLWSVGVILYECLFGRAPFasrsfeELEEKIR-SSKPIEIPTRPELSADCRDLLLRLLQRDPDRRISFEE 246
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
2-103 2.44e-09

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 60.96  E-value: 2.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKppIIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqkRAMVEEEITRNTTPM----YRTPE-----IVD 72
Cdd:NF033483  124 HRNG--IVHRDIKPQNILITKDGRVKVTDFGIA---------------RALSSTTMTQTNSVLgtvhYLSPEqarggTVD 186

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1331383559  73 lysnfpigEKQDIWALGCILY-LLCFRQhPFE 103
Cdd:NF033483  187 --------ARSDIYSLGIVLYeMLTGRP-PFD 209
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
 1-162 2.59e-09

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


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 60.01  E-value: 2.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqKRAMVEEEITRN--TTPMYRTPEIVdlySNFP 78
Cdd:cd05615   127 LHKKG--IIYRDLKLDNVMLDSEGHIKIADFGMC--------------KEHMVEGVTTRTfcGTPDYIAPEII---AYQP 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  79 IGEKQDIWALGCILYLLCFRQHPF----EDGAKLRIVNGKYSIPVNDTRYTVfhDLIRAMLKVNPEERLSIA-EVVRQLQ 153
Cdd:cd05615   188 YGRSVDWWAYGVLLYEMLAGQPPFdgedEDELFQSIMEHNVSYPKSLSKEAV--SICKGLMTKHPAKRLGCGpEGERDIR 265


                  ....*....
gi 1331383559 154 EIAAARNVN 162
Cdd:cd05615   266 EHAFFRRID 274
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 1-144 2.72e-09

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: 58.92  E-value: 2.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQ---GTIKLCDFGsattISHypdyswsaqkraMVEEEI--TRNTTPMYRTPEIVdlyS 75
Cdd:cd14083   117 LHSLG--IVHRDLKPENLLYYSPdedSKIMISDFG----LSK------------MEDSGVmsTACGTPGYVAPEVL---A 175

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331383559  76 NFPIGEKQDIWALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSI--PVNDTRYTVFHDLIRAMLKVNPEERLS 144
Cdd:cd14083   176 QKPYGKAVDCWSIGVISYILLCGYPPFydENDSKLfaQILKAEYEFdsPYWDDISDSAKDFIRHLMEKDPNKRYT 250
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
 1-173 2.79e-09

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: 59.30  E-value: 2.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKPpiIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswsaqkramvEEEITRNT---TPMYRTPEIVDLYSnf 77
Cdd:cd06640   117 LHSEKK--IHRDIKAANVLLSEQGDVKLADFGVAGQLT---------------DTQIKRNTfvgTPFWMAPEVIQQSA-- 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  78 pIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVngkYSIPVNDTRYTV------FHDLIRAMLKVNPEERLSIAEVvrq 151
Cdd:cd06640   178 -YDSKADIWSLGITAIELAKGEPPNSDMHPMRVL---FLIPKNNPPTLVgdfskpFKEFIDACLNKDPSFRPTAKEL--- 250

                         170       180
                  ....*....|....*....|..
gi 1331383559 152 LQEIAAARNVNPKAPITELLEQ 173
Cdd:cd06640   251 LKHKFIVKNAKKTSYLTELIDR 272
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
 8-162 3.01e-09

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: 58.99  E-value: 3.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFG-SATTISHYPDyswsaqkramveeeiTRNTTPMYRTPEIV--DLYSnfpigEKQD 84
Cdd:cd06620   126 IIHRDIKPSNILVNSKGQIKLCDFGvSGELINSIAD---------------TFVGTSTYMSPERIqgGKYS-----VKSD 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  85 IWALGCILYLLCFRQHPFEDGAKL---------------RIVNGKYSIPVNDTRYT-VFHDLIRAMLKVNPEERLSIAEV 148
Cdd:cd06620   186 VWSLGLSIIELALGEFPFAGSNDDddgyngpmgildllqRIVNEPPPRLPKDRIFPkDLRDFVDRCLLKDPRERPSPQLL 265

                         170
                  ....*....|....
gi 1331383559 149 VRQLQEIAAARNVN 162
Cdd:cd06620   266 LDHDPFIQAVRASD 279
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
 1-122 3.83e-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: 58.70  E-value: 3.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGsattIShypdyswsaqKRamVEEEITRNTTPMYR----------TPEI 70
Cdd:cd06628   122 LHNRG--IIHRDIKGANILVDNKGGIKISDFG----IS----------KK--LEANSLSTKNNGARpslqgsvfwmAPEV 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559  71 VD--LYSnfpigEKQDIWALGCILYLLCFRQHPFEDGAKLRIV-----NGKYSIPVNDT 122
Cdd:cd06628   184 VKqtSYT-----RKADIWSLGCLVVEMLTGTHPFPDCTQMQAIfkigeNASPTIPSNIS 237
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
 1-107 4.14e-09

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


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 58.88  E-value: 4.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATtisHYPDyswsaqkramvEEEIT-RNTTPMYRTPEIV--DLYSNF 77
Cdd:cd05630   118 LHRER--IVYRDLKPENILLDDHGHIRISDLGLAV---HVPE-----------GQTIKgRVGTVGYMAPEVVknERYTFS 181

                          90       100       110
                  ....*....|....*....|....*....|
gi 1331383559  78 PigekqDIWALGCILYLLCFRQHPFEDGAK 107
Cdd:cd05630   182 P-----DWWALGCLLYEMIAGQSPFQQRKK 206
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
 1-104 4.26e-09

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: 58.23  E-value: 4.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSAttishypdySWSAQKRAMVEEEITRNT--TPMYRTPEIVDLYSNFP 78
Cdd:cd13978   109 LHNMDPPLLHHDLKPENILLDNHFHVKISDFGLS---------KLGMKSISANRRRGTENLggTPIYMAPEAFDDFNKKP 179

                          90       100
                  ....*....|....*....|....*.
gi 1331383559  79 iGEKQDIWALGCILYLLCFRQHPFED 104
Cdd:cd13978   180 -TSKSDVYSFAIVIWAVLTRKEPFEN 204
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
 1-92 4.43e-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: 58.92  E-value: 4.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIshypdyswSAQKRAMVEEEITRNTTPMYRTPEIVdlysnfpIG 80
Cdd:cd07865   135 IHRNK--ILHRDMKAANILITKDGVLKLADFGLARAF--------SLAKNSQPNRYTNRVVTLWYRPPELL-------LG 197

                          90
                  ....*....|....*..
gi 1331383559  81 EKQ-----DIWALGCIL 92
Cdd:cd07865   198 ERDygppiDMWGAGCIM 214
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
 8-150 4.66e-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: 58.92  E-value: 4.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDyswsAQKRAMVEEEITRnttpMYRTPEIV---DLYSnfpigEKQD 84
Cdd:cd07855   130 VIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPE----EHKYFMTEYVATR----WYRAPELMlslPEYT-----QAID 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  85 IWALGCILYLLCFRQHPF-------------------------EDGAKL--RIVNGKYSIPVND--TRYTVFH----DLI 131
Cdd:cd07855   197 MWSVGCIFAEMLGRRQLFpgknyvhqlqliltvlgtpsqavinAIGADRvrRYIQNLPNKQPVPweTLYPKADqqalDLL 276

                         170
                  ....*....|....*....
gi 1331383559 132 RAMLKVNPEERLSIAEVVR 150
Cdd:cd07855   277 SQMLRFDPSERITVAEALQ 295
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
 8-143 4.68e-09

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: 58.57  E-value: 4.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFG-------SATTIShypdYSWSAQKRAMVEEEITRNTTPMYRTPEIVdLYSNFpiG 80
Cdd:cd05609   121 IVHRDLKPDNLLITSMGHIKLTDFGlskiglmSLTTNL----YEGHIEKDTREFLDKQVCGTPEYIAPEVI-LRQGY--G 193

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331383559  81 EKQDIWALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSIPVNDTRYTV-FHDLIRAMLKVNPEERL 143
Cdd:cd05609   194 KPVDWWAMGIILYEFLVGCVPFfgDTPEELfgQVISDEIEWPEGDDALPDdAQDLITRLLQQNPLERL 261
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 2-143 4.72e-09

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


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 58.17  E-value: 4.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPPIIHRDLKVENLLLSNQGTIKLCDFG-SATTISHYPD--YSWSAqkramveeeitrntTPMYRTPEIV---DLYS 75
Cdd:cd05583   114 HLHKLGIIYRDIKLENILLDSEGHVVLTDFGlSKEFLPGENDraYSFCG--------------TIEYMAPEVVrggSDGH 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  76 NFPIgekqDIWALGCILYLLCFRQHPFE-DGAK-------LRIVngKYSIPVNDTRYTVFHDLIRAMLKVNPEERL 143
Cdd:cd05583   180 DKAV----DWWSLGVLTYELLTGASPFTvDGERnsqseisKRIL--KSHPPIPKTFSAEAKDFILKLLEKDPKKRL 249
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
 8-147 4.84e-09

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: 58.15  E-value: 4.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQG---------TIKLCDFGSAttiSHYPDYSWSAqkramveeeiTRNTTPMYRTPE-IVDLYSNf 77
Cdd:cd14120   113 IVHRDLKPQNILLSHNSgrkpspndiRLKIADFGFA---RFLQDGMMAA----------TLCGSPMYMAPEvIMSLQYD- 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  78 pigEKQDIWALGCILYLLCFRQHPF------------EDGAKLRIvngkySIPVNDTRYtvFHDLIRAMLKVNPEERLSI 145
Cdd:cd14120   179 ---AKADLWSIGTIVYQCLTGKAPFqaqtpqelkafyEKNANLRP-----NIPSGTSPA--LKDLLLGLLKRNPKDRIDF 248


                  ..
gi 1331383559 146 AE 147
Cdd:cd14120   249 ED 250
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 1-153 5.10e-09

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: 58.12  E-value: 5.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFG------SATTISHypdyswsaqkrAMVeeeitrnTTPMYRTPE-IVDL 73
Cdd:cd08228   122 MHSRR--VMHRDIKPANVFITATGVVKLGDLGlgrffsSKTTAAH-----------SLV-------GTPYYMSPErIHEN 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  74 YSNFpigeKQDIWALGCILYLLCFRQHPFEdGAKLRIVNGKYSI------PVNDTRYT-VFHDLIRAMLKVNPEERLSIA 146
Cdd:cd08228   182 GYNF----KSDIWSLGCLLYEMAALQSPFY-GDKMNLFSLCQKIeqcdypPLPTEHYSeKLRELVSMCIYPDPDQRPDIG 256

                         170
                  ....*....|
gi 1331383559 147 ---EVVRQLQ 153
Cdd:cd08228   257 yvhQIAKQMH 266
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
 8-102 5.45e-09

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: 57.99  E-value: 5.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGT--IKLCDFGSATTIShyPDyswsaqkramvEEEITRNTTPMYRTPEIVDlysNFPIGEKQDI 85
Cdd:cd14108   118 VLHLDLKPENLLMADQKTdqVRICDFGNAQELT--PN-----------EPQYCKYGTPEFVAPEIVN---QSPVSKVTDI 181

                          90
                  ....*....|....*..
gi 1331383559  86 WALGCILYLLCFRQHPF 102
Cdd:cd14108   182 WPVGVIAYLCLTGISPF 198
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
 1-147 6.04e-09

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: 57.91  E-value: 6.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQgTIKLCDFGsattishypdyswsaQKRAMVEEEITRNT--TPMYRTPEIVDLYsnfP 78
Cdd:cd14109   115 MHDLG--IAHLDLRPEDILLQDD-KLKLADFG---------------QSRRLLRGKLTTLIygSPEFVSPEIVNSY---P 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331383559  79 IGEKQDIWALGCILYLLCFRQHPF---EDGAKLR-IVNGKYSIpvNDTRYTVF----HDLIRAMLKVNPEERLSIAE 147
Cdd:cd14109   174 VTLATDMWSVGVLTYVLLGGISPFlgdNDRETLTnVRSGKWSF--DSSPLGNIsddaRDFIKKLLVYIPESRLTVDE 248
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
 1-143 6.08e-09

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


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 58.66  E-value: 6.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqKRAMVEEEITRN--TTPMYRTPEIVdlySNFP 78
Cdd:cd05591   112 LHRHG--VIYRDLKLDNILLDAEGHCKLADFGMC--------------KEGILNGKTTTTfcGTPDYIAPEIL---QELE 172

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559  79 IGEKQDIWALGCILYLLCFRQHPF----EDGAKLRIVNGKYSIPVNDTRYTVfhDLIRAMLKVNPEERL 143
Cdd:cd05591   173 YGPSVDWWALGVLMYEMMAGQPPFeadnEDDLFESILHDDVLYPVWLSKEAV--SILKAFMTKNPAKRL 239
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
 8-92 6.14e-09

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: 58.86  E-value: 6.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSwsaqkRAMVEEEITRnttpMYRTPEIV---DLYSnfpigEKQD 84
Cdd:cd07849   127 VLHRDLKPSNLLLNTNCDLKICDFGLARIADPEHDHT-----GFLTEYVATR----WYRAPEIMlnsKGYT-----KAID 192


                  ....*...
gi 1331383559  85 IWALGCIL 92
Cdd:cd07849   193 IWSVGCIL 200
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
 8-163 6.24e-09

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


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 58.49  E-value: 6.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLL----SNQGTIKLCDFGsattishypdysWSAQKRAMVEEEITRNTTPMYRTPEIVdLYSNFPIGekQ 83
Cdd:cd14177   119 VVHRDLKPSNILYmddsANADSIRICDFG------------FAKQLRGENGLLLTPCYTANFVAPEVL-MRQGYDAA--C 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  84 DIWALGCILYLLCFRQHPFEDGAK-------LRIVNGKYSIPVN--DTRYTVFHDLIRAMLKVNPEERLSIAEVVRqlQE 154
Cdd:cd14177   184 DIWSLGVLLYTMLAGYTPFANGPNdtpeeilLRIGSGKFSLSGGnwDTVSDAAKDLLSHMLHVDPHQRYTAEQVLK--HS 261


                  ....*....
gi 1331383559 155 IAAARNVNP 163
Cdd:cd14177   262 WIACRDQLP 270
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
 9-144 6.31e-09

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


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 58.48  E-value: 6.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTI--SHYPDYsWSAQkrAMVeeeitrnTTPMYRTPEIVdlysnFPIGEKQ--D 84
Cdd:cd05598   123 IHRDIKPDNILIDRDGHIKLTDFGLCTGFrwTHDSKY-YLAH--SLV-------GTPNYIAPEVL-----LRTGYTQlcD 187

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  85 IWALGCILYLLCFRQHPF----EDGAKLRIVNGKYS--IPVNDTRYTVFHDLIRAMLkVNPEERLS 144
Cdd:cd05598   188 WWSVGVILYEMLVGQPPFlaqtPAETQLKVINWRTTlkIPHEANLSPEAKDLILRLC-CDAEDRLG 252
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
 8-102 6.92e-09

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: 58.05  E-value: 6.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTishypdYSWSAQKRAMVeeeitrnTTPMYRTPEIVdLYSNF--PIgekqDI 85
Cdd:cd07863   129 IVHRDLKPENILVTSGGQVKLADFGLARI------YSCQMALTPVV-------VTLWYRAPEVL-LQSTYatPV----DM 190

                          90
                  ....*....|....*..
gi 1331383559  86 WALGCILYLLcFRQHPF 102
Cdd:cd07863   191 WSVGCIFAEM-FRRKPL 206
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
 8-151 7.00e-09

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: 58.19  E-value: 7.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIShyPDYSwsaQKRAMVeeeitrnTTPMYRTPEIVdlySNFPIGEKQDIWA 87
Cdd:cd06656   136 VIHRDIKSDNILLGMDGSVKLTDFGFCAQIT--PEQS---KRSTMV-------GTPYWMAPEVV---TRKAYGPKVDIWS 200

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559  88 LGCILYLLCFRQHPFEDGAKLRIV-----NGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQ 151
Cdd:cd06656   201 LGIMAIEMVEGEPPYLNENPLRALyliatNGTPELQNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQH 269
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
 8-147 7.07e-09

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: 57.72  E-value: 7.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGT----IKLCDFGSATTISHYPDYswsaqkramveeeitRNT--TPMYRTPEIVDlYSnfPIGE 81
Cdd:cd14194   129 IAHFDLKPENIMLLDRNVpkprIKIIDFGLAHKIDFGNEF---------------KNIfgTPEFVAPEIVN-YE--PLGL 190

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331383559  82 KQDIWALGCILYLLCFRQHPF------EDGAKLRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAE 147
Cdd:cd14194   191 EADMWSIGVITYILLSGASPFlgdtkqETLANVSAVNYEFEDEYFSNTSALAKDFIRRLLVKDPKKRMTIQD 262
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
 1-92 7.48e-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: 7.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKPPIIHRDLKVENLLL-SNQGTIKLCDFGSATTISHypdyswsaQKRAMVeeeitrNTTPMYRTPEIVDLYSNfpi 79
Cdd:cd13983   118 LHTRDPPIIHRDLKCDNIFInGNTGEVKIGDLGLATLLRQ--------SFAKSV------IGTPEFMAPEMYEEHYD--- 180

                          90
                  ....*....|....
gi 1331383559  80 gEKQDIWALG-CIL 92
Cdd:cd13983   181 -EKVDIYAFGmCLL 193
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
 1-143 8.49e-09

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


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 58.14  E-value: 8.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGsattishypdyswsaqkraMVEEEIT--RNT-----TPMYRTPEIVDl 73
Cdd:cd05571   111 LHSQG--IVYRDLKLENLLLDKDGHIKITDFG-------------------LCKEEISygATTktfcgTPEYLAPEVLE- 168

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331383559  74 ysNFPIGEKQDIWALGCILY-LLCFRQhPF--EDGAKL--RIVNGKYSIPvnDTRYTVFHDLIRAMLKVNPEERL 143
Cdd:cd05571   169 --DNDYGRAVDWWGLGVVMYeMMCGRL-PFynRDHEVLfeLILMEEVRFP--STLSPEAKSLLAGLLKKDPKKRL 238
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
 8-151 9.32e-09

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: 57.73  E-value: 9.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQ---GTIKLCDF--GSATTIShypdyswSAQKRAMVEEEITRNTTPMYRTPEIVDLYSNFPI--G 80
Cdd:cd14174   121 IAHRDLKPENILCESPdkvSPVKICDFdlGSGVKLN-------SACTPITTPELTTPCGSAEYMAPEVVEVFTDEATfyD 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  81 EKQDIWALGCILYLLCFRQHPF----------EDGAKLR---------IVNGKYSIPVNDTRYTVFH--DLIRAMLKVNP 139
Cdd:cd14174   194 KRCDLWSLGVILYIMLSGYPPFvghcgtdcgwDRGEVCRvcqnklfesIQEGKYEFPDKDWSHISSEakDLISKLLVRDA 273

                         170
                  ....*....|..
gi 1331383559 140 EERLSIAEVVRQ 151
Cdd:cd14174   274 KERLSAAQVLQH 285
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
 8-143 1.00e-08

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


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 58.02  E-value: 1.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDF--------GSATTISHYPDYSWSAQ-----KRAMVEEEITR-NT---TPMYRTPEI 70
Cdd:cd05574   124 FVYRDLKPENILLHESGHIMLTDFdlskqssvTPPPVRKSLRKGSRRSSvksieKETFVAEPSARsNSfvgTEEYIAPEV 203

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331383559  71 VDLYSNfpiGEKQDIWALGCILYLLCFRQHPFEDGAK----LRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERL 143
Cdd:cd05574   204 IKGDGH---GSAVDWWTLGILLYEMLYGTTPFKGSNRdetfSNILKKELTFPESPPVSSEAKDLIRKLLVKDPSKRL 277
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
 8-149 1.01e-08

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: 57.58  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQKRAMVEEEITRNTTPMYRTPEivDLYSNfPIGEKQDIWA 87
Cdd:cd14048   139 LIHRDLKPSNVFFSLDDVVKVGDFGLVTAMDQGEPEQTVLTPMPAYAKHTGQVGTRLYMSPE--QIHGN-QYSEKVDIFA 215

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559  88 LGCILYLLCF-------RQHPFEDGAKLRIVngkysiPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVV 149
Cdd:cd14048   216 LGLILFELIYsfstqmeRIRTLTDVRKLKFP------ALFTNKYPEERDMVQQMLSPSPSERPEAHEVI 278
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
 2-93 1.20e-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: 57.32  E-value: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShYPDYSWSAQKramveeeitrnTTPMYRTPEIvdLYSNFPIGE 81
Cdd:cd07873   117 HRRK--VLHRDLKPQNLLINERGELKLADFGLARAKS-IPTKTYSNEV-----------VTLWYRPPDI--LLGSTDYST 180

                          90
                  ....*....|..
gi 1331383559  82 KQDIWALGCILY 93
Cdd:cd07873   181 QIDMWGVGCIFY 192
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
 1-150 1.27e-08

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: 56.98  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIshypdyswsaQKRAMVEEEITRNTTPMYRTPEIV--DLYsnfp 78
Cdd:cd06625   118 LHSNM--IVHRDIKGANILRDSNGNVKLGDFGASKRL----------QTICSSTGMKSVTGTPYWMSPEVIngEGY---- 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  79 iGEKQDIWALGCILYLLCFRQHP---FEDGAKLrivngkYSIPVNDTRYTV-------FHDLIRAMLKVNPEERLSIAEV 148
Cdd:cd06625   182 -GRKADIWSVGCTVVEMLTTKPPwaeFEPMAAI------FKIATQPTNPQLpphvsedARDFLSLIFVRNKKQRPSAEEL 254


                  ..
gi 1331383559 149 VR 150
Cdd:cd06625   255 LS 256
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
 2-148 1.33e-08

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: 57.01  E-value: 1.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswsaqKRAMVEEEITRNT-TPMYRTPEIvdLYSNFPiG 80
Cdd:cd13979   120 HSHG--IVHLDVKPANILISEQGVCKLCDFGCSVKLG----------EGNEVGTPRSHIGgTYTYRAPEL--LKGERV-T 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331383559  81 EKQDIWALGCILYLLCFRQHPFED----------GAKLRIVNGKYSipvNDTRYTVFHDLIRAMLKVNPEERLSIAEV 148
Cdd:cd13979   185 PKADIYSFGITLWQMLTRELPYAGlrqhvlyavvAKDLRPDLSGLE---DSEFGQRLRSLISRCWSAQPAERPNADES 259
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
 1-150 1.39e-08

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: 56.73  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGT----IKLCDFGSATTISHYPDYswsaqkramveeeitRNT--TPMYRTPEIVdly 74
Cdd:cd14105   124 LHTKN--IAHFDLKPENIMLLDKNVpiprIKLIDFGLAHKIEDGNEF---------------KNIfgTPEFVAPEIV--- 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  75 sNF-PIGEKQDIWALGCILYLLCFRQHPFEDGAK----LRIVNGKYSIpvnDTRY-----TVFHDLIRAMLKVNPEERLS 144
Cdd:cd14105   184 -NYePLGLEADMWSIGVITYILLSGASPFLGDTKqetlANITAVNYDF---DDEYfsntsELAKDFIRQLLVKDPRKRMT 259


                  ....*.
gi 1331383559 145 IAEVVR 150
Cdd:cd14105   260 IQESLR 265
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
 2-93 1.50e-08

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: 56.94  E-value: 1.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShYPDYSWSAQKramveeeitrnTTPMYRTPEIV---DLYSNfP 78
Cdd:cd07871   120 HKRK--ILHRDLKPQNLLINEKGELKLADFGLARAKS-VPTKTYSNEV-----------VTLWYRPPDVLlgsTEYST-P 184

                          90
                  ....*....|....*
gi 1331383559  79 IgekqDIWALGCILY 93
Cdd:cd07871   185 I----DMWGVGCILY 195
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
 1-150 1.50e-08

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: 56.68  E-value: 1.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdySWSAQKRAMVeeeitrnTTPMYRTPEIVdlySNFPIG 80
Cdd:cd06648   119 LHSQG--VIHRDIKSDSILLTSDGRVKLSDFGFCAQVS-----KEVPRRKSLV-------GTPYWMAPEVI---SRLPYG 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559  81 EKQDIWALGCILYLLC------FRQHPFEDGAKLRIV---NGKYSIPVNdtryTVFHDLIRAMLKVNPEERLSIAEVVR 150
Cdd:cd06648   182 TEVDIWSLGIMVIEMVdgeppyFNEPPLQAMKRIRDNeppKLKNLHKVS----PRLRSFLDRMLVRDPAQRATAAELLN 256
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
 5-156 1.59e-08

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 57.06  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   5 KPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSwsaqkramveeEITRNT---TPMYRTPEIVD---LYSNFP 78
Cdd:cd14142   128 KPAIAHRDLKSKNILVKSNGQCCIADLGLAVTHSQETNQL-----------DVGNNPrvgTKRYMAPEVLDetiNTDCFE 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  79 IGEKQDIWALGCILYLLCFR----------QHP----------FEDGAKLRIVNG-KYSIP---VNDTRYTVFHDLIRAM 134
Cdd:cd14142   197 SYKRVDIYAFGLVLWEVARRcvsggiveeyKPPfydvvpsdpsFEDMRKVVCVDQqRPNIPnrwSSDPTLTAMAKLMKEC 276

                         170       180
                  ....*....|....*....|..
gi 1331383559 135 LKVNPEERLSIAEVVRQLQEIA 156
Cdd:cd14142   277 WYQNPSARLTALRIKKTLLKIL 298
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 8-144 1.70e-08

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: 56.76  E-value: 1.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGT---IKLCDFGSATtishypdyswsaqkraMVEEEITRNT---TPMYRTPEIVdlySNFPIGE 81
Cdd:cd14085   119 IVHRDLKPENLLYATPAPdapLKIADFGLSK----------------IVDQQVTMKTvcgTPGYCAPEIL---RGCAYGP 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  82 KQDIWALGCILYLLCFRQHPFEDGAK-----LRIVNGKYSI--PVNDTRYTVFHDLIRAMLKVNPEERLS 144
Cdd:cd14085   180 EVDMWSVGVITYILLCGFEPFYDERGdqymfKRILNCDYDFvsPWWDDVSLNAKDLVKKLIVLDPKKRLT 249
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
 4-103 1.81e-08

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


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 57.32  E-value: 1.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   4 QKPPIIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqKRAMVEEEITRN--TTPMYRTPEIVDLYsnfPIGE 81
Cdd:cd05616   118 QSKGIIYRDLKLDNVMLDSEGHIKIADFGMC--------------KENIWDGVTTKTfcGTPDYIAPEIIAYQ---PYGK 180

                          90       100
                  ....*....|....*....|..
gi 1331383559  82 KQDIWALGCILYLLCFRQHPFE 103
Cdd:cd05616   181 SVDWWAFGVLLYEMLAGQAPFE 202
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
 8-147 1.82e-08

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: 56.56  E-value: 1.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQG---------TIKLCDFGSATTIshypdyswsaQKRAMVEeeiTRNTTPMYRTPEIVdLYSNFp 78
Cdd:cd14202   122 IIHRDLKPQNILLSYSGgrksnpnniRIKIADFGFARYL----------QNNMMAA---TLCGSPMYMAPEVI-MSQHY- 186

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331383559  79 iGEKQDIWALGCILYLLCFRQHPFEDGA--KLRIVNGK-YSIPVNDTRYTVFH--DLIRAMLKVNPEERLSIAE 147
Cdd:cd14202   187 -DAKADLWSIGTIIYQCLTGKAPFQASSpqDLRLFYEKnKSLSPNIPRETSSHlrQLLLGLLQRNQKDRMDFDE 259
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 8-151 1.91e-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: 56.54  E-value: 1.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLL---SNQGTIKLCDFGSATtishypdyswsaqkraMVEEEI--TRNTTPMYRTPEIVdlySNFPIGEK 82
Cdd:cd14166   121 IVHRDLKPENLLYltpDENSKIMITDFGLSK----------------MEQNGImsTACGTPGYVAPEVL---AQKPYSKA 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331383559  83 QDIWALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSI--PVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQ 151
Cdd:cd14166   182 VDCWSIGVITYILLCGYPPFyeETESRLfeKIKEGYYEFesPFWDDISESAKDFIRHLLEKNPSKRYTCEKALSH 256
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
 1-102 2.19e-08

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: 56.59  E-value: 2.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswsaqkramvEEEITRNT--TPMYRTPEIVD--LYSN 76
Cdd:cd05605   118 LHSER--IVYRDLKPENILLDDHGHVRISDLGLAVEIP---------------EGETIRGRvgTVGYMAPEVVKneRYTF 180

                          90       100
                  ....*....|....*....|....*.
gi 1331383559  77 FPigekqDIWALGCILYLLCFRQHPF 102
Cdd:cd05605   181 SP-----DWWGLGCLIYEMIEGQAPF 201
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
 8-156 2.21e-08

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 56.22  E-value: 2.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTISHypdysWSAQKRAmveEEITRNTtpMYRTPEIVDLYSNFPIGEKQDIWA 87
Cdd:cd14151   125 IIHRDLKSNNIFLHEDLTVKIGDFGLATVKSR-----WSGSHQF---EQLSGSI--LWMAPEVIRMQDKNPYSFQSDVYA 194

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331383559  88 LGCILYLLCFRQHPF-----EDGAKLRIVNGKYSIPVNDTRYTVFHDLIRAM---LKVNPEERLSIAEVVRQLQEIA 156
Cdd:cd14151   195 FGIVLYELMTGQLPYsninnRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMaecLKKKRDERPLFPQILASIELLA 271
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
 9-142 2.22e-08

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


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 56.19  E-value: 2.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTIShypdySWSAQKRAMVeeeitrnTTPMYRTPEIVDLYSNFPIGEKQDIWAL 88
Cdd:cd06646   128 MHRDIKGANILLTDNGDVKLADFGVAAKIT-----ATIAKRKSFI-------GTPYWMAPEVAAVEKNGGYNQLCDIWAV 195

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331383559  89 GCILYLLCFRQHPFEDGAKLR----IVNGKYSIP--VNDTRY-TVFHDLIRAMLKVNPEER 142
Cdd:cd06646   196 GITAIELAELQPPMFDLHPMRalflMSKSNFQPPklKDKTKWsSTFHNFVKISLTKNPKKR 256
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
 8-151 2.23e-08

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: 56.57  E-value: 2.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLL--SNQ-GTIKLCDFGSATTISHYPDYSWSAqkramVEEEITRNTTPMYRTPEIVDLYSN-FPIGEKQ 83
Cdd:cd14173   121 IAHRDLKPENILCehPNQvSPVKICDFDLGSGIKLNSDCSPIS-----TPELLTPCGSAEYMAPEVVEAFNEeASIYDKR 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  84 -DIWALGCILYLLCFRQHPF-------------------EDGAKLRIVNGKYSIPVNDTRYTVF--HDLIRAMLKVNPEE 141
Cdd:cd14173   196 cDLWSLGVILYIMLSGYPPFvgrcgsdcgwdrgeacpacQNMLFESIQEGKYEFPEKDWAHISCaaKDLISKLLVRDAKQ 275

                         170
                  ....*....|
gi 1331383559 142 RLSIAEVVRQ 151
Cdd:cd14173   276 RLSAAQVLQH 285
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
 1-155 2.93e-08

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 55.76  E-value: 2.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKP-PIIHRDLKVENLL---------LSNQgTIKLCDFGSA------TTISHYPDYSWSAqkramveeeitrnttpm 64
Cdd:cd14148   108 LHNEAIvPIIHRDLKSSNILilepienddLSGK-TLKITDFGLArewhktTKMSAAGTYAWMA----------------- 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  65 yrtPEIVDLySNFpiGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVNG----KYSIPVNDTRYTVFHDLIRAMLKVNPE 140
Cdd:cd14148   170 ---PEVIRL-SLF--SKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGvamnKLTLPIPSTCPEPFARLLEECWDPDPH 243

                         170
                  ....*....|....*
gi 1331383559 141 ERLSIAEVVRQLQEI 155
Cdd:cd14148   244 GRPDFGSILKRLEDI 258
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
 63-149 3.00e-08

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 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: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 55.44  E-value: 3.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  63 PMYRTPEIVDLYSNFPiGEKQDIWALGCILYLLCFRQHPFEDG------AKLRivNGKYSIPvnDTRYTVFHDLIRAMLK 136
Cdd:cd14023   150 PAYVSPEILNTTGTYS-GKSADVWSLGVMLYTLLVGRYPFHDSdpsalfSKIR--RGQFCIP--DHVSPKARCLIRSLLR 224

                          90
                  ....*....|...
gi 1331383559 137 VNPEERLSIAEVV 149
Cdd:cd14023   225 REPSERLTAPEIL 237
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
 8-151 3.07e-08

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: 55.77  E-value: 3.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLL----SNQGTIKLCDFGSATTISHyPDYswsaqkramveeeiTRNTTPMYRTPEIVdlySNFPIGEKQ 83
Cdd:cd14183   125 IVHRDIKPENLLVyehqDGSKSLKLGDFGLATVVDG-PLY--------------TVCGTPTYVAPEII---AETGYGLKV 186

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  84 DIWALGCILYLLCFRQHPF----EDGAKL--RIVNGK--YSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQ 151
Cdd:cd14183   187 DIWAAGVITYILLCGFPPFrgsgDDQEVLfdQILMGQvdFPSPYWDNVSDSAKELITMMLQVDVDQRYSALQVLEH 262
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
 4-143 3.12e-08

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


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 56.15  E-value: 3.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   4 QKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswsaqkramvEEEITRNT--TPMYRTPEIV--DLYSNFPi 79
Cdd:cd05631   119 QRERIVYRDLKPENILLDDRGHIRISDLGLAVQIP---------------EGETVRGRvgTVGYMAPEVInnEKYTFSP- 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331383559  80 gekqDIWALGCILYLLCFRQHPFE--------DGAKLRIVNGK--YSIPVNDTRytvfHDLIRAMLKVNPEERL 143
Cdd:cd05631   183 ----DWWGLGCLIYEMIQGQSPFRkrkervkrEEVDRRVKEDQeeYSEKFSEDA----KSICRMLLTKNPKERL 248
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
 2-91 3.14e-08

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: 55.97  E-value: 3.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRqkppIIHRDLKVENLLLSNQGTIKLCDFGSATtishypdySWSAQKRAMVEEEITRnttpMYRTPEIV---DLYSNfP 78
Cdd:cd07860   119 HR----VLHRDLKPQNLLINTEGAIKLADFGLAR--------AFGVPVRTYTHEVVTL----WYRAPEILlgcKYYST-A 181

                          90
                  ....*....|...
gi 1331383559  79 IgekqDIWALGCI 91
Cdd:cd07860   182 V----DIWSLGCI 190
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
 1-151 3.21e-08

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: 55.73  E-value: 3.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGT----IKLCDFGSATTISHYPDYswsaqkramveeeitRNT--TPMYRTPEIVDlY 74
Cdd:cd14196   124 LHTKK--IAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDGVEF---------------KNIfgTPEFVAPEIVN-Y 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  75 SnfPIGEKQDIWALGCILYLLCFRQHPF------EDGAKLRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEV 148
Cdd:cd14196   186 E--PLGLEADMWSIGVITYILLSGASPFlgdtkqETLANITAVSYDFDEEFFSHTSELAKDFIRKLLVKETRKRLTIQEA 263


                  ...
gi 1331383559 149 VRQ 151
Cdd:cd14196   264 LRH 266
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
 8-151 3.39e-08

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 56.47  E-value: 3.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqKRAMVEEEITRN--TTPMYRTPEIVdlysnfpIGEKQ-- 83
Cdd:cd05619   127 IVYRDLKLDNILLDKDGHIKIADFGMC--------------KENMLGDAKTSTfcGTPDYIAPEIL-------LGQKYnt 185

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331383559  84 --DIWALGCILYLLCFRQHPFEDGAKLRIVNgkySIPVNDTRYTVF-----HDLIRAMLKVNPEERLSIAEVVRQ 151
Cdd:cd05619   186 svDWWSFGVLLYEMLIGQSPFHGQDEEELFQ---SIRMDNPFYPRWlekeaKDILVKLFVREPERRLGVRGDIRQ 257
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 8-148 3.54e-08

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


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 56.03  E-value: 3.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQG---TIKLCDFGSATTishYPDYSWSAQkramveeeiTRNTTPMYRTPEivdLYSNFPIGEKQD 84
Cdd:cd14180   122 VVHRDLKPENILYADESdgaVLKVIDFGFARL---RPQGSRPLQ---------TPCFTLQYAAPE---LFSNQGYDESCD 186

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331383559  85 IWALGCILYLLCFRQHPFEDGAKLRIVNGKYSI--PVNDTRYTV-----------FHDLIRAMLKVNPEERLSIAEV 148
Cdd:cd14180   187 LWSLGVILYTMLSGQVPFQSKRGKMFHNHAADImhKIKEGDFSLegeawkgvseeAKDLVRGLLTVDPAKRLKLSEL 263
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
 8-93 3.56e-08

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


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 56.58  E-value: 3.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQK---------------------RAMVEEEITR-NT---T 62
Cdd:cd05600   132 YIHRDLKPENFLIDSSGHIKLTDFGLASGTLSPKKIESMKIRleevkntafleltakerrniyRAMRKEDQNYaNSvvgS 211

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1331383559  63 PMYRTPEIVDlysnfpiGEKQDI----WALGCILY 93
Cdd:cd05600   212 PDYMAPEVLR-------GEGYDLtvdyWSLGCILF 239
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
 8-143 3.59e-08

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


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 56.17  E-value: 3.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqKRAMVEEEITRN--TTPMYRTPEIVDlysNFPIGEKQDI 85
Cdd:cd05595   116 VVYRDIKLENLMLDKDGHIKITDFGLC--------------KEGITDGATMKTfcGTPEYLAPEVLE---DNDYGRAVDW 178

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331383559  86 WALGCILY-LLCFRQhPF--EDGAKL--RIVNGKYSIPVNDTRYTvfHDLIRAMLKVNPEERL 143
Cdd:cd05595   179 WGLGVVMYeMMCGRL-PFynQDHERLfeLILMEEIRFPRTLSPEA--KSLLAGLLKKDPKQRL 238
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
 3-103 3.69e-08

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: 55.84  E-value: 3.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   3 RQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQKRA-MVEEEITRNTTPMYrtpeivDLYSnfpige 81
Cdd:cd06618   131 KEKHGVIHRDVKPSNILLDESGNVKLCDFGISGRLVDSKAKTRSAGCAAyMAPERIDPPDNPKY------DIRA------ 198

                          90       100
                  ....*....|....*....|..
gi 1331383559  82 kqDIWALGCILYLLCFRQHPFE 103
Cdd:cd06618   199 --DVWSLGISLVELATGQFPYR 218
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
 8-143 4.27e-08

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


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 56.13  E-value: 4.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqKRAMVEEEITRN--TTPMYRTPEIVdlySNFPIGEKQDI 85
Cdd:cd05603   117 IIYRDLKPENILLDCQGHVVLTDFGLC--------------KEGMEPEETTSTfcGTPEYLAPEVL---RKEPYDRTVDW 179

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331383559  86 WALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSIPVNDTRYTVfhDLIRAMLKVNPEERL 143
Cdd:cd05603   180 WCLGAVLYEMLYGLPPFysRDVSQMydNILHKPLHLPGGKTVAAC--DLLQGLLHKDQRRRL 239
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
 7-155 4.66e-08

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 55.43  E-value: 4.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   7 PIIHRDLKVENLLLSNQ--------GTIKLCDFGSA------TTISHYPDYSWSAqkramveeeitrnttpmyrtPEIVD 72
Cdd:cd14146   125 PILHRDLKSSNILLLEKiehddicnKTLKITDFGLArewhrtTKMSAAGTYAWMA--------------------PEVIK 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  73 lYSNFPIGekQDIWALGCILYLLCFRQHPFEDGAKLRIVNG----KYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEV 148
Cdd:cd14146   185 -SSLFSKG--SDIWSYGVLLWELLTGEVPYRGIDGLAVAYGvavnKLTLPIPSTCPEPFAKLMKECWEQDPHIRPSFALI 261


                  ....*..
gi 1331383559 149 VRQLQEI 155
Cdd:cd14146   262 LEQLTAI 268
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
 2-93 5.14e-08

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: 55.46  E-value: 5.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShYPDYSWSaqkramveEEItrnTTPMYRTPEIV---DLYSNfp 78
Cdd:cd07844   115 HQRR--VLHRDLKPQNLLISERGELKLADFGLARAKS-VPSKTYS--------NEV---VTLWYRPPDVLlgsTEYST-- 178

                          90
                  ....*....|....*
gi 1331383559  79 igeKQDIWALGCILY 93
Cdd:cd07844   179 ---SLDMWGVGCIFY 190
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
 1-92 5.25e-08

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: 55.86  E-value: 5.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQG--TIKLCDFGSaTTISHYPDYSWsAQKRamveeeitrnttpMYRTPE-IVDLYSNF 77
Cdd:cd14225   162 LYRER--IIHCDLKPENILLRQRGqsSIKVIDFGS-SCYEHQRVYTY-IQSR-------------FYRSPEvILGLPYSM 224

                          90
                  ....*....|....*
gi 1331383559  78 PIgekqDIWALGCIL 92
Cdd:cd14225   225 AI----DMWSLGCIL 235
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
 2-91 6.11e-08

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: 55.12  E-value: 6.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATtishypdySWSAQKRAMVEEEITRnttpMYRTPEIV---DLYSNfP 78
Cdd:cd07861   118 HSRR--VLHRDLKPQNLLIDNKGVIKLADFGLAR--------AFGIPVRVYTHEVVTL----WYRAPEVLlgsPRYST-P 182

                          90
                  ....*....|...
gi 1331383559  79 IgekqDIWALGCI 91
Cdd:cd07861   183 V----DIWSIGTI 191
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
 8-149 6.23e-08

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


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 54.86  E-value: 6.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLS-NQGTIKLCDFGSATTI--SHYPDYswsaqkramveeeitrNTTPMYRTPEIVDL--YSNFPIgek 82
Cdd:cd14101   129 VVHRDIKDENILVDlRTGDIKLIDFGSGATLkdSMYTDF----------------DGTRVYSPPEWILYhqYHALPA--- 189

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331383559  83 qDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPV-NDTRytvfhDLIRAMLKVNPEERLSIAEVV 149
Cdd:cd14101   190 -TVWSLGILLYDMVCGDIPFERDTDILKAKPSFNKRVsNDCR-----SLIRSCLAYNPSDRPSLEQIL 251
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
 1-149 6.63e-08

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: 54.97  E-value: 6.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShYPDYSWSAQKramveeeitrnTTPMYRTPEIvdLYSNFPIG 80
Cdd:cd07870   114 IHGQH--ILHRDLKPQNLLISYLGELKLADFGLARAKS-IPSQTYSSEV-----------VTLWYRPPDV--LLGATDYS 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  81 EKQDIWALGCIlYLLCFRQHP--------FEDGAKLRIVNGkysIPVNDT------------------------------ 122
Cdd:cd07870   178 SALDIWGAGCI-FIEMLQGQPafpgvsdvFEQLEKIWTVLG---VPTEDTwpgvsklpnykpewflpckpqqlrvvwkrl 253

                         170       180
                  ....*....|....*....|....*...
gi 1331383559 123 -RYTVFHDLIRAMLKVNPEERLSIAEVV 149
Cdd:cd07870   254 sRPPKAEDLASQMLMMFPKDRISAQDAL 281
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 2-143 6.72e-08

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


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 55.31  E-value: 6.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqkRAMVEEEITRN----TTPMYRTPEIVDLYSNF 77
Cdd:cd05614   120 HLHKLGIVYRDIKLENILLDSEGHVVLTDFGLS---------------KEFLTEEKERTysfcGTIEYMAPEIIRGKSGH 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331383559  78 piGEKQDIWALGCILYLLCFRQHPFE-DGAK-------LRIVngKYSIPVNDTRYTVFHDLIRAMLKVNPEERL 143
Cdd:cd05614   185 --GKAVDWWSLGILMFELLTGASPFTlEGEKntqsevsRRIL--KCDPPFPSFIGPVARDLLQKLLCKDPKKRL 254
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
 8-102 7.04e-08

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: 54.66  E-value: 7.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTISHypdyswSAQKramveeeiTRNTTPMYRTPEIVD--LYSNfpigeKQDI 85
Cdd:cd06605   121 IIHRDVKPSNILVNSRGQVKLCDFGVSGQLVD------SLAK--------TFVGTRSYMAPERISggKYTV-----KSDI 181

                          90
                  ....*....|....*..
gi 1331383559  86 WALGCILYLLCFRQHPF 102
Cdd:cd06605   182 WSLGLSLVELATGRFPY 198
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
 8-143 7.18e-08

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


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 55.30  E-value: 7.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGsattishypdyswsaqkraMVEEEI----TRNT---TPMYRTPEIVD--LYsnfp 78
Cdd:cd05590   117 IIYRDLKLDNVLLDHEGHCKLADFG-------------------MCKEGIfngkTTSTfcgTPDYIAPEILQemLY---- 173

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559  79 iGEKQDIWALGCILYLLCFRQHPF----EDGAKLRIVNGKYSIPVNDTRYTVfhDLIRAMLKVNPEERL 143
Cdd:cd05590   174 -GPSVDWWAMGVLLYEMLCGHAPFeaenEDDLFEAILNDEVVYPTWLSQDAV--DILKAFMTKNPTMRL 239
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
 1-143 7.23e-08

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: 54.84  E-value: 7.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIshypdyswSAQKRAMveeeiTRNTTPMYRTPEIV--DLYSNFP 78
Cdd:cd05577   111 LHNRF--IVYRDLKPENILLDDHGHVRISDLGLAVEF--------KGGKKIK-----GRVGTHGYMAPEVLqkEVAYDFS 175

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331383559  79 IgekqDIWALGCILYLLCFRQHPFEDGAK------LRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERL 143
Cdd:cd05577   176 V----DWFALGCMLYEMIAGRSPFRQRKEkvdkeeLKRRTLEMAVEYPDSFSPEARSLCEGLLQKDPERRL 242
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
 9-89 7.72e-08

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: 54.67  E-value: 7.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDyswsAQKRAmveeeitRNT---TPMYRTPEIVDLYSNFpiGEKQDI 85
Cdd:cd06610   124 IHRDVKAGNILLGEDGSVKIADFGVSASLATGGD----RTRKV-------RKTfvgTPCWMAPEVMEQVRGY--DFKADI 190


                  ....
gi 1331383559  86 WALG 89
Cdd:cd06610   191 WSFG 194
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
 8-147 8.47e-08

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: 54.62  E-value: 8.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGT----IKLCDFGSATTISHYPDYswsaqkramveeeitRNT--TPMYRTPEIVDLYsnfPIGE 81
Cdd:cd14195   129 IAHFDLKPENIMLLDKNVpnprIKLIDFGIAHKIEAGNEF---------------KNIfgTPEFVAPEIVNYE---PLGL 190

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331383559  82 KQDIWALGCILYLLCFRQHPF------EDGAKLRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAE 147
Cdd:cd14195   191 EADMWSIGVITYILLSGASPFlgetkqETLTNISAVNYDFDEEYFSNTSELAKDFIRRLLVKDPKKRMTIAQ 262
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
 1-152 9.04e-08

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: 54.25  E-value: 9.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLL--SNQGTIKLCDFGsATtishypdyswsaQKRAMVEEEITRnTTPmYRTPEIVDLYSN-- 76
Cdd:cd13987   107 MHSKN--LVHRDIKPENVLLfdKDCRRVKLCDFG-LT------------RRVGSTVKRVSG-TIP-YTAPEVCEAKKNeg 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  77 FPIGEKQDIWALGCILYLL---CFrqhPFEDGAK--------LRIVNGK-YSIPVNDTRYT-VFHDLIRAMLKVNPEERL 143
Cdd:cd13987   170 FVVDPSIDVWAFGVLLFCCltgNF---PWEKADSddqfyeefVRWQKRKnTAVPSQWRRFTpKALRMFKKLLAPEPERRC 246


                  ....*....
gi 1331383559 144 SIAEVVRQL 152
Cdd:cd13987   247 SIKEVFKYL 255
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
 8-149 9.40e-08

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: 54.26  E-value: 9.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQgtIKlcdfGSATTIShypDYSWSAQKRAMVEEEITrntTPMYRTPEIVdlySNFPIGEKQDIWA 87
Cdd:cd14088   120 IVHRNLKLENLVYYNR--LK----NSKIVIS---DFHLAKLENGLIKEPCG---TPEYLAPEVV---GRQRYGRPVDCWA 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  88 LGCILYLLCFRQHPFEDGAK------------LRIVNGKYSI--PVNDTRYTVFHDLIRAMLKVNPEERLSIAEVV 149
Cdd:cd14088   185 IGVIMYILLSGNPPFYDEAEeddyenhdknlfRKILAGDYEFdsPYWDDISQAAKDLVTRLMEVEQDQRITAEEAI 260
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
 2-150 1.19e-07

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: 54.42  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswSAQKRAMVEEEITRnttpMYRTPEIVdlysnfpIGE 81
Cdd:cd07864   131 YCHKKNFLHRDIKCSNILLNNKGQIKLADFGLARLYN-------SEESRPYTNKVITL----WYRPPELL-------LGE 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  82 KQ-----DIWALGCILYLLcFRQHPFEDG----AKLRIVNGKYSIPVND-----TRYTVFH------------------- 128
Cdd:cd07864   193 ERygpaiDVWSCGCILGEL-FTKKPIFQAnqelAQLELISRLCGSPCPAvwpdvIKLPYFNtmkpkkqyrrrlreefsfi 271

                         170       180
                  ....*....|....*....|....*..
gi 1331383559 129 -----DLIRAMLKVNPEERLSIAEVVR 150
Cdd:cd07864   272 ptpalDLLDHMLTLDPSKRCTAEQALN 298
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
 1-151 1.20e-07

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: 54.34  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKPPIIHRDLKVENLLLSN-QGTIKLCDFGSATTIshypdyswsaqkRAMVEEEITrnTTPMYRTPEIVDLYSNfpi 79
Cdd:cd14031   129 LHTRTPPIIHRDLKCDNIFITGpTGSVKIGDLGLATLM------------RTSFAKSVI--GTPEFMAPEMYEEHYD--- 191

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331383559  80 gEKQDIWALGCILYLLCFRQHPF---EDGAKL--RIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQ 151
Cdd:cd14031   192 -ESVDVYAFGMCMLEMATSEYPYsecQNAAQIyrKVTSGIKPASFNKVTDPEVKEIIEGCIRQNKSERLSIKDLLNH 267
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
 8-146 1.21e-07

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: 53.96  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQG---TIKLCDFGSATTISHypdyswSAQKRAMVeeeitrnTTPMYRTPEIVdlySNFPIGEKQD 84
Cdd:cd14082   124 IVHCDLKPENVLLASAEpfpQVKLCDFGFARIIGE------KSFRRSVV-------GTPAYLAPEVL---RNKGYNRSLD 187

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  85 IWALGCILYLLCFRQHPF--EDGAKLRIVNGKYSIPVNDTRYTVFH--DLIRAMLKVNPEERLSIA 146
Cdd:cd14082   188 MWSVGVIIYVSLSGTFPFneDEDINDQIQNAAFMYPPNPWKEISPDaiDLINNLLQVKMRKRYSVD 253
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
 1-147 1.29e-07

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: 53.77  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGT--IKLCDFGSAttiSHY-PDyswsaqKRAMVeeeitRNTTPMYRTPEIVdlysNF 77
Cdd:cd14103   107 MHKQG--ILHLDLKPENILCVSRTGnqIKIIDFGLA---RKYdPD------KKLKV-----LFGTPEFVAPEVV----NY 166

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331383559  78 -PIGEKQDIWALGCILYLLCFRQHPF---EDGAKL-RIVNGKYSI--PVNDTRYTVFHDLIRAMLKVNPEERLSIAE 147
Cdd:cd14103   167 ePISYATDMWSVGVICYVLLSGLSPFmgdNDAETLaNVTRAKWDFddEAFDDISDEAKDFISKLLVKDPRKRMSAAQ 243
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
 8-91 1.37e-07

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: 54.56  E-value: 1.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGT--IKLCDFGSAtTISHYPDYSWsAQKRamveeeitrnttpMYRTPEIVdL---YSNfPIgek 82
Cdd:cd14212   124 IIHCDLKPENILLVNLDSpeIKLIDFGSA-CFENYTLYTY-IQSR-------------FYRSPEVL-LglpYST-AI--- 183


                  ....*....
gi 1331383559  83 qDIWALGCI 91
Cdd:cd14212   184 -DMWSLGCI 191
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
 9-155 1.39e-07

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 54.62  E-value: 1.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQKRAMVEeeitrnttpmYRTPE-IVD-LYSNfpigeKQDIW 86
Cdd:cd14207   202 IHRDLAARNILLSENNVVKICDFGLARDIYKNPDYVRKGDARLPLK----------WMAPEsIFDkIYST-----KSDVW 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  87 ALGCILY-LLCFRQHPF-------------EDGAKLRIvnGKYSIPvndTRYTVFHDLIRAmlkvNPEERLSIAEVVRQL 152
Cdd:cd14207   267 SYGVLLWeIFSLGASPYpgvqidedfcsklKEGIRMRA--PEFATS---EIYQIMLDCWQG----DPNERPRFSELVERL 337


                  ...
gi 1331383559 153 QEI 155
Cdd:cd14207   338 GDL 340
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 8-152 1.50e-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: 53.74  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSN---QGTIKLCDFGSAttishypdyswSAQKRAMVEeeiTRNTTPMYRTPEIVDlysNFPIGEKQD 84
Cdd:cd14169   122 IVHRDLKPENLLYATpfeDSKIMISDFGLS-----------KIEAQGMLS---TACGTPGYVAPELLE---QKPYGKAVD 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331383559  85 IWALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSI--PVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQL 152
Cdd:cd14169   185 VWAIGVISYILLCGYPPFydENDSELfnQILKAEYEFdsPYWDDISESAKDFIRHLLERDPEKRFTCEQALQHP 258
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 8-151 1.55e-07

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: 53.49  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLL---LSNQGTIKLCDFGsattISHYPDySWSAQKRAMveeeitrnTTPMYRTPEIVdlySNFPIGEKQD 84
Cdd:cd14167   122 IVHRDLKPENLLyysLDEDSKIMISDFG----LSKIEG-SGSVMSTAC--------GTPGYVAPEVL---AQKPYSKAVD 185

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331383559  85 IWALGCILYLLCFRQHPF--EDGAKL--RIVNGKYSI--PVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQ 151
Cdd:cd14167   186 CWSIGVIAYILLCGYPPFydENDAKLfeQILKAEYEFdsPYWDDISDSAKDFIQHLMEKDPEKRFTCEQALQH 258
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
 2-151 2.02e-07

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


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 53.48  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSattishypdyswSAQkraMVEEEITRNT---TPMYRTPEIV----DLY 74
Cdd:cd06638   139 HLHVNKTIHRDVKGNNILLTTEGGVKLVDFGV------------SAQ---LTSTRLRRNTsvgTPFWMAPEVIaceqQLD 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  75 SNFpiGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVngkYSIPVN--------DTRYTVFHDLIRAMLKVNPEERLSIA 146
Cdd:cd06638   204 STY--DARCDVWSLGITAIELGDGDPPLADLHPMRAL---FKIPRNppptlhqpELWSNEFNDFIRKCLTKDYEKRPTVS 278


                  ....*
gi 1331383559 147 EVVRQ 151
Cdd:cd06638   279 DLLQH 283
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
 8-92 2.08e-07

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 54.27  E-value: 2.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLS-NQGTIKLCDFGSATTIshypdyswSAQKRAmveeeITRNTTPMYRTPEIVDLYSNFPIgeKQDIW 86
Cdd:PTZ00036  191 ICHRDLKPQNLLIDpNTHTLKLCDFGSAKNL--------LAGQRS-----VSYICSRFYRAPELMLGATNYTT--HIDLW 255


                  ....*.
gi 1331383559  87 ALGCIL 92
Cdd:PTZ00036  256 SLGCII 261
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
 1-149 2.17e-07

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 53.16  E-value: 2.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKPPIIHRDLKVENLLLSN-QGTIKLCDFGSATTishypdyswsaqKRAMVEEEITrnTTPMYRTPEIVDLYSNfpi 79
Cdd:cd14032   120 LHTRTPPIIHRDLKCDNIFITGpTGSVKIGDLGLATL------------KRASFAKSVI--GTPEFMAPEMYEEHYD--- 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331383559  80 gEKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPVNDTRYTVFHD-----LIRAMLKVNPEERLSIAEVV 149
Cdd:cd14032   183 -ESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTCGIKPASFEKVTDpeikeIIGECICKNKEERYEIKDLL 256
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
 9-152 2.32e-07

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 53.65  E-value: 2.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQKRAMVEeeitrnttpmYRTPE-IVD-LYSNfpigeKQDIW 86
Cdd:cd05054   160 IHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVRKGDARLPLK----------WMAPEsIFDkVYTT-----QSDVW 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  87 ALGCILYLL-----------------CFRqhpFEDGAKLRivNGKYSIPvndtrytvfhDLIRAMLKV---NPEERLSIA 146
Cdd:cd05054   225 SFGVLLWEIfslgaspypgvqmdeefCRR---LKEGTRMR--APEYTTP----------EIYQIMLDCwhgEPKERPTFS 289


                  ....*.
gi 1331383559 147 EVVRQL 152
Cdd:cd05054   290 ELVEKL 295
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
 8-149 2.49e-07

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


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 53.45  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTISH-YPdyswsaQKRAMVeeeitrnTTPMYRTPEIVdlySNFPIGEKQDIW 86
Cdd:cd06659   138 VIHRDIKSDSILLTLDGRVKLSDFGFCAQISKdVP------KRKSLV-------GTPYWMAPEVI---SRCPYGTEVDIW 201

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331383559  87 ALGCILYLLC------FRQHPFEDGAKLR------IVNGKYSIPvndtrytVFHDLIRAMLKVNPEERLSIAEVV 149
Cdd:cd06659   202 SLGIMVIEMVdgeppyFSDSPVQAMKRLRdspppkLKNSHKASP-------VLRDFLERMLVRDPQERATAQELL 269
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
 7-155 2.50e-07

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 53.12  E-value: 2.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   7 PIIHRDLKVENLL---------LSNQgTIKLCDFGSA------TTISHYPDYSWSAqkramveeeitrnttpmyrtPEIV 71
Cdd:cd14145   127 PVIHRDLKSSNILilekvengdLSNK-ILKITDFGLArewhrtTKMSAAGTYAWMA--------------------PEVI 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  72 DlYSNFPIGekQDIWALGCILYLLCFRQHPFEDGAKLRIVNG----KYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAE 147
Cdd:cd14145   186 R-SSMFSKG--SDVWSYGVLLWELLTGEVPFRGIDGLAVAYGvamnKLSLPIPSTCPEPFARLMEDCWNPDPHSRPPFTN 262


                  ....*...
gi 1331383559 148 VVRQLQEI 155
Cdd:cd14145   263 ILDQLTAI 270
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
 8-105 2.54e-07

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: 53.50  E-value: 2.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTishypdYSWSAQKRAMVeeeitrnTTPMYRTPEIVdLYSNF--PIgekqDI 85
Cdd:cd07862   131 VVHRDLKPQNILVTSSGQIKLADFGLARI------YSFQMALTSVV-------VTLWYRAPEVL-LQSSYatPV----DL 192

                          90       100
                  ....*....|....*....|
gi 1331383559  86 WALGCILYLLcFRQHPFEDG 105
Cdd:cd07862   193 WSVGCIFAEM-FRRKPLFRG 211
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
 1-153 2.56e-07

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


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 52.93  E-value: 2.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYswSAQKRAMVeeeitrnttPMYRT-PEIVD--LYSnf 77
Cdd:cd00192   121 LASKK--FVHRDLAARNCLVGEDLVVKISDFGLSRDIYDDDYY--RKKTGGKL---------PIRWMaPESLKdgIFT-- 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  78 pigEKQDIWALGCILY-LLCFRQHPFE----DGAKLRIVNGKY-SIPVNdtrytVFHDLIRAMLKV---NPEERLSIAEV 148
Cdd:cd00192   186 ---SKSDVWSFGVLLWeIFTLGATPYPglsnEEVLEYLRKGYRlPKPEN-----CPDELYELMLSCwqlDPEDRPTFSEL 257


                  ....*
gi 1331383559 149 VRQLQ 153
Cdd:cd00192   258 VERLE 262
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
 8-143 2.68e-07

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: 53.09  E-value: 2.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQG---------TIKLCDFGSATTIshypdyswsaQKRAMVEeeiTRNTTPMYRTPEIVdLYSNFp 78
Cdd:cd14201   126 IIHRDLKPQNILLSYASrkkssvsgiRIKIADFGFARYL----------QSNMMAA---TLCGSPMYMAPEVI-MSQHY- 190

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331383559  79 iGEKQDIWALGCILYLLCFRQHPFEDGA--KLRIVNGKY-----SIPVNDTRYtvFHDLIRAMLKVNPEERL 143
Cdd:cd14201   191 -DAKADLWSIGTVIYQCLVGKPPFQANSpqDLRMFYEKNknlqpSIPRETSPY--LADLLLGLLQRNQKDRM 259
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
 1-173 2.71e-07

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: 53.15  E-value: 2.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKPpiIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswsaqkramvEEEITRNT---TPMYRTPEIVdlySNF 77
Cdd:cd06641   117 LHSEKK--IHRDIKAANVLLSEHGEVKLADFGVAGQLT---------------DTQIKRN*fvgTPFWMAPEVI---KQS 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  78 PIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVN--GKYSIPVNDTRYTV-FHDLIRAMLKVNPEERLSIAEVvrqLQE 154
Cdd:cd06641   177 AYDSKADIWSLGITAIELARGEPPHSELHPMKVLFliPKNNPPTLEGNYSKpLKEFVEACLNKEPSFRPTAKEL---LKH 253

                         170
                  ....*....|....*....
gi 1331383559 155 IAAARNVNPKAPITELLEQ 173
Cdd:cd06641   254 KFILRNAKKTSYLTELIDR 272
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
 63-149 2.81e-07

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 52.73  E-value: 2.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  63 PMYRTPEIVDLYSNFPiGEKQDIWALGCILYLLCFRQHPFED------GAKLRivNGKYSIPvnDTRYTVFHDLIRAMLK 136
Cdd:cd14022   150 PAYVSPEILNTSGSYS-GKAADVWSLGVMLYTMLVGRYPFHDiepsslFSKIR--RGQFNIP--ETLSPKAKCLIRSILR 224

                          90
                  ....*....|...
gi 1331383559 137 VNPEERLSIAEVV 149
Cdd:cd14022   225 REPSERLTSQEIL 237
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
 7-152 2.84e-07

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: 52.94  E-value: 2.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559    7 PIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYS---------WSAqkramveeeitrnttpmyrtPEIVDlYSNF 77
Cdd:smart00221 123 NFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYKvkggklpirWMA--------------------PESLK-EGKF 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   78 piGEKQDIWALGCILY-LLCFRQHPFE--DGAKL--RIVNGKY-SIPVNDTryTVFHDLIRAMLKVNPEERLSIAEVVRQ 151
Cdd:smart00221 182 --TSKSDVWSFGVLLWeIFTLGEEPYPgmSNAEVleYLKKGYRlPKPPNCP--PELYKLMLQCWAEDPEDRPTFSELVEI 257


                   .
gi 1331383559  152 L 152
Cdd:smart00221 258 L 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
 7-152 2.98e-07

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 52.53  E-value: 2.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559    7 PIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYS---------WSAqkramveeeitrnttpmyrtPEIVDL--YS 75
Cdd:smart00219 122 NFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYRkrggklpirWMA--------------------PESLKEgkFT 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   76 nfpigEKQDIWALGCILY-LLCFRQHPFED--GAKL--RIVNGKY-SIPVNDTryTVFHDLIRAMLKVNPEERLSIAEVV 149
Cdd:smart00219 182 -----SKSDVWSFGVLLWeIFTLGEQPYPGmsNEEVleYLKNGYRlPQPPNCP--PELYDLMLQCWAEDPEDRPTFSELV 254


                   ...
gi 1331383559  150 RQL 152
Cdd:smart00219 255 EIL 257
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
 8-147 3.94e-07

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 53.23  E-value: 3.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIShYPDYS--WSAQKRAMVEEEIT-RNTTPMYRTPEIV---DLYsNFPIge 81
Cdd:PTZ00024  140 FMHRDLSPANIFINSKGICKIADFGLARRYG-YPPYSdtLSKDETMQRREEMTsKVVTLWYRAPELLmgaEKY-HFAV-- 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  82 kqDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSI---PVNDT--------RYTVFH-------------------DLI 131
Cdd:PTZ00024  216 --DMWSVGCIFAELLTGKPLFPGENEIDQLGRIFELlgtPNEDNwpqakklpLYTEFTprkpkdlktifpnasddaiDLL 293

                         170
                  ....*....|....*.
gi 1331383559 132 RAMLKVNPEERLSIAE 147
Cdd:PTZ00024  294 QSLLKLNPLERISAKE 309
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
 1-147 4.73e-07

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: 52.20  E-value: 4.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGT--IKLCDFGSATTIShyPDyswsaqkramveeEITRNTTPM--YRTPEIVDlysN 76
Cdd:cd14114   116 MHENN--IVHLDIKPENIMCTTKRSneVKLIDFGLATHLD--PK-------------ESVKVTTGTaeFAAPEIVE---R 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  77 FPIGEKQDIWALGCILYLLCFRQHPF---EDGAKLRIVNG--------KYSIPVNDTRytvfhDLIRAMLKVNPEERLSI 145
Cdd:cd14114   176 EPVGFYTDMWAVGVLSYVLLSGLSPFageNDDETLRNVKScdwnfddsAFSGISEEAK-----DFIRKLLLADPNKRMTI 250


                  ..
gi 1331383559 146 AE 147
Cdd:cd14114   251 HQ 252
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
 8-92 5.61e-07

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: 52.42  E-value: 5.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTishypdyswSAQKRAMVEEEITRnttpMYRTPEIVdlySNFPIGEKQDIWA 87
Cdd:cd07850   123 IIHRDLKPSNIVVKSDCTLKILDFGLART---------AGTSFMMTPYVVTR----YYRAPEVI---LGMGYKENVDIWS 186


                  ....*
gi 1331383559  88 LGCIL 92
Cdd:cd07850   187 VGCIM 191
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
 5-93 6.42e-07

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 51.98  E-value: 6.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   5 KPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHypdyswSAQKRAMVEEE----ITRNTTPMYRTPEIVDLYSNFPIG 80
Cdd:cd14054   120 KPAIAHRDLNSRNVLVKADGSCVICDFGLAMVLRG------SSLVRGRPGAAenasISEVGTLRYMAPEVLEGAVNLRDC 193

                          90
                  ....*....|....*..
gi 1331383559  81 E---KQ-DIWALGCILY 93
Cdd:cd14054   194 EsalKQvDVYALGLVLW 210
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
 8-152 6.49e-07

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


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 52.36  E-value: 6.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIShyPDYSWSAqkramveeeitrntTPMYRTPEIVDLYSNFPIGEKQDIWA 87
Cdd:cd06635   146 MIHRDIKAGNILLTEPGQVKLADFGSASIAS--PANSFVG--------------TPYWMAPEVILAMDEGQYDGKVDVWS 209

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331383559  88 LGCILYLLCFRQHPFEDgakLRIVNGKYSIPVND------TRYT-VFHDLIRAMLKVNPEERLSIAEVVRQL 152
Cdd:cd06635   210 LGITCIELAERKPPLFN---MNAMSALYHIAQNEsptlqsNEWSdYFRNFVDSCLQKIPQDRPTSEELLKHM 278
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
 1-103 6.65e-07

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: 52.04  E-value: 6.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFG-SATTIShypdyswsaqKRAMveeeiTRNTTPMYRTPEIVdlySNFPI 79
Cdd:cd06621   121 LHSRK--IIHRDIKPSNILLTRKGQVKLCDFGvSGELVN----------SLAG-----TFTGTSYYMAPERI---QGGPY 180

                          90       100
                  ....*....|....*....|....
gi 1331383559  80 GEKQDIWALGCILYLLCFRQHPFE 103
Cdd:cd06621   181 SITSDVWSLGLTLLEVAQNRFPFP 204
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
 1-152 6.81e-07

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 51.85  E-value: 6.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLL-----SNQGTIKLCDFGsattISHYpdyswSAQKRAMVEEeitrnTTPMYRTPEIVDlyS 75
Cdd:cd14000   128 LHSAM--IIYRDLKSHNVLVwtlypNSAIIIKIADYG----ISRQ-----CCRMGAKGSE-----GTPGFRAPEIAR--G 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  76 NFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLRI---VNGKYSIPV---NDTRYTVFHDLIRAMLKVNPEERLSIAEVV 149
Cdd:cd14000   190 NVIYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNefdIHGGLRPPLkqyECAPWPEVEVLMKKCWKENPQQRPTAVTVV 269


                  ...
gi 1331383559 150 RQL 152
Cdd:cd14000   270 SIL 272
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
 8-147 7.20e-07

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: 51.59  E-value: 7.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQ---GTIKLCDFGsattISHYPDYSWSAQKRAMVEEeitrnttPMYRTPEIVDlySNFPIGEKQD 84
Cdd:cd14012   125 VVHKSLHAGNVLLDRDagtGIVKLTDYS----LGKTLLDMCSRGSLDEFKQ-------TYWLPPELAQ--GSKSPTRKTD 191

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331383559  85 IWALGCILYLLCFRQHPFE--DGAKLRIVNGKYSIPvndtrytvFHDLIRAMLKVNPEERLSIAE 147
Cdd:cd14012   192 VWDLGLLFLQMLFGLDVLEkyTSPNPVLVSLDLSAS--------LQDFLSKCLSLDPKKRPTALE 248
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
 1-92 7.26e-07

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: 52.44  E-value: 7.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGT--IKLCDFGSaTTISHYPDYSWsAQKRamveeeitrnttpMYRTPEIVdLYSNFp 78
Cdd:cd14224   184 LHRNK--IIHCDLKPENILLKQQGRsgIKVIDFGS-SCYEHQRIYTY-IQSR-------------FYRAPEVI-LGARY- 244

                          90
                  ....*....|....
gi 1331383559  79 iGEKQDIWALGCIL 92
Cdd:cd14224   245 -GMPIDMWSFGCIL 257
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
 8-95 7.46e-07

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: 51.56  E-value: 7.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTISHypdysWSAQKRamVEEEitrNTTPMYRTPEIVDLYSNFPIGEKQDIWA 87
Cdd:cd14150   117 IIHRDLKSNNIFLHEGLTVKIGDFGLATVKTR-----WSGSQQ--VEQP---SGSILWMAPEVIRMQDTNPYSFQSDVYA 186


                  ....*...
gi 1331383559  88 LGCILYLL 95
Cdd:cd14150   187 YGVVLYEL 194
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
 1-96 7.47e-07

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: 52.19  E-value: 7.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRqKPPIIHRDLKVENLLLS-NQGTIKLCDFGSATTISHYpdYSwsaqkramveEEI-TRNttpmYRTPEIVdLYSNFp 78
Cdd:cd14136   135 LHT-KCGIIHTDIKPENVLLCiSKIEVKIADLGNACWTDKH--FT----------EDIqTRQ----YRSPEVI-LGAGY- 195

                          90
                  ....*....|....*...
gi 1331383559  79 iGEKQDIWALGCILYLLC 96
Cdd:cd14136   196 -GTPADIWSTACMAFELA 212
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
 4-142 7.75e-07

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 51.58  E-value: 7.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   4 QKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTIShypDYSWSAQKRAMVEEEITrnttpmyrTPEIVDlYSNFPIgeKQ 83
Cdd:cd05072   121 ERKNYIHRDLRAANVLVSESLMCKIADFGLARVIE---DNEYTAREGAKFPIKWT--------APEAIN-FGSFTI--KS 186

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331383559  84 DIWALGCILY-LLCFRQHPF---EDGAKLRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEER 142
Cdd:cd05072   187 DVWSFGILLYeIVTYGKIPYpgmSNSDVMSALQRGYRMPRMENCPDELYDIMKTCWKEKAEER 249
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
 9-93 7.90e-07

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


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 51.85  E-value: 7.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTI--SHYPdYSwsaqkraMVeeeitrnTTPMYRTPEiVDLYSNFpiGEKQDIW 86
Cdd:cd05599   123 IHRDIKPDNLLLDARGHIKLSDFGLCTGLkkSHLA-YS-------TV-------GTPDYIAPE-VFLQKGY--GKECDWW 184


                  ....*..
gi 1331383559  87 ALGCILY 93
Cdd:cd05599   185 SLGVIMY 191
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
 1-151 8.28e-07

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: 51.47  E-value: 8.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQ---GTIKLCDFGSATTISHypdyswSAQKRAMVeeeitrnTTPMYRTPEIVdlySNF 77
Cdd:cd14197   127 LHNNN--VVHLDLKPQNILLTSEsplGDIKIVDFGLSRILKN------SEELREIM-------GTPEYVAPEIL---SYE 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  78 PIGEKQDIWALGCILYLLCFRQHPF--EDGAKLRIVNGKYSIPVNDTRYTVFH----DLIRAMLKVNPEERLSIAEVVRQ 151
Cdd:cd14197   189 PISTATDMWSIGVLAYVMLTGISPFlgDDKQETFLNISQMNVSYSEEEFEHLSesaiDFIKTLLIKKPENRATAEDCLKH 268
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
 1-143 9.60e-07

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: 51.44  E-value: 9.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTIshyPDYSWSAQkramveeeitRNTTPMYRTPEIV-DLYSNFPI 79
Cdd:cd05607   118 LHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEV---KEGKPITQ----------RAGTNGYMAPEILkEESYSYPV 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331383559  80 gekqDIWALGCILYLLCFRQHPFED--------GAKLRIVNG--KYSIPVNDTRYTvfhDLIRAMLKVNPEERL 143
Cdd:cd05607   185 ----DWFAMGCSIYEMVAGRTPFRDhkekvskeELKRRTLEDevKFEHQNFTEEAK---DICRLFLAKKPENRL 251
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
 4-155 1.13e-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: 51.12  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   4 QKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTIshypDYSWSAQKRAMVEeeitrnTTPMYRTPEivdlYSNFPI-GEK 82
Cdd:cd14066   113 CPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLI----PPSESVSKTSAVK------GTIGYLAPE----YIRTGRvSTK 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  83 QDIWALGCILYLLCFRQHPFEDGAK-------LRIVNGKYSIPVND-------TRYTVFHDLIRAMLKV-------NPEE 141
Cdd:cd14066   179 SDVYSFGVVLLELLTGKPAVDENREnasrkdlVEWVESKGKEELEDildkrlvDDDGVEEEEVEALLRLallctrsDPSL 258

                         170
                  ....*....|....
gi 1331383559 142 RLSIAEVVRQLQEI 155
Cdd:cd14066   259 RPSMKEVVQMLEKL 272
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
 2-93 1.16e-06

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: 51.53  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShYPDYSWSAQKramveeeitrnTTPMYRTPEIVDLYSNFpiGE 81
Cdd:cd07872   121 HRRK--VLHRDLKPQNLLINERGELKLADFGLARAKS-VPTKTYSNEV-----------VTLWYRPPDVLLGSSEY--ST 184

                          90
                  ....*....|..
gi 1331383559  82 KQDIWALGCILY 93
Cdd:cd07872   185 QIDMWGVGCIFF 196
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
 8-147 1.17e-06

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: 50.68  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQ-GTIKLCDFGSATTISHYPdyswsaQKRAmveeeiTRNTTPMYRTPEIvdLYSNFPIGEKQDIW 86
Cdd:cd14019   122 IIHRDVKPGNFLYNREtGKGVLVDFGLAQREEDRP------EQRA------PRAGTRGFRAPEV--LFKCPHQTTAIDIW 187

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559  87 ALGCI-LYLLCfRQHPF----ED-GAKLRIVN--GKYSIpvndtrytvfHDLIRAMLKVNPEERLSIAE 147
Cdd:cd14019   188 SAGVIlLSILS-GRFPFffssDDiDALAEIATifGSDEA----------YDLLDKLLELDPSKRITAEE 245
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
 2-120 1.23e-06

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


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 51.15  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSattishypdyswSAQkraMVEEEITRNT---TPMYRTPEIV--DLYSN 76
Cdd:cd06639   143 HLHNNRIIHRDVKGNNILLTTEGGVKLVDFGV------------SAQ---LTSARLRRNTsvgTPFWMAPEVIacEQQYD 207

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1331383559  77 FPIGEKQDIWALGCILYLLCFRQHPFEDgakLRIVNGKYSIPVN 120
Cdd:cd06639   208 YSYDARCDVWSLGITAIELADGDPPLFD---MHPVKALFKIPRN 248
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
 1-149 1.45e-06

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


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 50.81  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGsattishypdysWSAQKRAMVEEEITRNTTPMYRTPEIVdlySNFPIG 80
Cdd:cd06658   134 LHNQG--VIHRDIKSDSILLTSDGRIKLSDFG------------FCAQVSKEVPKRKSLVGTPYWMAPEVI---SRLPYG 196

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331383559  81 EKQDIWALGCILYLLCFRQHPFEDGAKLRIVNG-KYSIP--VNDTR--YTVFHDLIRAMLKVNPEERLSIAEVV 149
Cdd:cd06658   197 TEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRiRDNLPprVKDSHkvSSVLRGFLDLMLVREPSQRATAQELL 270
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 2-146 1.62e-06

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


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 50.81  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPPIIHRDLKVENLLLSNQG---TIKLCDFGSATTIShyPDYswsaqkramvEEEITRNTTPMYRTPEIVDlYSNFp 78
Cdd:cd14179   117 HMHDVGVVHRDLKPENLLFTDESdnsEIKIIDFGFARLKP--PDN----------QPLKTPCFTLHYAAPELLN-YNGY- 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  79 iGEKQDIWALGCILYLLCFRQHPFEDGAKL-----------RIVNGKYSIPVNDTRYTV--FHDLIRAMLKVNPEERLSI 145
Cdd:cd14179   183 -DESCDLWSLGVILYTMLSGQVPFQCHDKSltctsaeeimkKIKQGDFSFEGEAWKNVSqeAKDLIQGLLTVDPNKRIKM 261


                  .
gi 1331383559 146 A 146
Cdd:cd14179   262 S 262
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
 8-143 1.64e-06

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


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 51.03  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqKRAMVEEEITrNT---TPMYRTPEivdLYSNFPIGEKQD 84
Cdd:cd05585   115 VIYRDLKPENILLDYTGHIALCDFGLC--------------KLNMKDDDKT-NTfcgTPEYLAPE---LLLGHGYTKAVD 176

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331383559  85 IWALGCILYLLCFRQHPFEDgaklRIVNGKYSIPVNDTryTVFH--------DLIRAMLKVNPEERL 143
Cdd:cd05585   177 WWTLGVLLYEMLTGLPPFYD----ENTNEMYRKILQEP--LRFPdgfdrdakDLLIGLLNRDPTKRL 237
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
 8-104 1.85e-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: 50.08  E-value: 1.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTISHypdysWSAqkrAMVEEEITRNTTPMyrTPEIVDLYSNFPIGEKQDIWA 87
Cdd:cd14062   110 IIHRDLKSNNIFLHEDLTVKIGDFGLATVKTR-----WSG---SQQFEQPTGSILWM--APEVIRMQDENPYSFQSDVYA 179

                          90
                  ....*....|....*..
gi 1331383559  88 LGCILYLLCFRQHPFED 104
Cdd:cd14062   180 FGIVLYELLTGQLPYSH 196
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
 8-102 1.97e-06

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 50.41  E-value: 1.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTISHypdysWSAQKRAmveEEITRNTtpMYRTPEIVDLYSNFPIGEKQDIWA 87
Cdd:cd14149   129 IIHRDMKSNNIFLHEGLTVKIGDFGLATVKSR-----WSGSQQV---EQPTGSI--LWMAPEVIRMQDNNPFSFQSDVYS 198

                          90
                  ....*....|....*
gi 1331383559  88 LGCILYLLCFRQHPF 102
Cdd:cd14149   199 YGIVLYELMTGELPY 213
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
 9-102 2.07e-06

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


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 51.16  E-value: 2.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswsaqKRAMVEEEITRNtTPMYRTPEIVDLYSN--FPIGEKQDIW 86
Cdd:cd05624   195 VHRDIKPDNVLLDMNGHIRLADFGSCLKMN----------DDGTVQSSVAVG-TPDYISPEILQAMEDgmGKYGPECDWW 263

                          90
                  ....*....|....*.
gi 1331383559  87 ALGCILYLLCFRQHPF 102
Cdd:cd05624   264 SLGVCMYEMLYGETPF 279
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
 8-151 2.09e-06

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


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 49.99  E-value: 2.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLsnQG-TIKLCDFGSATTIShypdyswsaqkRAMVEEEITRNTTPMYRTPEIVdlySNFP-IGEKQDI 85
Cdd:cd14163   122 VAHRDLKCENALL--QGfTLKLTDFGFAKQLP-----------KGGRELSQTFCGSTAYAAPEVL---QGVPhDSRKGDI 185

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559  86 WALGCILYLLCFRQHPFEDGAKLRIV---NGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQ 151
Cdd:cd14163   186 WSMGVVLYVMLCAQLPFDDTDIPKMLcqqQKGVSLPGHLGVSRTCQDLLKRLLEPDMVLRPSIEEVSWH 254
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
 1-155 2.13e-06

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: 50.20  E-value: 2.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGT-IKLCDFGSATTIShyPDySWSaqKRAMVEEEITRNTTPMyrTPEIVdlySNFPI 79
Cdd:cd13991   114 LHSRK--ILHGDVKADNVLLSSDGSdAFLCDFGHAECLD--PD-GLG--KSLFTGDYIPGTETHM--APEVV---LGKPC 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  80 GEKQDIWALGCILYLLCFRQHP----FEDGAKLRIVNGK---YSIPVNDTRYTVfhDLIRAMLKVNPEERLSIAE----V 148
Cdd:cd13991   182 DAKVDVWSSCCMMLHMLNGCHPwtqyYSGPLCLKIANEPpplREIPPSCAPLTA--QAIQAGLRKEPVHRASAAElrrkT 259


                  ....*..
gi 1331383559 149 VRQLQEI 155
Cdd:cd13991   260 NRALQEV 266
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
 8-102 2.35e-06

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: 50.44  E-value: 2.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGsattISHYPDYSWSAQKRA-----MVEEEITRNttpmyRTPEIVDLYSnfpigek 82
Cdd:cd06616   131 IIHRDVKPSNILLDRNGNIKLCDFG----ISGQLVDSIAKTRDAgcrpyMAPERIDPS-----ASRDGYDVRS------- 194

                          90       100
                  ....*....|....*....|
gi 1331383559  83 qDIWALGCILYLLCFRQHPF 102
Cdd:cd06616   195 -DVWSLGITLYEVATGKFPY 213
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
 1-149 2.41e-06

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: 50.00  E-value: 2.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKPPIIHRDLKVENLLLSN-QGTIKLCDFGSATTishypdyswsaqKRAMVEEEITrnTTPMYRTPEIVDLYSNfpi 79
Cdd:cd14033   120 LHSRCPPILHRDLKCDNIFITGpTGSVKIGDLGLATL------------KRASFAKSVI--GTPEFMAPEMYEEKYD--- 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331383559  80 gEKQDIWALGCILYLLCFRQHPF---EDGAKL--RIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVV 149
Cdd:cd14033   183 -EAVDVYAFGMCILEMATSEYPYsecQNAAQIyrKVTSGIKPDSFYKVKVPELKEIIEGCIRTDKDERFTIQDLL 256
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
 8-143 2.73e-06

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


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 50.48  E-value: 2.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFG-SATTISHYPD-YSWSAqkramveeeitrntTPMYRTPEIVDLYSNfpiGEKQDI 85
Cdd:cd05582   118 IIYRDLKPENILLDEDGHIKLTDFGlSKESIDHEKKaYSFCG--------------TVEYMAPEVVNRRGH---TQSADW 180

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331383559  86 WALGCILYLLCFRQHPFEdgAKLR------IVNGKYSIPVNDTRYTvfHDLIRAMLKVNPEERL 143
Cdd:cd05582   181 WSFGVLMFEMLTGSLPFQ--GKDRketmtmILKAKLGMPQFLSPEA--QSLLRALFKRNPANRL 240
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
 1-148 2.82e-06

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


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 50.26  E-value: 2.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSA--------------TTISHYP---DYSWSAQKRAMVEEEITRNTTP 63
Cdd:cd05610   120 LHRHG--IIHRDLKPDNMLISNEGHIKLTDFGLSkvtlnrelnmmdilTTPSMAKpknDYSRTPGQVLSLISSLGFNTPT 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  64 MYRTPEIV---------------------DLYSNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLR----IVNGKYSIP 118
Cdd:cd05610   198 PYRTPKSVrrgaarvegerilgtpdylapELLLGKPHGPAVDWWALGVCLFEFLTGIPPFNDETPQQvfqnILNRDIPWP 277

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1331383559 119 VNDTRYTV-FHDLIRAMLKVNPEERLSIAEV 148
Cdd:cd05610   278 EGEEELSVnAQNAIEILLTMDPTKRAGLKEL 308
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
 3-156 2.85e-06

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 50.07  E-value: 2.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   3 RQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTIshypDYSWSAQKRAmveeeitrNT----TPMYRTPEIVDLYSNFP 78
Cdd:cd14055   123 RPKIPIAHRDLKSSNILVKNDGTCVLADFGLALRL----DPSLSVDELA--------NSgqvgTARYMAPEALESRVNLE 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  79 IGE--KQ-DIWALGCIL---------------YLLCF----RQHPFEDGAKLRIVNGKYSIPVNDTRYTvfHDLIRAMLK 136
Cdd:cd14055   191 DLEsfKQiDVYSMALVLwemasrceasgevkpYELPFgskvRERPCVESMKDLVLRDRGRPEIPDSWLT--HQGMCVLCD 268

                         170       180
                  ....*....|....*....|....*..
gi 1331383559 137 V-------NPEERLSIAEVVRQLQEIA 156
Cdd:cd14055   269 TitecwdhDPEARLTASCVAERFNELK 295
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
 8-148 2.85e-06

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: 50.12  E-value: 2.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGsattISHYPDYSwsaqkramVEEEITRNTTPmYRTPEIVDlysnfPIGE------ 81
Cdd:cd06617   125 VIHRDVKPSNVLINRNGQVKLCDFG----ISGYLVDS--------VAKTIDAGCKP-YMAPERIN-----PELNqkgydv 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  82 KQDIWALGCILYLLCFRQHPFE-------------DGAKLRIVNGKYSIPvndtrytvFHDLIRAMLKVNPEERLSIAEV 148
Cdd:cd06617   187 KSDVWSLGITMIELATGRFPYDswktpfqqlkqvvEEPSPQLPAEKFSPE--------FQDFVNKCLKKNYKERPNYPEL 258
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
 8-150 2.85e-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: 50.12  E-value: 2.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIShYPDYSWSAQKramveeeitrnTTPMYRTPEIV---DLYSNfpigeKQD 84
Cdd:cd07839   120 VLHRDLKPQNLLINKNGELKLADFGLARAFG-IPVRCYSAEV-----------VTLWYRPPDVLfgaKLYST-----SID 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  85 IWALGCILYLLCFRQHPFEDGA----KLRIVNGKYSIPVNDT--------RYTVF--------------------HDLIR 132
Cdd:cd07839   183 MWSAGCIFAELANAGRPLFPGNdvddQLKRIFRLLGTPTEESwpgvsklpDYKPYpmypattslvnvvpklnstgRDLLQ 262

                         170
                  ....*....|....*...
gi 1331383559 133 AMLKVNPEERLSIAEVVR 150
Cdd:cd07839   263 NLLVCNPVQRISAEEALQ 280
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
 8-92 2.87e-06

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: 50.14  E-value: 2.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGT----IKLCDFGSATTIShypdyswsaqkRAMVEeeiTRNTTPMYRTPEIVdlySNFPIGEKQ 83
Cdd:cd14211   122 LIHADLKPENIMLVDPVRqpyrVKVIDFGSASHVS-----------KAVCS---TYLQSRYYRAPEII---LGLPFCEAI 184


                  ....*....
gi 1331383559  84 DIWALGCIL 92
Cdd:cd14211   185 DMWSLGCVI 193
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
 8-151 2.98e-06

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


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 49.66  E-value: 2.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIshypdyswsaQKRAMVEEEITRNT-TPMYRTPEIVdlySNFPIGEKQDIW 86
Cdd:cd06652   127 IVHRDIKGANILRDSVGNVKLGDFGASKRL----------QTICLSGTGMKSVTgTPYWMSPEVI---SGEGYGRKADIW 193

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331383559  87 ALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPVNDTRYTVFHDLIRAMLK---VNPEERLSIAEVVRQ 151
Cdd:cd06652   194 SVGCTVVEMLTEKPPWAEFEAMAAIFKIATQPTNPQLPAHVSDHCRDFLKrifVEAKLRPSADELLRH 261
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
 7-155 3.17e-06

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 49.64  E-value: 3.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   7 PIIHRDLKVENLLLSNQG--------TIKLCDFGSA------TTISHYPDYSWSAqkramveeeitrnttpmyrtPEIVD 72
Cdd:cd14147   124 PVIHRDLKSNNILLLQPIenddmehkTLKITDFGLArewhktTQMSAAGTYAWMA--------------------PEVIK 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  73 lYSNFPIGekQDIWALGCILYLLCFRQHPFEDGAKLRIVNG----KYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEV 148
Cdd:cd14147   184 -ASTFSKG--SDVWSFGVLLWELLTGEVPYRGIDCLAVAYGvavnKLTLPIPSTCPEPFAQLMADCWAQDPHRRPDFASI 260


                  ....*..
gi 1331383559 149 VRQLQEI 155
Cdd:cd14147   261 LQQLEAL 267
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
 8-102 3.23e-06

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


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 49.96  E-value: 3.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGsattishypdysWSAQKRAMVEEEITRNTTPMYRTPEIVdlySNFPIGEKQDIWA 87
Cdd:cd05604   118 IVYRDLKPENILLDSQGHIVLTDFG------------LCKEGISNSDTTTTFCGTPEYLAPEVI---RKQPYDNTVDWWC 182

                          90
                  ....*....|....*
gi 1331383559  88 LGCILYLLCFRQHPF 102
Cdd:cd05604   183 LGSVLYEMLYGLPPF 197
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
 1-110 3.24e-06

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


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 49.97  E-value: 3.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswsaqkramvEEEITRNT--TPMYRTPEIVDlysNFP 78
Cdd:cd05632   120 LHREN--TVYRDLKPENILLDDYGHIRISDLGLAVKIP---------------EGESIRGRvgTVGYMAPEVLN---NQR 179

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1331383559  79 IGEKQDIWALGCILYLLCFRQHPFEdGAKLRI 110
Cdd:cd05632   180 YTLSPDYWGLGCLIYEMIEGQSPFR-GRKEKV 210
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
 9-148 3.69e-06

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


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 50.07  E-value: 3.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswsaqKRAMVEEEiTRNTTPMYRTPEIVDLYSNFPI-GEKQDIWA 87
Cdd:cd05596   147 VHRDVKPDNMLLDASGHLKLADFGTCMKMD----------KDGLVRSD-TAVGTPDYISPEVLKSQGGDGVyGRECDWWS 215

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  88 LGCILYLLCFRQHPFED----GAKLRIVNGKYSI--PVNDTRYTVFHDLIRAMLkVNPEERL---SIAEV 148
Cdd:cd05596   216 VGVFLYEMLVGDTPFYAdslvGTYGKIMNHKNSLqfPDDVEISKDAKSLICAFL-TDREVRLgrnGIEEI 284
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 8-151 4.47e-06

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: 49.66  E-value: 4.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQgtiklcDFGSATTISHYPDYSWSAQKRAMVeeeiTRNTTPMYRTPEIVdlySNFPIGEKQDIWA 87
Cdd:cd14168   129 IVHRDLKPENLLYFSQ------DEESKIMISDFGLSKMEGKGDVMS----TACGTPGYVAPEVL---AQKPYSKAVDCWS 195

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  88 LGCILYLLCFRQHPF--EDGAKL--RIVNGKYSI--PVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQ 151
Cdd:cd14168   196 IGVIAYILLCGYPPFydENDSKLfeQILKADYEFdsPYWDDISDSAKDFIRNLMEKDPNKRYTCEQALRH 265
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 2-143 4.51e-06

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


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 49.61  E-value: 4.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqkRAMVEEEITRN----TTPMYRTPEIVDLYSNf 77
Cdd:cd05613   120 HLHKLGIIYRDIKLENILLDSSGHVVLTDFGLS---------------KEFLLDENERAysfcGTIEYMAPEIVRGGDS- 183

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  78 piGEKQ--DIWALGCILYLLCFRQHPFE-DGAK-------LRIVngKYSIPVNDTRYTVFHDLIRAMLKVNPEERL 143
Cdd:cd05613   184 --GHDKavDWWSLGVLMYELLTGASPFTvDGEKnsqaeisRRIL--KSEPPYPQEMSALAKDIIQRLLMKDPKKRL 255
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
 8-150 4.70e-06

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 49.56  E-value: 4.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGsattishypdyswsaqkraMVEEEI-------TRNTTPMYRTPEIVD-LYSNFPI 79
Cdd:cd05620   117 IIYRDLKLDNVMLDRDGHIKIADFG-------------------MCKENVfgdnrasTFCGTPDYIAPEILQgLKYTFSV 177

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  80 gekqDIWALGCILYLLCFRQHPFEDGAKLRIVNgkySIPVNDTRYTVF-----HDLIRAMLKVNPEERLSIAEVVR 150
Cdd:cd05620   178 ----DWWSFGVLLYEMLIGQSPFHGDDEDELFE---SIRVDTPHYPRWitkesKDILEKLFERDPTRRLGVVGNIR 246
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
 9-142 4.79e-06

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


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 49.27  E-value: 4.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSattishypdyswSAQKRAMVEEEITRNTTPMYRTPEIVDLYSNFPIGEKQDIWAL 88
Cdd:cd06645   130 MHRDIKGANILLTDNGHVKLADFGV------------SAQITATIAKRKSFIGTPYWMAPEVAAVERKGGYNQLCDIWAV 197

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331383559  89 GCILYLLCFRQHPFEDGAKLR----IVNGKYSIP--VNDTRYT-VFHDLIRAMLKVNPEER 142
Cdd:cd06645   198 GITAIELAELQPPMFDLHPMRalflMTKSNFQPPklKDKMKWSnSFHHFVKMALTKNPKKR 258
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
 8-102 4.86e-06

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 50.51  E-value: 4.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559    8 IIHRDLKVENLLLSNQ----GTI-------------KLCDFGSATTIShypdyswsaqKRAMVEEEITrntTPMYRTPEI 70
Cdd:PTZ00266   146 VLHRDLKPQNIFLSTGirhiGKItaqannlngrpiaKIGDFGLSKNIG----------IESMAHSCVG---TPYYWSPEL 212

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1331383559   71 VdLYSNFPIGEKQDIWALGCILYLLCFRQHPF 102
Cdd:PTZ00266   213 L-LHETKSYDDKSDMWALGCIIYELCSGKTPF 243
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
 1-104 5.23e-06

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-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: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 49.03  E-value: 5.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSAttishypdySWSAQKRAMVEEEITRNTTPMYRTPEIVdLYSNFPIG 80
Cdd:cd14025   108 LHCMKPPLLHLDLKPANILLDAHYHVKISDFGLA---------KWNGLSHSHDLSRDGLRGTIAYLPPERF-KEKNRCPD 177

                          90       100
                  ....*....|....*....|....
gi 1331383559  81 EKQDIWALGCILYLLCFRQHPFED 104
Cdd:cd14025   178 TKHDVYSFAIVIWGILTQKKPFAG 201
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
 1-143 5.31e-06

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


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 49.64  E-value: 5.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKPpIIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqkRAMVEEEITRNT---TPMYRTPEIVDlysNF 77
Cdd:cd05594   141 LHSEKN-VVYRDLKLENLMLDKDGHIKITDFGLC---------------KEGIKDGATMKTfcgTPEYLAPEVLE---DN 201

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331383559  78 PIGEKQDIWALGCILYLLCFRQHPF--EDGAKLRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERL 143
Cdd:cd05594   202 DYGRAVDWWGLGVVMYEMMCGRLPFynQDHEKLFELILMEEIRFPRTLSPEAKSLLSGLLKKDPKQRL 269
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
 1-149 5.46e-06

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 49.28  E-value: 5.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKPPIIHRDLKVENLLLSN-QGTIKLCDFGSATTishypdyswsaqKRAMVEEEITrnTTPMYRTPEIVDLYSNfpi 79
Cdd:cd14030   144 LHTRTPPIIHRDLKCDNIFITGpTGSVKIGDLGLATL------------KRASFAKSVI--GTPEFMAPEMYEEKYD--- 206

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331383559  80 gEKQDIWALGCILYLLCFRQHPF---EDGAKL--RIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVV 149
Cdd:cd14030   207 -ESVDVYAFGMCMLEMATSEYPYsecQNAAQIyrRVTSGVKPASFDKVAIPEVKEIIEGCIRQNKDERYAIKDLL 280
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
 2-92 5.48e-06

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: 49.66  E-value: 5.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTishypdyswsAQKRAMVEEEItrnTTPMYRTPEIVdlysnFPIGE 81
Cdd:cd07875   141 HLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLART----------AGTSFMMTPYV---VTRYYRAPEVI-----LGMGY 202

                          90
                  ....*....|...
gi 1331383559  82 KQ--DIWALGCIL 92
Cdd:cd07875   203 KEnvDIWSVGCIM 215
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
 8-92 5.70e-06

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: 49.49  E-value: 5.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTishypdyswsaQKRAMVEEEITRnttpMYRTPEIVDLYSNFpiGEKQDIWA 87
Cdd:cd07856   129 VIHRDLKPSNILVNENCDLKICDFGLARI-----------QDPQMTGYVSTR----YYRAPEIMLTWQKY--DVEVDIWS 191


                  ....*
gi 1331383559  88 LGCIL 92
Cdd:cd07856   192 AGCIF 196
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
 8-149 5.73e-06

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


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 48.81  E-value: 5.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLS-NQGTIKLCDFGSATTISH--YPDYswsaqkramveeeitrNTTPMYRTPEIVDLYSNFpiGEKQD 84
Cdd:cd14100   127 VLHRDIKDENILIDlNTGELKLIDFGSGALLKDtvYTDF----------------DGTRVYSPPEWIRFHRYH--GRSAA 188

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331383559  85 IWALGCILYLLCFRQHPFEDGAKlrIVNGKysIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVV 149
Cdd:cd14100   189 VWSLGILLYDMVCGDIPFEHDEE--IIRGQ--VFFRQRVSSECQHLIKWCLALRPSDRPSFEDIQ 249
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
 8-104 5.96e-06

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: 48.87  E-value: 5.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIshypdyswsaQKRAMVEEEITRNT-TPMYRTPEIVdlySNFPIGEKQDIW 86
Cdd:cd06653   127 IVHRDIKGANILRDSAGNVKLGDFGASKRI----------QTICMSGTGIKSVTgTPYWMSPEVI---SGEGYGRKADVW 193

                          90
                  ....*....|....*...
gi 1331383559  87 ALGCILYLLCFRQHPFED 104
Cdd:cd06653   194 SVACTVVEMLTEKPPWAE 211
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
 8-92 6.55e-06

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


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 48.96  E-value: 6.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATtishypdySWSAQKraMVEEEITRNttpmYRTPEIVdlySNFPIGEKQDIWA 87
Cdd:cd14052   127 FVHLDLKPANVLITFEGTLKIGDFGMAT--------VWPLIR--GIEREGDRE----YIAPEIL---SEHMYDKPADIFS 189


                  ....*
gi 1331383559  88 LGCIL 92
Cdd:cd14052   190 LGLIL 194
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
 9-93 6.96e-06

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 49.21  E-value: 6.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQKRAMVEeeitrnttpmYRTPE-IVD-LYSNfpigeKQDIW 86
Cdd:cd05103   201 IHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVRKGDARLPLK----------WMAPEtIFDrVYTI-----QSDVW 265


                  ....*..
gi 1331383559  87 ALGCILY 93
Cdd:cd05103   266 SFGVLLW 272
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
 8-174 7.08e-06

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


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 48.87  E-value: 7.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGsattishypdysWSAQKRAMVEEEITRNTTPMYRTPEIVdlySNFPIGEKQDIWA 87
Cdd:cd06657   137 VIHRDIKSDSILLTHDGRVKLSDFG------------FCAQVSKEVPRRKSLVGTPYWMAPELI---SRLPYGPEVDIWS 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  88 LGCILYLLCFRQHPFEDGAKLRIVNG-KYSIPVNDTRYTVFHDLIRA----MLKVNPEERLSIAEVVRQlqeiAAARNVN 162
Cdd:cd06657   202 LGIMVIEMVDGEPPYFNEPPLKAMKMiRDNLPPKLKNLHKVSPSLKGfldrLLVRDPAQRATAAELLKH----PFLAKAG 277

                         170
                  ....*....|..
gi 1331383559 163 PKAPITELLEQN 174
Cdd:cd06657   278 PPSCIVPLMRQN 289
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 1-102 7.29e-06

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


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 48.87  E-value: 7.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdySWSAQKRAMVeeeitrnTTPMYRTPE-IVDLYSNFpi 79
Cdd:cd08229   144 MHSRR--VMHRDIKPANVFITATGVVKLGDLGLGRFFS-----SKTTAAHSLV-------GTPYYMSPErIHENGYNF-- 207

                          90       100
                  ....*....|....*....|...
gi 1331383559  80 geKQDIWALGCILYLLCFRQHPF 102
Cdd:cd08229   208 --KSDIWSLGCLLYEMAALQSPF 228
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
 9-93 8.76e-06

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 48.82  E-value: 8.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQKRAMVEeeitrnttpmYRTPE-IVD-LYSNfpigeKQDIW 86
Cdd:cd05102   194 IHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVRKGSARLPLK----------WMAPEsIFDkVYTT-----QSDVW 258


                  ....*..
gi 1331383559  87 ALGCILY 93
Cdd:cd05102   259 SFGVLLW 265
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
 8-102 8.86e-06

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


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 48.86  E-value: 8.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqkRAMVEEEITRNT---TPMYRTPEIVdlySNFPIGEKQD 84
Cdd:cd05602   129 IVYRDLKPENILLDSQGHIVLTDFGLC---------------KENIEPNGTTSTfcgTPEYLAPEVL---HKQPYDRTVD 190

                          90
                  ....*....|....*...
gi 1331383559  85 IWALGCILYLLCFRQHPF 102
Cdd:cd05602   191 WWCLGAVLYEMLYGLPPF 208
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
 8-92 9.86e-06

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: 48.25  E-value: 9.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIShYPDYSWSAQKramveeeitrnTTPMYRTPEIV---DLYSNfpigeKQD 84
Cdd:cd07836   121 VLHRDLKPQNLLINKRGELKLADFGLARAFG-IPVNTFSNEV-----------VTLWYRAPDVLlgsRTYST-----SID 183


                  ....*...
gi 1331383559  85 IWALGCIL 92
Cdd:cd07836   184 IWSVGCIM 191
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
 8-102 1.10e-05

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


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 48.48  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIShyPDYSWSAqkramveeeitrntTPMYRTPEIVDLYSNFPIGEKQDIWA 87
Cdd:cd06634   136 MIHRDVKAGNILLTEPGLVKLGDFGSASIMA--PANSFVG--------------TPYWMAPEVILAMDEGQYDGKVDVWS 199

                          90
                  ....*....|....*
gi 1331383559  88 LGCILYLLCFRQHPF 102
Cdd:cd06634   200 LGITCIELAERKPPL 214
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
 9-143 1.11e-05

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


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 48.50  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTishypdyswsaqkraMVEEEITRNT----TPMYRTPEIV----DLYSNFpiG 80
Cdd:cd05597   124 VHRDIKPDNVLLDRNGHIRLADFGSCLK---------------LREDGTVQSSvavgTPDYISPEILqameDGKGRY--G 186

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  81 EKQDIWALGCILYLLCFRQHPF--EDGAKL--RIVN--GKYSIPVNDTRYT-VFHDLIRAMLkVNPEERL 143
Cdd:cd05597   187 PECDWWSLGVCMYEMLYGETPFyaESLVETygKIMNhkEHFSFPDDEDDVSeEAKDLIRRLI-CSRERRL 255
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
 8-102 1.11e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 48.69  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPD----YSWSAqkramveeeitrntTPMYRTPEIVDLYsnfPIGEKQ 83
Cdd:PHA03207  206 IIHRDVKTENIFLDEPENAVLGDFGAACKLDAHPDtpqcYGWSG--------------TLETNSPELLALD---PYCAKT 268

                          90
                  ....*....|....*....
gi 1331383559  84 DIWALGCILYLLCFRQHPF 102
Cdd:PHA03207  269 DIWSAGLVLFEMSVKNVTL 287
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
 8-143 1.12e-05

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


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 48.54  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqkRAMVEEEITRNT---TPMYRTPEIVDlysNFPIGEKQD 84
Cdd:cd05593   136 IVYRDLKLENLMLDKDGHIKITDFGLC---------------KEGITDAATMKTfcgTPEYLAPEVLE---DNDYGRAVD 197

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331383559  85 IWALGCILYLLCFRQHPF--EDGAKLRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERL 143
Cdd:cd05593   198 WWGLGVVMYEMMCGRLPFynQDHEKLFELILMEDIKFPRTLSADAKSLLSGLLIKDPNKRL 258
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
 1-102 1.14e-05

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: 47.99  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGT--IKLCDFGSAttishypdyswsaqKRAMVEEEITRN-TTPMYRTPEIVdlysNF 77
Cdd:cd14190   118 MHQMR--VLHLDLKPENILCVNRTGhqVKIIDFGLA--------------RRYNPREKLKVNfGTPEFLSPEVV----NY 177

                          90       100
                  ....*....|....*....|....*.
gi 1331383559  78 P-IGEKQDIWALGCILYLLCFRQHPF 102
Cdd:cd14190   178 DqVSFPTDMWSMGVITYMLLSGLSPF 203
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
 8-148 1.21e-05

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


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 47.64  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLS-NQGTIKLCDFGSATTISH--YPDYswsaqkramveeeitrNTTPMYRTPEIVDLYSNFpiGEKQD 84
Cdd:cd14102   126 VVHRDIKDENLLVDlRTGELKLIDFGSGALLKDtvYTDF----------------DGTRVYSPPEWIRYHRYH--GRSAT 187

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331383559  85 IWALGCILYLLCFRQHPFEDGAKlrIVNGKYSIPVNDTryTVFHDLIRAMLKVNPEERLSIAEV 148
Cdd:cd14102   188 VWSLGVLLYDMVCGDIPFEQDEE--ILRGRLYFRRRVS--PECQQLIKWCLSLRPSDRPTLEQI 247
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
 9-142 1.23e-05

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 47.79  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTIshypdyswsaqkraMVEEEIT-RNTT--PMYRT-PEIVdLYSNFPIgeKQD 84
Cdd:cd05068   126 IHRDLAARNVLVGENNICKVADFGLARVI--------------KVEDEYEaREGAkfPIKWTaPEAA-NYNRFSI--KSD 188

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331383559  85 IWALGCILY-LLCFRQHPFE--DGAK-LRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEER 142
Cdd:cd05068   189 VWSFGILLTeIVTYGRIPYPgmTNAEvLQQVERGYRMPCPPNCPPQLYDIMLECWKADPMER 250
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
 2-92 1.23e-05

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: 48.49  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTishypdyswSAQKRAMVEEEITRnttpMYRTPEIVdlySNFPIGE 81
Cdd:cd07876   138 HLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLART---------ACTNFMMTPYVVTR----YYRAPEVI---LGMGYKE 201

                          90
                  ....*....|.
gi 1331383559  82 KQDIWALGCIL 92
Cdd:cd07876   202 NVDIWSVGCIM 212
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
 8-92 1.33e-05

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: 48.15  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIShYPDYSWSAQKramveeeitrnTTPMYRTPEIvdLYSNFPIGEKQDIWA 87
Cdd:cd07869   124 ILHRDLKPQNLLISDTGELKLADFGLARAKS-VPSHTYSNEV-----------VTLWYRPPDV--LLGSTEYSTCLDMWG 189


                  ....*
gi 1331383559  88 LGCIL 92
Cdd:cd07869   190 VGCIF 194
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
 9-117 1.36e-05

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


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 48.46  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswsaqKRAMVEEEiTRNTTPMYRTPEIV-----DLYsnfpIGEKQ 83
Cdd:cd05622   194 IHRDVKPDNMLLDKSGHLKLADFGTCMKMN----------KEGMVRCD-TAVGTPDYISPEVLksqggDGY----YGREC 258

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1331383559  84 DIWALGCILYLLCFRQHPFED----GAKLRIVNGKYSI 117
Cdd:cd05622   259 DWWSVGVFLYEMLVGDTPFYAdslvGTYSKIMNHKNSL 296
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
 1-102 1.55e-05

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: 47.60  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGT--IKLCDFGSAttishypdyswsaqKRAMVEEEITRN-TTPMYRTPEIVDL-YSN 76
Cdd:cd14193   118 MHQMY--ILHLDLKPENILCVSREAnqVKIIDFGLA--------------RRYKPREKLRVNfGTPEFLAPEVVNYeFVS 181

                          90       100
                  ....*....|....*....|....*.
gi 1331383559  77 FPigekQDIWALGCILYLLCFRQHPF 102
Cdd:cd14193   182 FP----TDMWSLGVIAYMLLSGLSPF 203
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
 1-102 1.59e-05

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: 47.65  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQ--GTIKLCDFGSAttishypdyswsaqKRAMVEEEITRN-TTPMYRTPEIVDL-YSN 76
Cdd:cd14192   118 LHQHY--ILHLDLKPENILCVNStgNQIKIIDFGLA--------------RRYKPREKLKVNfGTPEFLAPEVVNYdFVS 181

                          90       100
                  ....*....|....*....|....*.
gi 1331383559  77 FPigekQDIWALGCILYLLCFRQHPF 102
Cdd:cd14192   182 FP----TDMWSVGVITYMLLSGLSPF 203
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
 9-142 1.75e-05

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 47.33  E-value: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTIShypDYSWSAQKRAMVEEEITrnttpmyrTPEIVDlYSNFPIgeKQDIWAL 88
Cdd:cd05073   129 IHRDLRAANILVSASLVCKIADFGLARVIE---DNEYTAREGAKFPIKWT--------APEAIN-FGSFTI--KSDVWSF 194

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1331383559  89 GCILY-LLCFRQHPF---EDGAKLRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEER 142
Cdd:cd05073   195 GILLMeIVTYGRIPYpgmSNPEVIRALERGYRMPRPENCPEELYNIMMRCWKNRPEER 252
pknD PRK13184
serine/threonine-protein kinase PknD;
8-108 1.83e-05

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 48.61  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDY--SWSAQKRAMVEEEITRN----TTPMYRTPEivDLYSNfPIGE 81
Cdd:PRK13184  134 VLHRDLKPDNILLGLFGEVVILDWGAAIFKKLEEEDllDIDVDERNICYSSMTIPgkivGTPDYMAPE--RLLGV-PASE 210

                          90       100
                  ....*....|....*....|....*....
gi 1331383559  82 KQDIWALGCILYLLCFRQHPF--EDGAKL 108
Cdd:PRK13184  211 STDIYALGVILYQMLTLSFPYrrKKGRKI 239
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
 9-156 1.90e-05

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 47.16  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqkRAMVEEEITRNTT---PMYRTPEIVDLYSNFpiGEKQDI 85
Cdd:cd05114   122 IHRDLAARNCLVNDTGVVKVSDFGMT---------------RYVLDDQYTSSSGakfPVKWSPPEVFNYSKF--SSKSDV 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  86 WALGCILY-LLCFRQHPFEDGAKLRIVngkysipvndTRYTVFHDLIRAMLKVN-------------PEERLSIAEVVRQ 151
Cdd:cd05114   185 WSFGVLMWeVFTEGKMPFESKSNYEVV----------EMVSRGHRLYRPKLASKsvyevmyscwhekPEGRPTFADLLRT 254


                  ....*
gi 1331383559 152 LQEIA 156
Cdd:cd05114   255 ITEIA 259
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
 9-142 1.94e-05

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 47.19  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTIShypDYSWSAQKRAMVEEEITrnttpmyrTPEIVDlYSNFPIgeKQDIWAL 88
Cdd:cd05067   125 IHRDLRAANILVSDTLSCKIADFGLARLIE---DNEYTAREGAKFPIKWT--------APEAIN-YGTFTI--KSDVWSF 190

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1331383559  89 GCILY-LLCFRQHPF---EDGAKLRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEER 142
Cdd:cd05067   191 GILLTeIVTHGRIPYpgmTNPEVIQNLERGYRMPRPDNCPEELYQLMRLCWKERPEDR 248
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
 2-155 2.01e-05

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 47.10  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQKramveeeitrnTTPMYRTPEIVdlySNFPIGE 81
Cdd:cd14664   112 HDCSPLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKDSHVMSSVA-----------GSYGYIAPEYA---YTGKVSE 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  82 KQDIWALGCILYLLCFRQHPF-----EDGAKL-----RIVNGKYSIPVNDTRYT-------VFHDLIRAMLKVN--PEER 142
Cdd:cd14664   178 KSDVYSYGVVLLELITGKRPFdeaflDDGVDIvdwvrGLLEEKKVEALVDPDLQgvykleeVEQVFQVALLCTQssPMER 257

                         170
                  ....*....|...
gi 1331383559 143 LSIAEVVRQLQEI 155
Cdd:cd14664   258 PTMREVVRMLEGD 270
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
 8-92 2.02e-05

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: 47.73  E-value: 2.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqkRAMVEEEITRNTTPMYRTPEIVDLYSNFpiGEKQDIWA 87
Cdd:cd07877   141 IIHRDLKPSNLAVNEDCELKILDFGLA---------------RHTDDEMTGYVATRWYRAPEIMLNWMHY--NQTVDIWS 203


                  ....*
gi 1331383559  88 LGCIL 92
Cdd:cd07877   204 VGCIM 208
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
 2-149 2.24e-05

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 46.80  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPPIIHRDLKVENLLLSNQGTIKLC--DFGSATTISHYPDYSWSaqkramveeeitRNTTPMYRTPEIVDLYSNFPi 79
Cdd:cd14024    99 HCHQHGVILRDLKLRRFVFTDELRTKLVlvNLEDSCPLNGDDDSLTD------------KHGCPAYVGPEILSSRRSYS- 165

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  80 GEKQDIWALGCILYLLCFRQHPFEDG------AKLRivNGKYSIPvnDTRYTVFHDLIRAMLKVNPEERLSIAEVV 149
Cdd:cd14024   166 GKAADVWSLGVCLYTMLLGRYPFQDTepaalfAKIR--RGAFSLP--AWLSPGARCLVSCMLRRSPAERLKASEIL 237
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
 3-32 2.27e-05

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: 47.43  E-value: 2.27e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1331383559   3 RQKPPIIHRDLKVENLLLSNQGTIKLCDFG 32
Cdd:cd06615   116 REKHKIMHRDVKPSNILVNSRGEIKLCDFG 145
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
 2-92 2.44e-05

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: 47.39  E-value: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTishypdyswSAQKRAMVEEEITRnttpMYRTPEIVdlysnFPIGE 81
Cdd:cd07874   134 HLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLART---------AGTSFMMTPYVVTR----YYRAPEVI-----LGMGY 195

                          90
                  ....*....|...
gi 1331383559  82 KQ--DIWALGCIL 92
Cdd:cd07874   196 KEnvDIWSVGCIM 208
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
 1-92 2.45e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 47.77  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYP---DYSWSAQkramveeeITRNttpmyrTPEIV--DLYS 75
Cdd:PHA03210  283 IHDKK--LIHRDIKLENIFLNCDGKIVLGDFGTAMPFEKEReafDYGWVGT--------VATN------SPEILagDGYC 346

                          90
                  ....*....|....*..
gi 1331383559  76 nfpigEKQDIWALGCIL 92
Cdd:PHA03210  347 -----EITDIWSCGLIL 358
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
 8-105 2.49e-05

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: 47.15  E-value: 2.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLL-SNQGTIKLCDFGSATTISHYPDYSwsaqkramveeeiTRNTTPMYRTPEI-VDL----YSnfpige 81
Cdd:cd14132   133 IMHRDVKPHNIMIdHEKRKLRLIDWGLAEFYHPGQEYN-------------VRVASRYYKGPELlVDYqyydYS------ 193

                          90       100
                  ....*....|....*....|....
gi 1331383559  82 kQDIWALGCILYLLCFRQHPFEDG 105
Cdd:cd14132   194 -LDMWSLGCMLASMIFRKEPFFHG 216
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
 1-147 2.50e-05

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 47.30  E-value: 2.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqKRAMVEEEITrNT---TPMYRTPEIVDLYSnf 77
Cdd:cd05589   117 LHEHK--IVYRDLKLDNLLLDTEGYVKIADFGLC--------------KEGMGFGDRT-STfcgTPEFLAPEVLTDTS-- 177

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559  78 pIGEKQDIWALGCILYLLCFRQHPF----EDGAKLRIVNgkysipvNDTRYTVFHD-----LIRAMLKVNPEERLSIAE 147
Cdd:cd05589   178 -YTRAVDWWGLGVLIYEMLVGESPFpgddEEEVFDSIVN-------DEVRYPRFLSteaisIMRRLLRKNPERRLGASE 248
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
 63-150 2.55e-05

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 46.65  E-value: 2.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  63 PMYRTPEIVD---LYSnfpiGEKQDIWALGCILYLLCFRQHPFEDGAKL----RIVNGKYSIPvnDTRYTVFHDLIRAML 135
Cdd:cd13976   150 PAYVSPEILNsgaTYS----GKAADVWSLGVILYTMLVGRYPFHDSEPAslfaKIRRGQFAIP--ETLSPRARCLIRSLL 223

                          90
                  ....*....|....*
gi 1331383559 136 KVNPEERLSIAEVVR 150
Cdd:cd13976   224 RREPSERLTAEDILL 238
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
 9-142 2.65e-05

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: 46.83  E-value: 2.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTIShypDYSWSAQKRAMVeeeitrnttPMYRTPEIVDLYSNFPIgeKQDIWAL 88
Cdd:cd14203   113 IHRDLRAANILVGDNLVCKIADFGLARLIE---DNEYTARQGAKF---------PIKWTAPEAALYGRFTI--KSDVWSF 178

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1331383559  89 GCILYLLCFRQH-PFEDGAK---LRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEER 142
Cdd:cd14203   179 GILLTELVTKGRvPYPGMNNrevLEQVERGYRMPCPPGCPESLHELMCQCWRKDPEER 236
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
 7-152 2.89e-05

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: 46.72  E-value: 2.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   7 PIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYS----------WSAqkramveeeitrnttpmyrtPEIVD--LY 74
Cdd:pfam07714 122 NFVHRDLAARNCLVSENLVVKISDFGLSRDIYDDDYYRkrgggklpikWMA--------------------PESLKdgKF 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  75 SnfpigEKQDIWALGCILY-LLCFRQHPFED----GAKLRIVNGKY-SIPVNDTRYtvFHDLIRAMLKVNPEERLSIAEV 148
Cdd:pfam07714 182 T-----SKSDVWSFGVLLWeIFTLGEQPYPGmsneEVLEFLEDGYRlPQPENCPDE--LYDLMKQCWAYDPEDRPTFSEL 254


                  ....
gi 1331383559 149 VRQL 152
Cdd:pfam07714 255 VEDL 258
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
 4-102 3.10e-05

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 47.28  E-value: 3.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   4 QKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswsaqkramvEEEITRNTTPMYRTPEIVdlySNFPIGEKQ 83
Cdd:PTZ00426  148 QSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVVD---------------TRTYTLCGTPEYIAPEIL---LNVGHGKAA 209

                          90
                  ....*....|....*....
gi 1331383559  84 DIWALGCILYLLCFRQHPF 102
Cdd:PTZ00426  210 DWWTLGIFIYEILVGCPPF 228
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
 9-102 3.21e-05

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


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 47.32  E-value: 3.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTIshypdyswsaQKRAMVEEEITRNtTPMYRTPEIVDLYSNFP--IGEKQDIW 86
Cdd:cd05623   195 VHRDIKPDNILMDMNGHIRLADFGSCLKL----------MEDGTVQSSVAVG-TPDYISPEILQAMEDGKgkYGPECDWW 263

                          90
                  ....*....|....*.
gi 1331383559  87 ALGCILYLLCFRQHPF 102
Cdd:cd05623   264 SLGVCMYEMLYGETPF 279
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
 8-104 3.43e-05

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: 46.51  E-value: 3.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLL---SNQGTIKLCDFGSATTISHYPdyswsaqkraMVEEEITrntTPMYRTPEIVdlYSNfPIGEKQD 84
Cdd:cd14113   124 IAHLDLKPENILVdqsLSKPTIKLADFGDAVQLNTTY----------YIHQLLG---SPEFAAPEII--LGN-PVSLTSD 187

                          90       100
                  ....*....|....*....|
gi 1331383559  85 IWALGCILYLLCFRQHPFED 104
Cdd:cd14113   188 LWSIGVLTYVLLSGVSPFLD 207
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
 8-104 3.70e-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: 46.61  E-value: 3.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIshypdyswsaQKRAMVEEEITRNT-TPMYRTPEIVdlySNFPIGEKQDIW 86
Cdd:cd06651   132 IVHRDIKGANILRDSAGNVKLGDFGASKRL----------QTICMSGTGIRSVTgTPYWMSPEVI---SGEGYGRKADVW 198

                          90
                  ....*....|....*...
gi 1331383559  87 ALGCILYLLCFRQHPFED 104
Cdd:cd06651   199 SLGCTVVEMLTEKPPWAE 216
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
 1-143 4.06e-05

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: 46.28  E-value: 4.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATtishypDYSwSAQKRAMVeeeitrnTTPMYRTPEIvdLYSNFPIG 80
Cdd:cd05606   114 MHNRF--IVYRDLKPANILLDEHGHVRISDLGLAC------DFS-KKKPHASV-------GTHGYMAPEV--LQKGVAYD 175

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331383559  81 EKQDIWALGCILYLLC-----FRQHPFEDGAKLRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERL 143
Cdd:cd05606   176 SSADWFSLGCMLYKLLkghspFRQHKTKDKHEIDRMTLTMNVELPDSFSPELKSLLEGLLQRDVSKRL 243
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
 8-103 5.03e-05

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


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 46.26  E-value: 5.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGsattishypdyswsaqkraMVEEEI----TRNT---TPMYRTPEIV--DLYSnFP 78
Cdd:cd05588   117 IIYRDLKLDNVLLDSEGHIKLTDYG-------------------MCKEGLrpgdTTSTfcgTPNYIAPEILrgEDYG-FS 176

                          90       100
                  ....*....|....*....|....*
gi 1331383559  79 IgekqDIWALGCILYLLCFRQHPFE 103
Cdd:cd05588   177 V----DWWALGVLMFEMLAGRSPFD 197
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
 8-118 5.40e-05

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: 46.18  E-value: 5.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQ----GTIKLCDFGSATTISHYPDYSWsAQKRamveeeitrnttpMYRTPEIVdlySNFPIGEKQ 83
Cdd:cd14229   123 LIHADLKPENIMLVDPvrqpYRVKVIDFGSASHVSKTVCSTY-LQSR-------------YYRAPEII---LGLPFCEAI 185

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1331383559  84 DIWALGCILYLLcFRQHPFEDGA----KLRIVNGKYSIP 118
Cdd:cd14229   186 DMWSLGCVIAEL-FLGWPLYPGAleydQIRYISQTQGLP 223
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
 9-102 5.68e-05

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 46.59  E-value: 5.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSAT------------TISHYP--DYS------------WSAQKRAMVEEEItrnTT 62
Cdd:cd05627   124 IHRDIKPDNLLLDAKGHVKLSDFGLCTglkkahrtefyrNLTHNPpsDFSfqnmnskrkaetWKKNRRQLAYSTV---GT 200

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1331383559  63 PMYRTPEIvdlYSNFPIGEKQDIWALGCILYLLCFRQHPF 102
Cdd:cd05627   201 PDYIAPEV---FMQTGYNKLCDWWSLGVIMYEMLIGYPPF 237
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
 4-102 5.93e-05

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: 45.77  E-value: 5.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   4 QKPPIIHRDLKVENLLLSNQ--GTIKLCDFGSATTISHypdyswSAQKRAMVeeeitrnTTPMYRTPEIVDLYsnfPIGE 81
Cdd:cd14191   117 HKQGIVHLDLKPENIMCVNKtgTKIKLIDFGLARRLEN------AGSLKVLF-------GTPEFVAPEVINYE---PIGY 180

                          90       100
                  ....*....|....*....|.
gi 1331383559  82 KQDIWALGCILYLLCFRQHPF 102
Cdd:cd14191   181 ATDMWSIGVICYILVSGLSPF 201
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
 8-92 6.17e-05

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: 46.31  E-value: 6.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQG-TIKLCDFGSATTIShyPDYSWSAQkramveeeITRN-TTPMYRTPEIVDLYSNFPigEKQDI 85
Cdd:cd07854   135 VLHRDLKPANVFINTEDlVLKIGDFGLARIVD--PHYSHKGY--------LSEGlVTKWYRSPRLLLSPNNYT--KAIDM 202


                  ....*..
gi 1331383559  86 WALGCIL 92
Cdd:cd07854   203 WAAGCIF 209
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
 8-92 6.53e-05

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: 46.13  E-value: 6.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATtishypdyswsaqkraMVEEEITRN-TTPMYRTPEIVDLYSNFpiGEKQDIW 86
Cdd:cd07851   139 IIHRDLKPSNLAVNEDCELKILDFGLAR----------------HTDDEMTGYvATRWYRAPEIMLNWMHY--NQTVDIW 200


                  ....*.
gi 1331383559  87 ALGCIL 92
Cdd:cd07851   201 SVGCIM 206
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
 8-92 6.53e-05

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: 46.12  E-value: 6.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLL----SNQGTIKLCDFGSAtTISHYPDYSWSAQKRAMVeeeitrntTPMYRTPEIVdlysnfpIGEKQ 83
Cdd:cd07842   129 VLHRDLKPANILVmgegPERGVVKIGDLGLA-RLFNAPLKPLADLDPVVV--------TIWYRAPELL-------LGARH 192

                          90
                  ....*....|....
gi 1331383559  84 -----DIWALGCIL 92
Cdd:cd07842   193 ytkaiDIWAIGCIF 206
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
 1-141 9.09e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 45.64  E-value: 9.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAqkrAMVEEEitrnttpmyrTPEIV--DLYSNfp 78
Cdd:PHA03209  173 LHAQR--IIHRDVKTENIFINDVDQVCIGDLGAAQFPVVAPAFLGLA---GTVETN----------APEVLarDKYNS-- 235

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  79 igeKQDIWALGCILY-LLCFRQHPFEDgaklrivngKYSIPVNDTRYTVFH--DLIRAmLKVNPEE 141
Cdd:PHA03209  236 ---KADIWSAGIVLFeMLAYPSTIFED---------PPSTPEEYVKSCHSHllKIIST-LKVHPEE 288
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
 8-92 1.02e-04

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: 45.43  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqkRAMVEEEITRNTTPMYRTPEIVDLYSNFpiGEKQDIWA 87
Cdd:cd07878   139 IIHRDLKPSNVAVNEDCELRILDFGLA---------------RQADDEMTGYVATRWYRAPEIMLNWMHY--NQTVDIWS 201


                  ....*
gi 1331383559  88 LGCIL 92
Cdd:cd07878   202 VGCIM 206
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
 8-147 1.08e-04

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: 44.83  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSN--QGTIKLCDFGSATTIShypdyswsaqKRAMVEEEITRNTTPmyrtPEIvdLYSNFPIGEKQDI 85
Cdd:cd14112   120 IAHLDVQPDNIMFQSvrSWQVKLVDFGRAQKVS----------KLGKVPVDGDTDWAS----PEF--HNPETPITVQSDI 183

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331383559  86 WALGCILYLLCFRQHPF------EDGAKLRIVNGKYS---IPVNDTRYTVfhDLIRAMLKVNPEERLSIAE 147
Cdd:cd14112   184 WGLGVLTFCLLSGFHPFtseyddEEETKENVIFVKCRpnlIFVEATQEAL--RFATWALKKSPTRRMRTDE 252
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
 2-89 1.15e-04

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


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 45.09  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSattishypdyswSAQKRAMVEEEITRNTTPMYRTPEIV--DLYSNFPI 79
Cdd:cd06637   126 HLHQHKVIHRDIKGQNVLLTENAEVKLVDFGV------------SAQLDRTVGRRNTFIGTPYWMAPEVIacDENPDATY 193

                          90
                  ....*....|
gi 1331383559  80 GEKQDIWALG 89
Cdd:cd06637   194 DFKSDLWSLG 203
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
 9-142 1.22e-04

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 45.06  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTIShypDYSWSAQKRAMVeeeitrnttPMYRTPEIVDLYSNFPIgeKQDIWAL 88
Cdd:cd05069   130 IHRDLRAANILVGDNLVCKIADFGLARLIE---DNEYTARQGAKF---------PIKWTAPEAALYGRFTI--KSDVWSF 195

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1331383559  89 GCILYLLCFRQH-PFE---DGAKLRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEER 142
Cdd:cd05069   196 GILLTELVTKGRvPYPgmvNREVLEQVERGYRMPCPQGCPESLHELMKLCWKKDPDER 253
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
 9-142 1.40e-04

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 44.67  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTIShypDYSWSAQKRAMVeeeitrnttPMYRTPEIVDLYSNFPIgeKQDIWAL 88
Cdd:cd05070   127 IHRDLRSANILVGNGLICKIADFGLARLIE---DNEYTARQGAKF---------PIKWTAPEAALYGRFTI--KSDVWSF 192

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1331383559  89 GCILYLLCFRQH-PF---EDGAKLRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEER 142
Cdd:cd05070   193 GILLTELVTKGRvPYpgmNNREVLEQVERGYRMPCPQDCPISLHELMIHCWKKDPEER 250
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
 5-102 1.45e-04

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: 45.05  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   5 KPPIIHRDLKVENLLLSNQ---GTIKLCDFGSATTIShypDYSWSAQKRAmveeEITRN--TTPMYRTPEIVDLYSNFP- 78
Cdd:cd14041   131 KPPIIHYDLKPGNILLVNGtacGEIKITDFGLSKIMD---DDSYNSVDGM----ELTSQgaGTYWYLPPECFVVGKEPPk 203

                          90       100
                  ....*....|....*....|....
gi 1331383559  79 IGEKQDIWALGCILYLLCFRQHPF 102
Cdd:cd14041   204 ISNKVDVWSVGVIFYQCLYGRKPF 227
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
 1-102 1.47e-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: 44.52  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswsaQKRAMVEEEITRNTTPMyrTPEIVDLYSNFPig 80
Cdd:cd14110   115 LHSRR--ILHLDLRSENMIITEKNLLKIVDLGNAQPFN---------QGKVLMTDKKGDYVETM--APELLEGQGAGP-- 179

                          90       100
                  ....*....|....*....|..
gi 1331383559  81 eKQDIWALGCILYLLCFRQHPF 102
Cdd:cd14110   180 -QTDIWAIGVTAFIMLSADYPV 200
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
 8-32 1.49e-04

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


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 44.84  E-value: 1.49e-04
                          10        20
                  ....*....|....*....|....*
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFG 32
Cdd:cd06622   124 IIHRDVKPTNVLVNGNGQVKLCDFG 148
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
 8-102 1.55e-04

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


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 44.99  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswsaqKRAMVEEEiTRNTTPMYRTPEIV-----DLYsnfpIGEK 82
Cdd:cd05621   172 LIHRDVKPDNMLLDKYGHLKLADFGTCMKMD----------ETGMVHCD-TAVGTPDYISPEVLksqggDGY----YGRE 236

                          90       100
                  ....*....|....*....|
gi 1331383559  83 QDIWALGCILYLLCFRQHPF 102
Cdd:cd05621   237 CDWWSVGVFLFEMLVGDTPF 256
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
 2-89 1.68e-04

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


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 44.61  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSattishypdyswSAQKRAMVEEEITRNTTPMYRTPEIV--DLYSNFPI 79
Cdd:cd06636   136 HLHAHKVIHRDIKGQNVLLTENAEVKLVDFGV------------SAQLDRTVGRRNTFIGTPYWMAPEVIacDENPDATY 203

                          90
                  ....*....|
gi 1331383559  80 GEKQDIWALG 89
Cdd:cd06636   204 DYRSDIWSLG 213
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
 8-93 1.75e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 44.99  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSA---TTISHYPDYSWSAQkramveeeITRNttpmyrTPEivdLYSNFPIGEKQD 84
Cdd:PHA03212  203 IIHRDIKAENIFINHPGDVCLGDFGAAcfpVDINANKYYGWAGT--------IATN------APE---LLARDPYGPAVD 265


                  ....*....
gi 1331383559  85 IWALGCILY 93
Cdd:PHA03212  266 IWSAGIVLF 274
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
 9-93 1.87e-04

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 44.10  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqkRAMVEEEITRNTT---PMYRTPEIVDLYSNFpiGEKQDI 85
Cdd:cd05113   122 LHRDLAARNCLVNDQGVVKVSDFGLS---------------RYVLDDEYTSSVGskfPVRWSPPEVLMYSKF--SSKSDV 184


                  ....*...
gi 1331383559  86 WALGCILY 93
Cdd:cd05113   185 WAFGVLMW 192
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
 3-32 1.89e-04

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


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 44.66  E-value: 1.89e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1331383559   3 RQKPPIIHRDLKVENLLLSNQGTIKLCDFG 32
Cdd:cd06650   120 REKHKIMHRDVKPSNILVNSRGEIKLCDFG 149
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
 8-92 1.92e-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: 44.56  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqkRAMVEEEITRNTTPMYRTPEIVDLYSNFPigEKQDIWA 87
Cdd:cd07880   139 IIHRDLKPGNLAVNEDCELKILDFGLA---------------RQTDSEMTGYVVTRWYRAPEVILNWMHYT--QTVDIWS 201


                  ....*
gi 1331383559  88 LGCIL 92
Cdd:cd07880   202 VGCIM 206
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
 9-93 2.11e-04

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 44.63  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYswsaqkramveeeITRNTT--PM-YRTPEIV--DLYSNFpigekQ 83
Cdd:cd05105   259 VHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNY-------------VSKGSTflPVkWMAPESIfdNLYTTL-----S 320

                          90
                  ....*....|
gi 1331383559  84 DIWALGCILY 93
Cdd:cd05105   321 DVWSYGILLW 330
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
 5-102 2.19e-04

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: 44.28  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   5 KPPIIHRDLKVENLLLSNQ---GTIKLCDFGSATTIShypDYSWSAQKRAMVEEEItrnTTPMYRTPEIVDLYSNFP-IG 80
Cdd:cd14040   131 KPPIIHYDLKPGNILLVDGtacGEIKITDFGLSKIMD---DDSYGVDGMDLTSQGA---GTYWYLPPECFVVGKEPPkIS 204

                          90       100
                  ....*....|....*....|..
gi 1331383559  81 EKQDIWALGCILYLLCFRQHPF 102
Cdd:cd14040   205 NKVDVWSVGVIFFQCLYGRKPF 226
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
 2-143 2.46e-04

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: 44.10  E-value: 2.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHypdyswsaqkramvEEEITRN--TTPMYRTPEIVdlysnfpI 79
Cdd:cd05608   120 HLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKD--------------GQTKTKGyaGTPGFMAPELL-------L 178

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331383559  80 GEKQDI----WALGCILYLLCFRQHPFE-DGAKL-------RIVNGKYSIPVNDTRYTvfHDLIRAMLKVNPEERL 143
Cdd:cd05608   179 GEEYDYsvdyFTLGVTLYEMIAARGPFRaRGEKVenkelkqRILNDSVTYSEKFSPAS--KSICEALLAKDPEKRL 252
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
 8-142 2.47e-04

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: 44.04  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQG-TIKLCDFGSATTISHYPDYSWSAQKRAMVEEEITRNTTPMYRTPEIVDLYSNFPigeKQDIW 86
Cdd:cd14049   141 IVHRDLKPRNIFLHGSDiHVRIGDFGLACPDILQDGNDSTTMSRLNGLTHTSGVGTCLYAAPEQLEGSHYDF---KSDMY 217

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  87 ALGCILYLLCfrqHPFE-DGAKLRIVNG--KYSIPVN-DTRYTVFHDLIRAMLKVNPEER 142
Cdd:cd14049   218 SIGVILLELF---QPFGtEMERAEVLTQlrNGQIPKSlCKRWPVQAKYIKLLTSTEPSER 274
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
 3-155 2.49e-04

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 43.80  E-value: 2.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   3 RQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTishypdyswsaQKRAMVEEEITRNT---TPMYRTPEIVDL---YSN 76
Cdd:cd14056   116 QGKPAIAHRDLKSKNILVKRDGTCCIADLGLAVR-----------YDSDTNTIDIPPNPrvgTKRYMAPEVLDDsinPKS 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  77 FPIGEKQDIWALGCILYLLCFR----------QHPFED----------------GAKLRivngkysiPVNDTRYTVfHDL 130
Cdd:cd14056   185 FESFKMADIYSFGLVLWEIARRceiggiaeeyQLPYFGmvpsdpsfeemrkvvcVEKLR--------PPIPNRWKS-DPV 255

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1331383559 131 IRAMLKV-------NPEERLSIAEVVRQLQEI 155
Cdd:cd14056   256 LRSMVKLmqecwseNPHARLTALRVKKTLAKL 287
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
 8-118 2.72e-04

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: 44.31  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGT----IKLCDFGSATTIShypdyswsaqkRAMVEeeiTRNTTPMYRTPEIVdlySNFPIGEKQ 83
Cdd:cd14227   138 LIHADLKPENIMLVDPSRqpyrVKVIDFGSASHVS-----------KAVCS---TYLQSRYYRAPEII---LGLPFCEAI 200

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1331383559  84 DIWALGCILYLLcFRQHPFEDGA----KLRIVNGKYSIP 118
Cdd:cd14227   201 DMWSLGCVIAEL-FLGWPLYPGAseydQIRYISQTQGLP 238
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
 1-152 3.32e-04

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 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: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 43.64  E-value: 3.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGT----IKLCDFGSATT----------ISHYPDYSWSAqkrAMVEEEITrNTTPmyr 66
Cdd:cd14018   154 LVRHG--IAHRDLKSDNILLELDFDgcpwLVIADFGCCLAddsiglqlpfSSWYVDRGGNA---CLMAPEVS-TAVP--- 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  67 TPEIVDLYSnfpigeKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYS----IPVNDTRYTVFHDLIRAMLKVNPEER 142
Cdd:cd14018   225 GPGVVINYS------KADAWAVGAIAYEIFGLSNPFYGLGDTMLESRSYQesqlPALPSAVPPDVRQVVKDLLQRDPNKR 298

                         170
                  ....*....|..
gi 1331383559 143 LS--IAEVVRQL 152
Cdd:cd14018   299 VSarVAANVLHL 310
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
 8-91 3.45e-04

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 43.65  E-value: 3.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQ-GTIKLCDFGSATtishypdySWSAQKRAMVEEEITRnttpMYRTPEIVdlysnfpIGEKQ--- 83
Cdd:PLN00009  123 VLHRDLKPQNLLIDRRtNALKLADFGLAR--------AFGIPVRTFTHEVVTL----WYRAPEIL-------LGSRHyst 183

                          90
                  ....*....|
gi 1331383559  84 --DIWALGCI 91
Cdd:PLN00009  184 pvDIWSVGCI 193
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
 5-155 3.58e-04

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 43.49  E-value: 3.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   5 KPPIIHRDLKVENLLLSNQGTIKLCDFGSATTI---SHYPDYSWSaqkramveeeiTRNTTPMYRTPEIVDLYSN---FP 78
Cdd:cd14220   118 KPAIAHRDLKSKNILIKKNGTCCIADLGLAVKFnsdTNEVDVPLN-----------TRVGTKRYMAPEVLDESLNknhFQ 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  79 IGEKQDIWALGCILYLLCFR----------QHP----------FEDgaKLRIVNGKYSIPVNDTRYTVfHDLIRAMLKV- 137
Cdd:cd14220   187 AYIMADIYSFGLIIWEMARRcvtggiveeyQLPyydmvpsdpsYED--MREVVCVKRLRPTVSNRWNS-DECLRAVLKLm 263

                         170       180
                  ....*....|....*....|....
gi 1331383559 138 ------NPEERLSIAEVVRQLQEI 155
Cdd:cd14220   264 secwahNPASRLTALRIKKTLAKM 287
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
 2-206 3.67e-04

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 43.50  E-value: 3.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAqkramveeeitrntTPMYRTPEIvdLYSNFPIGE 81
Cdd:cd14223   118 HMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDFSKKKPHASVG--------------THGYMAPEV--LQKGVAYDS 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  82 KQDIWALGCILYLLC-----FRQHPFEDGAKLRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIaeVVRQLQEIA 156
Cdd:cd14223   182 SADWFSLGCMLFKLLrghspFRQHKTKDKHEIDRMTLTMAVELPDSFSPELRSLLEGLLQRDVNRRLGC--MGRGAQEVK 259

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1331383559 157 aarnvnpKAPITELLEQNGGYGNSGPSRAQPPcGGTVNSSGVLALAEYDQ 206
Cdd:cd14223   260 -------EEPFFRGLDWQMVFLQKYPPPLIPP-RGEVNAADAFDIGSFDE 301
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
 9-102 4.48e-04

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 43.49  E-value: 4.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTI--------------SHYPDYSWSAQKRAMVEEEITRNT---------TPMY 65
Cdd:cd05628   123 IHRDIKPDNLLLDSKGHVKLSDFGLCTGLkkahrtefyrnlnhSLPSDFTFQNMNSKRKAETWKRNRrqlafstvgTPDY 202

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1331383559  66 RTPEIvdlYSNFPIGEKQDIWALGCILYLLCFRQHPF 102
Cdd:cd05628   203 IAPEV---FMQTGYNKLCDWWSLGVIMYEMLIGYPPF 236
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
 5-35 4.64e-04

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 43.09  E-value: 4.64e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1331383559   5 KPPIIHRDLKVENLLLSNQGTIKLCDFGSAT 35
Cdd:cd14053   120 KPSIAHRDFKSKNVLLKSDLTACIADFGLAL 150
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
 1-90 4.72e-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: 43.17  E-value: 4.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSN-QGTIKLCDFGSAttishypdyswsaqKRA----MVEEEITrnTTPMYRTPEIVDL-- 73
Cdd:cd06624   124 LHDNK--IVHRDIKGDNVLVNTySGVVKISDFGTS--------------KRLaginPCTETFT--GTLQYMAPEVIDKgq 185

                          90
                  ....*....|....*....
gi 1331383559  74 --YsnfpiGEKQDIWALGC 90
Cdd:cd06624   186 rgY-----GPPADIWSLGC 199
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
 8-93 5.43e-04

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: 43.07  E-value: 5.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSN-------------------QGTIKLCDFGSATtISHypdyswsaqkramvEEEITRNTTPMYRTP 68
Cdd:cd14214   138 LTHTDLKPENILFVNsefdtlynesksceeksvkNTSIRVADFGSAT-FDH--------------EHHTTIVATRHYRPP 202

                          90       100
                  ....*....|....*....|....*..
gi 1331383559  69 EIVdlysnFPIGEKQ--DIWALGCILY 93
Cdd:cd14214   203 EVI-----LELGWAQpcDVWSLGCILF 224
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
 9-157 5.58e-04

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 43.08  E-value: 5.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQKRAMVEeeitrnttpmYRTPEIV--DLYSNfpigeKQDIW 86
Cdd:cd05098   157 IHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVK----------WMAPEALfdRIYTH-----QSDVW 221

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559  87 ALGCILYLLC------FRQHPFEDGAKLRIVNGKYSIPVNDTR--YTVFHDLIRAMlkvnPEERLSIAEVVRQLQEIAA 157
Cdd:cd05098   222 SFGVLLWEIFtlggspYPGVPVEELFKLLKEGHRMDKPSNCTNelYMMMRDCWHAV----PSQRPTFKQLVEDLDRIVA 296
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
 8-118 5.70e-04

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: 43.15  E-value: 5.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQ----GTIKLCDFGSATTIShypdyswsaqkRAMVEeeiTRNTTPMYRTPEIVdlySNFPIGEKQ 83
Cdd:cd14228   138 LIHADLKPENIMLVDPvrqpYRVKVIDFGSASHVS-----------KAVCS---TYLQSRYYRAPEII---LGLPFCEAI 200

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1331383559  84 DIWALGCILYLLcFRQHPFEDGA----KLRIVNGKYSIP 118
Cdd:cd14228   201 DMWSLGCVIAEL-FLGWPLYPGAseydQIRYISQTQGLP 238
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
 8-152 5.72e-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: 42.63  E-value: 5.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGsattishypdyswsaQKRAMVEEEITRNTT---PM-YRTPEIVDlYSNFpiGEKQ 83
Cdd:cd05112   121 VIHRDLAARNCLVGENQVVKVSDFG---------------MTRFVLDDQYTSSTGtkfPVkWSSPEVFS-FSRY--SSKS 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331383559  84 DIWALGCILY-LLCFRQHPFEDGAKLRIV---NGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQL 152
Cdd:cd05112   183 DVWSFGVLMWeVFSEGKIPYENRSNSEVVediNAGFRLYKPRLASTHVYEIMNHCWKERPEDRPSFSLLLRQL 255
PLN03224 PLN03224
probable serine/threonine protein kinase; Provisional
 8-77 5.72e-04

probable serine/threonine protein kinase; Provisional


Pssm-ID: 178763 [Multi-domain]  Cd Length: 507  Bit Score: 43.52  E-value: 5.72e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSA----TTISHYPDYSWSAQKRAMVEEEITRNTTPMYRTPEIVDLYSNF 77
Cdd:PLN03224  330 IVHRDIKPENLLVTVDGQVKIIDFGAAvdmcTGINFNPLYGMLDPRYSPPEELVMPQSCPRAPAPAMAALLSPF 403
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
 8-152 6.67e-04

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 42.25  E-value: 6.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTiklcdfgSATTISHYPDYSWSAQKRAMVEEeiTRNTTPMYRTPEIVDlySNFPIGEKQDIWA 87
Cdd:cd14068   107 IIYRDLKPHNVLLFTLYP-------NCAIIAKIADYGIAQYCCRMGIK--TSEGTPGFRAPEVAR--GNVIYNQQADVYS 175

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331383559  88 LGCILYLLCFRQHPFEDGAKLR------IVNGKYSIPVND---TRYTVFHDLIRAMLKVNPEERLSIAEVVRQL 152
Cdd:cd14068   176 FGLLLYDILTCGERIVEGLKFPnefdelAIQGKLPDPVKEygcAPWPGVEALIKDCLKENPQCRPTSAQVFDIL 249
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
 3-121 6.75e-04

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


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 42.73  E-value: 6.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   3 RQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQKRAMVEEEITRNTTPMyrtpeivdlysnfpigeK 82
Cdd:cd06649   120 REKHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGTRSYMSPERLQGTHYSV-----------------Q 182

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1331383559  83 QDIWALGCILYLLCFRQHPF--EDGAKLRIVNGKysiPVND 121
Cdd:cd06649   183 SDIWSMGLSLVELAIGRYPIppPDAKELEAIFGR---PVVD 220
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
 8-92 7.23e-04

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: 42.97  E-value: 7.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATtishypdySWSAQKRAMVeeeITRnttpMYRTPEIVDLYSNFpiGEKQDIWA 87
Cdd:cd07879   138 IIHRDLKPGNLAVNEDCELKILDFGLAR--------HADAEMTGYV---VTR----WYRAPEVILNWMHY--NQTVDIWS 200


                  ....*
gi 1331383559  88 LGCIL 92
Cdd:cd07879   201 VGCIM 205
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
 1-104 7.53e-04

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: 42.49  E-value: 7.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATtishYPDYSWSAQKRAMVEEEITRNT-----TPMYRTPEIVDLYS 75
Cdd:cd14027   106 LHGKG--VIHKDLKPENILVDNDFHIKIADLGLAS----FKMWSKLTKEEHNEQREVDGTAkknagTLYYMAPEHLNDVN 179

                          90       100
                  ....*....|....*....|....*....
gi 1331383559  76 NFPIgEKQDIWALGCILYLLCFRQHPFED 104
Cdd:cd14027   180 AKPT-EKSDVYSFAIVLWAIFANKEPYEN 207
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
 8-152 8.50e-04

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


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 42.71  E-value: 8.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqKRAMVEEEITRN--TTPMYRTPEIVdlySNFPIGEKQDI 85
Cdd:cd05618   142 IIYRDLKLDNVLLDSEGHIKLTDYGMC--------------KEGLRPGDTTSTfcGTPNYIAPEIL---RGEDYGFSVDW 204

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331383559  86 WALGCILYLLCFRQHPFEdgaklriVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQL 152
Cdd:cd05618   205 WALGVLMFEMMAGRSPFD-------IVGSSDNPDQNTEDYLFQVILEKQIRIPRSLSVKAASVLKSF 264
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
 9-93 1.05e-03

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 42.31  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYswsaqkramveeeITRNTT--PM-YRTPEIV--DLYSNFpigekQ 83
Cdd:cd05107   261 VHRDLAARNVLICEGKLVKICDFGLARDIMRDSNY-------------ISKGSTflPLkWMAPESIfnNLYTTL-----S 322

                          90
                  ....*....|
gi 1331383559  84 DIWALGCILY 93
Cdd:cd05107   323 DVWSFGILLW 332
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
 8-103 1.24e-03

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


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 41.93  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqKRAMVEEEITRN--TTPMYRTPEIVdlySNFPIGEKQDI 85
Cdd:cd05617   137 IIYRDLKLDNVLLDADGHIKLTDYGMC--------------KEGLGPGDTTSTfcGTPNYIAPEIL---RGEEYGFSVDW 199

                          90
                  ....*....|....*...
gi 1331383559  86 WALGCILYLLCFRQHPFE 103
Cdd:cd05617   200 WALGVLMFEMMAGRSPFD 217
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
 8-142 1.24e-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: 41.92  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWsaqkraMVEEEITRNTTPM-----YRTPEIVDLYSNFPigeK 82
Cdd:cd14011   136 LVHGNICPESVVINSNGEWKLAGFDFCISSEQATDQFP------YFREYDPNLPPLAqpnlnYLAPEYILSKTCDP---A 206

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331383559  83 QDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPVNDTRYTVFH-------DLIRAMLKVNPEER 142
Cdd:cd14011   207 SDMFSLGVLIYAIYNKGKPLFDCVNNLLSYKKNSNQLRQLSLSLLEkvpeelrDHVKTLLNVTPEVR 273
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
 9-95 1.31e-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: 41.84  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSwsaqkraMVEEEitRNTTPMYRTPEIVdLYSNFPIGekQDIWAL 88
Cdd:cd05079   131 VHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYY-------TVKDD--LDSPVFWYAPECL-IQSKFYIA--SDVWSF 198


                  ....*..
gi 1331383559  89 GCILYLL 95
Cdd:cd05079   199 GVTLYEL 205
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
 8-102 1.44e-03

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


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 41.40  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTISHypdyswSAQKramveeeiTRNTTPMYRTPEIVdlySNFPIGEKQDIWA 87
Cdd:cd06619   116 ILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVN------SIAK--------TYVGTNAYMAPERI---SGEQYGIHSDVWS 178

                          90
                  ....*....|....*
gi 1331383559  88 LGCILYLLCFRQHPF 102
Cdd:cd06619   179 LGISFMELALGRFPY 193
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
 8-155 1.47e-03

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


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 41.27  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSA--------TTISHYPDYSWSAqkramvEEEITRNTtpmyrtpeivdlYSNfpi 79
Cdd:cd05148   125 SIHRDLAARNILVGEDLVCKVADFGLArlikedvyLSSDKKIPYKWTA------PEAASHGT------------FST--- 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  80 geKQDIWALGCILY-LLCFRQHPFE---DGAKLRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQLQEI 155
Cdd:cd05148   184 --KSDVWSFGILLYeMFTYGQVPYPgmnNHEVYDQITAGYRMPCPAKCPQEIYKIMLECWAAEPEDRPSFKALREELDNI 261
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
 9-93 1.49e-03

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


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 41.28  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSAttishypdyswsaqkRAMVEEEITRNTT---PMYRTPEIVDLYSNFpiGEKQDI 85
Cdd:cd05059   122 IHRDLAARNCLVGEQNVVKVSDFGLA---------------RYVLDDEYTSSVGtkfPVKWSPPEVFMYSKF--SSKSDV 184


                  ....*...
gi 1331383559  86 WALGCILY 93
Cdd:cd05059   185 WSFGVLMW 192
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
 1-155 1.94e-03

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: 40.94  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGSATTishypdyswsaqkRAMVEEEITrnTTPMYRTPEIVD-LYSNfpi 79
Cdd:cd13975   118 LHSQG--LVHRDIKLKNVLLDKKNRAKITDLGFCKP-------------EAMMSGSIV--GTPIHMAPELFSgKYDN--- 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  80 geKQDIWALGCILYLLC---------FRQHPFEDGAKLRIVNGkysipVNDTRYTVFHD----LIRAMLKVNPEERLSIA 146
Cdd:cd13975   178 --SVDVYAFGILFWYLCaghvklpeaFEQCASKDHLWNNVRKG-----VRPERLPVFDEecwnLMEACWSGDPSQRPLLG 250


                  ....*....
gi 1331383559 147 EVVRQLQEI 155
Cdd:cd13975   251 IVQPKLQGI 259
PTZ00284 PTZ00284
protein kinase; Provisional
 8-96 2.17e-03

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 41.49  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGT----------------IKLCDFGSATTISHypdyswsaQKRAMVeeeitrnTTPMYRTPEIV 71
Cdd:PTZ00284  253 LMHTDLKPENILMETSDTvvdpvtnralppdpcrVRICDLGGCCDERH--------SRTAIV-------STRHYRSPEVV 317

                          90       100
                  ....*....|....*....|....*....
gi 1331383559  72 D----LYSNfpigekqDIWALGCILYLLC 96
Cdd:PTZ00284  318 LglgwMYST-------DMWSMGCIIYELY 339
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
 9-142 2.18e-03

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 40.83  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTIShypDYSWSAQKRAMVeeeitrnttPMYRTPEIVDLYSNFPIgeKQDIWAL 88
Cdd:cd05071   127 VHRDLRAANILVGENLVCKVADFGLARLIE---DNEYTARQGAKF---------PIKWTAPEAALYGRFTI--KSDVWSF 192

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1331383559  89 GCILYLLCFRQH-PFEDGAKLRI---VNGKYSIPVNDTRYTVFHDLIRAMLKVNPEER 142
Cdd:cd05071   193 GILLTELTTKGRvPYPGMVNREVldqVERGYRMPCPPECPESLHDLMCQCWRKEPEER 250
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
 8-91 2.45e-03

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: 40.92  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSA--------TTIsHYPDYSwsaqkramveeeitrnTTPMYRTPEIV-DLYSNFP 78
Cdd:cd07859   124 VFHRDLKPKNILANADCKLKICDFGLArvafndtpTAI-FWTDYV----------------ATRWYRAPELCgSFFSKYT 186

                          90
                  ....*....|...
gi 1331383559  79 igEKQDIWALGCI 91
Cdd:cd07859   187 --PAIDIWSIGCI 197
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
 1-147 2.77e-03

Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3. RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. The RPK118-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: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 40.61  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQGTIKLCDFGsattishypdySWSAQKRAMVEEEITRnttpMYRTPEIVDLYSNfpiG 80
Cdd:cd05576   129 LHREG--IVCRDLNPNNILLNDRGHIQLTYFS-----------RWSEVEDSCDSDAIEN----MYCAPEVGGISEE---T 188

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331383559  81 EKQDIWALGCILYLLCFRQ-----HPFEDGAKLRIvngkySIPVNDTRYTvfHDLIRAMLKVNPEERLSIAE 147
Cdd:cd05576   189 EACDWWSLGALLFELLTGKalvecHPAGINTHTTL-----NIPEWVSEEA--RSLLQQLLQFNPTERLGAGV 253
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
 9-93 3.13e-03

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 40.34  E-value: 3.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTIShypDYSWSAQKRAMVeeeitrnttPMYRT-PEIVdLYSNFPIgeKQDIWA 87
Cdd:cd05034   114 IHRDLAARNILVGENNVCKVADFGLARLIE---DDEYTAREGAKF---------PIKWTaPEAA-LYGRFTI--KSDVWS 178


                  ....*.
gi 1331383559  88 LGCILY 93
Cdd:cd05034   179 FGILLY 184
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
 9-93 3.17e-03

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 40.55  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQKRA----MVEEEITRNttpMYRTpeivdlysnfpigeKQD 84
Cdd:cd05055   163 IHRDLAARNVLLTHGKIVKICDFGLARDIMNDSNYVVKGNARLpvkwMAPESIFNC---VYTF--------------ESD 225


                  ....*....
gi 1331383559  85 IWALGCILY 93
Cdd:cd05055   226 VWSYGILLW 234
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
 8-97 3.41e-03

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: 40.50  E-value: 3.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   8 IIHRDLKVENLLLSNQ-GTIKLCDFGSA----TTISHYPDYSWSAQKRAMVEEEITRNTTPMYRTPEIVDLYS------N 76
Cdd:cd14013   141 IVHRDVKPQNIIVSEGdGQFKIIDLGAAadlrIGINYIPKEFLLDPRYAPPEQYIMSTQTPSAPPAPVAAALSpvlwqmN 220

                          90       100
                  ....*....|....*....|.
gi 1331383559  77 FPigEKQDIWALGCILYLLCF 97
Cdd:cd14013   221 LP--DRFDMYSAGVILLQMAF 239
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
 2-143 3.52e-03

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 40.82  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTIShypdyswSAQKRAMVeeeitrnTTPMYRTPEIVDLYSNFpiGE 81
Cdd:cd05633   123 HMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFS-------KKKPHASV-------GTHGYMAPEVLQKGTAY--DS 186

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331383559  82 KQDIWALGCILYLLC-----FRQHPFEDGAKLRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERL 143
Cdd:cd05633   187 SADWFSLGCMLFKLLrghspFRQHKTKDKHEIDRMTLTVNVELPDSFSPELKSLLEGLLQRDVSKRL 253
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
 5-93 3.55e-03

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 40.50  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   5 KPPIIHRDLKVENLLLSNQGTIKLCDFGSAttISHypDYSWSAQkramveeEITRNT---TPMYRTPEIVDLYSN---FP 78
Cdd:cd14143   118 KPAIAHRDLKSKNILVKKNGTCCIADLGLA--VRH--DSATDTI-------DIAPNHrvgTKRYMAPEVLDDTINmkhFE 186

                          90
                  ....*....|....*
gi 1331383559  79 IGEKQDIWALGCILY 93
Cdd:cd14143   187 SFKRADIYALGLVFW 201
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
 2-102 3.67e-03

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: 40.20  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   2 HRQKPPIIHRDLKVENLLLSNQ-GTIKLCDFG--SATTIshyPDYSWSaqkramveEEItrnTTPMYRTPEIV---DLYS 75
Cdd:cd07837   124 HCHSHGVMHRDLKPQNLLVDKQkGLLKIADLGlgRAFTI---PIKSYT--------HEI---VTLWYRAPEVLlgsTHYS 189

                          90       100
                  ....*....|....*....|....*..
gi 1331383559  76 NfPIgekqDIWALGCILYLLCFRQHPF 102
Cdd:cd07837   190 T-PV----DMWSVGCIFAEMSRKQPLF 211
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
 8-43 3.96e-03

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


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 40.09  E-value: 3.96e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1331383559   8 IIHRDLKVENLLLSNQGTIKLCDFGSATTIsHYPDY 43
Cdd:cd05053   154 CIHRDLAARNVLVTEDNVMKIADFGLARDI-HHIDY 188
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
 5-155 4.16e-03

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 40.15  E-value: 4.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   5 KPPIIHRDLKVENLLLSNQGTIKLCDFGSAttISHYPDYSwsaqkramvEEEITRNT---TPMYRTPEIVDLYSN---FP 78
Cdd:cd14144   118 KPAIAHRDIKSKNILVKKNGTCCIADLGLA--VKFISETN---------EVDLPPNTrvgTKRYMAPEVLDESLNrnhFD 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  79 IGEKQDIWALGCILYLLCFR----------QHPFEDGAKL--------RIVNGKYSIPVNDTRYTVfHDLIRAMLKV--- 137
Cdd:cd14144   187 AYKMADMYSFGLVLWEIARRcisggiveeyQLPYYDAVPSdpsyedmrRVVCVERRRPSIPNRWSS-DEVLRTMSKLmse 265

                         170       180
                  ....*....|....*....|..
gi 1331383559 138 ----NPEERLSIAEVVRQLQEI 155
Cdd:cd14144   266 cwahNPAARLTALRVKKTLGKL 287
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
 1-103 4.49e-03

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: 39.84  E-value: 4.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLLLSNQ--GTIKLCDFGSATTIShyPDYSWSAQKramveeeitrnTTPMYRTPEIvdlYSNFP 78
Cdd:cd14104   113 LHSKN--IGHFDIRPENIIYCTRrgSYIKIIEFGQSRQLK--PGDKFRLQY-----------TSAEFYAPEV---HQHES 174

                          90       100
                  ....*....|....*....|....*
gi 1331383559  79 IGEKQDIWALGCILYLLCFRQHPFE 103
Cdd:cd14104   175 VSTATDMWSLGCLVYVLLSGINPFE 199
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
 1-151 7.30e-03

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: 39.45  E-value: 7.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   1 MHRQKppIIHRDLKVENLL--------------------LSNQgTIKLCDFGSATtishYPDyswsaqkramvEEEITRN 60
Cdd:cd14213   132 LHHNK--LTHTDLKPENILfvqsdyvvkynpkmkrdertLKNP-DIKVVDFGSAT----YDD-----------EHHSTLV 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559  61 TTPMYRTPEIVdlysnFPIGEKQ--DIWALGCIL--YLLCFR----------------------QHPFEDGAKLRIVN-- 112
Cdd:cd14213   194 STRHYRAPEVI-----LALGWSQpcDVWSIGCILieYYLGFTvfqthdskehlammerilgplpKHMIQKTRKRKYFHhd 268

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1331383559 113 ----------GKYS----------IPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQ 151
Cdd:cd14213   269 qldwdehssaGRYVrrrckplkefMLSQDVDHEQLFDLIQKMLEYDPAKRITLDEALKH 327
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
 9-154 9.00e-03

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 39.50  E-value: 9.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331383559   9 IHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQKRAMVEeeitrnttpmYRTPE-IVDLYSNFpigeKQDIWA 87
Cdd:cd05104   236 IHRDLAARNILLTHGRITKICDFGLARDIRNDSNYVVKGNARLPVK----------WMAPEsIFECVYTF----ESDVWS 301

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331383559  88 LGCILY-LLCFRQHPFE----DGAKLRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPEERLSIAEVVRQLQE 154
Cdd:cd05104   302 YGILLWeIFSLGSSPYPgmpvDSKFYKMIKEGYRMDSPEFAPSEMYDIMRSCWDADPLKRPTFKQIVQLIEQ 373
 
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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