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Conserved domains on  [gi|1333886239|ref|NP_001346926|]
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receptor-interacting serine/threonine-protein kinase 1 [Mus musculus]

Protein Classification

receptor-interacting serine/threonine-protein kinase 1( domain architecture ID 10391585)

receptor-interacting serine/threonine-protein kinase 1 (RIP1 or RIPK1) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
23-291 4.27e-163

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 cd14027:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 267  Bit Score: 468.13  E-value: 4.27e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMH 102
Cdd:cd14027     1 LDSGGFGKVSLCFHRTQGLVVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLKtQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTWSKLTKEKDNKQKEVSST 182
Cdd:cd14027    81 VLK-KVSVPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLTKEEHNEQREVDGT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 183 TKkNNGGTLYYMAPEHLNDINAKPTEKSDVYSFGIVLWAIFAKKEPYENVICTEQFVICIKSGNRPNVEEILEYCPREII 262
Cdd:cd14027   160 AK-KNAGTLYYMAPEHLNDVNAKPTEKSDVYSFAIVLWAIFANKEPYENAINEDQIIMCIKSGNRPDVDDITEYCPREII 238
                         250       260
                  ....*....|....*....|....*....
gi 1333886239 263 SLMERCWQAIPEDRPTFLGIEEEFRPFYL 291
Cdd:cd14027   239 DLMKLCWEANPEARPTFPGIEEKFRPFYL 267
Death_RIP1 cd08777
Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in ...
568-653 5.69e-48

Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in Receptor-Interacting Protein 1 (RIP1) and related proteins. RIP kinases serve as essential sensors of cellular stress. Vertebrates contain several types containing a homologous N-terminal kinase domain and varying C-terminal domains. RIP1 harbors a C-terminal 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 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 accumulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


:

Pssm-ID: 260048  Cd Length: 86  Bit Score: 162.99  E-value: 5.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 568 TDEHLNPIRENLGRQWKNCARKLGFTESQIDEIDHDYERDGLKEKVYQMLQKWLMREGTKGATVGKLAQALHQCCRIDLL 647
Cdd:cd08777     1 TEKHLDLLRENLGKKWKRCARRLGLTEVEIEEIDHDYERDGLKEKVHQMLEKWKMKEGSKGATVGKLAKALEGCIKSDLL 80

                  ....*.
gi 1333886239 648 NHLIRA 653
Cdd:cd08777    81 VSLLQV 86
 
Name Accession Description Interval E-value
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
23-291 4.27e-163

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: 468.13  E-value: 4.27e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMH 102
Cdd:cd14027     1 LDSGGFGKVSLCFHRTQGLVVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLKtQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTWSKLTKEKDNKQKEVSST 182
Cdd:cd14027    81 VLK-KVSVPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLTKEEHNEQREVDGT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 183 TKkNNGGTLYYMAPEHLNDINAKPTEKSDVYSFGIVLWAIFAKKEPYENVICTEQFVICIKSGNRPNVEEILEYCPREII 262
Cdd:cd14027   160 AK-KNAGTLYYMAPEHLNDVNAKPTEKSDVYSFAIVLWAIFANKEPYENAINEDQIIMCIKSGNRPDVDDITEYCPREII 238
                         250       260
                  ....*....|....*....|....*....
gi 1333886239 263 SLMERCWQAIPEDRPTFLGIEEEFRPFYL 291
Cdd:cd14027   239 DLMKLCWEANPEARPTFPGIEEKFRPFYL 267
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
23-286 1.28e-63

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: 211.25  E-value: 1.28e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239   23 LDSGGFGKVSLC--YHRSHGFVIL---KKVYTGPNRAEYNEvLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEK 97
Cdd:smart00221   7 LGEGAFGEVYKGtlKGKGDGKEVEvavKTLKEDASEQQIEE-FLREARIMRKLDHPNIVKLLGVCTEEEPLMIVMEYMPG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239   98 GNLMHVLKTQIDVPLSLKG--RIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasfktwskLTKEKDNK 175
Cdd:smart00221  86 GDLLDYLRKNRPKELSLSDllSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFG---------LSRDLYDD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  176 QKEVSSTTKknngGTLYYMAPEHLNDinAKPTEKSDVYSFGIVLWAIFAK-KEPYENVIcTEQFVICIKSGNRPnveEIL 254
Cdd:smart00221 157 DYYKVKGGK----LPIRWMAPESLKE--GKFTSKSDVWSFGVLLWEIFTLgEEPYPGMS-NAEVLEYLKKGYRL---PKP 226
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1333886239  255 EYCPREIISLMERCWQAIPEDRPTFLGIEEEF 286
Cdd:smart00221 227 PNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
23-286 1.63e-57

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: 195.02  E-value: 1.63e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFV--------ILKKVYTGPNRAEynevLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEY 94
Cdd:pfam07714   7 LGEGAFGEVYKGTLKGEGENtkikvavkTLKEGADEEERED----FLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKGNLMHVLKTQID-VPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekd 173
Cdd:pfam07714  83 MPGGDLLDFLRKHKRkLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLS------------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 174 nKQKEVSSTTKKNNGGTL--YYMAPEHLNDinAKPTEKSDVYSFGIVLWAIFAK-KEPYENVIcTEQFVICIKSGNRPnv 250
Cdd:pfam07714 150 -RDIYDDDYYRKRGGGKLpiKWMAPESLKD--GKFTSKSDVWSFGVLLWEIFTLgEQPYPGMS-NEEVLEFLEDGYRL-- 223
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1333886239 251 eEILEYCPREIISLMERCWQAIPEDRPTFLGIEEEF 286
Cdd:pfam07714 224 -PQPENCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
Death_RIP1 cd08777
Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in ...
568-653 5.69e-48

Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in Receptor-Interacting Protein 1 (RIP1) and related proteins. RIP kinases serve as essential sensors of cellular stress. Vertebrates contain several types containing a homologous N-terminal kinase domain and varying C-terminal domains. RIP1 harbors a C-terminal 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 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 accumulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260048  Cd Length: 86  Bit Score: 162.99  E-value: 5.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 568 TDEHLNPIRENLGRQWKNCARKLGFTESQIDEIDHDYERDGLKEKVYQMLQKWLMREGTKGATVGKLAQALHQCCRIDLL 647
Cdd:cd08777     1 TEKHLDLLRENLGKKWKRCARRLGLTEVEIEEIDHDYERDGLKEKVHQMLEKWKMKEGSKGATVGKLAKALEGCIKSDLL 80

                  ....*.
gi 1333886239 648 NHLIRA 653
Cdd:cd08777    81 VSLLQV 86
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
23-277 1.39e-37

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 146.31  E-value: 1.39e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHG-FVILKKVYTG-PNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNL 100
Cdd:COG0515    15 LGRGGMGVVYLARDLRLGrPVALKVLRPElAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEGESL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 MHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnkqKEVS 180
Cdd:COG0515    95 ADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIA----------------RALG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 181 STTKKNNG---GTLYYMAPEHLNDinAKPTEKSDVYSFGIVLWAIFAKKEPYEnVICTEQFVICIKSGNRPNVEEILEYC 257
Cdd:COG0515   159 GATLTQTGtvvGTPGYMAPEQARG--EPVDPRSDVYSLGVTLYELLTGRPPFD-GDSPAELLRAHLREPPPPPSELRPDL 235
                         250       260
                  ....*....|....*....|
gi 1333886239 258 PREIISLMERCWQAIPEDRP 277
Cdd:COG0515   236 PPALDAIVLRALAKDPEERY 255
PHA02988 PHA02988
hypothetical protein; Provisional
63-278 4.33e-23

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 99.82  E-value: 4.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  63 EGKMMHRLRHSRVVKLLGIIIEEGN----YSLVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDK-GVIHK 137
Cdd:PHA02988   68 EIKNLRRIDSNNILKIYGFIIDIVDdlprLSLILEYCTRGYLREVLDKEKDLSFKTKLDMAIDCCKGLYNLYKYtNKPYK 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 138 DLKPENILVDRDFHIKIadLGVASFKTWSkltkekdnkqkevSSTTKKNNggTLYYMAPEHLNDINAKPTEKSDVYSFGI 217
Cdd:PHA02988  148 NLTSVSFLVTENYKLKI--ICHGLEKILS-------------SPPFKNVN--FMVYFSYKMLNDIFSEYTIKDDIYSLGV 210
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333886239 218 VLWAIFAKKEPYENVICTEQFVICIKSgnrpNVEEILEY-CPREIISLMERCWQAIPEDRPT 278
Cdd:PHA02988  211 VLWEIFTGKIPFENLTTKEIYDLIINK----NNSLKLPLdCPLEIKCIVEACTSHDSIKRPN 268
Death pfam00531
Death domain;
569-654 9.97e-22

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 89.73  E-value: 9.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 569 DEHLNPIREN---LGRQWKNCARKLGFTESQIDEIDHDYERdgLKEKVYQMLQKWLMREGtKGATVGKLAQALHQCCRID 645
Cdd:pfam00531   1 RKQLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR--LRSQTYELLRLWEQREG-KNATVGTLLEALRKLGRRD 77

                  ....*....
gi 1333886239 646 LLNHLIRAS 654
Cdd:pfam00531  78 AAEKIQSIL 86
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
565-647 1.35e-19

DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers.


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 83.61  E-value: 1.35e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  565 TSLTDEHLNPIREN-LGRQWKNCARKLGFTESQIDEIDHDYERDgLKEKVYQMLQKWLMREGtKGATVGKLAQALHQCCR 643
Cdd:smart00005   1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRD-LAEQSVQLLRLWEQREG-KNATLGTLLEALRKMGR 78

                   ....
gi 1333886239  644 IDLL 647
Cdd:smart00005  79 DDAV 82
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
84-219 1.44e-17

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 86.39  E-value: 1.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  84 EEGNYS-LVMEYMEKGNLMHVLKTQidVPLSLKG--RIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVA 160
Cdd:NF033483   77 EDGGIPyIVMEYVDGRTLKDYIREH--GPLSPEEavEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIA 154
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333886239 161 sfktwskltkekdnkqKEVSSTTKKNNG---GTLYYMAPEHLNDINAkpTEKSDVYSFGIVL 219
Cdd:NF033483  155 ----------------RALSSTTMTQTNsvlGTVHYLSPEQARGGTV--DARSDIYSLGIVL 198
 
Name Accession Description Interval E-value
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
23-291 4.27e-163

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: 468.13  E-value: 4.27e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMH 102
Cdd:cd14027     1 LDSGGFGKVSLCFHRTQGLVVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLKtQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTWSKLTKEKDNKQKEVSST 182
Cdd:cd14027    81 VLK-KVSVPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLTKEEHNEQREVDGT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 183 TKkNNGGTLYYMAPEHLNDINAKPTEKSDVYSFGIVLWAIFAKKEPYENVICTEQFVICIKSGNRPNVEEILEYCPREII 262
Cdd:cd14027   160 AK-KNAGTLYYMAPEHLNDVNAKPTEKSDVYSFAIVLWAIFANKEPYENAINEDQIIMCIKSGNRPDVDDITEYCPREII 238
                         250       260
                  ....*....|....*....|....*....
gi 1333886239 263 SLMERCWQAIPEDRPTFLGIEEEFRPFYL 291
Cdd:cd14027   239 DLMKLCWEANPEARPTFPGIEEKFRPFYL 267
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
23-288 6.60e-108

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: 326.72  E-value: 6.60e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRS-HGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLM 101
Cdd:cd13978     1 LGSGGFGTVSKARHVSwFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 HVLKTQI-DVPLSLKGRIIVEAIEGMCYLH--DKGVIHKDLKPENILVDRDFHIKIADLGVASFKTWSKLTKEkdnkqke 178
Cdd:cd13978    81 SLLEREIqDVPWSLRFRIIHEIALGMNFLHnmDPPLLHHDLKPENILLDNHFHVKISDFGLSKLGMKSISANR------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 179 vsSTTKKNNGGTLYYMAPEHLNDINAKPTEKSDVYSFGIVLWAIFAKKEPYENVICTEQFVICIKSGNRPNVEEILEYC- 257
Cdd:cd13978   154 --RRGTENLGGTPIYMAPEAFDDFNKKPTSKSDVYSFAIVIWAVLTRKEPFENAINPLLIMQIVSKGDRPSLDDIGRLKq 231
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1333886239 258 ---PREIISLMERCWQAIPEDRPTFLgiEEEFRP 288
Cdd:cd13978   232 ienVQELISLMIRCWDGNPDARPTFL--ECLDRL 263
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
25-286 8.11e-66

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: 216.63  E-value: 8.11e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSLCYHRShGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVL 104
Cdd:cd13999     3 SGSFGEVYKGKWRG-TDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLYDLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 105 KTQ-IDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnKQKEVSSTT 183
Cdd:cd13999    82 HKKkIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLS--------------RIKNSTTEK 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 184 KKNNGGTLYYMAPEHlndINAKP-TEKSDVYSFGIVLWAIFAKKEPYENVictEQFVICIKSGNRPNVEEILEYCPREII 262
Cdd:cd13999   148 MTGVVGTPRWMAPEV---LRGEPyTEKADVYSFGIVLWELLTGEVPFKEL---SPIQIAAAVVQKGLRPPIPPDCPPELS 221
                         250       260
                  ....*....|....*....|....
gi 1333886239 263 SLMERCWQAIPEDRPTFLGIEEEF 286
Cdd:cd13999   222 KLIKRCWNEDPEKRPSFSEIVKRL 245
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
23-286 1.28e-63

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: 211.25  E-value: 1.28e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239   23 LDSGGFGKVSLC--YHRSHGFVIL---KKVYTGPNRAEYNEvLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEK 97
Cdd:smart00221   7 LGEGAFGEVYKGtlKGKGDGKEVEvavKTLKEDASEQQIEE-FLREARIMRKLDHPNIVKLLGVCTEEEPLMIVMEYMPG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239   98 GNLMHVLKTQIDVPLSLKG--RIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasfktwskLTKEKDNK 175
Cdd:smart00221  86 GDLLDYLRKNRPKELSLSDllSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFG---------LSRDLYDD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  176 QKEVSSTTKknngGTLYYMAPEHLNDinAKPTEKSDVYSFGIVLWAIFAK-KEPYENVIcTEQFVICIKSGNRPnveEIL 254
Cdd:smart00221 157 DYYKVKGGK----LPIRWMAPESLKE--GKFTSKSDVWSFGVLLWEIFTLgEEPYPGMS-NAEVLEYLKKGYRL---PKP 226
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1333886239  255 EYCPREIISLMERCWQAIPEDRPTFLGIEEEF 286
Cdd:smart00221 227 PNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
23-286 1.11e-62

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 208.54  E-value: 1.11e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239   23 LDSGGFGKVSLCYHRSHGF-----VILKKVYTGPNRAEYNEvLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEK 97
Cdd:smart00219   7 LGEGAFGEVYKGKLKGKGGkkkveVAVKTLKEDASEQQIEE-FLREARIMRKLDHPNVVKLLGVCTEEEPLYIVMEYMEG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239   98 GNLMHVLKTQID-VPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasfktwskLTKEKDNKQ 176
Cdd:smart00219  86 GDLLSYLRKNRPkLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFG---------LSRDLYDDD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  177 KEVSSTTKknngGTLYYMAPEHLNDinAKPTEKSDVYSFGIVLWAIFAK-KEPYENVIcTEQFVICIKSGNRPnveEILE 255
Cdd:smart00219 157 YYRKRGGK----LPIRWMAPESLKE--GKFTSKSDVWSFGVLLWEIFTLgEQPYPGMS-NEEVLEYLKNGYRL---PQPP 226
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1333886239  256 YCPREIISLMERCWQAIPEDRPTFLGIEEEF 286
Cdd:smart00219 227 NCPPELYDLMLQCWAEDPEDRPTFSELVEIL 257
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
23-287 2.33e-59

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: 200.07  E-value: 2.33e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLC-YHRSHGFVILKKVYTGPNRAEYNEV--LLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGN 99
Cdd:cd00192     3 LGEGAFGEVYKGkLKGGDGKTVDVAVKTLKEDASESERkdFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYMEGGD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 100 LMHVLKTQIDVPLSLKG---------RIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasfktwskLTK 170
Cdd:cd00192    83 LLDFLRKSRPVFPSPEPstlslkdllSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFG---------LSR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 171 EKDNKQKEVSSTTKKNNggtLYYMAPEHLNDinAKPTEKSDVYSFGIVLWAIFAK-KEPYENVIcTEQFVICIKSGNRPn 249
Cdd:cd00192   154 DIYDDDYYRKKTGGKLP---IRWMAPESLKD--GIFTSKSDVWSFGVLLWEIFTLgATPYPGLS-NEEVLEYLRKGYRL- 226
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1333886239 250 veEILEYCPREIISLMERCWQAIPEDRPTFLGIEEEFR 287
Cdd:cd00192   227 --PKPENCPDELYELMLSCWQLDPEDRPTFSELVERLE 262
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
23-286 1.63e-57

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: 195.02  E-value: 1.63e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFV--------ILKKVYTGPNRAEynevLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEY 94
Cdd:pfam07714   7 LGEGAFGEVYKGTLKGEGENtkikvavkTLKEGADEEERED----FLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKGNLMHVLKTQID-VPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekd 173
Cdd:pfam07714  83 MPGGDLLDFLRKHKRkLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLS------------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 174 nKQKEVSSTTKKNNGGTL--YYMAPEHLNDinAKPTEKSDVYSFGIVLWAIFAK-KEPYENVIcTEQFVICIKSGNRPnv 250
Cdd:pfam07714 150 -RDIYDDDYYRKRGGGKLpiKWMAPESLKD--GKFTSKSDVWSFGVLLWEIFTLgEQPYPGMS-NEEVLEFLEDGYRL-- 223
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1333886239 251 eEILEYCPREIISLMERCWQAIPEDRPTFLGIEEEF 286
Cdd:pfam07714 224 -PQPENCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
25-279 3.32e-55

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 188.51  E-value: 3.32e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239   25 SGGFGKVSLCYHRSHG-FVILKKVYTgPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHV 103
Cdd:smart00220   9 EGSFGKVYLARDKKTGkLVAIKVIKK-KKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCEGGDLFDL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  104 LKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnkqKEVSSTT 183
Cdd:smart00220  88 LKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLA----------------RQLDPGE 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  184 KKNNG-GTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPYENvICTEQFVICIKSGNRPNVEEILEYCPREII 262
Cdd:smart00220 152 KLTTFvGTPEYMAPEVLL--GKGYGKAVDIWSLGVILYELLTGKPPFPG-DDQLLELFKKIGKPKPPFPPPEWDISPEAK 228
                          250
                   ....*....|....*..
gi 1333886239  263 SLMERCWQAIPEDRPTF 279
Cdd:smart00220 229 DLIRKLLVKDPEKRLTA 245
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
23-282 1.15e-48

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: 169.37  E-value: 1.15e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMH 102
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLKTQID-VPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkeKDNKQKEvSS 181
Cdd:cd00180    81 LLKENKGpLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLA-----------KDLDSDD-SL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 182 TTKKNNGGTLYYMAPEHLNDINAkpTEKSDVYSFGIVLWAIfakkepyenvicteqfviciksgnrpnveeileycpREI 261
Cdd:cd00180   149 LKTTGGTTPPYYAPPELLGGRYY--GPKVDIWSLGVILYEL------------------------------------EEL 190
                         250       260
                  ....*....|....*....|.
gi 1333886239 262 ISLMERCWQAIPEDRPTFLGI 282
Cdd:cd00180   191 KDLIRRMLQYDPKKRPSAKEL 211
Death_RIP1 cd08777
Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in ...
568-653 5.69e-48

Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in Receptor-Interacting Protein 1 (RIP1) and related proteins. RIP kinases serve as essential sensors of cellular stress. Vertebrates contain several types containing a homologous N-terminal kinase domain and varying C-terminal domains. RIP1 harbors a C-terminal 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 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 accumulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260048  Cd Length: 86  Bit Score: 162.99  E-value: 5.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 568 TDEHLNPIRENLGRQWKNCARKLGFTESQIDEIDHDYERDGLKEKVYQMLQKWLMREGTKGATVGKLAQALHQCCRIDLL 647
Cdd:cd08777     1 TEKHLDLLRENLGKKWKRCARRLGLTEVEIEEIDHDYERDGLKEKVHQMLEKWKMKEGSKGATVGKLAKALEGCIKSDLL 80

                  ....*.
gi 1333886239 648 NHLIRA 653
Cdd:cd08777    81 VSLLQV 86
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
23-278 1.12e-47

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: 168.53  E-value: 1.12e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHG-FVILKKV-YTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNL 100
Cdd:cd14014     8 LGRGGMGEVYRARDTLLGrPVAIKVLrPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEYVEGGSL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 MHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKtwskltkekdnkqKEVS 180
Cdd:cd14014    88 ADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARAL-------------GDSG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 181 STTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPYENVIcTEQFVICIKSGNRPNVEEILEYCPRE 260
Cdd:cd14014   155 LTQTGSVLGTPAYMAPEQAR--GGPVDPRSDIYSLGVVLYELLTGRPPFDGDS-PAAVLAKHLQEAPPPPSPLNPDVPPA 231
                         250
                  ....*....|....*...
gi 1333886239 261 IISLMERCWQAIPEDRPT 278
Cdd:cd14014   232 LDAIILRALAKDPEERPQ 249
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
14-285 1.38e-42

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 154.43  E-value: 1.38e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  14 SSDLLEKTDLDSGGFGKVSLCYHRSHgFVILKKVYTGPNRAEyneVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVME 93
Cdd:cd05039     5 KKDLKLGELIGKGEFGDVMLGDYRGQ-KVAVKCLKDDSTAAQ---AFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIVTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  94 YMEKGNLMHVLKTQIDVPLSLKGRII--VEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltke 171
Cdd:cd05039    81 YMAKGSLVDYLRSRGRAVITRKDQLGfaLDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLA----------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 172 kdnkqKEVSSTTkknNGGTL--YYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFA-KKEPYENvICTEQFVICIKSGNRp 248
Cdd:cd05039   150 -----KEASSNQ---DGGKLpiKWTAPEALR--EKKFSTKSDVWSFGILLWEIYSfGRVPYPR-IPLKDVVPHVEKGYR- 217
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1333886239 249 nvEEILEYCPREIISLMERCWQAIPEDRPTFLGIEEE 285
Cdd:cd05039   218 --MEAPEGCPPEVYKVMKNCWELDPAKRPTFKQLREK 252
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
25-285 3.69e-42

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: 153.42  E-value: 3.69e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSLCYHRSHG--FVILKKVYTGPNRAEYNEvLLEEGKMMHRLRHSRVVKLLGIIIEEgnYSLVMEYMEKGNLMH 102
Cdd:cd14025     6 SGGFGQVYKVRHKHWKtwLAIKCPPSLHVDDSERME-LLEEAKKMEMAKFRHILPVYGICSEP--VGLVMEYMETGSLEK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLKTQiDVPLSLKGRIIVEAIEGMCYLH--DKGVIHKDLKPENILVDRDFHIKIADLGVASfktWSKLTKEKDnkqkeVS 180
Cdd:cd14025    83 LLASE-PLPWELRFRIIHETAVGMNFLHcmKPPLLHLDLKPANILLDAHYHVKISDFGLAK---WNGLSHSHD-----LS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 181 STTKKnngGTLYYMAPEHLNDINAKPTEKSDVYSFGIVLWAIFAKKEPY--ENVICTeqFVICIKSGNRPNVEEILEYCP 258
Cdd:cd14025   154 RDGLR---GTIAYLPPERFKEKNRCPDTKHDVYSFAIVIWGILTQKKPFagENNILH--IMVKVVKGHRPSLSPIPRQRP 228
                         250       260       270
                  ....*....|....*....|....*....|
gi 1333886239 259 RE---IISLMERCWQAIPEDRPTFLGIEEE 285
Cdd:cd14025   229 SEcqqMICLMKRCWDQDPRKRPTFQDITSE 258
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
23-278 5.27e-42

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: 152.67  E-value: 5.27e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVI-LKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLM 101
Cdd:cd06606     8 LGKGSFGSVYLALNLDTGELMaVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVPGGSLA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 HVLKTqidvplslKGRI-----------IVEAIEgmcYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltK 170
Cdd:cd06606    88 SLLKK--------FGKLpepvvrkytrqILEGLE---YLHSNGIVHRDIKGANILVDSDGVVKLADFGCA---------K 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 171 EKDNKQKEVSSTTKKnngGTLYYMAPEHLNDinAKPTEKSDVYSFGIVLWAIFAKKEPYENviCTEQFVICIKSGNRPNV 250
Cdd:cd06606   148 RLAEIATGEGTKSLR---GTPYWMAPEVIRG--EGYGRAADIWSLGCTVIEMATGKPPWSE--LGNPVAALFKIGSSGEP 220
                         250       260
                  ....*....|....*....|....*...
gi 1333886239 251 EEILEYCPREIISLMERCWQAIPEDRPT 278
Cdd:cd06606   221 PPIPEHLSEEAKDFLRKCLQRDPKKRPT 248
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
23-296 8.67e-41

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: 150.45  E-value: 8.67e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNE--VLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNL 100
Cdd:cd14026     5 LSRGAFGTVSRARHADWRVTVAIKCLKLDSPVGDSErnCLLKEAEILHKARFSYILPILGICNEPEFLGIVTEYMTNGSL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 MHVLKTQI---DVPLSLKGRIIVEAIEGMCYLHDKG--VIHKDLKPENILVDRDFHIKIADLGVASFKTWSkLTKEKDNK 175
Cdd:cd14026    85 NELLHEKDiypDVAWPLRLRILYEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLSKWRQLS-ISQSRSSK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 176 QKEvssttkknNGGTLYYMAPEHLNDINAKPTE-KSDVYSFGIVLWAIFAKKEPYENVICTEQFVICIKSGNRPNVEEil 254
Cdd:cd14026   164 SAP--------EGGTIIYMPPEEYEPSQKRRASvKHDIYSYAIIMWEVLSRKIPFEEVTNPLQIMYSVSQGHRPDTGE-- 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1333886239 255 EYCPREI------ISLMERCWQAIPEDRPTFLGIEEEFRPFyLSHFEE 296
Cdd:cd14026   234 DSLPVDIphratlINLIESGWAQNPDERPSFLKCLIELEPV-LRTFDE 280
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
63-283 6.50e-38

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: 141.42  E-value: 6.50e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  63 EGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAI---EGMCYLH---DKGVIH 136
Cdd:cd14058    36 EVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLYNVLHGKEPKPIYTAAHAMSWALqcaKGVAYLHsmkPKALIH 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 137 KDLKPENIL-VDRDFHIKIADLGVASFKtwskltkekdnkqkevsSTTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSF 215
Cdd:cd14058   116 RDLKPPNLLlTNGGTVLKICDFGTACDI-----------------STHMTNNKGSAAWMAPEVFE--GSKYSEKCDVFSW 176
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 216 GIVLWAIFAKKEPYENvICTE--QFVICIKSGNRPNVEEIleyCPREIISLMERCWQAIPEDRPTFLGIE 283
Cdd:cd14058   177 GIILWEVITRRKPFDH-IGGPafRIMWAVHNGERPPLIKN---CPKPIESLMTRCWSKDPEKRPSMKEIV 242
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
23-278 8.96e-38

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: 141.37  E-value: 8.96e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKV-SLCYHRSHgfVILKKVYT-GPNRAEYNEVLLEegKMMHRLRHSRVVKLLGII--IEEGNYSLV-MEYMEK 97
Cdd:cd13979    11 LGSGGFGSVyKATYKGET--VAVKIVRRrRKNRASRQSFWAE--LNAARLRHENIVRVLAAEtgTDFASLGLIiMEYCGN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  98 GNLMHVLKTQIDvPLSLKGR--IIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVasfktwSKLTKEKDNK 175
Cdd:cd13979    87 GTLQQLIYEGSE-PLPLAHRilISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGC------SVKLGEGNEV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 176 QkevssTTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPYENVictEQFVI--CIKSGNRPNVEEI 253
Cdd:cd13979   160 G-----TPRSHIGGTYTYRAPELLK--GERVTPKADIYSFGITLWQMLTRELPYAGL---RQHVLyaVVAKDLRPDLSGL 229
                         250       260
                  ....*....|....*....|....*.
gi 1333886239 254 LEYCPREII-SLMERCWQAIPEDRPT 278
Cdd:cd13979   230 EDSEFGQRLrSLISRCWSAQPAERPN 255
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
25-278 1.05e-37

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: 140.80  E-value: 1.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSLCYHRSHGFVI-LKKVYTgpNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHV 103
Cdd:cd05122    10 KGGFGVVYKARHKKTGQIVaIKKINL--ESKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFCSGGSLKDL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 104 LKTQIDV-PLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTwskltkekdnkqkevSST 182
Cdd:cd05122    88 LKNTNKTlTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLS---------------DGK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 183 TKKNNGGTLYYMAPEHlndINAKP-TEKSDVYSFGIVLWAIFAKKEPYENVICTEQFVIcIKSGNRPNVEEIlEYCPREI 261
Cdd:cd05122   153 TRNTFVGTPYWMAPEV---IQGKPyGFKADIWSLGITAIEMAEGKPPYSELPPMKALFL-IATNGPPGLRNP-KKWSKEF 227
                         250
                  ....*....|....*..
gi 1333886239 262 ISLMERCWQAIPEDRPT 278
Cdd:cd05122   228 KDFLKKCLQKDPEKRPT 244
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
23-286 1.30e-37

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: 140.87  E-value: 1.30e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGpNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMH 102
Cdd:cd14066     1 IGSGGFGTVYKGVLENGTVVAVKRLNEM-NCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLKTQID-VPLSLKGR--IIVEAIEGMCYLHDKG---VIHKDLKPENILVDRDFHIKIADLGVAsfktwsKLTKEKDNKQ 176
Cdd:cd14066    80 RLHCHKGsPPLPWPQRlkIAKGIARGLEYLHEECpppIIHGDIKSSNILLDEDFEPKLTDFGLA------RLIPPSESVS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 177 KEVSSTtkknngGTLYYMAPEHLNDinAKPTEKSDVYSFGIVLWAIFAKKEPYENVICTEQF---VICIKSGNRPNVEEI 253
Cdd:cd14066   154 KTSAVK------GTIGYLAPEYIRT--GRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRkdlVEWVESKGKEELEDI 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1333886239 254 LEYCPR-----------EIISLMERCWQAIPEDRPTFLGIEEEF 286
Cdd:cd14066   226 LDKRLVdddgveeeeveALLRLALLCTRSDPSLRPSMKEVVQML 269
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
23-277 1.39e-37

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 146.31  E-value: 1.39e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHG-FVILKKVYTG-PNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNL 100
Cdd:COG0515    15 LGRGGMGVVYLARDLRLGrPVALKVLRPElAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEGESL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 MHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnkqKEVS 180
Cdd:COG0515    95 ADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIA----------------RALG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 181 STTKKNNG---GTLYYMAPEHLNDinAKPTEKSDVYSFGIVLWAIFAKKEPYEnVICTEQFVICIKSGNRPNVEEILEYC 257
Cdd:COG0515   159 GATLTQTGtvvGTPGYMAPEQARG--EPVDPRSDVYSLGVTLYELLTGRPPFD-GDSPAELLRAHLREPPPPPSELRPDL 235
                         250       260
                  ....*....|....*....|
gi 1333886239 258 PREIISLMERCWQAIPEDRP 277
Cdd:COG0515   236 PPALDAIVLRALAKDPEERY 255
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
20-283 2.37e-37

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 140.22  E-value: 2.37e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  20 KTDLDSGGFGKVSLCYHRSHgfVILKKVYTgpnRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGN 99
Cdd:cd13992     8 SSHTGEPKYVKKVGVYGGRT--VAIKHITF---SRTEKRTILQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 100 LMHVLKTQiDVPLS--LKGRIIVEAIEGMCYLHD-KGVIHKDLKPENILVDRDFHIKIADLGVASFKtwskltKEKDNKQ 176
Cdd:cd13992    83 LQDVLLNR-EIKMDwmFKSSFIKDIVKGMNYLHSsSIGYHGRLKSSNCLVDSRWVVKLTDFGLRNLL------EEQTNHQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 177 KEVSSTTKKnnggtLYYMAPEHLNDI--NAKPTEKSDVYSFGIVLWAIFAKKEPYENVICTEQFVICIKSGN---RPNVE 251
Cdd:cd13992   156 LDEDAQHKK-----LLWTAPELLRGSllEVRGTQKGDVYSFAIILYEILFRSDPFALEREVAIVEKVISGGNkpfRPELA 230
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1333886239 252 EILEYCPREIISLMERCWQAIPEDRPTFLGIE 283
Cdd:cd13992   231 VLLDEFPPRLVLLVKQCWAENPEKRPSFKQIK 262
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
15-279 1.72e-36

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: 137.58  E-value: 1.72e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  15 SDLLEKTDLDSGGFGKVSLCYHRSHGFVILKKVYTGpnrAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEY 94
Cdd:cd05059     4 SELTFLKELGSGQFGVVHLGKWRGKIDVAIKMIKEG---SMSEDDFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKGNLMHVLKTQidvPLSLKGRIIVEAI----EGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFktwskltk 170
Cdd:cd05059    81 MANGCLLNYLRER---RGKFQTEQLLEMCkdvcEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARY-------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 171 ekdnkqkeVSSTTKKNNGGTLY---YMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAK-KEPYENVICTEQfviciksgn 246
Cdd:cd05059   150 --------VLDDEYTSSVGTKFpvkWSPPEVFM--YSKFSSKSDVWSFGVLMWEVFSEgKMPYERFSNSEV--------- 210
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1333886239 247 rpnVEEILE--------YCPREIISLMERCWQAIPEDRPTF 279
Cdd:cd05059   211 ---VEHISQgyrlyrphLAPTEVYTIMYSCWHEKPEERPTF 248
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
22-286 4.66e-36

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


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 137.13  E-value: 4.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  22 DLDSGGFGKVSLCYHRSHG-----FVILKKVYTGPNRAEYNEvLLEEGKMMHRLRHSRVVKLLGIIIEEGNYS--LVMEY 94
Cdd:cd05038    11 QLGEGHFGSVELCRYDPLGdntgeQVAVKSLQPSGEEQHMSD-FKREIEILRTLDHEYIVKYKGVCESPGRRSlrLIMEY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKGNLMHVL---KTQIDVPLSLkgRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFktwskLTKE 171
Cdd:cd05038    90 LPSGSLRDYLqrhRDQIDLKRLL--LFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKV-----LPED 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 172 KDnkqkevSSTTKKNNGGTLYYMAPEHLNDinAKPTEKSDVYSFGIVLWAIFAKKEPYENVICT--------------EQ 237
Cdd:cd05038   163 KE------YYYVKEPGESPIFWYAPECLRE--SRFSSASDVWSFGVTLYELFTYGDPSQSPPALflrmigiaqgqmivTR 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333886239 238 FVICIKSG---NRPnveeilEYCPREIISLMERCWQAIPEDRPTFLGIEEEF 286
Cdd:cd05038   235 LLELLKSGerlPRP------PSCPDEVYDLMKECWEYEPQDRPSFSDLILII 280
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
26-285 1.61e-35

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


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 134.49  E-value: 1.61e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLK 105
Cdd:cd05041     6 GNFGDVYRGVLKPDNTEVAVKTCRETLPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGSLLTFLR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 106 TQIDvPLSLKG--RIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasfktwskLTKEKDNKQKEVSSTT 183
Cdd:cd05041    86 KKGA-RLTVKQllQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFG---------MSREEEDGEYTVSDGL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 184 KKNnggTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKE-PYENvICTEQFVICIKSGNR---PnveeilEYCPR 259
Cdd:cd05041   156 KQI---PIKWTAPEALN--YGRYTSESDVWSFGILLWEIFSLGAtPYPG-MSNQQTREQIESGYRmpaP------ELCPE 223
                         250       260
                  ....*....|....*....|....*.
gi 1333886239 260 EIISLMERCWQAIPEDRPTFLGIEEE 285
Cdd:cd05041   224 AVYRLMLQCWAYDPENRPSFSEIYNE 249
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
17-278 5.66e-35

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: 133.03  E-value: 5.66e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  17 LLEKTdLDSGGFGKVSLCYHR-SHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYM 95
Cdd:cd14003     3 ELGKT-LGEGSFGKVKLARHKlTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  96 EKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwsklTKEKDNK 175
Cdd:cd14003    82 SGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLS--------NEFRGGS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 176 QKEVSSttkknngGTLYYMAPEHLNDINaKPTEKSDVYSFGIVLWAIFAKKEPYE--NVICTEQFvicIKSGNrpnvEEI 253
Cdd:cd14003   154 LLKTFC-------GTPAYAAPEVLLGRK-YDGPKADVWSLGVILYAMLTGYLPFDddNDSKLFRK---ILKGK----YPI 218
                         250       260
                  ....*....|....*....|....*
gi 1333886239 254 LEYCPREIISLMERCWQAIPEDRPT 278
Cdd:cd14003   219 PSHLSPDARDLIRRMLVVDPSKRIT 243
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
4-297 7.51e-35

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: 133.24  E-value: 7.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239   4 DMSLDNIKMASSdllektdLDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEyneVLLEEGKMMHRLRHSRVVKLLGIII 83
Cdd:cd05072     3 EIPRESIKLVKK-------LGAGQFGEVWMGYYNNSTKVAVKTLKPGTMSVQ---AFLEEANLMKTLQHDKLVRLYAVVT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  84 EEGNYSLVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEA--IEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAS 161
Cdd:cd05072    73 KEEPIYIITEYMAKGSLLDFLKSDEGGKVLLPKLIDFSAqiAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLAR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 162 FKtwskltkeKDNKQkevssTTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFA-KKEPYENVICTEQFVI 240
Cdd:cd05072   153 VI--------EDNEY-----TAREGAKFPIKWTAPEAIN--FGSFTIKSDVWSFGILLYEIVTyGKIPYPGMSNSDVMSA 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333886239 241 CIKSGNRPNVEEileyCPREIISLMERCWQAIPEDRPTFLGIEEEFRPFYLSHFEEY 297
Cdd:cd05072   218 LQRGYRMPRMEN----CPDELYDIMKTCWKEKAEERPTFDYLQSVLDDFYTATEGQY 270
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
15-279 1.26e-34

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: 132.00  E-value: 1.26e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  15 SDLLEKTDLDSGGFGKVSLCYHRSHGFVILKKVYTGpnrAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEY 94
Cdd:cd05112     4 SELTFVQEIGSGQFGLVHLGYWLNKDKVAIKTIREG---AMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKGNLMHVLKTQidvplslKGRIIVEAI--------EGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTWS 166
Cdd:cd05112    81 MEHGCLSDYLRTQ-------RGLFSAETLlgmcldvcEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 167 KLTkekdnkqkevSSTTKKNnggTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAK-KEPYENVICTEqFVICIKSG 245
Cdd:cd05112   154 QYT----------SSTGTKF---PVKWSSPEVFS--FSRYSSKSDVWSFGVLMWEVFSEgKIPYENRSNSE-VVEDINAG 217
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1333886239 246 NR---PNVeeileyCPREIISLMERCWQAIPEDRPTF 279
Cdd:cd05112   218 FRlykPRL------ASTHVYEIMNHCWKERPEDRPSF 248
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
23-278 1.29e-34

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: 132.29  E-value: 1.29e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHG--FVI-------LKKVYTGPNRAEYNEVLLE----EGKMMHRLRHSRVVKLLGII-IEEGNY 88
Cdd:cd14008     1 LGRGSFGKVKLALDTETGqlYAIkifnksrLRKRREGKNDRGKIKNALDdvrrEIAIMKKLDHPNIVRLYEVIdDPESDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  89 -SLVMEYMEKGNLMHVLKTQIDVPLSLKG-----RIIVEAIEgmcYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASF 162
Cdd:cd14008    81 lYLVLEYCEGGPVMELDSGDRVPPLPEETarkyfRDLVLGLE---YLHENGIVHRDIKPENLLLTADGTVKISDFGVSEM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 163 ktwskLTKEKDnkqkevsstTKKNNGGTLYYMAPEHLnDINAKP--TEKSDVYSFGIVLWAIFAKKEPYEnviCTEQFVI 240
Cdd:cd14008   158 -----FEDGND---------TLQKTAGTPAFLAPELC-DGDSKTysGKAADIWALGVTLYCLVFGRLPFN---GDNILEL 219
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1333886239 241 CIKSGNRPNVEEILEYCPREIISLMERCWQAIPEDRPT 278
Cdd:cd14008   220 YEAIQNQNDEFPIPPELSPELKDLLRRMLEKDPEKRIT 257
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
58-286 1.73e-34

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 131.53  E-value: 1.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  58 EVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYsLVMEYMEKGNLMHVLKTQ--IDVPLSLKGRIIVEAIEGMCYLHDKGVI 135
Cdd:cd05083    44 QAFLEETAVMTKLQHKNLVRLLGVILHNGLY-IVMELMSKGNLVNFLRSRgrALVPVIQLLQFSLDVAEGMEYLESKKLV 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 136 HKDLKPENILVDRDFHIKIADLGVASFKtwsklTKEKDNKQKEVSSTtkknnggtlyymAPEHLNdiNAKPTEKSDVYSF 215
Cdd:cd05083   123 HRDLAARNILVSEDGVAKISDFGLAKVG-----SMGVDNSRLPVKWT------------APEALK--NKKFSSKSDVWSY 183
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333886239 216 GIVLWAIFA-KKEPYENVICTEqFVICIKSGNRpnvEEILEYCPREIISLMERCWQAIPEDRPTFLGIEEEF 286
Cdd:cd05083   184 GVLLWEVFSyGRAPYPKMSVKE-VKEAVEKGYR---MEPPEGCPPDVYSIMTSCWEAEPGKRPSFKKLREKL 251
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
25-279 2.38e-34

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: 131.36  E-value: 2.38e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSLCyhRSHGFVILKKV-YTGPN----RAEYNEVlleegKMMHRLRHSRVVKLLGIIIEEgNYSLVMEYMEKGN 99
Cdd:cd14062     3 SGSFGTVYKG--RWHGDVAVKKLnVTDPTpsqlQAFKNEV-----AVLRKTRHVNILLFMGYMTKP-QLAIVTQWCEGSS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 100 L---MHVLKTQIDVPLSLKgrIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTWSklTKEKDNKQ 176
Cdd:cd14062    75 LykhLHVLETKFEMLQLID--IARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLATVKTRW--SGSQQFEQ 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 177 KEvssttkknngGTLYYMAPEHLNDINAKP-TEKSDVYSFGIVLWAIFAKKEPYENVICTEQFVICIKSGN-RPNVEEIL 254
Cdd:cd14062   151 PT----------GSILWMAPEVIRMQDENPySFQSDVYAFGIVLYELLTGQLPYSHINNRDQILFMVGRGYlRPDLSKVR 220
                         250       260
                  ....*....|....*....|....*
gi 1333886239 255 EYCPREIISLMERCWQAIPEDRPTF 279
Cdd:cd14062   221 SDTPKALRRLMEDCIKFQRDERPLF 245
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
23-279 3.42e-34

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: 131.16  E-value: 3.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEyneVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYsLVMEYMEKGNLMH 102
Cdd:cd05067    15 LGAGQFGEVWMGYYNGHTKVAIKSLKQGSMSPD---AFLAEANLMKQLQHQRLVRLYAVVTQEPIY-IITEYMENGSLVD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLKTQIDVPLSLKGRIIVEA--IEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwsKLTKEKDNKQKEVS 180
Cdd:cd05067    91 FLKTPSGIKLTINKLLDMAAqiAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLA------RLIEDNEYTAREGA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 181 STTKKnnggtlyYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFA-KKEPYENVICTEqfviCIKSGNRPNVEEILEYCPR 259
Cdd:cd05067   165 KFPIK-------WTAPEAIN--YGTFTIKSDVWSFGILLTEIVThGRIPYPGMTNPE----VIQNLERGYRMPRPDNCPE 231
                         250       260
                  ....*....|....*....|
gi 1333886239 260 EIISLMERCWQAIPEDRPTF 279
Cdd:cd05067   232 ELYQLMRLCWKERPEDRPTF 251
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
25-278 1.03e-33

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: 129.50  E-value: 1.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSLCYHRSHG-FVILKKVYTGP----NRAE-YNEVlleegKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKG 98
Cdd:cd08215    10 KGSFGSAYLVRRKSDGkLYVLKEIDLSNmsekEREEaLNEV-----KLLSKLKHPNIVKYYESFEENGKLCIVMEYADGG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  99 NLMHVLKTQIDVPLSLKGRII----VEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdn 174
Cdd:cd08215    85 DLAQKIKKQKKKGQPFPEEQIldwfVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGIS-------------- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 175 kqKEVSSTTKKNNG--GTLYYMAPEHLNDinaKP-TEKSDVYSFGIVLWAIFAKKEPYE--NVIcteQFVICIKSGNRPN 249
Cdd:cd08215   151 --KVLESTTDLAKTvvGTPYYLSPELCEN---KPyNYKSDIWALGCVLYELCTLKHPFEanNLP---ALVYKIVKGQYPP 222
                         250       260
                  ....*....|....*....|....*....
gi 1333886239 250 VEEIleYcPREIISLMERCWQAIPEDRPT 278
Cdd:cd08215   223 IPSQ--Y-SSELRDLVNSMLQKDPEKRPS 248
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
23-285 1.94e-33

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


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 128.76  E-value: 1.94e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRaeyNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMH 102
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGKVMVMKELKRFDE---QRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLEE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLKTQiDVPLSLKGRIIV--EAIEGMCYLHDKGVIHKDLKPENILV---DRDFHIKIADLGVAsfktwsklTKEKDNKQK 177
Cdd:cd14065    78 LLKSM-DEQLPWSQRVSLakDIASGMAYLHSKNIIHRDLNSKNCLVreaNRGRNAVVADFGLA--------REMPDEKTK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 178 EVSSTTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAK--KEPyENVICTEQFVIciksgnrpNVEEILE 255
Cdd:cd14065   149 KPDRKKRLTVVGSPYWMAPEMLR--GESYDEKVDVFSFGIVLCEIIGRvpADP-DYLPRTMDFGL--------DVRAFRT 217
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1333886239 256 Y----CPREIISLMERCWQAIPEDRPTFLGIEEE 285
Cdd:cd14065   218 LyvpdCPPSFLPLAIRCCQLDPEKRPSFVELEHH 251
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
25-219 2.43e-33

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: 128.36  E-value: 2.43e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSLCYHRSHGF-----VILKKVYTGPNRaeynEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGN 99
Cdd:cd05117    10 RGSFGVVRLAVHKKTGEeyavkIIDKKKLKSEDE----EMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMELCTGGE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 100 LM-HVLKTQIdvpLSLK-GRIIVEAI-EGMCYLHDKGVIHKDLKPENILV---DRDFHIKIADLGVASFktwskltKEKD 173
Cdd:cd05117    86 LFdRIVKKGS---FSEReAAKIMKQIlSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGLAKI-------FEEG 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1333886239 174 NKQKEVSsttkknngGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVL 219
Cdd:cd05117   156 EKLKTVC--------GTPYYVAPEVLK--GKGYGKKCDIWSLGVIL 191
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
25-282 3.37e-33

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: 128.28  E-value: 3.37e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSLCYHRSHgFVILKKVYTGPNR--AEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMH 102
Cdd:cd14061     4 VGGFGKVYRGIWRGE-EVAVKAARQDPDEdiSVTLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGGALNR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLkTQIDVPLSLKGRIIVEAIEGMCYLHDKG---VIHKDLKPENILVDR--------DFHIKIADLGVAsfktwskltke 171
Cdd:cd14061    83 VL-AGRKIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILEaienedleNKTLKITDFGLA----------- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 172 kdnkqKEVSSTTKKNNGGTLYYMAPEHlndINAKPTEK-SDVYSFGIVLWAIFAKKEPYENVICTE-QFVICIKSGNRPn 249
Cdd:cd14061   151 -----REWHKTTRMSAAGTYAWMAPEV---IKSSTFSKaSDVWSYGVLLWELLTGEVPYKGIDGLAvAYGVAVNKLTLP- 221
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1333886239 250 veeILEYCPREIISLMERCWQAIPEDRPTFLGI 282
Cdd:cd14061   222 ---IPSTCPEPFAQLMKDCWQPDPHDRPSFADI 251
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
41-289 3.48e-33

Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-A binds and is activated by the atrial and B-type natriuretic peptides, ANP and BNP, which are important in blood pressure regulation and cardiac pathophysiology. GC-B binds the C-type natriuretic peptide, CNP, which is a potent vasorelaxant and functions in vascular remodeling and bone growth regulation. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-A/B subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 128.87  E-value: 3.48e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  41 FVILKKVYTgpNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQiDVPL------SL 114
Cdd:cd14042    32 LVAIKKVNK--KRIDLTREVLKELKHMRDLQHDNLTRFIGACVDPPNICILTEYCPKGSLQDILENE-DIKLdwmfrySL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 115 kgriIVEAIEGMCYLHDKGVI-HKDLKPENILVDRDFHIKIADLGVASFKtwskltKEKDNKQKEVSSTTKknnggtLYY 193
Cdd:cd14042   109 ----IHDIVKGMHYLHDSEIKsHGNLKSSNCVVDSRFVLKITDFGLHSFR------SGQEPPDDSHAYYAK------LLW 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 194 MAPEHL--NDINAKPTEKSDVYSFGIVLWAIFAKKEP-YENVIC--TEQFVICIKSGN-----RPNVEEILeyCPREIIS 263
Cdd:cd14042   173 TAPELLrdPNPPPPGTQKGDVYSFGIILQEIATRQGPfYEEGPDlsPKEIIKKKVRNGekppfRPSLDELE--CPDEVLS 250
                         250       260
                  ....*....|....*....|....*.
gi 1333886239 264 LMERCWQAIPEDRPTFLGIEEEFRPF 289
Cdd:cd14042   251 LMQRCWAEDPEERPDFSTLRNKLKKL 276
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
21-282 8.25e-33

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


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 127.46  E-value: 8.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  21 TDLDSGGFGKVSLCYHRS----HGF--VILKKVYTGPNRAEYNEvLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEY 94
Cdd:cd05032    12 RELGQGSFGMVYEGLAKGvvkgEPEtrVAIKTVNENASMRERIE-FLNEASVMKEFNCHHVVRLLGVVSTGQPTLVVMEL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKGNLMHVLKTQ---------IDVPLSlkGRIIVEAIE---GMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsf 162
Cdd:cd05032    91 MAKGDLKSYLRSRrpeaennpgLGPPTL--QKFIQMAAEiadGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGDFGMT-- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 163 ktwsKLTKEKDnkqkevssTTKKNNGGTL--YYMAPEHLNDinAKPTEKSDVYSFGIVLWAI--FAkKEPY-----ENVI 233
Cdd:cd05032   167 ----RDIYETD--------YYRKGGKGLLpvRWMAPESLKD--GVFTTKSDVWSFGVVLWEMatLA-EQPYqglsnEEVL 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1333886239 234 cteQFVICIKSGNRPnveeilEYCPREIISLMERCWQAIPEDRPTFLGI 282
Cdd:cd05032   232 ---KFVIDGGHLDLP------ENCPDKLLELMRMCWQYNPKMRPTFLEI 271
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
15-278 1.33e-32

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: 126.69  E-value: 1.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  15 SDLLEKTDLDSGGFGKVSLCYHRSHGFVI-LKKVYTGPNRAEYNEvLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVME 93
Cdd:cd06605     1 DDLEYLGELGEGNGGVVSKVRHRPSGQIMaVKVIRLEIDEALQKQ-ILRELDVLHKCNSPYIVGFYGAFYSEGDISICME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  94 YMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDK-GVIHKDLKPENILVDRDFHIKIADLGVASfktwskltkek 172
Cdd:cd06605    80 YMDGGSLDKILKEVGRIPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQVKLCDFGVSG----------- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 173 dnkqkEVSSTTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPYENvicteqfvicIKSGNRPNVEE 252
Cdd:cd06605   149 -----QLVDSLAKTFVGTRSYMAPERIS--GGKYTVKSDIWSLGLSLVELATGRFPYPP----------PNAKPSMMIFE 211
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1333886239 253 ILEYC-----PR--------EIISLMERCWQAIPEDRPT 278
Cdd:cd06605   212 LLSYIvdeppPLlpsgkfspDFQDFVSQCLQKDPTERPS 250
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
15-278 2.50e-32

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: 125.78  E-value: 2.50e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  15 SDLLEKTDLDSGGFGKVSLCYHR-SHGFVILKKVYtGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVME 93
Cdd:cd06623     1 SDLERVKVLGQGSSGVVYKVRHKpTGKIYALKKIH-VDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  94 YMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLH-DKGVIHKDLKPENILVDRDFHIKIADLGVASFktwskltkek 172
Cdd:cd06623    80 YMDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHtKRHIIHRDIKPSNLLINSKGEVKIADFGISKV---------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 173 dnkqkeVSSTTKKNNG--GTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPYENVICTEQFVIC--IKSGNRP 248
Cdd:cd06623   150 ------LENTLDQCNTfvGTVTYMSPERIQ--GESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFFELMqaICDGPPP 221
                         250       260       270
                  ....*....|....*....|....*....|
gi 1333886239 249 NVEEilEYCPREIISLMERCWQAIPEDRPT 278
Cdd:cd06623   222 SLPA--EEFSPEFRDFISACLQKDPKKRPS 249
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
60-299 6.10e-32

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


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 126.23  E-value: 6.10e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  60 LLEEGKMMHRL-RHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQ--------IDVPLSLKGRIIVEAI------- 123
Cdd:cd05099    64 LISEMELMKLIgKHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARrppgpdytFDITKVPEEQLSFKDLvscayqv 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 124 -EGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdNKQKEVSSTTKKNNGGT-LYYMAPEHLND 201
Cdd:cd05099   144 aRGMEYLESRRCIHRDLAARNVLVTEDNVMKIADFGLA-------------RGVHDIDYYKKTSNGRLpVKWMAPEALFD 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 202 inAKPTEKSDVYSFGIVLWAIFA-KKEPYENVICTEQFVIcIKSGNR----PNveeileyCPREIISLMERCWQAIPEDR 276
Cdd:cd05099   211 --RVYTHQSDVWSFGILMWEIFTlGGSPYPGIPVEELFKL-LREGHRmdkpSN-------CTHELYMLMRECWHAVPTQR 280
                         250       260
                  ....*....|....*....|...
gi 1333886239 277 PTFLGIEEEFRPFYLSHFEEYVE 299
Cdd:cd05099   281 PTFKQLVEALDKVLAAVSEEYLD 303
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
23-279 6.50e-32

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: 124.32  E-value: 6.50e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEyneVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMH 102
Cdd:cd05034     3 LGAGQFGEVWMGVWNGTTKVAVKTLKPGTMSPE---AFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSKGSLLD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLKTQIDVPLSLKGRIIVEA--IEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwsKLTKEKDNKQKEVS 180
Cdd:cd05034    80 YLRTGEGRALRLPQLIDMAAqiASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLA------RLIEDDEYTAREGA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 181 STTKKnnggtlyYMAPEHLNDinAKPTEKSDVYSFGIVLWAIFAK-KEPYENVICTEqfVI-CIKSGNRpnvEEILEYCP 258
Cdd:cd05034   154 KFPIK-------WTAPEAALY--GRFTIKSDVWSFGILLYEIVTYgRVPYPGMTNRE--VLeQVERGYR---MPKPPGCP 219
                         250       260
                  ....*....|....*....|.
gi 1333886239 259 REIISLMERCWQAIPEDRPTF 279
Cdd:cd05034   220 DELYDIMLQCWKKEPEERPTF 240
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
62-282 1.36e-31

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: 123.14  E-value: 1.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  62 EEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQIDVPLSLKgRIIVEAIE---GMCYLHDKG---VI 135
Cdd:cd14060    31 KEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFDYLNSNESEEMDMD-QIMTWATDiakGMHYLHMEApvkVI 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 136 HKDLKPENILVDRDFHIKIADLGVASFktwskltkekdnkqkeVSSTTKKNNGGTLYYMAPEHlndINAKPT-EKSDVYS 214
Cdd:cd14060   110 HRDLKSRNVVIAADGVLKICDFGASRF----------------HSHTTHMSLVGTFPWMAPEV---IQSLPVsETCDTYS 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333886239 215 FGIVLWAIFAKKEPYENVICTEQFVICIKSGNRPNveeILEYCPREIISLMERCWQAIPEDRPTFLGI 282
Cdd:cd14060   171 YGVVLWEMLTREVPFKGLEGLQVAWLVVEKNERPT---IPSSCPRSFAELMRRCWEADVKERPSFKQI 235
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
23-295 3.52e-31

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: 121.83  E-value: 3.52e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSL-CYHRSHgfVILKKVytgpnraeyNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLM 101
Cdd:cd14059     1 LGSGAQGAVFLgKFRGEE--VAVKKV---------RDEKETDIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLY 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 HVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGvaSFKTWSKltkekdnkqkevsS 181
Cdd:cd14059    70 EVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFG--TSKELSE-------------K 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 182 TTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPYENVictEQFVICIKSGNRPNVEEILEYCPREI 261
Cdd:cd14059   135 STKMSFAGTVAWMAPEVIR--NEPCSEKVDIWSFGVVLWELLTGEIPYKDV---DSSAIIWGVGSNSLQLPVPSTCPDGF 209
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1333886239 262 ISLMERCWQAIPEDRPTFLGIeeefrpfyLSHFE 295
Cdd:cd14059   210 KLLMKQCWNSKPRNRPSFRQI--------LMHLD 235
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
23-279 5.84e-31

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 122.83  E-value: 5.84e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLC-YHRSHGFV----ILKKVYTGPN-------RAEYNEVLLE----EGKMMHRLRHSRVVKLLGIIIEEG 86
Cdd:cd05051    13 LGEGQFGEVHLCeANGLSDLTsddfIGNDNKDEPVlvavkmlRPDASKNAREdflkEVKIMSQLKDPNIVRLLGVCTRDE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  87 NYSLVMEYMEKGNL-----MHVLKTQIDVPLSLKG-------RIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKI 154
Cdd:cd05051    93 PLCMIVEYMENGDLnqflqKHEAETQGASATNSKTlsygtllYMATQIASGMKYLESLNFVHRDLATRNCLVGPNYTIKI 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 155 ADLGvasfktwskltkekdnkqkevsstTKKNNGGTLYY------------MAPEHLndINAKPTEKSDVYSFGIVLWAI 222
Cdd:cd05051   173 ADFG------------------------MSRNLYSGDYYriegravlpirwMAWESI--LLGKFTTKSDVWAFGVTLWEI 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333886239 223 --FAKKEPYEnVICTEQfVI--CIKSGNRPNVEEILEY---CPREIISLMERCWQAIPEDRPTF 279
Cdd:cd05051   227 ltLCKEQPYE-HLTDEQ-VIenAGEFFRDDGMEVYLSRppnCPKEIYELMLECWRRDEEDRPTF 288
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
23-279 6.21e-31

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: 122.06  E-value: 6.21e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEyneVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYsLVMEYMEKGNLMH 102
Cdd:cd05073    19 LGAGQFGEVWMATYNKHTKVAVKTMKPGSMSVE---AFLAEANVMKTLQHDKLVKLHAVVTKEPIY-IITEFMAKGSLLD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLKTQI--DVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKtwskltkeKDNKQkevs 180
Cdd:cd05073    95 FLKSDEgsKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVI--------EDNEY---- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 181 sTTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFA-KKEPYENVICTEqfviCIKSGNRPNVEEILEYCPR 259
Cdd:cd05073   163 -TAREGAKFPIKWTAPEAIN--FGSFTIKSDVWSFGILLMEIVTyGRIPYPGMSNPE----VIRALERGYRMPRPENCPE 235
                         250       260
                  ....*....|....*....|
gi 1333886239 260 EIISLMERCWQAIPEDRPTF 279
Cdd:cd05073   236 ELYNIMMRCWKNRPEERPTF 255
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
26-286 9.65e-31

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: 121.68  E-value: 9.65e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGfVILKKVYTGPNR--AEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHV 103
Cdd:cd14146     5 GGFGKVYRATWKGQE-VAVKAARQDPDEdiKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGTLNRA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 104 LKTQIDVPLSLKGRII---------VEAIEGMCYLHDKGV---IHKDLKPENILVDRDFH--------IKIADLGVAsfK 163
Cdd:cd14146    84 LAAANAAPGPRRARRIpphilvnwaVQIARGMLYLHEEAVvpiLHRDLKSSNILLLEKIEhddicnktLKITDFGLA--R 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 164 TWSKltkekdnkqkevssTTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPYENVI-CTEQFVICI 242
Cdd:cd14146   162 EWHR--------------TTKMSAAGTYAWMAPEVIK--SSLFSKGSDIWSYGVLLWELLTGEVPYRGIDgLAVAYGVAV 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1333886239 243 KSGNRPnveeILEYCPREIISLMERCWQAIPEDRPTFLGIEEEF 286
Cdd:cd14146   226 NKLTLP----IPSTCPEPFAKLMKECWEQDPHIRPSFALILEQL 265
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
17-285 1.16e-30

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: 121.00  E-value: 1.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  17 LLEKtdLDSGGFGKVSLCYHRSHGFVILKKVYTgpNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYME 96
Cdd:cd05148    10 LERK--LGSGYFGEVWEGLWKNRVRVAIKILKS--DDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITELME 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  97 KGNLMHVLKTQIDVPLSLKGRIIV--EAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwsKLTKEkdn 174
Cdd:cd05148    86 KGSLLAFLRSPEGQVLPVASLIDMacQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLA------RLIKE--- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 175 kqkEVSSTTKKNNggTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAK-KEPYENVICTEQFVIcIKSGNR-PNVEE 252
Cdd:cd05148   157 ---DVYLSSDKKI--PYKWTAPEAAS--HGTFSTKSDVWSFGILLYEMFTYgQVPYPGMNNHEVYDQ-ITAGYRmPCPAK 228
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1333886239 253 ileyCPREIISLMERCWQAIPEDRPTFLGIEEE 285
Cdd:cd05148   229 ----CPQEIYKIMLECWAAEPEDRPSFKALREE 257
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
23-285 1.32e-30

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: 121.76  E-value: 1.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSL-------CYHRSHGFVILKKVYTGPNRAEYNEvLLEEGKMMHRL-RHSRVVKLLGIIIEEGNYSLVMEY 94
Cdd:cd05053    20 LGEGAFGQVVKaeavgldNKPNEVVTVAVKMLKDDATEKDLSD-LVSEMEMMKMIgKHKNIINLLGACTQDGPLYVVVEY 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKGNLMHVLKTQIDVPLSLKGRIIVEAIE----------------GMCYLHDKGVIHKDLKPENILVDRDFHIKIADLG 158
Cdd:cd05053    99 ASKGNLREFLRARRPPGEEASPDDPRVPEEqltqkdlvsfayqvarGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFG 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 159 VAsfktwskltkekdnkqKEVSSTT--KKNNGGTLYY--MAPEHLNDinAKPTEKSDVYSFGIVLWAIFA-KKEPYENvI 233
Cdd:cd05053   179 LA----------------RDIHHIDyyRKTTNGRLPVkwMAPEALFD--RVYTHQSDVWSFGVLLWEIFTlGGSPYPG-I 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333886239 234 CTEQFVICIKSGNRpnvEEILEYCPREIISLMERCWQAIPEDRPTFLGIEEE 285
Cdd:cd05053   240 PVEELFKLLKEGHR---MEKPQNCTQELYMLMRDCWHEVPSQRPTFKQLVED 288
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
23-285 2.98e-30

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, 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. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros 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: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 120.21  E-value: 2.98e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKV-------SLCYHRSHGFVILKKVYTGPNRAEYNEvLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYM 95
Cdd:cd05044     3 LGSGAFGEVfegtakdILGDGSGETKVAVKTLRKGATDQEKAE-FLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILELM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  96 EKGNLMHVLK-----TQIDVPLSLKG--RIIVEAIEGMCYLHDKGVIHKDLKPENILV-DRDFH---IKIADLGVAsfkt 164
Cdd:cd05044    82 EGGDLLSYLRaarptAFTPPLLTLKDllSICVDVAKGCVYLEDMHFVHRDLAARNCLVsSKDYRervVKIGDFGLA---- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 165 wsKLTKEKDNKQKEvssttkknnGGTLY---YMAPEHLNDinAKPTEKSDVYSFGIVLWAIFAK-KEPY--ENVICTEQF 238
Cdd:cd05044   158 --RDIYKNDYYRKE---------GEGLLpvrWMAPESLVD--GVFTTQSDVWAFGVLMWEILTLgQQPYpaRNNLEVLHF 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1333886239 239 ViciKSGNR---PnveeilEYCPREIISLMERCWQAIPEDRPTFLGIEEE 285
Cdd:cd05044   225 V---RAGGRldqP------DNCPDDLYELMLRCWSTDPEERPSFARILEQ 265
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
25-282 3.32e-30

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 119.50  E-value: 3.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSLCYHRSHGFVILKKVYTGP-NRAEynevLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHV 103
Cdd:cd14155     3 SGFFSEVYKVRHRTSGQVMALKMNTLSsNRAN----MLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNLEQL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 104 LKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRD---FHIKIADLGVAsfktwSKLTKEKDNKQK-EV 179
Cdd:cd14155    79 LDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDengYTAVVGDFGLA-----EKIPDYSDGKEKlAV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 180 SsttkknngGTLYYMAPEHLNDinAKPTEKSDVYSFGIVLWAIFAKKEPYENVIC-TEQFVIciksgNRPNVEEILEYCP 258
Cdd:cd14155   154 V--------GSPYWMAPEVLRG--EPYNEKADVFSYGIILCEIIARIQADPDYLPrTEDFGL-----DYDAFQHMVGDCP 218
                         250       260
                  ....*....|....*....|....
gi 1333886239 259 REIISLMERCWQAIPEDRPTFLGI 282
Cdd:cd14155   219 PDFLQLAFNCCNMDPKSRPSFHDI 242
Pkinase pfam00069
Protein kinase domain;
25-279 8.18e-30

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 117.34  E-value: 8.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSLCYHR-SHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHV 103
Cdd:pfam00069   9 SGSFGTVYKAKHRdTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYVEGGSLFDL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 104 LKTQIDVPLSLKGRI---IVEAIEgmcylhdkgvihkdlkpenilvdrdfhikiadlgvasfktwskltkekdnkqkevS 180
Cdd:pfam00069  89 LSEKGAFSEREAKFImkqILEGLE-------------------------------------------------------S 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 181 STTKKNNGGTLYYMAPEHLNDinaKP-TEKSDVYSFGIVLWAIFAKKEPYENVICTEQFVICIKSGNRPNveEILEYCPR 259
Cdd:pfam00069 114 GSSLTTFVGTPWYMAPEVLGG---NPyGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFP--ELPSNLSE 188
                         250       260
                  ....*....|....*....|
gi 1333886239 260 EIISLMERCWQAIPEDRPTF 279
Cdd:pfam00069 189 EAKDLLKKLLKKDPSKRLTA 208
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
23-219 8.87e-30

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: 119.01  E-value: 8.87e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHG-FVILKKVyTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLM 101
Cdd:cd14046    14 LGKGAFGQVVKVRNKLDGrYYAIKKI-KLRSESKNNSRILREVMLLSRLNHQHVVRYYQAWIERANLYIQMEYCEKSTLR 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 HVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfkTWSKLTKEKDNkqKEVSS 181
Cdd:cd14046    93 DLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLA---TSNKLNVELAT--QDINK 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1333886239 182 TTKKNNG---------GTLYYMAPEHLNDINAKPTEKSDVYSFGIVL 219
Cdd:cd14046   168 STSAALGssgdltgnvGTALYVAPEVQSGTKSTYNEKVDMYSLGIIF 214
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
23-291 1.07e-29

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


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 118.76  E-value: 1.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFV-ILKKVYTGPNRAEYNevLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLM 101
Cdd:cd14154     1 LGKGFFGQAIKVTHRETGEVmVMKELIRFDEEAQRN--FLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTLK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 HVLKTQIDV-PLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASF----KTWSKLTKEKDNKQ 176
Cdd:cd14154    79 DVLKDMARPlPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLiveeRLPSGNMSPSETLR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 177 KEVSSTTKKNNG--GTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPYENVIC-TEQFVIciksgnrpNVEEI 253
Cdd:cd14154   159 HLKSPDRKKRYTvvGNPYWMAPEMLN--GRSYDEKVDIFSFGIVLCEIIGRVEADPDYLPrTKDFGL--------NVDSF 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1333886239 254 LEY----CPREIISLMERCWQAIPEDRPTFLGIEEEFRPFYL 291
Cdd:cd14154   229 REKfcagCPPPFFKLAFLCCDLDPEKRPPFETLEEWLEALYL 270
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
16-230 1.09e-29

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: 118.28  E-value: 1.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  16 DLLEKtdLDSGGFGKVSLCYHRSHGFV-ILKKV-YTGPNRAEYNEVLlEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVME 93
Cdd:cd08529     3 EILNK--LGKGSFGVVYKVVRKVDGRVyALKQIdISRMSRKMREEAI-DEARVLSKLNSPYVIKYYDSFVDKGKLNIVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  94 YMEKGNLMHVLKTQIDVPLSLKG--RIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwsKLTKE 171
Cdd:cd08529    80 YAENGDLHSLIKSQRGRPLPEDQiwKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVA------KILSD 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 172 KDNKQKEVSsttkknngGTLYYMAPEHLNDinaKP-TEKSDVYSFGIVLWAIFAKKEPYE 230
Cdd:cd08529   154 TTNFAQTIV--------GTPYYLSPELCED---KPyNEKSDVWALGCVLYELCTGKHPFE 202
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
26-278 1.16e-29

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: 118.10  E-value: 1.16e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVslcYH----RSHGFVILKKV-YTGPNRAEYNEVLlEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNL 100
Cdd:cd06627    11 GAFGSV---YKglnlNTGEFVAIKQIsLEKIPKSDLKSVM-GEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYVENGSL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 MHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwsklTKEKDNKQKEVS 180
Cdd:cd06627    87 ASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVA--------TKLNEVEKDENS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 181 STtkknngGTLYYMAPEhlnDINAKP-TEKSDVYSFGIVLWAIFAKKEPYENVICTeQFVICIKSGNRPnveEILEYCPR 259
Cdd:cd06627   159 VV------GTPYWMAPE---VIEMSGvTTASDIWSVGCTVIELLTGNPPYYDLQPM-AALFRIVQDDHP---PLPENISP 225
                         250
                  ....*....|....*....
gi 1333886239 260 EIISLMERCWQAIPEDRPT 278
Cdd:cd06627   226 ELRDFLLQCFQKDPTLRPS 244
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
58-280 1.20e-29

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron 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: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 118.35  E-value: 1.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  58 EVLLEEGKMMHRLRHSRVVKLLGIII-EEGNYSLVMEYMEKGNLMHVLKTQIDVPlSLKGRII--VEAIEGMCYLHDKGV 134
Cdd:cd05058    41 EQFLKEGIIMKDFSHPNVLSLLGICLpSEGSPLVVLPYMKHGDLRNFIRSETHNP-TVKDLIGfgLQVAKGMEYLASKKF 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 135 IHKDLKPENILVDRDFHIKIADLGVAsfktwskltkeKDNKQKEVSSTTKKNNGG-TLYYMAPEHLNdiNAKPTEKSDVY 213
Cdd:cd05058   120 VHRDLAARNCMLDESFTVKVADFGLA-----------RDIYDKEYYSVHNHTGAKlPVKWMALESLQ--TQKFTTKSDVW 186
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333886239 214 SFGIVLWAIFAK-KEPYENViCTEQFVICIKSGNR---PnveeilEYCPREIISLMERCWQAIPEDRPTFL 280
Cdd:cd05058   187 SFGVLLWELMTRgAPPYPDV-DSFDITVYLLQGRRllqP------EYCPDPLYEVMLSCWHPKPEMRPTFS 250
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
21-290 1.79e-29

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


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 117.37  E-value: 1.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  21 TDLDSGGFGKVSLCYH---RSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIiEEGNYSLVMEYMEK 97
Cdd:cd05116     1 GELGSGNFGTVKKGYYqmkKVVKTVAVKILKNEANDPALKDELLREANVMQQLDNPYIVRMIGIC-EAESWMLVMEMAEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  98 GNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVasfktwSKLTKEKDNKQK 177
Cdd:cd05116    80 GPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGL------SKALRADENYYK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 178 evsstTKKNNGGTLYYMAPEHLNDInaKPTEKSDVYSFGIVLWAIFA-KKEPYENVICTEQFVIcIKSGNRpnvEEILEY 256
Cdd:cd05116   154 -----AQTHGKWPVKWYAPECMNYY--KFSSKSDVWSFGVLMWEAFSyGQKPYKGMKGNEVTQM-IEKGER---MECPAG 222
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1333886239 257 CPREIISLMERCWQAIPEDRPTFLGIEEEFRPFY 290
Cdd:cd05116   223 CPPEMYDLMKLCWTYDVDERPGFAAVELRLRNYY 256
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
23-278 2.28e-29

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: 116.95  E-value: 2.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHG-FVILKKVYTGPNRAEYNevlLEEGKMMHRLR----HSRVVKLLGII--IEEGNYSLVMEYM 95
Cdd:cd05118     7 IGEGAFGTVWLARDKVTGeKVAIKKIKNDFRHPKAA---LREIKLLKHLNdvegHPNIVKLLDVFehRGGNHLCLVFELM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  96 EKgNLMHVLKT-QIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVD-RDFHIKIADLGVASFktwskltkekd 173
Cdd:cd05118    84 GM-NLYELIKDyPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINlELGQLKLADFGLARS----------- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 174 nkqkeVSSTTKKNNGGTLYYMAPEHLndINAKP-TEKSDVYSFGIVLWAIFakkepyenvicTEQFVICIKSgnrpNVEE 252
Cdd:cd05118   152 -----FTSPPYTPYVATRWYRAPEVL--LGAKPyGSSIDIWSLGCILAELL-----------TGRPLFPGDS----EVDQ 209
                         250       260       270
                  ....*....|....*....|....*....|
gi 1333886239 253 ILEYC----PREIISLMERCWQAIPEDRPT 278
Cdd:cd05118   210 LAKIVrllgTPEALDLLSKMLKYDPAKRIT 239
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
22-290 2.48e-29

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 117.07  E-value: 2.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  22 DLDSGGFGKVSLCYHRSHGF----VILKKVYTGPNRAEYNEvLLEEGKMMHRLRHSRVVKLLGIIIEEGnYSLVMEYMEK 97
Cdd:cd05060     2 ELGHGNFGSVRKGVYLMKSGkeveVAVKTLKQEHEKAGKKE-FLREASVMAQLDHPCIVRLIGVCKGEP-LMLVMELAPL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  98 GNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVasfktwSKLTKEKDNKQK 177
Cdd:cd05060    80 GPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGM------SRALGAGSDYYR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 178 evsSTTkknnGGT--LYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKE-PYENvICTEQFVICIKSGNRPNVEEIl 254
Cdd:cd05060   154 ---ATT----AGRwpLKWYAPECIN--YGKFSSKSDVWSYGVTLWEAFSYGAkPYGE-MKGPEVIAMLESGERLPRPEE- 222
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1333886239 255 eyCPREIISLMERCWQAIPEDRPTFLGIEEEFRPFY 290
Cdd:cd05060   223 --CPQEIYSIMLSCWKYRPEDRPTFSELESTFRRDP 256
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
58-287 2.84e-29

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 117.00  E-value: 2.84e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  58 EVLLEEGKMMHRLRHSRVVKLLGIIIEE-GNYSLVMEYMEKGNLMHVLKTqidvplslKGRIIV----------EAIEGM 126
Cdd:cd05082    44 QAFLAEASVMTQLRHSNLVQLLGVIVEEkGGLYIVTEYMAKGSLVDYLRS--------RGRSVLggdcllkfslDVCEAM 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 127 CYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasfktwskLTKEkdnkqkevSSTTKKNNGGTLYYMAPEHLNDinAKP 206
Cdd:cd05082   116 EYLEGNNFVHRDLAARNVLVSEDNVAKVSDFG---------LTKE--------ASSTQDTGKLPVKWTAPEALRE--KKF 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 207 TEKSDVYSFGIVLWAIFA-KKEPYENvICTEQFVICIKSGNRPNVEeilEYCPREIISLMERCWQAIPEDRPTFLGIEEE 285
Cdd:cd05082   177 STKSDVWSFGILLWEIYSfGRVPYPR-IPLKDVVPRVEKGYKMDAP---DGCPPAVYDVMKNCWHLDAAMRPSFLQLREQ 252

                  ..
gi 1333886239 286 FR 287
Cdd:cd05082   253 LE 254
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
62-284 3.81e-29

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: 116.94  E-value: 3.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  62 EEGKMMHRLRHSRVVKLLGIIIEEgnYSLVMEYMEKGNLMHVLK--TQIDVPLS--LKGRIIVEAIEGMCYLHDKGVIHK 137
Cdd:cd14000    59 QELTVLSHLHHPSIVYLLGIGIHP--LMLVLELAPLGSLDHLLQqdSRSFASLGrtLQQRIALQVADGLRYLHSAMIIYR 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 138 DLKPENILV-----DRDFHIKIADLGVAsfktwskltkekdnkqKEVSSTTKKNNGGTLYYMAPEhLNDINAKPTEKSDV 212
Cdd:cd14000   137 DLKSHNVLVwtlypNSAIIIKIADYGIS----------------RQCCRMGAKGSEGTPGFRAPE-IARGNVIYNEKVDV 199
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333886239 213 YSFGIVLWAIFAKKEPYENvicTEQFVICIK--SGNRPNVEEILEYCPREIISLMERCWQAIPEDRPTFLGIEE 284
Cdd:cd14000   200 FSFGMLLYEILSGGAPMVG---HLKFPNEFDihGGLRPPLKQYECAPWPEVEVLMKKCWKENPQQRPTAVTVVS 270
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
23-282 4.32e-29

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: 117.59  E-value: 4.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKV--SLCYHRSHGFVILK---KVYTGPNRAEYNEVLLEEGKMMHRL-RHSRVVKLLGIIIEEGNYSLVMEYME 96
Cdd:cd05055    43 LGAGAFGKVveATAYGLSKSDAVMKvavKMLKPTAHSSEREALMSELKIMSHLgNHENIVNLLGACTIGGPILVITEYCC 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  97 KGNLMHVLKTQIDVPLSLKGRI--IVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltKEKDN 174
Cdd:cd05055   123 YGDLLNFLRRKRESFLTLEDLLsfSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLA---------RDIMN 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 175 KQKEVSsttKKNNGGTLYYMAPEHLndINAKPTEKSDVYSFGIVLWAIFA-KKEPYENVICTEQFVICIKSGNR---Pnv 250
Cdd:cd05055   194 DSNYVV---KGNARLPVKWMAPESI--FNCVYTFESDVWSYGILLWEIFSlGSNPYPGMPVDSKFYKLIKEGYRmaqP-- 266
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1333886239 251 eeilEYCPREIISLMERCWQAIPEDRPTFLGI 282
Cdd:cd05055   267 ----EHAPAEIYDIMKTCWDADPLKRPTFKQI 294
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
23-278 4.47e-29

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: 116.62  E-value: 4.47e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHR--SHGFVIlKKVYTGpNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNL 100
Cdd:cd13996    14 LGSGGFGSVYKVRNKvdGVTYAI-KKIRLT-EKSSASEKVLREVKALAKLNHPNIVRYYTAWVEEPPLYIQMELCEGGTL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 MHVL-------KTQIDVPLSLKGRIIveaiEGMCYLHDKGVIHKDLKPENILVD-RDFHIKIADLGVASFKTWSKLTKEK 172
Cdd:cd13996    92 RDWIdrrnsssKNDRKLALELFKQIL----KGVSYIHSKGIVHRDLKPSNIFLDnDDLQVKIGDFGLATSIGNQKRELNN 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 173 DNKQKEVSSTTKKNNGGTLYYMAPEHLNDINAkpTEKSDVYSFGIVLWAIFAkkePYENVICTEQFVICIKSGNRPnvEE 252
Cdd:cd13996   168 LNNNNNGNTSNNSVGIGTPLYASPEQLDGENY--NEKADIYSLGIILFEMLH---PFKTAMERSTILTDLRNGILP--ES 240
                         250       260
                  ....*....|....*....|....*.
gi 1333886239 253 ILEYCPREiISLMERCWQAIPEDRPT 278
Cdd:cd13996   241 FKAKHPKE-ADLIQSLLSKNPEERPS 265
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
23-282 7.03e-29

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: 115.65  E-value: 7.03e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEV--LLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNL 100
Cdd:cd14007     8 LGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSGLEhqLRREIEIQSHLRHPNILRLYGYFEDKKRIYLILEYAPNGEL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 MHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasfktWSklTKEKDNKQKEVS 180
Cdd:cd14007    88 YKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFG------WS--VHAPSNRRKTFC 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 181 sttkknngGTLYYMAPEHlndINAKP-TEKSDVYSFGIVLWAIFAKKEPYENVicTEQFVI-CIKSGNRpnveEILEYCP 258
Cdd:cd14007   160 --------GTLDYLPPEM---VEGKEyDYKVDIWSLGVLCYELLVGKPPFESK--SHQETYkRIQNVDI----KFPSSVS 222
                         250       260
                  ....*....|....*....|....
gi 1333886239 259 REIISLMERCWQAIPEDRPTFLGI 282
Cdd:cd14007   223 PEAKDLISKLLQKDPSKRLSLEQV 246
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
25-279 9.87e-29

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: 115.50  E-value: 9.87e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSlcYHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEgNYSLVMEYMEKGNL---M 101
Cdd:cd14150    10 TGSFGTVF--RGKWHGDVAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGFMTRP-NFAIITQWCEGSSLyrhL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 HVLKTQIDVPLSLKgrIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKT-WSkltkekDNKQKEVS 180
Cdd:cd14150    87 HVTETRFDTMQLID--VARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTrWS------GSQQVEQP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 181 SttkknngGTLYYMAPEHLNDINAKP-TEKSDVYSFGIVLWAIFAKKEPYENVICTEQFVICIKSGN-RPNVEEILEYCP 258
Cdd:cd14150   159 S-------GSILWMAPEVIRMQDTNPySFQSDVYAYGVVLYELMSGTLPYSNINNRDQIIFMVGRGYlSPDLSKLSSNCP 231
                         250       260
                  ....*....|....*....|.
gi 1333886239 259 REIISLMERCWQAIPEDRPTF 279
Cdd:cd14150   232 KAMKRLLIDCLKFKREERPLF 252
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
16-287 1.39e-28

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 115.64  E-value: 1.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  16 DLLEKTDLDSGGFGKVSL--CYHRSHG---FVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSL 90
Cdd:cd05049     6 TIVLKRELGEGAFGKVFLgeCYNLEPEqdkMLVAVKTLKDASSPDARKDFEREAELLTNLQHENIVKFYGVCTEGDPLLM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  91 VMEYMEKGNLMHVLKTQIDVPLSLKG--------------RIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIAD 156
Cdd:cd05049    86 VFEYMEHGDLNKFLRSHGPDAAFLASedsapgeltlsqllHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLVVKIGD 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 157 LGVAsfktwskltkekdnkqKEVSSTTKKNNGGT----LYYMAPEHLndINAKPTEKSDVYSFGIVLWAIFA-KKEPYEN 231
Cdd:cd05049   166 FGMS----------------RDIYSTDYYRVGGHtmlpIRWMPPESI--LYRKFTTESDVWSFGVVLWEIFTyGKQPWFQ 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 232 VICTEqfVI-CIKSG---NRPnveeilEYCPREIISLMERCWQAIPEDRPTFLGIEEEFR 287
Cdd:cd05049   228 LSNTE--VIeCITQGrllQRP------RTCPSEVYAVMLGCWKREPQQRLNIKDIHKRLQ 279
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
15-280 4.28e-28

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: 113.80  E-value: 4.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  15 SDLLEKTDLDSGGFGKVSLCYHRSHGFVILKKVYTGpnrAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEY 94
Cdd:cd05114     4 SELTFMKELGSGLFGVVRLGKWRAQYKVAIKAIREG---AMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKGNLMHVLKTQI-----DVPLSLkgriIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTwsklt 169
Cdd:cd05114    81 MENGCLLNYLRQRRgklsrDMLLSM----CQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVL----- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 170 kekdnKQKEVSSTTKKNnggTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAK-KEPYENViCTEQFVICIKSGNR- 247
Cdd:cd05114   152 -----DDQYTSSSGAKF---PVKWSPPEVFN--YSKFSSKSDVWSFGVLMWEVFTEgKMPFESK-SNYEVVEMVSRGHRl 220
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1333886239 248 --PNVeeileyCPREIISLMERCWQAIPEDRPTFL 280
Cdd:cd05114   221 yrPKL------ASKSVYEVMYSCWHEKPEGRPTFA 249
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
60-278 4.74e-28

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: 113.61  E-value: 4.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  60 LLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQID---VPLSLKGRIIVEAIEGMCYLHDKGVIH 136
Cdd:cd06610    46 LRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPLLSGGSLLDIMKSSYPrggLDEAIIATVLKEVLKGLEYLHSNGQIH 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 137 KDLKPENILVDRDFHIKIADLGVASFktwskLTKEKDNKQKevsstTKKNNGGTLYYMAPEHLNDINAKpTEKSDVYSFG 216
Cdd:cd06610   126 RDVKAGNILLGEDGSVKIADFGVSAS-----LATGGDRTRK-----VRKTFVGTPCWMAPEVMEQVRGY-DFKADIWSFG 194
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333886239 217 IVLWAIFAKKEPYENVICTEQFVICIKSgNRPNVEEILEYCP-----REIISLmerCWQAIPEDRPT 278
Cdd:cd06610   195 ITAIELATGAAPYSKYPPMKVLMLTLQN-DPPSLETGADYKKysksfRKMISL---CLQKDPSKRPT 257
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
26-220 5.81e-28

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: 113.07  E-value: 5.81e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGF-VILKKV-YTGPNRaeynEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHV 103
Cdd:cd06614    11 GASGEVYKATDRATGKeVAIKKMrLRKQNK----ELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMDGGSLTDI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 104 LkTQIDVPL--SLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwSKLTKEKDNKQKEVss 181
Cdd:cd06614    87 I-TQNPVRMneSQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFA-----AQLTKEKSKRNSVV-- 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1333886239 182 ttkknngGTLYYMAPEHlndINAKP-TEKSDVYSFGIVLW 220
Cdd:cd06614   159 -------GTPYWMAPEV---IKRKDyGPKVDIWSLGIMCI 188
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
26-278 6.71e-28

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: 113.25  E-value: 6.71e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGFVI-LKKVYTGPNRAEYN--------EVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYME 96
Cdd:cd06629    12 GTYGRVYLAMNATTGEMLaVKQVELPKTSSDRAdsrqktvvDALKSEIDTLKDLDHPNIVQYLGFEETEDYFSIFLEYVP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  97 KGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVasfktwsklTKEKDNKQ 176
Cdd:cd06629    92 GGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGI---------SKKSDDIY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 177 KEVSSTTKKnngGTLYYMAPEHLNDINAKPTEKSDVYSFGIVLWAIFAKKEPYENvicTEQFVICIKSGN---RPNVEEI 253
Cdd:cd06629   163 GNNGATSMQ---GSVFWMAPEVIHSQGQGYSAKVDIWSLGCVVLEMLAGRRPWSD---DEAIAAMFKLGNkrsAPPVPED 236
                         250       260
                  ....*....|....*....|....*
gi 1333886239 254 LEYCPrEIISLMERCWQAIPEDRPT 278
Cdd:cd06629   237 VNLSP-EALDFLNACFAIDPRDRPT 260
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
26-284 1.75e-27

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: 111.45  E-value: 1.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHG----------FVILKKvytgpNRAEYnevLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYM 95
Cdd:cd05123     4 GSFGKVLLVRKKDTGklyamkvlrkKEIIKR-----KEVEH---TLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  96 EKGNLMHVLKTQIDVPLslkGRI------IVEAIEgmcYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwsklt 169
Cdd:cd05123    76 PGGELFSHLSKEGRFPE---ERArfyaaeIVLALE---YLHSLGIIYRDLKPENILLDSDGHIKLTDFGLA--------- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 170 kekdnkqKEVSSTTKKNNG--GTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPY--ENVICTEQFVICIKsg 245
Cdd:cd05123   141 -------KELSSDGDRTYTfcGTPEYLAPEVLL--GKGYGKAVDWWSLGVLLYEMLTGKPPFyaENRKEIYEKILKSP-- 209
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1333886239 246 nrpnvEEILEYCPREIISLMERCWQAIPEDRPTFLGIEE 284
Cdd:cd05123   210 -----LKFPEYVSPEAKSLISGLLQKDPTKRLGSGGAEE 243
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
26-286 1.87e-27

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: 111.62  E-value: 1.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGfVILKKVYTGPNR--AEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHV 103
Cdd:cd14148     5 GGFGKVYKGLWRGEE-VAVKAARQDPDEdiAVTAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGALNRA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 104 LKTQiDVPLSLKGRIIVEAIEGMCYLHDKG---VIHKDLKPENILV-----DRDFH---IKIADLGVAsfKTWSKltkek 172
Cdd:cd14148    84 LAGK-KVPPHVLVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILIlepieNDDLSgktLKITDFGLA--REWHK----- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 173 dnkqkevssTTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPYENVictEQFVICIKSGNRPNVEE 252
Cdd:cd14148   156 ---------TTKMSAAGTYAWMAPEVIR--LSLFSKSSDVWSFGVLLWELLTGEVPYREI---DALAVAYGVAMNKLTLP 221
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1333886239 253 ILEYCPREIISLMERCWQAIPEDRPTFLGIEEEF 286
Cdd:cd14148   222 IPSTCPEPFARLLEECWDPDPHGRPDFGSILKRL 255
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
54-286 2.21e-27

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


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 111.56  E-value: 2.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  54 AEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQ-IDVPLSLKGRIIVEAIEGMCYLHDK 132
Cdd:cd05084    35 PDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDFLTFLRTEgPRLKVKELIRMVENAAAGMEYLESK 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 133 GVIHKDLKPENILVDRDFHIKIADLGVASfktwskltKEKDNkqkeVSSTTKKNNGGTLYYMAPEHLNdiNAKPTEKSDV 212
Cdd:cd05084   115 HCIHRDLAARNCLVTEKNVLKISDFGMSR--------EEEDG----VYAATGGMKQIPVKWTAPEALN--YGRYSSESDV 180
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333886239 213 YSFGIVLWAIFAK-KEPYENvICTEQFVICIKSGNRpnvEEILEYCPREIISLMERCWQAIPEDRPTFLGIEEEF 286
Cdd:cd05084   181 WSFGILLWETFSLgAVPYAN-LSNQQTREAVEQGVR---LPCPENCPDEVYRLMEQCWEYDPRKRPSFSTVHQDL 251
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
22-286 3.14e-27

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: 111.94  E-value: 3.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  22 DLDSGGFGKVSLCYHRSHG-----FVILKKVYTGpNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYS--LVMEY 94
Cdd:cd05079    11 DLGEGHFGKVELCRYDPEGdntgeQVAVKSLKPE-SGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGikLIMEF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKGNLMHVL-KTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasfktwskLTKE-K 172
Cdd:cd05079    90 LPSGSLKEYLpRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFG---------LTKAiE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 173 DNKQkevSSTTKKNNGGTLYYMAPEHLndINAKPTEKSDVYSFGIVLW-------------AIFAKK-EPYENVICTEQF 238
Cdd:cd05079   161 TDKE---YYTVKDDLDSPVFWYAPECL--IQSKFYIASDVWSFGVTLYelltycdsesspmTLFLKMiGPTHGQMTVTRL 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333886239 239 VICIKSGNR----PNveeileyCPREIISLMERCWQAIPEDRPTFLGIEEEF 286
Cdd:cd05079   236 VRVLEEGKRlprpPN-------CPEEVYQLMRKCWEFQPSKRTTFQNLIEGF 280
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
23-286 3.30e-27

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 111.74  E-value: 3.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGF-----VILKKVYTGPNRAEYNEvLLEEGKMMHRLRHSRVVKLLGIIIEEgNYSLVMEYMEK 97
Cdd:cd05057    15 LGSGAFGTVYKGVWIPEGEkvkipVAIKVLREETGPKANEE-ILDEAYVMASVDHPHLVRLLGICLSS-QVQLITQLMPL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  98 GNLMHVLKTQIDvplSLKGRII----VEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasfktwskLTKEKD 173
Cdd:cd05057    93 GCLLDYVRNHRD---NIGSQLLlnwcVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFG---------LAKLLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 174 NKQKEVSSTtkknnGGT--LYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFA-KKEPYENVICTEQFVICIKsGNRPNV 250
Cdd:cd05057   161 VDEKEYHAE-----GGKvpIKWMALESIQ--YRIYTHKSDVWSYGVTVWELMTfGAKPYEGIPAVEIPDLLEK-GERLPQ 232
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1333886239 251 EEIleyCPREIISLMERCWQAIPEDRPTFLGIEEEF 286
Cdd:cd05057   233 PPI---CTIDVYMVLVKCWMIDAESRPTFKELANEF 265
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
60-286 5.17e-27

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


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 110.48  E-value: 5.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  60 LLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQIDvPLSLKG--RIIVEAIEGMCYLHDKGVIHK 137
Cdd:cd05085    40 FLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGGDFLSFLRKKKD-ELKTKQlvKFSLDAAAGMAYLESKNCIHR 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 138 DLKPENILVDRDFHIKIADLGvasfktwskLTKEKDNKQKEVSSTTKKnnggTLYYMAPEHLNdiNAKPTEKSDVYSFGI 217
Cdd:cd05085   119 DLAARNCLVGENNALKISDFG---------MSRQEDDGVYSSSGLKQI----PIKWTAPEALN--YGRYSSESDVWSFGI 183
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 218 VLWAIFAKKE-PYENvICTEQFVICIKSGNRPNVEEileYCPREIISLMERCWQAIPEDRPTFLGIEEEF 286
Cdd:cd05085   184 LLWETFSLGVcPYPG-MTNQQAREQVEKGYRMSAPQ---RCPEDIYKIMQRCWDYNPENRPKFSELQKEL 249
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
23-229 6.39e-27

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: 110.77  E-value: 6.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFV----ILKKVYtgpnraeynevLLEEGKM---------MHRLRHSRVVKLLGIIIEEGNYS 89
Cdd:cd05581     9 LGEGSYSTVVLAKEKETGKEyaikVLDKRH-----------IIKEKKVkyvtiekevLSRLAHPGIVKLYYTFQDESKLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  90 LVMEYMEKGNLMHVLKT--QIDVPLSlkgRI----IVEAIEgmcYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFK 163
Cdd:cd05581    78 FVLEYAPNGDLLEYIRKygSLDEKCT---RFytaeIVLALE---YLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKVL 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 164 TWSKLTKEKDNKQKEVSSTTKKNNG---GTLYYMAPEHLNDinaKPTEK-SDVYSFGIVLWAIFAKKEPY 229
Cdd:cd05581   152 GPDSSPESTKGDADSQIAYNQARAAsfvGTAEYVSPELLNE---KPAGKsSDLWALGCIIYQMLTGKPPF 218
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
44-279 6.55e-27

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 110.54  E-value: 6.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  44 LKKVYTGPNRAEYnevlLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQidvplslKGRIIVEAI 123
Cdd:cd05033    40 LKSGYSDKQRLDF----LTEASIMGQFDHPNVIRLEGVVTKSRPVMIVTEYMENGSLDKFLREN-------DGKFTVTQL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 124 --------EGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasfktwskLTKEKDNKQKEVssTTKknnGG--TLYY 193
Cdd:cd05033   109 vgmlrgiaSGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFG---------LSRRLEDSEATY--TTK---GGkiPIRW 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 194 MAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKE-PYENVicTEQFVI-CIKSGNR-PNVEEileyCPREIISLMERCWQ 270
Cdd:cd05033   175 TAPEAIA--YRKFTSASDVWSFGIVMWEVMSYGErPYWDM--SNQDVIkAVEDGYRlPPPMD----CPSALYQLMLDCWQ 246

                  ....*....
gi 1333886239 271 AIPEDRPTF 279
Cdd:cd05033   247 KDRNERPTF 255
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
26-282 6.67e-27

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: 110.52  E-value: 6.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGfVILKKVYTGPNR--AEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHV 103
Cdd:cd14145    17 GGFGKVYRAIWIGDE-VAVKAARHDPDEdiSQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFARGGPLNRV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 104 LKTQiDVPLSLKGRIIVEAIEGMCYLHDKG---VIHKDLKPENILV-----DRDFH---IKIADLGVAsfKTWSKltkek 172
Cdd:cd14145    96 LSGK-RIPPDILVNWAVQIARGMNYLHCEAivpVIHRDLKSSNILIlekveNGDLSnkiLKITDFGLA--REWHR----- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 173 dnkqkevssTTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPYENVictEQFVICIKSGNRPNVEE 252
Cdd:cd14145   168 ---------TTKMSAAGTYAWMAPEVIR--SSMFSKGSDVWSYGVLLWELLTGEVPFRGI---DGLAVAYGVAMNKLSLP 233
                         250       260       270
                  ....*....|....*....|....*....|
gi 1333886239 253 ILEYCPREIISLMERCWQAIPEDRPTFLGI 282
Cdd:cd14145   234 IPSTCPEPFARLMEDCWNPDPHSRPPFTNI 263
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
25-284 6.74e-27

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: 110.38  E-value: 6.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSLCYHRSHG--F---VILKKVYTGPNRaeyNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGN 99
Cdd:cd05579     3 RGAYGRVYLAKKKSTGdlYaikVIKKRDMIRKNQ---VDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 100 LMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFkTWSKLTKEKDNKQKEV 179
Cdd:cd05579    80 LYSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKV-GLVRRQIKLSIQKKSN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 180 SSTTKKNNG--GTLYYMAPEHLNDINAKPTekSDVYSFGIVLwaifakkepYEnvicteqFVICIKSGNRPNVEEILE-- 255
Cdd:cd05579   159 GAPEKEDRRivGTPDYLAPEILLGQGHGKT--VDWWSLGVIL---------YE-------FLVGIPPFHAETPEEIFQni 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1333886239 256 ----YCPREIISLMERCWQAI-------PEDRPTFLGIEE 284
Cdd:cd05579   221 lngkIEWPEDPEVSDEAKDLIsklltpdPEKRLGAKGIEE 260
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
25-280 6.81e-27

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: 110.82  E-value: 6.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSLCYHRSHgFVILKKVYTGPNRAEYNEVLLEEGKMmhrLRHSRVVKLLG--IIIEEGN--YSLVMEYMEKGNL 100
Cdd:cd14056     5 KGRYGEVWLGKYRGE-KVAVKIFSSRDEDSWFRETEIYQTVM---LRHENILGFIAadIKSTGSWtqLWLITEYHEHGSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 MHVL-KTQIDVPLSLkgRIIVEAIEGMCYLH-------DKGVI-HKDLKPENILVDRDFHIKIADLGVA-SFKTWSKLTK 170
Cdd:cd14056    81 YDYLqRNTLDTEEAL--RLAYSAASGLAHLHteivgtqGKPAIaHRDLKSKNILVKRDGTCCIADLGLAvRYDSDTNTID 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 171 EKDNKQKevssttkknngGTLYYMAPEHLND-INAKPTE---KSDVYSFGIVLWAIFAKKEpyENVICTE---------- 236
Cdd:cd14056   159 IPPNPRV-----------GTKRYMAPEVLDDsINPKSFEsfkMADIYSFGLVLWEIARRCE--IGGIAEEyqlpyfgmvp 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333886239 237 --------QFVICIKsGNRPNVEEILEYCP--REIISLMERCWQAIPEDRPTFL 280
Cdd:cd14056   226 sdpsfeemRKVVCVE-KLRPPIPNRWKSDPvlRSMVKLMQECWSENPHARLTAL 278
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
23-230 7.50e-27

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: 110.28  E-value: 7.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVyTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMH 102
Cdd:cd14664     1 IGRGGAGTVYKGVMPNGTLVAVKRL-KGEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGSLGE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLKTQIDVPLSL----KGRIIVEAIEGMCYLHDK---GVIHKDLKPENILVDRDFHIKIADLGVASFktwskltkeKDNK 175
Cdd:cd14664    80 LLHSRPESQPPLdwetRQRIALGSARGLAYLHHDcspLIIHRDVKSNNILLDEEFEAHVADFGLAKL---------MDDK 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1333886239 176 QKEVSSTTKknngGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPYE 230
Cdd:cd14664   151 DSHVMSSVA----GSYGYIAPEYAY--TGKVSEKSDVYSYGVVLLELITGKRPFD 199
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
17-292 9.03e-27

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 110.04  E-value: 9.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  17 LLEKTDLDSGGFGKVSLCYH--RSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIiEEGNYSLVMEY 94
Cdd:cd05115     6 LIDEVELGSGNFGCVKKGVYkmRKKQIDVAIKVLKQGNEKAVRDEMMREAQIMHQLDNPYIVRMIGVC-EAEALMLVMEM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKGNLMHVLKTQID-VPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVasfktwSKLTKEKD 173
Cdd:cd05115    85 ASGGPLNKFLSGKKDeITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGL------SKALGADD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 174 NKQKevsstTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFA-KKEPYENVICTEqFVICIKSGNRpnvEE 252
Cdd:cd05115   159 SYYK-----ARSAGKWPLKWYAPECIN--FRKFSSRSDVWSYGVTMWEAFSyGQKPYKKMKGPE-VMSFIEQGKR---MD 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1333886239 253 ILEYCPREIISLMERCWQAIPEDRPTFLGIEEEFRPFYLS 292
Cdd:cd05115   228 CPAECPPEMYALMSDCWIYKWEDRPNFLTVEQRMRTYYYS 267
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
58-279 9.68e-27

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: 109.24  E-value: 9.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  58 EVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYsLVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEA--IEGMCYLHDKGVI 135
Cdd:cd14203    35 EAFLEEAQIMKKLRHDKLVQLYAVVSEEPIY-IVTEFMSKGSLLDFLKDGEGKYLKLPQLVDMAAqiASGMAYIERMNYI 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 136 HKDLKPENILVDRDFHIKIADLGVASFKtwskltkeKDNKQkevssTTKKNNGGTLYYMAPEHLndINAKPTEKSDVYSF 215
Cdd:cd14203   114 HRDLRAANILVGDNLVCKIADFGLARLI--------EDNEY-----TARQGAKFPIKWTAPEAA--LYGRFTIKSDVWSF 178
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333886239 216 GIVLWAIFAK-KEPYENVICTEQFVICIKSGNRPNVEEileyCPREIISLMERCWQAIPEDRPTF 279
Cdd:cd14203   179 GILLTELVTKgRVPYPGMNNREVLEQVERGYRMPCPPG----CPESLHELMCQCWRKDPEERPTF 239
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
25-282 1.95e-26

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


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 108.77  E-value: 1.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSLCYHRshGFVILKKVYTGPNRAEYNEV--LLEEGKMMHRLRHSRVVKLLGIIIEE-GNYSLVMEYMEKGNL- 100
Cdd:cd14064     3 SGSFGKVYKGRCR--NKIVAIKRYRANTYCSKSDVdmFCREVSILCRLNHPCVIQFVGACLDDpSQFAIVTQYVSGGSLf 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 --MHVLKTQIDvpLSLKGRIIVEAIEGMCYLHD--KGVIHKDLKPENILVDRDFHIKIADLGVASFKTwsklTKEKDNKQ 176
Cdd:cd14064    81 slLHEQKRVID--LQSKLIIAVDVAKGMEYLHNltQPIIHRDLNSHNILLYEDGHAVVADFGESRFLQ----SLDEDNMT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 177 KEvssttkknnGGTLYYMAPEHLNDiNAKPTEKSDVYSFGIVLWAIFAKKEPYENVICTEQFVICIKSGNRPNVEEILey 256
Cdd:cd14064   155 KQ---------PGNLRWMAPEVFTQ-CTRYSIKADVFSYALCLWELLTGEIPFAHLKPAAAAADMAYHHIRPPIGYSI-- 222
                         250       260
                  ....*....|....*....|....*.
gi 1333886239 257 cPREIISLMERCWQAIPEDRPTFLGI 282
Cdd:cd14064   223 -PKPISSLLMRGWNAEPESRPSFVEI 247
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
67-287 2.45e-26

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-2D is allso called Retinal Guanylyl Cyclase 1 (RETGC-1) or Rod Outer Segment membrane Guanylate Cyclase (ROS-GC). It is found in the photoreceptors of the retina where it anchors the reciprocal feedback loop between calcium and cGMP, which regulates the dark, light, and recovery phases in phototransduction. It is also found in other sensory neurons and may be a universal transduction component that plays a role in the perception of all senses. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-2D subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 108.65  E-value: 2.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  67 MHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQiDVPLS--LKGRIIVEAIEGMCYLHDKGVIHKDLKPENI 144
Cdd:cd14043    50 LRELRHENVNLFLGLFVDCGILAIVSEHCSRGSLEDLLRND-DMKLDwmFKSSLLLDLIKGMRYLHHRGIVHGRLKSRNC 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 145 LVDRDFHIKIADLGVASFKTWSKLTKEKDNKQKevssttkknnggtLYYMAPEHLNDINA--KPTEKSDVYSFGIVLWAI 222
Cdd:cd14043   129 VVDGRFVLKITDYGYNEILEAQNLPLPEPAPEE-------------LLWTAPELLRDPRLerRGTFPGDVFSFAIIMQEV 195
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333886239 223 FAKKEPYENVICTEQFVI---------CiksgnRPNVEeiLEYCPREIISLMERCWQAIPEDRPTFLGIEEEFR 287
Cdd:cd14043   196 IVRGAPYCMLGLSPEEIIekvrsppplC-----RPSVS--MDQAPLECIQLMKQCWSEAPERRPTFDQIFDQFK 262
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
23-248 2.99e-26

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: 108.19  E-value: 2.99e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHR-SHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLM 101
Cdd:cd14069     9 LGEGAFGEVFLAVNRnTEEAVAVKFVDMKRAPGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEYASGGELF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 HVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAS-FKtwskltkekdNKQKEVS 180
Cdd:cd14069    89 DKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATvFR----------YKGKERL 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333886239 181 STTKKnngGTLYYMAPEhlndINAKPT---EKSDVYSFGIVLWAIFAKK----EPYENVICTEQFVICIKSGNRP 248
Cdd:cd14069   159 LNKMC---GTLPYVAPE----LLAKKKyraEPVDVWSCGIVLFAMLAGElpwdQPSDSCQEYSDWKENKKTYLTP 226
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
60-296 3.13e-26

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR 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: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 108.90  E-value: 3.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  60 LLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKT--------QIDVPLSLKGRIIV--EAIEGMCYL 129
Cdd:cd05061    56 FLNEASVMKGFTCHHVVRLLGVVSKGQPTLVVMELMAHGDLKSYLRSlrpeaennPGRPPPTLQEMIQMaaEIADGMAYL 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 130 HDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnkqKEVSSTTKKNNGGT----LYYMAPEHLNDinAK 205
Cdd:cd05061   136 NAKKFVHRDLAARNCMVAHDFTVKIGDFGMT----------------RDIYETDYYRKGGKgllpVRWMAPESLKD--GV 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 206 PTEKSDVYSFGIVLWAIFAKKE-PYENvICTEQFVICIKSG---NRPnveeilEYCPREIISLMERCWQAIPEDRPTFLG 281
Cdd:cd05061   198 FTTSSDMWSFGVVLWEITSLAEqPYQG-LSNEQVLKFVMDGgylDQP------DNCPERVTDLMRMCWQFNPKMRPTFLE 270
                         250
                  ....*....|....*
gi 1333886239 282 IEEEFRPFYLSHFEE 296
Cdd:cd05061   271 IVNLLKDDLHPSFPE 285
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
23-278 3.14e-26

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: 108.26  E-value: 3.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHG-FVILKKVYTGPNRAEYNEV---LLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKG 98
Cdd:cd06632     8 LGSGSFGSVYEGFNGDTGdFFAVKEVSLVDDDKKSRESvkqLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVPGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  99 NLMHVLKT--QIDVPL-SLKGRIIveaIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnK 175
Cdd:cd06632    88 SIHKLLQRygAFEEPViRLYTRQI---LSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMA--------------K 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 176 QKEVSSTTKKNNgGTLYYMAPEHLNDINAKPTEKSDVYSFGIVLWAIFAKKEPYENVictEQFVICIKSGNRPNVEEILE 255
Cdd:cd06632   151 HVEAFSFAKSFK-GSPYWMAPEVIMQKNSGYGLAVDIWSLGCTVLEMATGKPPWSQY---EGVAAIFKIGNSGELPPIPD 226
                         250       260
                  ....*....|....*....|...
gi 1333886239 256 YCPREIISLMERCWQAIPEDRPT 278
Cdd:cd06632   227 HLSPDAKDFIRLCLQRDPEDRPT 249
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
26-282 3.78e-26

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: 108.19  E-value: 3.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHgFVILKKVYTGPNR--AEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHV 103
Cdd:cd14147    14 GGFGKVYRGSWRGE-LVAVKAARQDPDEdiSVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAGGPLSRA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 104 LKTQiDVPLSLKGRIIVEAIEGMCYLHDKG---VIHKDLKPENILVD--------RDFHIKIADLGVAsfKTWSKltkek 172
Cdd:cd14147    93 LAGR-RVPPHVLVNWAVQIARGMHYLHCEAlvpVIHRDLKSNNILLLqpienddmEHKTLKITDFGLA--REWHK----- 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 173 dnkqkevssTTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPYENVICTE-QFVICIKSGNRPnve 251
Cdd:cd14147   165 ---------TTQMSAAGTYAWMAPEVIK--ASTFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAvAYGVAVNKLTLP--- 230
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1333886239 252 eILEYCPREIISLMERCWQAIPEDRPTFLGI 282
Cdd:cd14147   231 -IPSTCPEPFAQLMADCWAQDPHRRPDFASI 260
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
23-278 3.95e-26

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: 107.83  E-value: 3.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGF-VILKKVYTGPNRAEY-NEV--LLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKG 98
Cdd:cd06625     8 LGQGAFGQVYLCYDADTGReLAVKQVEIDPINTEAsKEVkaLECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  99 NLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwSKLtkekdnkQKE 178
Cdd:cd06625    88 SVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGAS-----KRL-------QTI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 179 VSSTTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPYENVictEQFVICIKSGNRPNVEEILEYCP 258
Cdd:cd06625   156 CSSTGMKSVTGTPYWMSPEVIN--GEGYGRKADIWSVGCTVVEMLTTKPPWAEF---EPMAAIFKIATQPTNPQLPPHVS 230
                         250       260
                  ....*....|....*....|
gi 1333886239 259 REIISLMERCWQAIPEDRPT 278
Cdd:cd06625   231 EDARDFLSLIFVRNKKQRPS 250
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
23-291 4.29e-26

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 108.11  E-value: 4.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRaEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMH 102
Cdd:cd14222     1 LGKGFFGQAIKVTHKATGKVMVMKELIRCDE-ETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVasfktwSKLTKEKDNKQKEVSST 182
Cdd:cd14222    80 FLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGL------SRLIVEEKKKPPPDKPT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 183 TKK-----NNG-------GTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAkkEPYENVIC---TEQFVICIksgnR 247
Cdd:cd14222   154 TKKrtlrkNDRkkrytvvGNPYWMAPEMLN--GKSYDEKVDIFSFGIVLCEIIG--QVYADPDClprTLDFGLNV----R 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1333886239 248 PNVEEIL-EYCPREIISLMERCWQAIPEDRPTFLGIEEEFRPFYL 291
Cdd:cd14222   226 LFWEKFVpKDCPPAFFPLAAICCRLEPDSRPAFSKLEDSFEALSL 270
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
15-219 4.49e-26

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: 108.68  E-value: 4.49e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  15 SDLLEKTDLDSGGFGKVSLCYHRSHGFVILKK-VYTGPNRAEYNEVLLEEGkMMHRLRHSRVVKLLGIII-EEGNYSLVM 92
Cdd:cd06620     5 QDLETLKDLGAGNGGSVSKVLHIPTGTIMAKKvIHIDAKSSVRKQILRELQ-ILHECHSPYIVSFYGAFLnENNNIIICM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  93 EYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDK-GVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltke 171
Cdd:cd06620    84 EYMDCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKGQIKLCDFGVS----------- 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1333886239 172 kdnkqKEVSSTTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVL 219
Cdd:cd06620   153 -----GELINSIADTFVGTSTYMSPERIQ--GGKYSVKSDVWSLGLSI 193
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
25-278 4.51e-26

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: 107.78  E-value: 4.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSLCYHRSH--GFVILKKVYTGP----NRAEYNEVLLEEGKMMHRLRHSRVVKLLGIII-EEGNYSLVMEYMEK 97
Cdd:cd13994     3 KGATSVVRIVTKKNPrsGVLYAVKEYRRRddesKRKDYVKRLTSEYIISSKLHHPNIVKVLDLCQdLHGKWCLVMEYCPG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  98 GNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkEKDNKQK 177
Cdd:cd13994    83 GDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTA----------EVFGMPA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 178 EVSSTTKKNNGGTLYYMAPEHLNDI--NAKPtekSDVYSFGIVLWAIFAKKEPYE-NVICTEQFVICIKSGNRPNV--EE 252
Cdd:cd13994   153 EKESPMSAGLCGSEPYMAPEVFTSGsyDGRA---VDVWSCGIVLFALFTGRFPWRsAKKSDSAYKAYEKSGDFTNGpyEP 229
                         250       260
                  ....*....|....*....|....*.
gi 1333886239 253 ILEYCPREIISLMERCWQAIPEDRPT 278
Cdd:cd13994   230 IENLLPSECRRLIYRMLHPDPEKRIT 255
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
22-287 4.87e-26

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 108.45  E-value: 4.87e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  22 DLDSGGFGKVSL-CYHRSH---GFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYS--LVMEYM 95
Cdd:cd05080    11 DLGEGHFGKVSLyCYDPTNdgtGEMVAVKALKADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQGGKSlqLIMEYV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  96 EKGNLMHVL-KTQIDVPLSLkgrIIVEAI-EGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkeKD 173
Cdd:cd05080    91 PLGSLRDYLpKHSIGLAQLL---LFAQQIcEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLA-----------KA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 174 NKQKEVSSTTKKNNGGTLYYMAPEHLNDinAKPTEKSDVYSFGIVLWAIFAKKEPYENVICTEQFVICIKSG--NRPNVE 251
Cdd:cd05080   157 VPEGHEYYRVREDGDSPVFWYAPECLKE--YKFYYASDVWSFGVTLYELLTHCDSSQSPPTKFLEMIGIAQGqmTVVRLI 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1333886239 252 EILEY---------CPREIISLMERCWQAIPEDRPTFLGIEEEFR 287
Cdd:cd05080   235 ELLERgerlpcpdkCPQEVYHLMKNCWETEASFRPTFENLIPILK 279
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
16-276 9.65e-26

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 107.36  E-value: 9.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  16 DLLEKTDLDSGGFGKVSL--CYH----RSHGFVILKKVYTGPNRAEYNevLLEEGKMMHRLRHSRVVKLLGIIIEEGNYS 89
Cdd:cd05092     6 DIVLKWELGEGAFGKVFLaeCHNllpeQDKMLVAVKALKEATESARQD--FQREAELLTVLQHQHIVRFYGVCTEGEPLI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  90 LVMEYMEKGNL----------MHVLKTQIDVPLSLKG-----RIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKI 154
Cdd:cd05092    84 MVFEYMRHGDLnrflrshgpdAKILDGGEGQAPGQLTlgqmlQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 155 ADLGVAsfktwskltkekdnkqKEVSSTTKKNNGG----TLYYMAPEHLndINAKPTEKSDVYSFGIVLWAIFA-KKEPY 229
Cdd:cd05092   164 GDFGMS----------------RDIYSTDYYRVGGrtmlPIRWMPPESI--LYRKFTTESDIWSFGVVLWEIFTyGKQPW 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1333886239 230 ENVICTEQfVICIKSG---NRPNVeeileyCPREIISLMERCWQAIPEDR 276
Cdd:cd05092   226 YQLSNTEA-IECITQGrelERPRT------CPPEVYAIMQGCWQREPQQR 268
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
16-278 1.36e-25

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: 106.20  E-value: 1.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  16 DLLEKtdLDSGGFGKVSLCYHRSHGFVI-LKKVYTGPNraeyNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEY 94
Cdd:cd06612     6 DILEK--LGEGSYGSVYKAIHKETGQVVaIKVVPVEED----LQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKGNLMHVLK-TQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwskltkekd 173
Cdd:cd06612    80 CGAGSVSDIMKiTNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSG------------ 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 174 nkqkEVSSTTKKNNG--GTLYYMAPEHLNDINAKptEKSDVYSFGIVLWAIFAKKEPYENVICTEQ-FVIciksGNRP-- 248
Cdd:cd06612   148 ----QLTDTMAKRNTviGTPFWMAPEVIQEIGYN--NKADIWSLGITAIEMAEGKPPYSDIHPMRAiFMI----PNKPpp 217
                         250       260       270
                  ....*....|....*....|....*....|
gi 1333886239 249 NVEEILEYCPrEIISLMERCWQAIPEDRPT 278
Cdd:cd06612   218 TLSDPEKWSP-EFNDFVKKCLVKDPEERPS 246
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
15-286 1.47e-25

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


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 106.35  E-value: 1.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  15 SDLLEKTDLDSGGFGKVSLCYHRSHGFVILKKVYtgpnRAEYNEV--LLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVM 92
Cdd:cd05052     6 TDITMKHKLGGGQYGEVYEGVWKKYNLTVAVKTL----KEDTMEVeeFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIIT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  93 EYMEKGNLMHVLKT--QIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTWSKLTK 170
Cdd:cd05052    82 EFMPYGNLLDYLREcnREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 171 EKDNKQKevssttkknnggtLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFA-KKEPYENVICTEQFVIcIKSGNRpn 249
Cdd:cd05052   162 HAGAKFP-------------IKWTAPESLA--YNKFSIKSDVWAFGVLLWEIATyGMSPYPGIDLSQVYEL-LEKGYR-- 223
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1333886239 250 vEEILEYCPREIISLMERCWQAIPEDRPTFLGIEEEF 286
Cdd:cd05052   224 -MERPEGCPPKVYELMRACWQWNPSDRPSFAEIHQAL 259
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
15-279 1.51e-25

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 106.78  E-value: 1.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  15 SDLLEKTDLDSGGFGKVSLCYHR------SHGFVILKKVYTGPNraeyNEVLLE---EGKMMHRLRHSRVVKLLGIIIEE 85
Cdd:cd05046     5 SNLQEITTLGRGEFGEVFLAKAKgieeegGETLVLVKALQKTKD----ENLQSEfrrELDMFRKLSHKNVVRLLGLCREA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  86 GNYSLVMEYMEKGNLMHVL---KTQIDV----PLSLKGRIIV--EAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIAD 156
Cdd:cd05046    81 EPHYMILEYTDLGDLKQFLratKSKDEKlkppPLSTKQKVALctQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 157 LGvasfktwskLTKEKDNKQkevsSTTKKNNGGTLYYMAPEHLNDINAkpTEKSDVYSFGIVLWAIFAKKE-PYENViCT 235
Cdd:cd05046   161 LS---------LSKDVYNSE----YYKLRNALIPLRWLAPEAVQEDDF--STKSDVWSFGVLMWEVFTQGElPFYGL-SD 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1333886239 236 EQFVICIKSGNrpnVE-EILEYCPREIISLMERCWQAIPEDRPTF 279
Cdd:cd05046   225 EEVLNRLQAGK---LElPVPEGCPSRLYKLMTRCWAVNPKDRPSF 266
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
23-278 2.29e-25

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: 106.02  E-value: 2.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFV-----ILKKVYTGPNRAEynEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEK 97
Cdd:cd14098     8 LGSGTFAEVKKAVEVETGKMraikqIVKRKVAGNDKNL--QLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVMEYVEG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  98 GNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILV--DRDFHIKIADLGVAsfktwsKLTKekdnk 175
Cdd:cd14098    86 GDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILItqDDPVIVKISDFGLA------KVIH----- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 176 qkevSSTTKKNNGGTLYYMAPEHL--NDINAKP--TEKSDVYSFGIVLWAIFAK--------KEPYENVICTEQFviCIK 243
Cdd:cd14098   155 ----TGTFLVTFCGTMAYLAPEILmsKEQNLQGgySNLVDMWSVGCLVYVMLTGalpfdgssQLPVEKRIRKGRY--TQP 228
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1333886239 244 SGNRPNVEEileycprEIISLMERCWQAIPEDRPT 278
Cdd:cd14098   229 PLVDFNISE-------EAIDFILRLLDVDPEKRMT 256
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
571-650 2.34e-25

Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. Structural analysis of DD-DD complexes show that the domains interact with each other in many different ways. DD-containing proteins serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes. In mammals, they are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways. In invertebrates, they are involved in transcriptional regulation of zygotic patterning genes in insect embryogenesis, and are components of the ToII/NF-kappaB pathway, a conserved innate immune pathway in animal cells.


Pssm-ID: 260017 [Multi-domain]  Cd Length: 79  Bit Score: 99.66  E-value: 2.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 571 HLNPIRENLGRQWKNCARKLGFTESQIDEIDHDYeRDGLKEKVYQMLQKWLMREGtKGATVGKLAQALHQCCRIDLLNHL 650
Cdd:cd01670     1 YFDLVAEELGRDWKKLARKLGLSEGDIDQIEEDN-RDDLKEQAYQMLERWREREG-DEATLGRLIQALREIGRRDLAEKL 78
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
60-286 2.41e-25

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: 106.63  E-value: 2.41e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  60 LLEEGKMMHRL-RHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQ-----------IDVP---LSLKGRI--IVEA 122
Cdd:cd05098    65 LISEMEMMKMIgKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARrppgmeycynpSHNPeeqLSSKDLVscAYQV 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 123 IEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkeKDNKQKEVsstTKKNNGGTL--YYMAPEHLN 200
Cdd:cd05098   145 ARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLA-----------RDIHHIDY---YKKTTNGRLpvKWMAPEALF 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 201 DinAKPTEKSDVYSFGIVLWAIFA-KKEPYENVICTEQFVIcIKSGNRPNVEeilEYCPREIISLMERCWQAIPEDRPTF 279
Cdd:cd05098   211 D--RIYTHQSDVWSFGVLLWEIFTlGGSPYPGVPVEELFKL-LKEGHRMDKP---SNCTNELYMMMRDCWHAVPSQRPTF 284

                  ....*..
gi 1333886239 280 LGIEEEF 286
Cdd:cd05098   285 KQLVEDL 291
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
25-278 3.78e-25

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: 105.08  E-value: 3.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSLCYHRSHGFVI-LKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHV 103
Cdd:cd06626    10 EGTFGKVYTAVNLDTGELMaMKEIRFQDNDPKTIKEIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQEGTLEEL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 104 LKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwsklTKEKDNKQK----EV 179
Cdd:cd06626    90 LRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSA--------VKLKNNTTTmapgEV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 180 SSTTkknngGTLYYMAPEHLNdiNAKPTEK---SDVYSFGIVLWAIFAKKEPYENviCTEQFVICIK--SGNRPNVEEIL 254
Cdd:cd06626   162 NSLV-----GTPAYMAPEVIT--GNKGEGHgraADIWSLGCVVLEMATGKRPWSE--LDNEWAIMYHvgMGHKPPIPDSL 232
                         250       260
                  ....*....|....*....|....
gi 1333886239 255 EYCPrEIISLMERCWQAIPEDRPT 278
Cdd:cd06626   233 QLSP-EGKDFLSRCLESDPKKRPT 255
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
60-296 6.66e-25

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


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 105.87  E-value: 6.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  60 LLEEGKMMHRL-RHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQ--------------IDVPLSLKGRI--IVEA 122
Cdd:cd05101    76 LVSEMEMMKMIgKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARrppgmeysydinrvPEEQMTFKDLVscTYQL 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 123 IEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltKEKDNkqkeVSSTTKKNNGG-TLYYMAPEHLND 201
Cdd:cd05101   156 ARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLA---------RDINN----IDYYKKTTNGRlPVKWMAPEALFD 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 202 inAKPTEKSDVYSFGIVLWAIFA-KKEPYENVICTEQFVIcIKSGNRPNVEeilEYCPREIISLMERCWQAIPEDRPTFL 280
Cdd:cd05101   223 --RVYTHQSDVWSFGVLMWEIFTlGGSPYPGIPVEELFKL-LKEGHRMDKP---ANCTNELYMMMRDCWHAVPSQRPTFK 296
                         250
                  ....*....|....*..
gi 1333886239 281 GIEEEF-RPFYLSHFEE 296
Cdd:cd05101   297 QLVEDLdRILTLTTNEE 313
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
17-279 7.43e-25

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 105.06  E-value: 7.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  17 LLEKTDLDSGGFGKVSLC---------------YHRSHGFVILKKVYTGPNRAEYNEvLLEEGKMMHRLRHSRVVKLLGI 81
Cdd:cd05097     7 LRLKEKLGEGQFGEVHLCeaeglaeflgegapeFDGQPVLVAVKMLRADVTKTARND-FLKEIKIMSRLKNPNIIRLLGV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  82 IIEEGNYSLVMEYMEKGNLMHVL-KTQIDVPLSLKGRI-----------IVEAIEGMCYLHDKGVIHKDLKPENILVDRD 149
Cdd:cd05097    86 CVSDDPLCMITEYMENGDLNQFLsQREIESTFTHANNIpsvsianllymAVQIASGMKYLASLNFVHRDLATRNCLVGNH 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 150 FHIKIADLGVAsfktwskltkekdnkQKEVSSTTKKNNGGT---LYYMAPEHLndINAKPTEKSDVYSFGIVLWAIFA-- 224
Cdd:cd05097   166 YTIKIADFGMS---------------RNLYSGDYYRIQGRAvlpIRWMAWESI--LLGKFTTASDVWAFGVTLWEMFTlc 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1333886239 225 KKEPYeNVICTEQFVICIKSGNRPNVEEIL----EYCPREIISLMERCWQAIPEDRPTF 279
Cdd:cd05097   229 KEQPY-SLLSDEQVIENTGEFFRNQGRQIYlsqtPLCPSPVFKLMMRCWSRDIKDRPTF 286
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
16-311 1.01e-24

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: 104.43  E-value: 1.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  16 DLLEKTDLDSGGFGKVSLCYHRSHGFVI-LKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEY 94
Cdd:cd06617     2 DLEVIEELGRGAYGVVDKMRHVPTGTIMaVKRIRATVNSQEQKRLLMDLDISMRSVDCPYTVTFYGALFREGDVWICMEV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKgNL----MHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDK-GVIHKDLKPENILVDRDFHIKIADLGVASFKtwsklt 169
Cdd:cd06617    82 MDT-SLdkfyKKVYDKGLTIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCDFGISGYL------ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 170 kekdnkqkeVSSTTKKNNGGTLYYMAPEHLN-DINAKPTE-KSDVYSFGIVLWAIFAKKEPYENVICTEQFVICIKSGNR 247
Cdd:cd06617   155 ---------VDSVAKTIDAGCKPYMAPERINpELNQKGYDvKSDVWSLGITMIELATGRFPYDSWKTPFQQLKQVVEEPS 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333886239 248 PNVEEilEYCPREIISLMERCWQAIPEDRPTFLGIEEefRPFYLSHFEEYVeeDVASLKKEYPD 311
Cdd:cd06617   226 PQLPA--EKFSPEFQDFVNKCLKKNYKERPNYPELLQ--HPFFELHLSKNT--DVASFVSLILG 283
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
22-282 1.04e-24

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: 103.72  E-value: 1.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  22 DLDSGGFGKVSLCYH-RSHGFVILKKVyTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEeGNYS--------LVM 92
Cdd:cd13975     7 ELGRGQYGVVYACDSwGGHFPCALKSV-VPPDDKHWNDLALEFHYTRSLPKHERIVSLHGSVID-YSYGggssiavlLIM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  93 EYMEKGnlmhvLKTQIDVPLSLKGR--IIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfKTWSKLtk 170
Cdd:cd13975    85 ERLHRD-----LYTGIKAGLSLEERlqIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFC--KPEAMM-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 171 ekdnkqkevssttkknNG---GTLYYMAPEHLndiNAKPTEKSDVYSFGIVLWAIFAKK----EPYENVICTEQFVICIK 243
Cdd:cd13975   156 ----------------SGsivGTPIHMAPELF---SGKYDNSVDVYAFGILFWYLCAGHvklpEAFEQCASKDHLWNNVR 216
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1333886239 244 SGNRPnveEILEYCPREIISLMERCWQAIPEDRPtFLGI 282
Cdd:cd13975   217 KGVRP---ERLPVFDEECWNLMEACWSGDPSQRP-LLGI 251
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
18-224 1.47e-24

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: 104.10  E-value: 1.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  18 LEKtdLDSGGFGKVSLCYHRSHG-FVILKKVytgpnRAEYNEV-----LLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLV 91
Cdd:cd07829     4 LEK--LGEGTYGVVYKAKDKKTGeIVALKKI-----RLDNEEEgipstALREISLLKELKHPNIVKLLDVIHTENKLYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  92 MEYMEKgNLMHVLKT-QIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltk 170
Cdd:cd07829    77 FEYCDQ-DLKKYLDKrPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLA---------- 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1333886239 171 ekdnkqKEVSSTTKK--NNGGTLYYMAPEHLndinakptEKSDVYSFGIVLWA---IFA 224
Cdd:cd07829   146 ------RAFGIPLRTytHEVVTLWYRAPEIL--------LGSKHYSTAVDIWSvgcIFA 190
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
60-302 1.66e-24

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 105.10  E-value: 1.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  60 LLEEGKMMHRL-RHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQ-----------IDVP---LSLKGRI--IVEA 122
Cdd:cd05100    64 LVSEMEMMKMIgKHKNIINLLGACTQDGPLYVLVEYASKGNLREYLRARrppgmdysfdtCKLPeeqLTFKDLVscAYQV 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 123 IEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnkqKEVSSTT--KKNNGGTL--YYMAPEH 198
Cdd:cd05100   144 ARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLA----------------RDVHNIDyyKKTTNGRLpvKWMAPEA 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 199 LNDinAKPTEKSDVYSFGIVLWAIFA-KKEPYENVICTEQFVIcIKSGNRPNVEeilEYCPREIISLMERCWQAIPEDRP 277
Cdd:cd05100   208 LFD--RVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKL-LKEGHRMDKP---ANCTHELYMIMRECWHAVPSQRP 281
                         250       260
                  ....*....|....*....|....*.
gi 1333886239 278 TFLGIEEEF-RPFYLSHFEEYVEEDV 302
Cdd:cd05100   282 TFKQLVEDLdRVLTVTSTDEYLDLSV 307
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
18-285 1.92e-24

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: 104.11  E-value: 1.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  18 LEKTdLDSGGFGKVSlcyhRSHGF----------VILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIE-EG 86
Cdd:cd05054    11 LGKP-LGRGAFGKVI----QASAFgidksatcrtVAVKMLKEGATASEHKALMTELKILIHIGHHLNVVNLLGACTKpGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  87 NYSLVMEYMEKGNLMHVLKTQID--VPLSLKGRIIVEAIE------------------------GMCYLHDKGVIHKDLK 140
Cdd:cd05054    86 PLMVIVEFCKFGNLSNYLRSKREefVPYRDKGARDVEEEEdddelykepltledlicysfqvarGMEFLASRKCIHRDLA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 141 PENILVDRDFHIKIADLGVASfktwsKLTKEKDNKQKevssttkknnGGT---LYYMAPEHLNDinAKPTEKSDVYSFGI 217
Cdd:cd05054   166 ARNILLSENNVVKICDFGLAR-----DIYKDPDYVRK----------GDArlpLKWMAPESIFD--KVYTTQSDVWSFGV 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333886239 218 VLWAIFA-KKEPYENVICTEQFVICIKSGNRPNVEEileYCPREIISLMERCWQAIPEDRPTFLGIEEE 285
Cdd:cd05054   229 LLWEIFSlGASPYPGVQMDEEFCRRLKEGTRMRAPE---YTTPEIYQIMLDCWHGEPKERPTFSELVEK 294
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
22-282 1.92e-24

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 103.76  E-value: 1.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  22 DLDSGGFGKVSLCyhRSHGFV-----------ILKKVYTGPNRAEYNEvlleEGKMMHRLRHSRVVKLLGIIIEEGNYSL 90
Cdd:cd05050    12 DIGQGAFGRVFQA--RAPGLLpyepftmvavkMLKEEASADMQADFQR----EAALMAEFDHPNIVKLLGVCAVGKPMCL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  91 VMEYMEKGNLMHVLK--------------------TQIDVPLSLKGRIIVEA--IEGMCYLHDKGVIHKDLKPENILVDR 148
Cdd:cd05050    86 LFEYMAYGDLNEFLRhrspraqcslshstssarkcGLNPLPLSCTEQLCIAKqvAAGMAYLSERKFVHRDLATRNCLVGE 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 149 DFHIKIADLGVaSFKTWSKLTKEKDnkqkevssttkKNNGGTLYYMAPEHLndINAKPTEKSDVYSFGIVLWAIFA-KKE 227
Cdd:cd05050   166 NMVVKIADFGL-SRNIYSADYYKAS-----------ENDAIPIRWMPPESI--FYNRYTTESDVWAYGVVLWEIFSyGMQ 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1333886239 228 PYENvICTEQFVICIKSGNrpnVEEILEYCPREIISLMERCWQAIPEDRPTFLGI 282
Cdd:cd05050   232 PYYG-MAHEEVIYYVRDGN---VLSCPDNCPLELYNLMRLCWSKLPSDRPSFASI 282
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
10-287 2.67e-24

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


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 103.22  E-value: 2.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  10 IKMASSDLLEktDLDSGGFGKV---SLCYHRSHGFVI------LKKVYTGPNRAEYNEvlleEGKMMHRLRHSRVVKLLG 80
Cdd:cd05048     2 IPLSAVRFLE--ELGEGAFGKVykgELLGPSSEESAIsvaiktLKENASPKTQQDFRR----EAELMSDLQHPNIVCLLG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  81 IIIEEGNYSLVMEYMEKGNL-----MHVLKTQIDVPLSLKG-----------RIIVEAIEGMCYLHDKGVIHKDLKPENI 144
Cdd:cd05048    76 VCTKEQPQCMLFEYMAHGDLheflvRHSPHSDVGVSSDDDGtassldqsdflHIAIQIAAGMEYLSSHHYVHRDLAARNC 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 145 LVDRDFHIKIADLGVAsfktwskltkekdnkqKEV-SSTTKKNNGGTLY---YMAPEHLndINAKPTEKSDVYSFGIVLW 220
Cdd:cd05048   156 LVGDGLTVKISDFGLS----------------RDIySSDYYRVQSKSLLpvrWMPPEAI--LYGKFTTESDVWSFGVVLW 217
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333886239 221 AIFA-KKEPYENVicTEQFVIciksgNRPNVEEIL---EYCPREIISLMERCWQAIPEDRPTFLGIEEEFR 287
Cdd:cd05048   218 EIFSyGLQPYYGY--SNQEVI-----EMIRSRQLLpcpEDCPARVYSLMVECWHEIPSRRPRFKEIHTRLR 281
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
10-279 2.73e-24

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 102.89  E-value: 2.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  10 IKMASSDLLEKTDLDSGGFGKVSL-CYHRSHGFVILKKVYTGPNRAE--YNEVLLEEGKMMHRLRHSRVVKLLGIIIEEG 86
Cdd:cd05056     1 YEIQREDITLGRCIGEGQFGDVYQgVYMSPENEKIAVAVKTCKNCTSpsVREKFLQEAYIMRQFDHPHIVKLIGVITENP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  87 NYsLVMEYMEKGNLMHVLKTQIDvplSLKGRIIVEAIEGMC----YLHDKGVIHKDLKPENILVDRDFHIKIADLGvasf 162
Cdd:cd05056    81 VW-IVMELAPLGELRSYLQVNKY---SLDLASLILYAYQLStalaYLESKRFVHRDIAARNVLVSSPDCVKLGDFG---- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 163 ktwskLTKEKDNKQKEVSSTTKKnnggTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAK-KEPYENVicTEQFVIC 241
Cdd:cd05056   153 -----LSRYMEDESYYKASKGKL----PIKWMAPESIN--FRRFTSASDVWMFGVCMWEILMLgVKPFQGV--KNNDVIG 219
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1333886239 242 -IKSGNRPNVEEIleyCPREIISLMERCWQAIPEDRPTF 279
Cdd:cd05056   220 rIENGERLPMPPN---CPPTLYSLMTKCWAYDPSKRPRF 255
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
60-286 3.79e-24

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 102.04  E-value: 3.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  60 LLEEGKMMHRLRHSRVVKLLGIIIEEgNYSLVMEYMEKGNLMHVL-KTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKD 138
Cdd:cd05040    45 FLKEVNAMHSLDHPNLIRLYGVVLSS-PLMMVTELAPLGSLLDRLrKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRD 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 139 LKPENILVDRDFHIKIADLGVAsfktwSKLTKEKD----NKQKEVSsttkknnggtLYYMAPEHLNdiNAKPTEKSDVYS 214
Cdd:cd05040   124 LAARNILLASKDKVKIGDFGLM-----RALPQNEDhyvmQEHRKVP----------FAWCAPESLK--TRKFSHASDVWM 186
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333886239 215 FGIVLWAIFA-KKEPYenVICT-EQFVICI-KSGNR---PnveeilEYCPREIISLMERCWQAIPEDRPTFLGIEEEF 286
Cdd:cd05040   187 FGVTLWEMFTyGEEPW--LGLNgSQILEKIdKEGERlerP------DDCPQDIYNVMLQCWAHKPADRPTFVALRDFL 256
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
11-279 4.44e-24

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: 102.80  E-value: 4.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  11 KMASSDLLEKTDLDSGGFGKVSlcYHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEeGNYSL 90
Cdd:cd14149     8 EIEASEVMLSTRIGSGSFGTVY--KGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTK-DNLAI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  91 VMEYMEKGNL---MHVLKTQIDVPLSLKgrIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKT-WS 166
Cdd:cd14149    85 VTQWCEGSSLykhLHVQETKFQMFQLID--IARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrWS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 167 kltkekdnKQKEVSSTTkknngGTLYYMAPEHLNDINAKP-TEKSDVYSFGIVLWAIFAKKEPYENVICTEQFVICI-KS 244
Cdd:cd14149   163 --------GSQQVEQPT-----GSILWMAPEVIRMQDNNPfSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVgRG 229
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1333886239 245 GNRPNVEEILEYCPREIISLMERCWQAIPEDRPTF 279
Cdd:cd14149   230 YASPDLSKLYKNCPKAMKRLVADCIKKVKEERPLF 264
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
43-284 4.89e-24

Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 102.24  E-value: 4.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  43 ILKKVYTgpnraeYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQiDVPLSLKGRI--IV 120
Cdd:cd14045    38 IAKKSFT------LSKRIRKEVKQVRELDHPNLCKFIGGCIEVPNVAIITEYCPKGSLNDVLLNE-DIPLNWGFRFsfAT 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 121 EAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKtwskltkeKDNKQKEVSSTTKKnngGTLYYMAPEHLN 200
Cdd:cd14045   111 DIARGMAYLHQHKIYHGRLKSSNCVIDDRWVCKIADYGLTTYR--------KEDGSENASGYQQR---LMQVYLPPENHS 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 201 DINAKPTEKSDVYSFGIVLWAIFAKKEPyenvicTEQFVICIKSGNRPNVEEILEY-------CPREIISLMERCWQAIP 273
Cdd:cd14045   180 NTDTEPTQATDVYSYAIILLEIATRNDP------VPEDDYSLDEAWCPPLPELISGktenscpCPADYVELIRRCRKNNP 253
                         250
                  ....*....|.
gi 1333886239 274 EDRPTFLGIEE 284
Cdd:cd14045   254 AQRPTFEQIKK 264
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
23-279 6.56e-24

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: 102.06  E-value: 6.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSlcYHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEgNYSLVMEYMEKGNLMH 102
Cdd:cd14151    16 IGSGSFGTVY--KGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKP-QLAIVTQWCEGSSLYH 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLKTqIDVPLSLKGRIIV--EAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKT-WSkltkekdnkqkev 179
Cdd:cd14151    93 HLHI-IETKFEMIKLIDIarQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSrWS------------- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 180 SSTTKKNNGGTLYYMAPEHLNDINAKPTE-KSDVYSFGIVLWAIFAKKEPYENVICTEQFVICIKSGN-RPNVEEILEYC 257
Cdd:cd14151   159 GSHQFEQLSGSILWMAPEVIRMQDKNPYSfQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYlSPDLSKVRSNC 238
                         250       260
                  ....*....|....*....|..
gi 1333886239 258 PREIISLMERCWQAIPEDRPTF 279
Cdd:cd14151   239 PKAMKRLMAECLKKKRDERPLF 260
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
22-289 6.65e-24

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: 101.64  E-value: 6.65e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  22 DLDSGGFGKVSLCYhrSHGFVI---LKKVYTgpNRAEYNEVLLEEGKMMHRL-RHSRVVKLLG--IIIEEGN--YSLVME 93
Cdd:cd13985     7 QLGEGGFSYVYLAH--DVNTGRryaLKRMYF--NDEEQLRVAIKEIEIMKRLcGHPNIVQYYDsaILSSEGRkeVLLLME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  94 YMEkGNLMHVLKTQIDVPLSLKG--RIIVEAIEGMCYLHDKG--VIHKDLKPENILVDRDFHIKIADLGVASFKTWSKLT 169
Cdd:cd13985    83 YCP-GSLVDILEKSPPSPLSEEEvlRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGSATTEHYPLER 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 170 KEKDNKQKEvssTTKKNNggTLYYMAPEHLNDINAKP-TEKSDVYSFGIVLWAIFAKKEPYEnvictEQFVICIKSGNRP 248
Cdd:cd13985   162 AEEVNIIEE---EIQKNT--TPMYRAPEMIDLYSKKPiGEKADIWALGCLLYKLCFFKLPFD-----ESSKLAIVAGKYS 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1333886239 249 NVEEilEYCPREIISLMERCWQAIPEDRPTFLGIEEEFRPF 289
Cdd:cd13985   232 IPEQ--PRYSPELHDLIRHMLTPDPAERPDIFQVINIITKD 270
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
23-286 8.94e-24

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: 100.76  E-value: 8.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVI-LKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLM 101
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVaIKEISRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 HVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILV---DRDFHIKIADLGVA-SFKTWSkltkekdnkqk 177
Cdd:cd14009    81 QYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLstsGDDPVLKIADFGFArSLQPAS----------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 178 eVSSTTKknngGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPY--ENVIcteQFVICIKSGNRPNVEEILE 255
Cdd:cd14009   150 -MAETLC----GSPLYMAPEILQ--FQKYDAKADLWSVGAILFEMLVGKPPFrgSNHV---QLLRNIERSDAVIPFPIAA 219
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1333886239 256 YCPREIISLMERCWQAIPEDRPTFlgieEEF 286
Cdd:cd14009   220 QLSPDCKDLLRRLLRRDPAERISF----EEF 246
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
15-219 9.07e-24

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: 102.13  E-value: 9.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  15 SDLLEKTDLDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEY 94
Cdd:cd06615     1 DDFEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHLEIKPAIRNQIIRELKVLHECNSPYIVGFYGAFYSDGEISICMEH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDK-GVIHKDLKPENILVDRDFHIKIADLGVASfktwskltkekd 173
Cdd:cd06615    81 MDGGSLDQVLKKAGRIPENILGKISIAVLRGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSG------------ 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1333886239 174 nkqkEVSSTTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVL 219
Cdd:cd06615   149 ----QLIDSMANSFVGTRSYMSPERLQ--GTHYTVQSDIWSLGLSL 188
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
23-283 9.15e-24

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


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 101.89  E-value: 9.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHG-----FVILKKVYTgpNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEG--NYSLVMEYM 95
Cdd:cd05081    12 LGKGNFGSVELCRYDPLGdntgaLVAVKQLQH--SGPDQQRDFQREIQILKALHSDFIVKYRGVSYGPGrrSLRLVMEYL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  96 EKGNLMHVLKTQIDVplsLKGRIIV----EAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFktwskLTKE 171
Cdd:cd05081    90 PSGCLRDFLQRHRAR---LDASRLLlyssQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKL-----LPLD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 172 KDnkqkevSSTTKKNNGGTLYYMAPEHLNDinAKPTEKSDVYSFGIVLWAIFAkkepYENVICT--EQFVICIKSGN-RP 248
Cdd:cd05081   162 KD------YYVVREPGQSPIFWYAPESLSD--NIFSRQSDVWSFGVVLYELFT----YCDKSCSpsAEFLRMMGCERdVP 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1333886239 249 NVEEILEY------------CPREIISLMERCWQAIPEDRPTFLGIE 283
Cdd:cd05081   230 ALCRLLELleegqrlpappaCPAEVHELMKLCWAPSPQDRPSFSALG 276
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
17-278 9.24e-24

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: 101.73  E-value: 9.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  17 LLEKTDLDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEE--GNYSLVMEY 94
Cdd:cd06621     3 IVELSSLGEGAGGSVTKCRLRNTKTIFALKTITTDPNPDVQKQILRELEINKSCASPYIVKYYGAFLDEqdSSIGIAMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKGNLMHVLKTQidvpLSLKGRI-------IVEAI-EGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktws 166
Cdd:cd06621    83 CEGGSLDSIYKKV----KKKGGRIgekvlgkIAESVlKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSG----- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 167 kltkekdnkqkEVSSTTKKNNGGTLYYMAPEHlndINAKP-TEKSDVYSFGIVLWAIFAKKEPYE-----NVICTEQFVI 240
Cdd:cd06621   154 -----------ELVNSLAGTFTGTSYYMAPER---IQGGPySITSDVWSLGLTLLEVAQNRFPFPpegepPLGPIELLSY 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1333886239 241 CIksgNRPNVEeiLEYCP-------REIISLMERCWQAIPEDRPT 278
Cdd:cd06621   220 IV---NMPNPE--LKDEPengikwsESFKDFIEKCLEKDGTRRPG 259
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
58-297 9.37e-24

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: 101.69  E-value: 9.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  58 EVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYsLVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEA--IEGMCYLHDKGVI 135
Cdd:cd05071    49 EAFLQEAQVMKKLRHEKLVQLYAVVSEEPIY-IVTEYMSKGSLLDFLKGEMGKYLRLPQLVDMAAqiASGMAYVERMNYV 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 136 HKDLKPENILVDRDFHIKIADLGVASFKtwskltkeKDNKQkevssTTKKNNGGTLYYMAPEHLndINAKPTEKSDVYSF 215
Cdd:cd05071   128 HRDLRAANILVGENLVCKVADFGLARLI--------EDNEY-----TARQGAKFPIKWTAPEAA--LYGRFTIKSDVWSF 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 216 GIVLWAIFAK-KEPYENVICTEQFVICIKSGNRPNVEEileyCPREIISLMERCWQAIPEDRPTFLGIEEEFRPFYLSHF 294
Cdd:cd05071   193 GILLTELTTKgRVPYPGMVNREVLDQVERGYRMPCPPE----CPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTE 268

                  ...
gi 1333886239 295 EEY 297
Cdd:cd05071   269 PQY 271
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
26-283 1.90e-23

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: 100.34  E-value: 1.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGF-------VILKKvyTGPnRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKG 98
Cdd:cd14080    11 GSYSKVKLAEYTKSGLkekvackIIDKK--KAP-KDFLEKFLPRELEILRKLRHPNIIQVYSIFERGSKVFIFMEYAEHG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  99 NLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTwskltkekDNKQKE 178
Cdd:cd14080    88 DLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLCP--------DDDGDV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 179 VSSTTkknnGGTLYYMAPEHLNDINAKPTeKSDVYSFGIVLWAIFAKKEPYE--NVICTEQFVICIKSGNRPNVEEILEY 256
Cdd:cd14080   160 LSKTF----CGSAAYAAPEILQGIPYDPK-KYDIWSLGVILYIMLCGSMPFDdsNIKKMLKDQQNRKVRFPSSVKKLSPE 234
                         250       260
                  ....*....|....*....|....*..
gi 1333886239 257 CPREIISLMErcwqAIPEDRPTFLGIE 283
Cdd:cd14080   235 CKDLIDQLLE----PDPTKRATIEEIL 257
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
25-278 2.02e-23

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: 100.30  E-value: 2.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSLCYHRSHGFVI-LKKVYTGPNRAEYN-------EVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYME 96
Cdd:cd06628    10 SGSFGSVYLGMNASSGELMaVKQVELPSVSAENKdrkksmlDALQREIALLRELQHENIVQYLGSSSDANHLNIFLEYVP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  97 KGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnKQ 176
Cdd:cd06628    90 GGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGIS--------------KK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 177 KEVSSTTKKNNG------GTLYYMAPEHLNDINAkpTEKSDVYSFGIVLWAIFAKKEPYENviCTE-QFVICIKSGNRPn 249
Cdd:cd06628   156 LEANSLSTKNNGarpslqGSVFWMAPEVVKQTSY--TRKADIWSLGCLVVEMLTGTHPFPD--CTQmQAIFKIGENASP- 230
                         250       260
                  ....*....|....*....|....*....
gi 1333886239 250 veEILEYCPREIISLMERCWQAIPEDRPT 278
Cdd:cd06628   231 --TIPSNISSEARDFLEKTFEIDHNKRPT 257
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
23-297 2.02e-23

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: 100.53  E-value: 2.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEyneVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYsLVMEYMEKGNLMH 102
Cdd:cd05069    20 LGQGCFGEVWMGTWNGTTKVAIKTLKPGTMMPE---AFLQEAQIMKKLRHDKLVPLYAVVSEEPIY-IVTEFMGKGSLLD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLKTQIDVPLSLKGRIIVEA--IEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKtwskltkeKDNKQkevs 180
Cdd:cd05069    96 FLKEGDGKYLKLPQLVDMAAqiADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLI--------EDNEY---- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 181 sTTKKNNGGTLYYMAPEHLndINAKPTEKSDVYSFGIVLWAIFAK-KEPYENVICTEqfviCIKSGNRPNVEEILEYCPR 259
Cdd:cd05069   164 -TARQGAKFPIKWTAPEAA--LYGRFTIKSDVWSFGILLTELVTKgRVPYPGMVNRE----VLEQVERGYRMPCPQGCPE 236
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1333886239 260 EIISLMERCWQAIPEDRPTFLGIEEEFRPFYLSHFEEY 297
Cdd:cd05069   237 SLHELMKLCWKKDPDERPTFEYIQSFLEDYFTATEPQY 274
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
23-283 2.21e-23

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


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 100.03  E-value: 2.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRaEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMH 102
Cdd:cd14221     1 LGKGCFGQAIKVTHRETGEVMVMKELIRFDE-ETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLKT-QIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTWSKLTKEKDNKQKEVSS 181
Cdd:cd14221    80 IIKSmDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMVDEKTQPEGLRSLKKPDR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 182 TTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPYENVIC-TEQFVIciksgnrpNVEEILEY---- 256
Cdd:cd14221   160 KKRYTVVGNPYWMAPEMIN--GRSYDEKVDVFSFGIVLCEIIGRVNADPDYLPrTMDFGL--------NVRGFLDRycpp 229
                         250       260
                  ....*....|....*....|....*...
gi 1333886239 257 -CPREIISLMERCWQAIPEDRPTFLGIE 283
Cdd:cd14221   230 nCPPSFFPIAVLCCDLDPEKRPSFSKLE 257
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
18-286 2.57e-23

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 100.42  E-value: 2.57e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  18 LEKTdLDSGGFGKV------SLCYHRSHGFVILKKVYTGPNRAEYNEvLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLV 91
Cdd:cd05045     4 LGKT-LGEGEFGKVvkatafRLKGRAGYTTVAVKMLKENASSSELRD-LLSEFNLLKQVNHPHVIKLYGACSQDGPLLLI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  92 MEYMEKGNLMHVLKTQIDV----------------------PLSLKGRIIV--EAIEGMCYLHDKGVIHKDLKPENILVD 147
Cdd:cd05045    82 VEYAKYGSLRSFLRESRKVgpsylgsdgnrnssyldnpderALTMGDLISFawQISRGMQYLAEMKLVHRDLAARNVLVA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 148 RDFHIKIADLGVasfktwSKLTKEKDnkqkevsSTTKKNNGGT-LYYMAPEHLNDinAKPTEKSDVYSFGIVLWAIFA-K 225
Cdd:cd05045   162 EGRKMKISDFGL------SRDVYEED-------SYVKRSKGRIpVKWMAIESLFD--HIYTTQSDVWSFGVLLWEIVTlG 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333886239 226 KEPYENvICTEQFVICIKSGNRpnvEEILEYCPREIISLMERCWQAIPEDRPTFLGIEEEF 286
Cdd:cd05045   227 GNPYPG-IAPERLFNLLKTGYR---MERPENCSEEMYNLMLTCWKQEPDKRPTFADISKEL 283
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
22-284 2.87e-23

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: 99.38  E-value: 2.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  22 DLDSGGFGKVSLCYHRSHGF-VILKKVYtgpnraeyNEVLLE--------------EGKMMHRLR---HSRVVKLLGIII 83
Cdd:cd14004     7 EMGEGAYGQVNLAIYKSKGKeVVIKFIF--------KERILVdtwvrdrklgtvplEIHILDTLNkrsHPNIVKLLDFFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  84 EEGNYSLVMEymEKGNLMHV-----LKTQIDVPLSlkGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLG 158
Cdd:cd14004    79 DDEFYYLVME--KHGSGMDLfdfieRKPNMDEKEA--KYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 159 VAS------FKTWSkltkekdnkqkevssttkknngGTLYYMAPEHL--NDINAKPtekSDVYSFGIVLWAIFAKKEPYE 230
Cdd:cd14004   155 SAAyiksgpFDTFV----------------------GTIDYAAPEVLrgNPYGGKE---QDIWALGVLLYTLVFKENPFY 209
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333886239 231 nvicteqfviciksgnrpNVEEILE-------YCPREIISLMERCWQAIPEDRPTflgIEE 284
Cdd:cd14004   210 ------------------NIEEILEadlripyAVSEDLIDLISRMLNRDVGDRPT---IEE 249
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
27-278 3.15e-23

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


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 99.81  E-value: 3.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  27 GFGKVSLCYH----RSHGFVILKKV-YTGPNRAEYNEV---LLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKG 98
Cdd:cd06630     9 GTGAFSSCYQardvKTGTLMAVKQVsFCRNSSSEQEEVveaIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMAGG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  99 NLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRD-FHIKIADLGVASfKTWSKLTKEKDNKQK 177
Cdd:cd06630    89 SVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTgQRLRIADFGAAA-RLASKGTGAGEFQGQ 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 178 EVssttkknngGTLYYMAPEHLNDINAKptEKSDVYSFGIVLWAIFAKKEPYENVICTEQFVIC--IKSGNR-PNVEEIL 254
Cdd:cd06630   168 LL---------GTIAFMAPEVLRGEQYG--RSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIfkIASATTpPPIPEHL 236
                         250       260
                  ....*....|....*....|....
gi 1333886239 255 EYCPREIISlmeRCWQAIPEDRPT 278
Cdd:cd06630   237 SPGLRDVTL---RCLELQPEDRPP 257
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
23-278 3.38e-23

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: 99.55  E-value: 3.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKvslCYH--------RSHGFVILKKVYTGPNraeYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEY 94
Cdd:cd14099     9 LGKGGFAK---CYEvtdmstgkVYAGKVVPKSSLTKPK---QREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKGNLMHVLKTQidVPLSLK--GRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwSKLTKEK 172
Cdd:cd14099    83 CSNGSLMELLKRR--KALTEPevRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLA-----ARLEYDG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 173 DNkqkevssttKKNNGGTLYYMAPEHLNDINAKPTEkSDVYSFGIVLWAIFAKKEPYENvICTEQFVICIKSGNRPNVEE 252
Cdd:cd14099   156 ER---------KKTLCGTPNYIAPEVLEKKKGHSFE-VDIWSLGVILYTLLVGKPPFET-SDVKETYKRIKKNEYSFPSH 224
                         250       260
                  ....*....|....*....|....*.
gi 1333886239 253 ILeyCPREIISLMERCWQAIPEDRPT 278
Cdd:cd14099   225 LS--ISDEAKDLIRSMLQPDPTKRPS 248
PHA02988 PHA02988
hypothetical protein; Provisional
63-278 4.33e-23

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 99.82  E-value: 4.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  63 EGKMMHRLRHSRVVKLLGIIIEEGN----YSLVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDK-GVIHK 137
Cdd:PHA02988   68 EIKNLRRIDSNNILKIYGFIIDIVDdlprLSLILEYCTRGYLREVLDKEKDLSFKTKLDMAIDCCKGLYNLYKYtNKPYK 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 138 DLKPENILVDRDFHIKIadLGVASFKTWSkltkekdnkqkevSSTTKKNNggTLYYMAPEHLNDINAKPTEKSDVYSFGI 217
Cdd:PHA02988  148 NLTSVSFLVTENYKLKI--ICHGLEKILS-------------SPPFKNVN--FMVYFSYKMLNDIFSEYTIKDDIYSLGV 210
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333886239 218 VLWAIFAKKEPYENVICTEQFVICIKSgnrpNVEEILEY-CPREIISLMERCWQAIPEDRPT 278
Cdd:PHA02988  211 VLWEIFTGKIPFENLTTKEIYDLIINK----NNSLKLPLdCPLEIKCIVEACTSHDSIKRPN 268
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
23-279 4.95e-23

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


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 99.70  E-value: 4.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYH-----RSHGFVILKKVYTgpNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEG--NYSLVMEYM 95
Cdd:cd14205    12 LGKGNFGSVEMCRYdplqdNTGEVVAVKKLQH--STEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGrrNLRLIMEYL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  96 EKGNLMHVL---KTQIDVPLSLKgrIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFktwskLTKEK 172
Cdd:cd14205    90 PYGSLRDYLqkhKERIDHIKLLQ--YTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKV-----LPQDK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 173 DnkqkevSSTTKKNNGGTLYYMAPEHLNDinAKPTEKSDVYSFGIVLWAIFAkkepYENVICTEQFVICIKSGNRPNVEE 252
Cdd:cd14205   163 E------YYKVKEPGESPIFWYAPESLTE--SKFSVASDVWSFGVVLYELFT----YIEKSKSPPAEFMRMIGNDKQGQM 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1333886239 253 IL----------------EYCPREIISLMERCWQAIPEDRPTF 279
Cdd:cd14205   231 IVfhliellknngrlprpDGCPDEIYMIMTECWNNNVNQRPSF 273
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
26-231 6.39e-23

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: 98.52  E-value: 6.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGFVILKKVYT---GPNraEY-NEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLM 101
Cdd:cd14162    11 GSYAVVKKAYSTKHKCKVAIKIVSkkkAPE--DYlQKFLPREIEVIKGLKHPNLICFYEAIETTSRVYIIMELAENGDLL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 HVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwSKLTKEKDNKQKeVSS 181
Cdd:cd14162    89 DYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFA-----RGVMKTKDGKPK-LSE 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1333886239 182 TTkknnGGTLYYMAPEHLNDINAKPTeKSDVYSFGIVLWAIFAKKEPYEN 231
Cdd:cd14162   163 TY----CGSYAYASPEILRGIPYDPF-LSDIWSMGVVLYTMVYGRLPFDD 207
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
16-276 8.67e-23

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC 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: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 98.93  E-value: 8.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  16 DLLEKTDLDSGGFGKVSL--CYHRS---HGFVILKKVYTGPNRAEYNEvLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSL 90
Cdd:cd05094     6 DIVLKRELGEGAFGKVFLaeCYNLSptkDKMLVAVKTLKDPTLAARKD-FQREAELLTNLQHDHIVKFYGVCGDGDPLIM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  91 VMEYMEKGNLMHVLKTQ-------ID-VPLSLKGR--------IIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKI 154
Cdd:cd05094    85 VFEYMKHGDLNKFLRAHgpdamilVDgQPRQAKGElglsqmlhIATQIASGMVYLASQHFVHRDLATRNCLVGANLLVKI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 155 ADLGVAsfktwskltkekdnkqKEVSSTTKKNNGG----TLYYMAPEHLndINAKPTEKSDVYSFGIVLWAIFA-KKEPY 229
Cdd:cd05094   165 GDFGMS----------------RDVYSTDYYRVGGhtmlPIRWMPPESI--MYRKFTTESDVWSFGVILWEIFTyGKQPW 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1333886239 230 ENVICTEqFVICIKSG---NRPNVeeileyCPREIISLMERCWQAIPEDR 276
Cdd:cd05094   227 FQLSNTE-VIECITQGrvlERPRV------CPKEVYDIMLGCWQREPQQR 269
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
22-304 9.87e-23

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: 98.99  E-value: 9.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  22 DLDSGGFGKVSLCYHRSHGFVI-LKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMekGNL 100
Cdd:cd06618    22 EIGSGTCGQVYKMRHKKTGHVMaVKQMRRSGNKEENKRILMDLDVVLKSHDCPYIVKCYGYFITDSDVFICMELM--STC 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 MHVLKTQID--VPLSLKGRIIVEAIEGMCYLHDK-GVIHKDLKPENILVDRDFHIKIADLGVASFKtwskltkekdnkqk 177
Cdd:cd06618   100 LDKLLKRIQgpIPEDILGKMTVSIVKALHYLKEKhGVIHRDVKPSNILLDESGNVKLCDFGISGRL-------------- 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 178 eVSSTTKKNNGGTLYYMAPEHLnDINAKPTE--KSDVYSFGIVLWAIFAKKEPYENviCTEQF-VICIKSGNRPNVEEIL 254
Cdd:cd06618   166 -VDSKAKTRSAGCAAYMAPERI-DPPDNPKYdiRADVWSLGISLVELATGQFPYRN--CKTEFeVLTKILNEEPPSLPPN 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1333886239 255 EYCPREIISLMERCWQAIPEDRPTFLGIEEEfrPFYLSHfeEYVEEDVAS 304
Cdd:cd06618   242 EGFSPDFCSFVDLCLTKDHRYRPKYRELLQH--PFIRRY--ETAEVDVAS 287
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
88-289 1.13e-22

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: 98.66  E-value: 1.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  88 YSLVMEYMEKGNLMHVLKTQIdvpLSLKG--RIIVEAIEGMCYLHDKGVI---------HKDLKPENILVDRDFHIKIAD 156
Cdd:cd13998    68 LWLVTAFHPNGSL*DYLSLHT---IDWVSlcRLALSVARGLAHLHSEIPGctqgkpaiaHRDLKSKNILVKNDGTCCIAD 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 157 LGVASFKTWSKLTKEKDNkQKEVssttkknngGTLYYMAPEHLND-INAKPTE---KSDVYSFGIVLWAIFAK------- 225
Cdd:cd13998   145 FGLAVRLSPSTGEEDNAN-NGQV---------GTKRYMAPEVLEGaINLRDFEsfkRVDIYAMGLVLWEMASRctdlfgi 214
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333886239 226 ----KEPYENVI----CTEQF--VICIKSGnRPNVEEILEYCP--REIISLMERCWQAIPEDRPTFLGIEEEFRPF 289
Cdd:cd13998   215 veeyKPPFYSEVpnhpSFEDMqeVVVRDKQ-RPNIPNRWLSHPglQSLAETIEECWDHDAEARLTAQCIEERLSEF 289
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
8-279 1.35e-22

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: 98.22  E-value: 1.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239   8 DNIKMASSDLLEKTDLDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEyneVLLEEGKMMHRLRHSRVVKLLGIIIEEGN 87
Cdd:cd05070     2 DVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPE---SFLEEAQIMKKLKHDKLVQLYAVVSEEPI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  88 YsLVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEA--IEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKtw 165
Cdd:cd05070    79 Y-IVTEYMSKGSLLDFLKDGEGRALKLPNLVDMAAqvAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLI-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 166 skltkeKDNKQkevssTTKKNNGGTLYYMAPEHLndINAKPTEKSDVYSFGIVLWAIFAK-KEPYENVICTEQFVICIKS 244
Cdd:cd05070   156 ------EDNEY-----TARQGAKFPIKWTAPEAA--LYGRFTIKSDVWSFGILLTELVTKgRVPYPGMNNREVLEQVERG 222
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1333886239 245 GNRPNVEEileyCPREIISLMERCWQAIPEDRPTF 279
Cdd:cd05070   223 YRMPCPQD----CPISLHELMIHCWKKDPEERPTF 253
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
41-287 1.39e-22

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 98.16  E-value: 1.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  41 FVILKKVYTGPNRAEYNEvLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVL---KTQIDVPLS---- 113
Cdd:cd05090    36 LVAIKTLKDYNNPQQWNE-FQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFEFMNQGDLHEFLimrSPHSDVGCSsded 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 114 --LKG--------RIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnkqKEVSST- 182
Cdd:cd05090   115 gtVKSsldhgdflHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKISDLGLS----------------REIYSSd 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 183 ---TKKNNGGTLYYMAPEHLndINAKPTEKSDVYSFGIVLWAIFAKK-EPYENVICTEQFVICIKSGNRPNVEEileyCP 258
Cdd:cd05090   179 yyrVQNKSLLPIRWMPPEAI--MYGKFSSDSDIWSFGVVLWEIFSFGlQPYYGFSNQEVIEMVRKRQLLPCSED----CP 252
                         250       260
                  ....*....|....*....|....*....
gi 1333886239 259 REIISLMERCWQAIPEDRPTFLGIEEEFR 287
Cdd:cd05090   253 PRMYSLMTECWQEIPSRRPRFKDIHARLR 281
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
23-222 1.62e-22

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


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 98.34  E-value: 1.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYhRSHGFVILKKVY--TGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNL 100
Cdd:cd14158    23 LGEGGFGVVFKGY-INDKNVAVKKLAamVDISTEDLTKQFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMPNGSL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 MHVLKTQIDV-PLSLKGR--IIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwsklTKEKDNKQK 177
Cdd:cd14158   102 LDRLACLNDTpPLSWHMRckIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLAR-------ASEKFSQTI 174
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1333886239 178 EVSSTTkknngGTLYYMAPEHLndiNAKPTEKSDVYSFGIVLWAI 222
Cdd:cd14158   175 MTERIV-----GTTAYMAPEAL---RGEITPKSDIFSFGVVLLEI 211
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
20-278 2.00e-22

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: 97.42  E-value: 2.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  20 KTDLDSGGFGKVSLCYH-RSHGFVILKKVYT-GPNRAEYNEVL----LEEGKMMHRL-RHSRVVKLLGIIIEEGNYSLVM 92
Cdd:cd13993     5 ISPIGEGAYGVVYLAVDlRTGRKYAIKCLYKsGPNSKDGNDFQklpqLREIDLHRRVsRHPNIITLHDVFETEVAIYIVL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  93 EYMEKGNLMHVLKTQIDVPLS--LKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDF-HIKIADLGVASFKTWSklt 169
Cdd:cd13993    85 EYCPNGDLFEAITENRIYVGKteLIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEgTVKLCDFGLATTEKIS--- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 170 kekdnkqKEVSSttkknngGTLYYMAPEHLNDiNAK-----PTEKSDVYSFGIVLWAIFAKKEPYENViCTEQFVICIKS 244
Cdd:cd13993   162 -------MDFGV-------GSEFYMAPECFDE-VGRslkgyPCAAGDIWSLGIILLNLTFGRNPWKIA-SESDPIFYDYY 225
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1333886239 245 GNRPNVEEILEYCPREIISLMERCWQAIPEDRPT 278
Cdd:cd13993   226 LNSPNLFDVILPMSDDFYNLLRQIFTVNPNNRIL 259
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
60-279 2.61e-22

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 97.52  E-value: 2.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  60 LLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVM-EYMEKGNLMHVLK----TQIDVPLSLKGRIIVE----AIEGMCYLH 130
Cdd:cd05043    54 LLQESSLLYGLSHQNLLPILHVCIEDGEKPMVLyPYMNWGNLKLFLQqcrlSEANNPQALSTQQLVHmalqIACGMSYLH 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 131 DKGVIHKDLKPENILVDRDFHIKIADlgvasfktwSKLTKE---------KDNKQKEVSsttkknnggtlyYMAPEHLnd 201
Cdd:cd05043   134 RRGVIHKDIAARNCVIDDELQVKITD---------NALSRDlfpmdyhclGDNENRPIK------------WMSLESL-- 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 202 INAKPTEKSDVYSFGIVLWAIFA-KKEPYENvICTEQFVICIKSGNR---PNveeileYCPREIISLMERCWQAIPEDRP 277
Cdd:cd05043   191 VNKEYSSASDVWSFGVLLWELMTlGQTPYVE-IDPFEMAAYLKDGYRlaqPI------NCPDELFAVMACCWALDPEERP 263

                  ..
gi 1333886239 278 TF 279
Cdd:cd05043   264 SF 265
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
22-279 3.99e-22

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: 96.10  E-value: 3.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  22 DLDSGGFGKVSLCYHRSHGFVILKKVYTGpnrAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLM 101
Cdd:cd05113    11 ELGTGQFGVVKYGKWRGQYDVAIKMIKEG---SMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 HVLKTQIDVPLSLKG-RIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTwskltkekdnKQKEVS 180
Cdd:cd05113    88 NYLREMRKRFQTQQLlEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVL----------DDEYTS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 181 STTKKNnggTLYYMAPEHLndINAKPTEKSDVYSFGIVLWAIFA-KKEPYENvICTEQFVICIKSGNRpnveeilEYCPR 259
Cdd:cd05113   158 SVGSKF---PVRWSPPEVL--MYSKFSSKSDVWAFGVLMWEVYSlGKMPYER-FTNSETVEHVSQGLR-------LYRPH 224
                         250       260
                  ....*....|....*....|....
gi 1333886239 260 ----EIISLMERCWQAIPEDRPTF 279
Cdd:cd05113   225 laseKVYTIMYSCWHEKADERPTF 248
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
26-292 4.41e-22

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: 96.40  E-value: 4.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNE---VLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMH 102
Cdd:cd05611     7 GAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQvtnVKAERAIMMIQGESPYVAKLYYSFQSKDYLYLVMEYLNGGDCAS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVasfktwSKLTKEKDNKQKEVsst 182
Cdd:cd05611    87 LIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGL------SRNGLEKRHNKKFV--- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 183 tkknngGTLYYMAPEHLNDINAkpTEKSDVYSFGIVLWAIFAKKEPYeNVICTEQFVICIKSGNRPNVEEILEYCPREII 262
Cdd:cd05611   158 ------GTPDYLAPETILGVGD--DKMSDWWSLGCVIFEFLFGYPPF-HAETPDAVFDNILSRRINWPEEVKEFCSPEAV 228
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1333886239 263 SLMERCWQAIPEDRPTFLGIEE-EFRPFYLS 292
Cdd:cd05611   229 DLINRLLCMDPAKRLGANGYQEiKSHPFFKS 259
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
17-290 4.47e-22

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: 96.17  E-value: 4.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  17 LLEKTdLDSGGFGKVSLCYHRSHGF-VILKKVytgPNRAEYNEVLL----EEGKMMHRLRHSRVVKLLGIIIEEGNYSLV 91
Cdd:cd14081     4 RLGKT-LGKGQTGLVKLAKHCVTGQkVAIKIV---NKEKLSKESVLmkveREIAIMKLIEHPNVLKLYDVYENKKYLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  92 MEYMEKGNLMHVLKTqidvplslKGRIIV-EA-------IEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFk 163
Cdd:cd14081    80 LEYVSGGELFDYLVK--------KGRLTEkEArkffrqiISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASL- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 164 twskltkEKDNKQKEVSSttkknngGTLYYMAPEHlndINAKPTE--KSDVYSFGIVLWAIFAKKEPY--ENVictEQFV 239
Cdd:cd14081   151 -------QPEGSLLETSC-------GSPHYACPEV---IKGEKYDgrKADIWSCGVILYALLVGALPFddDNL---RQLL 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333886239 240 ICIKSGnrpnVEEILEYCPREIISLMERCWQAIPEDRPTflgIEEEFR-PFY 290
Cdd:cd14081   211 EKVKRG----VFHIPHFISPDAQDLLRRMLEVNPEKRIT---IEEIKKhPWF 255
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
23-286 4.86e-22

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


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 96.05  E-value: 4.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYtgpNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMH 102
Cdd:cd14156     1 IGSGFFSKVYKVTHGATGKVMVVKIY---KNDVDQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLEE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLKTQiDVPLSL--KGRIIVEAIEGMCYLHDKGVIHKDLKPENILV---DRDFHIKIADLGVASfKTWSKLTKEKDNKQK 177
Cdd:cd14156    78 LLARE-ELPLSWreKVELACDISRGMVYLHSKNIYHRDLNSKNCLIrvtPRGREAVVTDFGLAR-EVGEMPANDPERKLS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 178 EVssttkknngGTLYYMAPEHLndiNAKP-TEKSDVYSFGIVLWAIFAK--KEPyENVICTEQFVICIKSgnrpnVEEIL 254
Cdd:cd14156   156 LV---------GSAFWMAPEML---RGEPyDRKVDVFSFGIVLCEILARipADP-EVLPRTGDFGLDVQA-----FKEMV 217
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1333886239 255 EYCPREIISLMERCWQAIPEDRPTFLGIEEEF 286
Cdd:cd14156   218 PGCPEPFLDLAASCCRMDAFKRPSFAELLDEL 249
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
61-279 4.88e-22

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: 96.32  E-value: 4.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  61 LEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVL---KTQIDVPLSLKGRIIVEAieGMCYLHDKGVIHK 137
Cdd:cd05068    51 LREAQIMKKLRHPKLIQLYAVCTLEEPIYIITELMKHGSLLEYLqgkGRSLQLPQLIDMAAQVAS--GMAYLESQNYIHR 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 138 DLKPENILVDRDFHIKIADLGVAsfktwsKLTKEKDNKQKEVssttkknngGT---LYYMAPEHLNdiNAKPTEKSDVYS 214
Cdd:cd05068   129 DLAARNVLVGENNICKVADFGLA------RVIKVEDEYEARE---------GAkfpIKWTAPEAAN--YNRFSIKSDVWS 191
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 215 FGIVLWAIFAK-KEPYENvICTEQFVICIKSGNR----PNveeileyCPREIISLMERCWQAIPEDRPTF 279
Cdd:cd05068   192 FGILLTEIVTYgRIPYPG-MTNAEVLQQVERGYRmpcpPN-------CPPQLYDIMLECWKADPMERPTF 253
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
16-279 9.97e-22

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 95.49  E-value: 9.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  16 DLLEKTDLDSGGFGKVslcyHRS--HGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVME 93
Cdd:cd14063     1 ELEIKEVIGKGRFGRV----HRGrwHGDVAIKLLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  94 YMEKGNLMHVLKTQ-IDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDfHIKIADLGVASFKTWSKLTKEK 172
Cdd:cd14063    77 LCKGRTLYSLIHERkEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLENG-RVVITDFGLFSLSGLLQPGRRE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 173 DnkqkevsstTKKNNGGTLYYMAPE-------HLNDINAKP-TEKSDVYSFGIVLWAIFAKKEPYENvICTEQFVICIKS 244
Cdd:cd14063   156 D---------TLVIPNGWLCYLAPEiiralspDLDFEESLPfTKASDVYAFGTVWYELLAGRWPFKE-QPAESIIWQVGC 225
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1333886239 245 GNRPNVEEIleYCPREIISLMERCWQAIPEDRPTF 279
Cdd:cd14063   226 GKKQSLSQL--DIGREVKDILMQCWAYDPEKRPTF 258
Death pfam00531
Death domain;
569-654 9.97e-22

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 89.73  E-value: 9.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 569 DEHLNPIREN---LGRQWKNCARKLGFTESQIDEIDHDYERdgLKEKVYQMLQKWLMREGtKGATVGKLAQALHQCCRID 645
Cdd:pfam00531   1 RKQLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR--LRSQTYELLRLWEQREG-KNATVGTLLEALRKLGRRD 77

                  ....*....
gi 1333886239 646 LLNHLIRAS 654
Cdd:pfam00531  78 AAEKIQSIL 86
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
44-287 1.04e-21

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


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 95.86  E-value: 1.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  44 LKKVYTGPNRAEYNEvlleEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVL---KTQIDVPLSLKGRIIV 120
Cdd:cd05091    44 LKDKAEGPLREEFRH----EAMLRSRLQHPNIVCLLGVVTKEQPMSMIFSYCSHGDLHEFLvmrSPHSDVGSTDDDKTVK 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 121 EAIE-------------GMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnkqKEV-SSTTKKN 186
Cdd:cd05091   120 STLEpadflhivtqiaaGMEYLSSHHVVHKDLATRNVLVFDKLNVKISDLGLF----------------REVyAADYYKL 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 187 NGGTLY---YMAPEHLndINAKPTEKSDVYSFGIVLWAIFAKK-EPYenviC--TEQFVICIKSgNRpNVEEILEYCPRE 260
Cdd:cd05091   184 MGNSLLpirWMSPEAI--MYGKFSIDSDIWSYGVVLWEVFSYGlQPY----CgySNQDVIEMIR-NR-QVLPCPDDCPAW 255
                         250       260
                  ....*....|....*....|....*..
gi 1333886239 261 IISLMERCWQAIPEDRPTFLGIEEEFR 287
Cdd:cd05091   256 VYTLMLECWNEFPSRRPRFKDIHSRLR 282
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
26-289 1.33e-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: 94.64  E-value: 1.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHG--FVI----LKKVYTGPNRAEYNEVLLeegkmMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGN 99
Cdd:cd08225    11 GSFGKIYLAKAKSDSehCVIkeidLTKMPVKEKEASKKEVIL-----LAKMKHPNIVTFFASFQENGRLFIVMEYCDGGD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 100 LMHVLKTQIDVPLSlKGRII---VEAIEGMCYLHDKGVIHKDLKPENILVDRDFHI-KIADLGVAsfktwskltkEKDNK 175
Cdd:cd08225    86 LMKRINRQRGVLFS-EDQILswfVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIA----------RQLND 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 176 QKEVSSTTkknnGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPYENViCTEQFVICIKSGnrpNVEEILE 255
Cdd:cd08225   155 SMELAYTC----VGTPYYLSPEICQ--NRPYNNKTDIWSLGCVLYELCTLKHPFEGN-NLHQLVLKICQG---YFAPISP 224
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1333886239 256 YCPREIISLMERCWQAIPEDRPTFLGIEEefRPF 289
Cdd:cd08225   225 NFSRDLRSLISQLFKVSPRDRPSITSILK--RPF 256
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
13-282 2.02e-21

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA 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: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 94.55  E-value: 2.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  13 ASSDLLEKTdLDSGGFGKVslCYHR---------SHGFVILKKVYTGPNRAEYnevlLEEGKMMHRLRHSRVVKLLGIII 83
Cdd:cd05066     3 ASCIKIEKV-IGAGEFGEV--CSGRlklpgkreiPVAIKTLKAGYTEKQRRDF----LSEASIMGQFDHPNIIHLEGVVT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  84 EEGNYSLVMEYMEKGNLMHVLKT---QIDVpLSLKGriIVEAI-EGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGV 159
Cdd:cd05066    76 RSKPVMIVTEYMENGSLDAFLRKhdgQFTV-IQLVG--MLRGIaSGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 160 ASfktwsklTKEKDnkqKEVSSTTKknnGGTL--YYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKE-PYENVicTE 236
Cdd:cd05066   153 SR-------VLEDD---PEAAYTTR---GGKIpiRWTAPEAIA--YRKFTSASDVWSYGIVMWEVMSYGErPYWEM--SN 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1333886239 237 QFVI-CIKSGNR-PNVEEileyCPREIISLMERCWQAIPEDRPTFLGI 282
Cdd:cd05066   216 QDVIkAIEEGYRlPAPMD----CPAALHQLMLDCWQKDRNERPKFEQI 259
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
66-266 2.17e-21

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: 94.35  E-value: 2.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  66 MMHRLRHSRVVKLLGIIIE--EGNYSLVMEYMEKGNLMHVLKTQidvPLS--LKGRIIVEAIEGMCYLHDKGVIHKDLKP 141
Cdd:cd14118    67 ILKKLDHPNVVKLVEVLDDpnEDNLYMVFELVDKGAVMEVPTDN---PLSeeTARSYFRDIVLGIEYLHYQKIIHRDIKP 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 142 ENILVDRDFHIKIADLGVASfktwskltkEKDNKQKEVSSTTkknngGTLYYMAPEHLNDINAKPTEKS-DVYSFGIVLW 220
Cdd:cd14118   144 SNLLLGDDGHVKIADFGVSN---------EFEGDDALLSSTA-----GTPAFMAPEALSESRKKFSGKAlDIWAMGVTLY 209
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333886239 221 AIFAKKEPYENV--------ICTEQFVICiksgNRPNVEEILEYC--------PREIISLME 266
Cdd:cd14118   210 CFVFGRCPFEDDhilglhekIKTDPVVFP----DDPVVSEQLKDLilrmldknPSERITLPE 267
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
16-282 2.34e-21

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB 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: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 94.72  E-value: 2.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  16 DLLEKTDLDSGGFGKV------SLCYHRSHGFVILK--KVYTGPNRAEYNEvlleEGKMMHRLRHSRVVKLLGIIIEEGN 87
Cdd:cd05093     6 NIVLKRELGEGAFGKVflaecyNLCPEQDKILVAVKtlKDASDNARKDFHR----EAELLTNLQHEHIVKFYGVCVEGDP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  88 YSLVMEYMEKGNLMHVLKTQ-IDVPLSLKGRIIVEAIE------------GMCYLHDKGVIHKDLKPENILVDRDFHIKI 154
Cdd:cd05093    82 LIMVFEYMKHGDLNKFLRAHgPDAVLMAEGNRPAELTQsqmlhiaqqiaaGMVYLASQHFVHRDLATRNCLVGENLLVKI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 155 ADLGVAsfktwskltkekdnkqKEVSSTTKKNNGG----TLYYMAPEHLndINAKPTEKSDVYSFGIVLWAIFA-KKEPY 229
Cdd:cd05093   162 GDFGMS----------------RDVYSTDYYRVGGhtmlPIRWMPPESI--MYRKFTTESDVWSLGVVLWEIFTyGKQPW 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333886239 230 ENvICTEQFVICIKSG---NRPNVeeileyCPREIISLMERCWQAIPEDRPTFLGI 282
Cdd:cd05093   224 YQ-LSNNEVIECITQGrvlQRPRT------CPKEVYDLMLGCWQREPHMRLNIKEI 272
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
15-219 2.55e-21

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: 94.57  E-value: 2.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  15 SDLLEKTDLDSGGFGKVSLCYHRSHGFV----ILKKVYTGPNRAEynEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSL 90
Cdd:cd05580     1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYyalkILKKAKIIKLKQV--EHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  91 VMEYMEKGNLMHVLKTqidvplslKGRI-----------IVEAIEgmcYLHDKGVIHKDLKPENILVDRDFHIKIADLGV 159
Cdd:cd05580    79 VMEYVPGGELFSLLRR--------SGRFpndvakfyaaeVVLALE---YLHSLDIVYRDLKPENLLLDSDGHIKITDFGF 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333886239 160 A---SFKTWSKLtkekdnkqkevssttkknngGTLYYMAPEhlnDINAKPTEKS-DVYSFGIVL 219
Cdd:cd05580   148 AkrvKDRTYTLC--------------------GTPEYLAPE---IILSKGHGKAvDWWALGILI 188
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
60-282 3.52e-21

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (IGF-1 or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R 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: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 93.94  E-value: 3.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  60 LLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKT--------QIDVPLSLKGRIIV--EAIEGMCYL 129
Cdd:cd05062    56 FLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELMTRGDLKSYLRSlrpemennPVQAPPSLKKMIQMagEIADGMAYL 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 130 HDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnkqKEVSSTTKKNNGGT----LYYMAPEHLNDinAK 205
Cdd:cd05062   136 NANKFVHRDLAARNCMVAEDFTVKIGDFGMT----------------RDIYETDYYRKGGKgllpVRWMSPESLKD--GV 197
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333886239 206 PTEKSDVYSFGIVLWAIFAKKE-PYENvICTEQFVICIKSGnrpNVEEILEYCPREIISLMERCWQAIPEDRPTFLGI 282
Cdd:cd05062   198 FTTYSDVWSFGVVLWEIATLAEqPYQG-MSNEQVLRFVMEG---GLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEI 271
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
58-285 3.56e-21

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM 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: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 93.75  E-value: 3.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  58 EVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYS------LVMEYMEKGNL------MHVLKTQIDVPLSLKGRIIVEAIEG 125
Cdd:cd05035    46 EEFLSEAACMKDFDHPNVMRLIGVCFTASDLNkppspmVILPFMKHGDLhsyllySRLGGLPEKLPLQTLLKFMVDIAKG 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 126 MCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwsKLTKEKDNKQKEVSSTTKKnnggtlyYMAPEHLNDinAK 205
Cdd:cd05035   126 MEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLSR-----KIYSGDYYRQGRISKMPVK-------WIALESLAD--NV 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 206 PTEKSDVYSFGIVLWAIFAK-KEPYENVICTEQFVIcIKSGNRPNVEEileYCPREIISLMERCWQAIPEDRPTFLGIEE 284
Cdd:cd05035   192 YTSKSDVWSFGVTMWEIATRgQTPYPGVENHEIYDY-LRNGNRLKQPE---DCLDEVYFLMYFCWTVDPKDRPTFTKLRE 267

                  .
gi 1333886239 285 E 285
Cdd:cd05035   268 V 268
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
22-278 4.72e-21

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: 93.65  E-value: 4.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  22 DLDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEgKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLM 101
Cdd:cd06611    12 ELGDGAFGKVYKAQHKETGLFAAAKIIQIESEEELEDFMVEI-DILSECKHPNIVGLYEAYFYENKLWILIEFCDGGALD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 HVLkTQIDVPLSlKGRIIV---EAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwskltKEKDNKQKE 178
Cdd:cd06611    91 SIM-LELERGLT-EPQIRYvcrQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSA--------KNKSTLQKR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 179 VSSTtkknngGTLYYMAPEHLNDINAKPTE---KSDVYSFGIVLWAIfAKKEPYENVICTEQFVICIKSGNRPNVEEILE 255
Cdd:cd06611   161 DTFI------GTPYWMAPEVVACETFKDNPydyKADIWSLGITLIEL-AQMEPPHHELNPMRVLLKILKSEPPTLDQPSK 233
                         250       260
                  ....*....|....*....|...
gi 1333886239 256 YcPREIISLMERCWQAIPEDRPT 278
Cdd:cd06611   234 W-SSSFNDFLKSCLVKDPDDRPT 255
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
23-229 4.83e-21

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: 93.61  E-value: 4.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRS----HGFVILKK-VYTGPNRAEYNEV--LLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYM 95
Cdd:cd14084    14 LGSGACGEVKLAYDKStckkVAIKIINKrKFTIGSRREINKPrnIETEIEILKKLSHPCIIKIEDFFDAEDDYYIVLELM 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  96 EKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILV---DRDFHIKIADLGVasfktwSKLTKEk 172
Cdd:cd14084    94 EGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLssqEEECLIKITDFGL------SKILGE- 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1333886239 173 dnkqkevsSTTKKNNGGTLYYMAPEHLNDINAKP-TEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14084   167 --------TSLMKTLCGTPTYLAPEVLRSFGTEGyTRAVDCWSLGVILFICLSGYPPF 216
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
23-231 5.27e-21

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: 93.31  E-value: 5.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGF-VILKKVYTGPNRAEYNEVLL-EEGKMMHRLRHSRVVKLLGII-IEEGNYSLVMEYMEKGN 99
Cdd:cd14165     9 LGEGSYAKVKSAYSERLKCnVAIKIIDKKKAPDDFVEKFLpRELEILARLNHKSIIKTYEIFeTSDGKVYIVMELGVQGD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 100 LMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasfktWSKLTKEKDNKQKEV 179
Cdd:cd14165    89 LLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFG------FSKRCLRDENGRIVL 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333886239 180 SSTTkknnGGTLYYMAPEHLNDINAKPtEKSDVYSFGIVLWAIFAKKEPYEN 231
Cdd:cd14165   163 SKTF----CGSAAYAAPEVLQGIPYDP-RIYDIWSLGVILYIMVCGSMPYDD 209
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
44-282 8.22e-21

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 92.73  E-value: 8.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  44 LKKVYTGPNRAEYnevlLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQID--VPLSLKGriIVE 121
Cdd:cd05063    41 LKPGYTEKQRQDF----LSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYMENGALDKYLRDHDGefSSYQLVG--MLR 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 122 AIE-GMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwsklTKEKDnkqKEVSSTTkknNGGT--LYYMAPEH 198
Cdd:cd05063   115 GIAaGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSR-------VLEDD---PEGTYTT---SGGKipIRWTAPEA 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 199 LNdiNAKPTEKSDVYSFGIVLWAIFAKKE-PYENvICTEQFVICIKSGNR-PNVEEileyCPREIISLMERCWQAIPEDR 276
Cdd:cd05063   182 IA--YRKFTSASDVWSFGIVMWEVMSFGErPYWD-MSNHEVMKAINDGFRlPAPMD----CPSAVYQLMLQCWQQDRARR 254

                  ....*.
gi 1333886239 277 PTFLGI 282
Cdd:cd05063   255 PRFVDI 260
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
25-226 9.45e-21

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: 93.01  E-value: 9.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSLCYHRSHG-FVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEE------GNYSLVMEYMEk 97
Cdd:cd07840     9 EGTYGQVYKARNKKTGeLVALKKIRMENEKEGFPITAIREIKLLQKLDHPNVVRLKEIVTSKgsakykGSIYMVFEYMD- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  98 gnlmHVLKTQIDVPLS------LKGrIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFktwskLTKE 171
Cdd:cd07840    88 ----HDLTGLLDNPEVkftesqIKC-YMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLARP-----YTKE 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333886239 172 KDNKQkevssttkKNNGGTLYYMAPEHL-NDINAKPteKSDVYSFGIVLWAIFAKK 226
Cdd:cd07840   158 NNADY--------TNRVITLWYRPPELLlGATRYGP--EVDMWSVGCILAELFTGK 203
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
23-222 1.70e-20

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


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 92.21  E-value: 1.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVI----LKKVYTGPNraEYNEvlLEEGKMMHRL-RHSRVVKLLGIIIEEGNYSLVMEYMEk 97
Cdd:cd07830     7 LGDGTFGSVYLARNKETGELVaikkMKKKFYSWE--ECMN--LREVKSLRKLnEHPNIVKLKEVFRENDELYFVFEYME- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  98 GNLMHVLKTQIDVPLS---LKGrIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwsKLTKEKDN 174
Cdd:cd07830    82 GNLYQLMKDRKGKPFSesvIRS-IIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLA------REIRSRPP 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1333886239 175 KQKEVSsttkknnggTLYYMAPEHLndinakptEKSDVYSFGIVLWAI 222
Cdd:cd07830   155 YTDYVS---------TRWYRAPEIL--------LRSTSYSSPVDIWAL 185
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
58-286 2.46e-20

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl 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: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 91.61  E-value: 2.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  58 EVLLEEGKMMHRLRHSRVVKLLGIIIE----EGNYS--LVMEYMEKGNL-MHVLKTQI-DVPLSLKGRIIVEAI----EG 125
Cdd:cd05075    46 EDFLSEAVCMKEFDHPNVMRLIGVCLQntesEGYPSpvVILPFMKHGDLhSFLLYSRLgDCPVYLPTQMLVKFMtdiaSG 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 126 MCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwSKLTKEKDNKQKEVSSTTKKnnggtlyYMAPEHLNDinAK 205
Cdd:cd05075   126 MEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLS-----KKIYNGDYYRQGRISKMPVK-------WIAIESLAD--RV 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 206 PTEKSDVYSFGIVLWAIFAK-KEPYENVICTEQFVIcIKSGNRpnVEEILEyCPREIISLMERCWQAIPEDRPTFLGIEE 284
Cdd:cd05075   192 YTTKSDVWSFGVTMWEIATRgQTPYPGVENSEIYDY-LRQGNR--LKQPPD-CLDGLYELMSSCWLLNPKDRPSFETLRC 267

                  ..
gi 1333886239 285 EF 286
Cdd:cd05075   268 EL 269
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
61-284 2.70e-20

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK 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: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 91.30  E-value: 2.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  61 LEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVL-----KTQIDVPLSLKG--RIIVEAIEGMCYLHDKG 133
Cdd:cd05036    57 LMEALIMSKFNHPNIVRCIGVCFQRLPRFILLELMAGGDLKSFLrenrpRPEQPSSLTMLDllQLAQDVAKGCRYLEENH 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 134 VIHKDLKPENIL-----VDRdfHIKIADLGVAsfktwskltkekdnkqKEVSSTTKKNNGGT----LYYMAPEHLNDinA 204
Cdd:cd05036   137 FIHRDIAARNCLltckgPGR--VAKIGDFGMA----------------RDIYRADYYRKGGKamlpVKWMPPEAFLD--G 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 205 KPTEKSDVYSFGIVLWAIFA-KKEPYENVICTE--QFVIcikSGNR---PNveeileYCPREIISLMERCWQAIPEDRPT 278
Cdd:cd05036   197 IFTSKTDVWSFGVLLWEIFSlGYMPYPGKSNQEvmEFVT---SGGRmdpPK------NCPGPVYRIMTQCWQHIPEDRPN 267

                  ....*.
gi 1333886239 279 FLGIEE 284
Cdd:cd05036   268 FSTILE 273
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
58-279 4.00e-20

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 91.13  E-value: 4.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  58 EVLLEEGKMMHRLRHSRVVKLLGIIIE---EGNYSLVM---EYMEKGNLMHVL------KTQIDVPLSLKGRIIVEAIEG 125
Cdd:cd05074    56 EEFLREAACMKEFDHPNVIKLIGVSLRsraKGRLPIPMvilPFMKHGDLHTFLlmsrigEEPFTLPLQTLVRFMIDIASG 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 126 MCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwSKLTKEKDNKQKEVSSTTKKnnggtlyYMAPEHLNDiNAK 205
Cdd:cd05074   136 MEYLSSKNFIHRDLAARNCMLNENMTVCVADFGLS-----KKIYSGDYYRQGCASKLPVK-------WLALESLAD-NVY 202
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333886239 206 pTEKSDVYSFGIVLWAIFAK-KEPYENVICTEQFVICIKsGNRpnVEEILEyCPREIISLMERCWQAIPEDRPTF 279
Cdd:cd05074   203 -TTHSDVWAFGVTMWEIMTRgQTPYAGVENSEIYNYLIK-GNR--LKQPPD-CLEDVYELMCQCWSPEPKCRPSF 272
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
58-230 4.17e-20

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 91.43  E-value: 4.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  58 EVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQIDVP-LSLKGR--IIVEAIEGMCYLHD--K 132
Cdd:cd14159    37 NSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVYLPNGSLEDRLHCQVSCPcLSWSQRlhVLLGTARAIQYLHSdsP 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 133 GVIHKDLKPENILVDRDFHIKIADLGVASFktwSKLTKEKDNKQKEVSSTTKKnngGTLYYMAPEHLNDinAKPTEKSDV 212
Cdd:cd14159   117 SLIHGDVKSSNILLDAALNPKLGDFGLARF---SRRPKQPGMSSTLARTQTVR---GTLAYLPEEYVKT--GTLSVEIDV 188
                         170
                  ....*....|....*...
gi 1333886239 213 YSFGIVLWAIFAKKEPYE 230
Cdd:cd14159   189 YSFGVVLLELLTGRRAME 206
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
20-282 4.91e-20

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 91.21  E-value: 4.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  20 KTDLDSGGFGKVSLCYHRS-HGF----------------VILKKVYTGPNRAEYNEvLLEEGKMMHRLRHSRVVKLLGII 82
Cdd:cd05095    10 KEKLGEGQFGEVHLCEAEGmEKFmdkdfalevsenqpvlVAVKMLRADANKNARND-FLKEIKIMSRLKDPNIIRLLAVC 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  83 IEEGNYSLVMEYMEKGNLMHVL-KTQIDVPLSLKGRII-----------VEAIEGMCYLHDKGVIHKDLKPENILVDRDF 150
Cdd:cd05095    89 ITDDPLCMITEYMENGDLNQFLsRQQPEGQLALPSNALtvsysdlrfmaAQIASGMKYLSSLNFVHRDLATRNCLVGKNY 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 151 HIKIADLGVasfktwSKLTKEKDNKQKEVSSTTKknnggtLYYMAPEHLndINAKPTEKSDVYSFGIVLWAI--FAKKEP 228
Cdd:cd05095   169 TIKIADFGM------SRNLYSGDYYRIQGRAVLP------IRWMSWESI--LLGKFTTASDVWAFGVTLWETltFCREQP 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1333886239 229 YENvICTEQFVICIKSGNRPNVEEIL----EYCPREIISLMERCWQAIPEDRPTFLGI 282
Cdd:cd05095   235 YSQ-LSDEQVIENTGEFFRDQGRQTYlpqpALCPDSVYKLMLSCWRRDTKDRPSFQEI 291
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
23-284 8.25e-20

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: 89.97  E-value: 8.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKV-YTGPNRAEYNEvLLEEGKMMHRLRHS-RVVKLLG--IIIEEGNYSLVMEYMEkG 98
Cdd:cd14131     9 LGKGGSSKVYKVLNPKKKIYALKRVdLEGADEQTLQS-YKNEIELLKKLKGSdRIIQLYDyeVTDEDDYLYMVMECGE-I 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  99 NLMHVLKTQIDVPLSLKGRIIV--EAIEGMCYLHDKGVIHKDLKPEN-ILVDRdfHIKIADLGVASfktwskltkekdNK 175
Cdd:cd14131    87 DLATILKKKRPKPIDPNFIRYYwkQMLEAVHTIHEEGIVHSDLKPANfLLVKG--RLKLIDFGIAK------------AI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 176 QKEVSSTTKKNNGGTLYYMAPEHLNDINAKPTEK--------SDVYSFGIVLWAIFAKKEPYENV---------ICTEQF 238
Cdd:cd14131   153 QNDTTSIVRDSQVGTLNYMSPEAIKDTSASGEGKpkskigrpSDVWSLGCILYQMVYGKTPFQHItnpiaklqaIIDPNH 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1333886239 239 VIciksgnrpnveEILEYCPREIISLMERCWQAIPEDRPTflgIEE 284
Cdd:cd14131   233 EI-----------EFPDIPNPDLIDVMKRCLQRDPKKRPS---IPE 264
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
23-230 8.69e-20

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: 89.31  E-value: 8.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRA------EYNEVLleegkmmHRLRHSRVVKLLGIIIE-EGNYSLVMEYM 95
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKlkdflrEYNISL-------ELSVHPHIIKTYDVAFEtEDYYVFAQEYA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  96 EKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILV-DRDF-HIKIADLGvasfktwskLTKEKD 173
Cdd:cd13987    74 PYGDLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfDKDCrRVKLCDFG---------LTRRVG 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333886239 174 nkqkevsSTTKKNNgGTLYYMAPEHLndiNAKPTEK------SDVYSFGIVLWAIFAKKEPYE 230
Cdd:cd13987   145 -------STVKRVS-GTIPYTAPEVC---EAKKNEGfvvdpsIDVWAFGVLLFCCLTGNFPWE 196
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
26-222 9.24e-20

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: 90.07  E-value: 9.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHG-FVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKgNLMHVL 104
Cdd:cd07833    12 GAYGVVLKCRNKATGeIVAIKKFKESEDDEDVKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFEYVER-TLLELL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 105 KTQID-VPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTWSKLTKEKDnkqkEVSstt 183
Cdd:cd07833    91 EASPGgLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTARPASPLTD----YVA--- 163
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1333886239 184 kknnggTLYYMAPEHLndinAKPTEksdvYSFGIVLWAI 222
Cdd:cd07833   164 ------TRWYRAPELL----VGDTN----YGKPVDVWAI 188
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
565-647 1.35e-19

DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers.


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 83.61  E-value: 1.35e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  565 TSLTDEHLNPIREN-LGRQWKNCARKLGFTESQIDEIDHDYERDgLKEKVYQMLQKWLMREGtKGATVGKLAQALHQCCR 643
Cdd:smart00005   1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRD-LAEQSVQLLRLWEQREG-KNATLGTLLEALRKMGR 78

                   ....
gi 1333886239  644 IDLL 647
Cdd:smart00005  79 DDAV 82
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
21-278 1.47e-19

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: 88.76  E-value: 1.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  21 TDLDSGGFGKVSLCYHRSH-GFVILKKVYTGPNRAEY-NEVLLEEGKMMHRLRHSRVVKLLGII-IEEGNYSLVMEYMEK 97
Cdd:cd14164     6 TTIGEGSFSKVKLATSQKYcCKVAIKIVDRRRASPDFvQKFLPRELSILRRVNHPNIVQMFECIeVANGRLYIVMEAAAT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  98 gNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRD-FHIKIADLGVASFKtwskltkekdNKQ 176
Cdd:cd14164    86 -DLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADdRKIKIADFGFARFV----------EDY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 177 KEVSSTTkknnGGTLYYMAPEHLNDINAKPtEKSDVYSFGIVLWAIFAKKEPYENVICteQFVICIKSG-NRPNVEEILE 255
Cdd:cd14164   155 PELSTTF----CGSRAYTPPEVILGTPYDP-KKYDVWSLGVVLYVMVTGTMPFDETNV--RRLRLQQRGvLYPSGVALEE 227
                         250       260
                  ....*....|....*....|...
gi 1333886239 256 YCPREIISLMercwQAIPEDRPT 278
Cdd:cd14164   228 PCRALIRTLL----QFNPSTRPS 246
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
11-219 1.67e-19

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: 90.11  E-value: 1.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  11 KMASSDLLEKTDLDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSL 90
Cdd:cd06650     1 ELKDDDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  91 VMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDK-GVIHKDLKPENILVDRDFHIKIADLGVASfktwsklt 169
Cdd:cd06650    81 CMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSG-------- 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1333886239 170 kekdnkqkEVSSTTKKNNGGTLYYMAPEHLNDINAkpTEKSDVYSFGIVL 219
Cdd:cd06650   153 --------QLIDSMANSFVGTRSYMSPERLQGTHY--SVQSDIWSMGLSL 192
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
26-251 1.91e-19

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: 88.93  E-value: 1.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHG-FVILKKVyTGPNRAE-YNEVLLEEGKMMHRLR-HSRVVKLLGIIIEEGNYSLVMEYMEKGnLMH 102
Cdd:cd07832    11 GAHGIVFKAKDRETGeTVALKKV-ALRKLEGgIPNQALREIKALQACQgHPYVVKLRDVFPHGTGFVLVFEYMLSS-LSE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLKtQIDVPLS---LKgRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwsKLTKEKDNKQ--K 177
Cdd:cd07832    89 VLR-DEERPLTeaqVK-RYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLA------RLFSEEDPRLysH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 178 EVssttkknngGTLYYMAPEHLNDinakptekSDVYSFGIVLWA---IFAkkE--------PYENVIctEQFVICIKSGN 246
Cdd:cd07832   161 QV---------ATRWYRAPELLYG--------SRKYDEGVDLWAvgcIFA--EllngsplfPGENDI--EQLAIVLRTLG 219

                  ....*
gi 1333886239 247 RPNVE 251
Cdd:cd07832   220 TPNEK 224
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
23-284 1.92e-19

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: 90.04  E-value: 1.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKV----SLCYHRSHG--FVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIE-EGNYSLVMEYM 95
Cdd:cd05102    15 LGHGAFGKVveasAFGIDKSSSceTVAVKMLKEGATASEHKALMSELKILIHIGNHLNVVNLLGACTKpNGPLMVIVEFC 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  96 EKGNLMHVLKTQID--VPLSLKG-------RIIVEAIE------------------------------------------ 124
Cdd:cd05102    95 KYGNLSNFLRAKREgfSPYRERSprtrsqvRSMVEAVRadrrsrqgsdrvasftestsstnqprqevddlwqspltmedl 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 125 ---------GMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwSKLTKEKDNKQKEVSSTTKKnnggtlyYMA 195
Cdd:cd05102   175 icysfqvarGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLA-----RDIYKDPDYVRKGSARLPLK-------WMA 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 196 PEHLNDinAKPTEKSDVYSFGIVLWAIFA-KKEPYENVICTEQFVICIKSGNRPNVEeilEYCPREIISLMERCWQAIPE 274
Cdd:cd05102   243 PESIFD--KVYTTQSDVWSFGVLLWEIFSlGASPYPGVQINEEFCQRLKDGTRMRAP---EYATPEIYRIMLSCWHGDPK 317
                         330
                  ....*....|
gi 1333886239 275 DRPTFLGIEE 284
Cdd:cd05102   318 ERPTFSDLVE 327
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
26-279 1.97e-19

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 88.87  E-value: 1.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVslCYHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMeKGNLMH--V 103
Cdd:cd14152    11 GRWGKV--HRGRWHGEVAIRLLEIDGNNQDHLKLFKKEVMNYRQTRHENVVLFMGACMHPPHLAIITSFC-KGRTLYsfV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 104 LKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDfHIKIADLGVASFktwSKLTKEkDNKQKEVsstt 183
Cdd:cd14152    88 RDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNG-KVVITDFGLFGI---SGVVQE-GRRENEL---- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 184 kKNNGGTLYYMAPEHL------NDINAKPTEK-SDVYSFGIVLWAIFAKKEPYENViCTEQFVICIKSGNrpNVEEILEY 256
Cdd:cd14152   159 -KLPHDWLCYLAPEIVremtpgKDEDCLPFSKaADVYAFGTIWYELQARDWPLKNQ-PAEALIWQIGSGE--GMKQVLTT 234
                         250       260
                  ....*....|....*....|....*
gi 1333886239 257 CP--REIISLMERCWQAIPEDRPTF 279
Cdd:cd14152   235 ISlgKEVTEILSACWAFDLEERPSF 259
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
18-278 2.39e-19

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: 88.21  E-value: 2.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  18 LEKTdLDSGGFGKVSLCYHRSHG----FVILKKVYTGPN--RAEynevllEEGKMMHRLRHSRVVKLLGIIIEEGNYSLV 91
Cdd:cd14078     7 LHET-IGSGGFAKVKLATHILTGekvaIKIMDKKALGDDlpRVK------TEIEALKNLSHQHICRLYHVIETDNKIFMV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  92 MEYMEKGNLMH--VLKTQIDVPLSLKG-RIIVEAIegmCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwskl 168
Cdd:cd14078    80 LEYCPGGELFDyiVAKDRLSEDEARVFfRQIVSAV---AYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCA------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 169 tKEKDNKQKEVSSTTkknngGTLYYMAPEHlndINAKP--TEKSDVYSFGIVLWAIFAKKEPYENVICTEQFVIcIKSGn 246
Cdd:cd14078   150 -KPKGGMDHHLETCC-----GSPAYAAPEL---IQGKPyiGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRK-IQSG- 218
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1333886239 247 rpnVEEILEYCPREIISLMERCWQAIPEDRPT 278
Cdd:cd14078   219 ---KYEEPEWLSPSSKLLLDQMLQVDPKKRIT 247
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
26-284 3.25e-19

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. The KSR2 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: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 88.14  E-value: 3.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVslcYH-RSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEyMEKGNLMHVL 104
Cdd:cd14153    11 GRFGQV---YHgRWHGEVAIRLIDIERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITS-LCKGRTLYSV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 105 ----KTQIDVplSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDfHIKIADLGVASFKTWSKLTKEKDNKQKEvs 180
Cdd:cd14153    87 vrdaKVVLDV--NKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNG-KVVITDFGLFTISGVLQAGRREDKLRIQ-- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 181 sttkknnGGTLYYMAPEHLNDINAKPTE-------KSDVYSFGIVLWAIFAKKEPYENVIcTEQFVICIKSGNRPNVEEI 253
Cdd:cd14153   162 -------SGWLCHLAPEIIRQLSPETEEdklpfskHSDVFAFGTIWYELHAREWPFKTQP-AEAIIWQVGSGMKPNLSQI 233
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1333886239 254 leYCPREIISLMERCWQAIPEDRPTFLGIEE 284
Cdd:cd14153   234 --GMGKEISDILLFCWAYEQEERPTFSKLME 262
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
25-278 3.27e-19

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: 87.98  E-value: 3.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSLCYHRSHGFVILKKV--YTGPNRAEyNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSL--VMEYMEKGNL 100
Cdd:cd08217    10 KGSFGTVRKVRRKSDGKILVWKEidYGKMSEKE-KQQLVSEVNILRELKHPNIVRYYDRIVDRANTTLyiVMEYCEGGDL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 MHVLKTQID----VPLSLKGRIIVEAIEGMCYLHDKG-----VIHKDLKPENILVDRDFHIKIADLGVAsfktwskltke 171
Cdd:cd08217    89 AQLIKKCKKenqyIPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFLDSDNNVKLGDFGLA----------- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 172 kdnkqKEVSSTTK--KNNGGTLYYMAPEHLNDinAKPTEKSDVYSFGIVLWAIFAKKEPYEnVICTEQFVICIKSGNRPN 249
Cdd:cd08217   158 -----RVLSHDSSfaKTYVGTPYYMSPELLNE--QSYDEKSDIWSLGCLIYELCALHPPFQ-AANQLELAKKIKEGKFPR 229
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1333886239 250 VEEIleYCP--REIISLMercWQAIPEDRPT 278
Cdd:cd08217   230 IPSR--YSSelNEVIKSM---LNVDPDKRPS 255
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
23-231 3.41e-19

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: 87.92  E-value: 3.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGF------VILKKVYTGPNRAEYNEV-LLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYM 95
Cdd:cd14076     9 LGEGEFGKVKLGWPLPKANhrsgvqVAIKLIRRDTQQENCQTSkIMREINILKGLTHPNIVRLLDVLKTKKYIGIVLEFV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  96 EKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwskltkEKDNK 175
Cdd:cd14076    89 SGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFAN---------TFDHF 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333886239 176 QKEVSSTTkknnGGTLYYMAPEHLNDINAKPTEKSDVYSFGIVLWAIFAKKEPYEN 231
Cdd:cd14076   160 NGDLMSTS----CGSPCYAAPELVVSDSMYAGRKADIWSCGVILYAMLAGYLPFDD 211
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
23-284 3.74e-19

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: 87.46  E-value: 3.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYN--EVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNL 100
Cdd:cd14663     8 LGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREGmvEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVMELVTGGEL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 MHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVasfktwSKLTKEkdNKQKEVS 180
Cdd:cd14663    88 FSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGL------SALSEQ--FRQDGLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 181 STTkknnGGTLYYMAPEHLNDiNAKPTEKSDVYSFGIVLWAIFAKKEPY--ENV------ICTEQFviciksgnrpnveE 252
Cdd:cd14663   160 HTT----CGTPNYVAPEVLAR-RGYDGAKADIWSCGVILFVLLAGYLPFddENLmalyrkIMKGEF-------------E 221
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1333886239 253 ILEYCPREIISLMERCWQAIPEDRPTFLGIEE 284
Cdd:cd14663   222 YPRWFSPGAKSLIKRILDPNPSTRITVEQIMA 253
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
22-289 4.51e-19

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: 88.16  E-value: 4.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  22 DLDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEgKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLM 101
Cdd:cd06644    19 ELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYMVEI-EILATCNHPYIVKLLGAFYWDGKLWIMIEFCPGGAVD 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 HVL--------KTQIDVplslkgrIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwskltkekd 173
Cdd:cd06644    98 AIMleldrgltEPQIQV-------ICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSA------------ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 174 nkqKEVSSTTKKNNG-GTLYYMAPEHLNDINAKPTE---KSDVYSFGIVLWAIfAKKEPYENVICTEQFVICIKSGNRPN 249
Cdd:cd06644   159 ---KNVKTLQRRDSFiGTPYWMAPEVVMCETMKDTPydyKADIWSLGITLIEM-AQIEPPHHELNPMRVLLKIAKSEPPT 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1333886239 250 VEEILEYCPrEIISLMERCWQAIPEDRPTFLGIEEEfrPF 289
Cdd:cd06644   235 LSQPSKWSM-EFRDFLKTALDKHPETRPSAAQLLEH--PF 271
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
23-279 4.70e-19

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: 88.91  E-value: 4.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKV------SLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVM-EYM 95
Cdd:cd14207    15 LGRGAFGKVvqasafGIKKSPTCRVVAVKMLKEGATASEYKALMTELKILIHIGHHLNVVNLLGACTKSGGPLMVIvEYC 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  96 EKGNLMHVLKTQIDV-----PLSLKGRIIVEAIE---------------------------------------------- 124
Cdd:cd14207    95 KYGNLSNYLKSKRDFfvtnkDTSLQEELIKEKKEaeptggkkkrlesvtssesfassgfqedkslsdveeeeedsgdfyk 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 125 -----------------GMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwSKLTKEKDNKQKEVSSTTKKnn 187
Cdd:cd14207   175 rpltmedlisysfqvarGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLA-----RDIYKNPDYVRKGDARLPLK-- 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 188 ggtlyYMAPEHLNDinAKPTEKSDVYSFGIVLWAIFA-KKEPYENVICTEQFVICIKSGNRPNVEeilEYCPREIISLME 266
Cdd:cd14207   248 -----WMAPESIFD--KIYSTKSDVWSYGVLLWEIFSlGASPYPGVQIDEDFCSKLKEGIRMRAP---EFATSEIYQIML 317
                         330
                  ....*....|...
gi 1333886239 267 RCWQAIPEDRPTF 279
Cdd:cd14207   318 DCWQGDPNERPRF 330
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
26-233 6.02e-19

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: 86.92  E-value: 6.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLL-EEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEkGNLMHVL 104
Cdd:cd14002    12 GSFGKVYKGRRKYTGQVVALKFIPKRGKSEKELRNLrQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEYAQ-GELFQIL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 105 KTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVA---SFKTwSKLTKEKdnkqkevss 181
Cdd:cd14002    91 EDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFAramSCNT-LVLTSIK--------- 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333886239 182 ttkknngGTLYYMAPEHlndINAKP-TEKSDVYSFGIVLWAIFAKKEP-YENVI 233
Cdd:cd14002   161 -------GTPLYMAPEL---VQEQPyDHTADLWSLGCILYELFVGQPPfYTNSI 204
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
26-278 6.16e-19

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: 86.79  E-value: 6.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHG--FVILKKVYTGPNRAEYNEVLlEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHV 103
Cdd:cd08218    11 GSFGKALLVKSKEDGkqYVIKEINISKMSPKEREESR-KEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYCDGGDLYKR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 104 LKTQIDVPLSlKGRII---VEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKtwskltkekdNKQKEVS 180
Cdd:cd08218    90 INAQRGVLFP-EDQILdwfVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVL----------NSTVELA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 181 STTKknngGTLYYMAPEHLNDinaKP-TEKSDVYSFGIVLWAIFAKKEPYE--NVictEQFVICIKSGNRPNVEEILEYc 257
Cdd:cd08218   159 RTCI----GTPYYLSPEICEN---KPyNNKSDIWALGCVLYEMCTLKHAFEagNM---KNLVLKIIRGSYPPVPSRYSY- 227
                         250       260
                  ....*....|....*....|.
gi 1333886239 258 prEIISLMERCWQAIPEDRPT 278
Cdd:cd08218   228 --DLRSLVSQLFKRNPRDRPS 246
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
57-286 6.44e-19

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 88.16  E-value: 6.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  57 NEVLLEEGKMMHRLRHSRVVKLLGIIIEEgNYSLVMEYMEKGNLMHVLKTQIDvplSLKGRII----VEAIEGMCYLHDK 132
Cdd:cd05108    53 NKEILDEAYVMASVDNPHVCRLLGICLTS-TVQLITQLMPFGCLLDYVREHKD---NIGSQYLlnwcVQIAKGMNYLEDR 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 133 GVIHKDLKPENILVDRDFHIKIADLGVASFktwskLTKEKDNKQKEvssttkknnGGT--LYYMAPEHLndINAKPTEKS 210
Cdd:cd05108   129 RLVHRDLAARNVLVKTPQHVKITDFGLAKL-----LGAEEKEYHAE---------GGKvpIKWMALESI--LHRIYTHQS 192
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333886239 211 DVYSFGIVLWAI--FAKKePYENVICTEQFVIcIKSGNRPNVEEIleyCPREIISLMERCWQAIPEDRPTFLGIEEEF 286
Cdd:cd05108   193 DVWSYGVTVWELmtFGSK-PYDGIPASEISSI-LEKGERLPQPPI---CTIDVYMIMVKCWMIDADSRPKFRELIIEF 265
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
53-277 9.14e-19

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: 86.99  E-value: 9.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  53 RAEYNEVLLEEGKMMHRLRHSRVVKLLGII-IEEGNYSLVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYL-- 129
Cdd:cd13990    44 KQNYIKHALREYEIHKSLDHPRIVKLYDVFeIDTDSFCTVLEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLne 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 130 HDKGVIHKDLKPENILVDRDFH---IKIADLGVasfktwSKL-TKEKDNKQK-EVSSttkkNNGGTLYYMAPE--HLNDI 202
Cdd:cd13990   124 IKPPIIHYDLKPGNILLHSGNVsgeIKITDFGL------SKImDDESYNSDGmELTS----QGAGTYWYLPPEcfVVGKT 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 203 NAKPTEKSDVYSFGIVLWAIFAKKEPYENVICTEQFV---ICIKS-----GNRPNVEEileycprEIISLMERCWQAIPE 274
Cdd:cd13990   194 PPKISSKVDVWSVGVIFYQMLYGRKPFGHNQSQEAILeenTILKAtevefPSKPVVSS-------EAKDFIRRCLTYRKE 266

                  ...
gi 1333886239 275 DRP 277
Cdd:cd13990   267 DRP 269
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
26-284 1.08e-18

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: 87.02  E-value: 1.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGfVILKKVYTGPNRAEYNEVLLEEGKMMhrlRHSRVVKLLGIIIE-EGNYS---LVMEYMEKGNLM 101
Cdd:cd14220     6 GRYGEVWMGKWRGEK-VAVKVFFTTEEASWFRETEIYQTVLM---RHENILGFIAADIKgTGSWTqlyLITDYHENGSLY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 HVLK-TQIDVPLSLKgrIIVEAIEGMCYLHDK--------GVIHKDLKPENILVDRDFHIKIADLGVAsfktwskLTKEK 172
Cdd:cd14220    82 DFLKcTTLDTRALLK--LAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGTCCIADLGLA-------VKFNS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 173 DNKQKEVSSTTKKnngGTLYYMAP----EHLNDINAKPTEKSDVYSFGIVLWAIFAK----------KEPYENVICTE-- 236
Cdd:cd14220   153 DTNEVDVPLNTRV---GTKRYMAPevldESLNKNHFQAYIMADIYSFGLIIWEMARRcvtggiveeyQLPYYDMVPSDps 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333886239 237 ----QFVICIKS-----GNRPNVEEileyCPREIISLMERCWQAIPEDRPTFLGIEE 284
Cdd:cd14220   230 yedmREVVCVKRlrptvSNRWNSDE----CLRAVLKLMSECWAHNPASRLTALRIKK 282
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
25-231 1.30e-18

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: 85.77  E-value: 1.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSLCYHRSHgfvilKKVYTGP--NRA---EYNEV--LLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEK 97
Cdd:cd05578    10 KGSFGKVCIVQKKDT-----KKMFAMKymNKQkciEKDSVrnVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDLLLG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  98 GNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTWSKLTKEKdnkqk 177
Cdd:cd05578    85 GDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLTDGTLATST----- 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333886239 178 evssttkknnGGTLYYMAPEHLndINAKPTEKSDVYSFGIVLWAIFAKKEPYEN 231
Cdd:cd05578   160 ----------SGTKPYMAPEVF--MRAGYSFAVDWWSLGVTAYEMLRGKRPYEI 201
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
26-290 1.47e-18

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: 87.73  E-value: 1.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHG----------FVILKKVYTGPNRAEyNEVLLEEgkmmhrlrHSR-VVKLLGIIIEEGNYSLVMEY 94
Cdd:cd05573    12 GAFGEVWLVRDKDTGqvyamkilrkSDMLKREQIAHVRAE-RDILADA--------DSPwIVRLHYAFQDEDHLYLVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKGNLMHVLKTQIDVPLSLKGRIIVE---AIEgmcYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTWSKLTKE 171
Cdd:cd05573    83 MPGGDLMNLLIKYDVFPEETARFYIAElvlALD---SLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMNKSGDRES 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 172 KDNKQKEVSSTTKKNNG---------------GTLYYMAPEHLndINAKPTEKSDVYSFGIVLWAIFAKKEPY--ENVIC 234
Cdd:cd05573   160 YLNDSVNTLFQDNVLARrrphkqrrvraysavGTPDYIAPEVL--RGTGYGPECDWWSLGVILYEMLYGFPPFysDSLVE 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1333886239 235 TEQFVI-CIKSGNRPNVEEIleycPREIISLMERCWqAIPEDRptfLGIEEEFR--PFY 290
Cdd:cd05573   238 TYSKIMnWKESLVFPDDPDV----SPEAIDLIRRLL-CDPEDR---LGSAEEIKahPFF 288
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
16-217 1.77e-18

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: 85.43  E-value: 1.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  16 DLLEKtdLDSGGFGKVSLCYHRSHGFVILKKVytgpnraeyneVLLEEGK----------MMHRLRHSRVVKLLGIIIEE 85
Cdd:cd06613     3 ELIQR--IGSGTYGDVYKARNIATGELAAVKV-----------IKLEPGDdfeiiqqeisMLKECRHPNIVAYFGSYLRR 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  86 GNYSLVMEYMEKGNL---MHVLKtqidvPLS--LKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVA 160
Cdd:cd06613    70 DKLWIVMEYCGGGSLqdiYQVTG-----PLSelQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVS 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 161 SfktwskltkekdnkqkEVSSTTKKNNG--GTLYYMAPEHL-NDINAKPTEKSDVYSFGI 217
Cdd:cd06613   145 A----------------QLTATIAKRKSfiGTPYWMAPEVAaVERKGGYDGKCDIWALGI 188
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
71-282 1.91e-18

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 85.86  E-value: 1.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  71 RHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKT----QIDVPLSLKG------------RIIVEAIEGMCYLHDKGV 134
Cdd:cd05047    54 HHPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLRKsrvlETDPAFAIANstastlssqqllHFAADVARGMDYLSQKQF 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 135 IHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnKQKEVssTTKKNNGG-TLYYMAPEHLNdiNAKPTEKSDVY 213
Cdd:cd05047   134 IHRDLAARNILVGENYVAKIADFGLS--------------RGQEV--YVKKTMGRlPVRWMAIESLN--YSVYTTNSDVW 195
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 214 SFGIVLWAIFA-KKEPYENVICTEQFVIcIKSGNRpnVEEILEyCPREIISLMERCWQAIPEDRPTFLGI 282
Cdd:cd05047   196 SYGVLLWEIVSlGGTPYCGMTCAELYEK-LPQGYR--LEKPLN-CDDEVYDLMRQCWREKPYERPSFAQI 261
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
18-230 2.50e-18

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: 85.01  E-value: 2.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  18 LEKTdLDSGGFGKVSLCYHRSHGF-VILKKVytgpNR-----AEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLV 91
Cdd:cd14079     6 LGKT-LGVGSFGKVKLAEHELTGHkVAVKIL----NRqkiksLDMEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  92 MEYMEKGNLM-HVLKtqidvplslKGRII-VEA-------IEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASF 162
Cdd:cd14079    81 MEYVSGGELFdYIVQ---------KGRLSeDEArrffqqiISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNI 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333886239 163 KtwskltkeKDNKQKEVSSttkknngGTLYYMAPEHLN-DINAKPteKSDVYSFGIVLWAIFAKKEPYE 230
Cdd:cd14079   152 M--------RDGEFLKTSC-------GSPNYAAPEVISgKLYAGP--EVDVWSCGVILYALLCGSLPFD 203
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
58-278 3.01e-18

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: 85.39  E-value: 3.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  58 EVLLEEGKMMHRLRHSRVVKLLGIIIE--EGNYSLVMEYMEKGNLMHVlktQIDVPLS-----LKGRIIVEAIEgmcYLH 130
Cdd:cd14200    68 ERVYQEIAILKKLDHVNIVKLIEVLDDpaEDNLYMVFDLLRKGPVMEV---PSDKPFSedqarLYFRDIVLGIE---YLH 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 131 DKGVIHKDLKPENILVDRDFHIKIADLGVASfktwskltkEKDNKQKEVSSTtkknnGGTLYYMAPEHLNDINAKPTEKS 210
Cdd:cd14200   142 YQKIVHRDIKPSNLLLGDDGHVKIADFGVSN---------QFEGNDALLSST-----AGTPAFMAPETLSDSGQSFSGKA 207
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 211 -DVYSFGIVLWAIFAKKEPY-ENVICTEQFVICIKSGNRPNVEEILEycprEIISLMERCWQAIPEDRPT 278
Cdd:cd14200   208 lDVWAMGVTLYCFVYGKCPFiDEFILALHNKIKNKPVEFPEEPEISE----ELKDLILKMLDKNPETRIT 273
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
42-283 3.15e-18

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-C binds and is activated by the intestinal hormones, guanylin (GN) and uroguanylin (UGN), which are secreted after salty meals to inhibit sodium absorption and induce the secretion of chloride, bicarbonate, and water. GN and UGN are also present in the kidney, where they induce increased salt and water secretion. This prevents the development of hypernatremia and hypervolemia after ingestion of high amounts of salt. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-C subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270946 [Multi-domain]  Cd Length: 271  Bit Score: 85.32  E-value: 3.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  42 VILKKV------YTGPNRAEYNEVLleegkmmhRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQIDVP---- 111
Cdd:cd14044    34 VILKDLknnegnFTEKQKIELNKLL--------QIDYYNLTKFYGTVKLDTMIFGVIEYCERGSLRDVLNDKISYPdgtf 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 112 --LSLKGRIIVEAIEGMCYLH-DKGVIHKDLKPENILVDRDFHIKIADLGVASFktwskLTKEKDnkqkevssttkknng 188
Cdd:cd14044   106 mdWEFKISVMYDIAKGMSYLHsSKTEVHGRLKSTNCVVDSRMVVKITDFGCNSI-----LPPSKD--------------- 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 189 gtlYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPYENVICTEQFVICIKSGN-------RPNVE-EILEYCPRE 260
Cdd:cd14044   166 ---LWTAPEHLR--QAGTSQKGDVYSYGIIAQEIILRKETFYTAACSDRKEKIYRVQNpkgmkpfRPDLNlESAGERERE 240
                         250       260
                  ....*....|....*....|...
gi 1333886239 261 IISLMERCWQAIPEDRPTFLGIE 283
Cdd:cd14044   241 VYGLVKNCWEEDPEKRPDFKKIE 263
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
57-286 3.49e-18

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 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: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 85.08  E-value: 3.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  57 NEVLLEEGKMMHRLRHSRVVKLLGIIIEEgNYSLVMEYMEKGNLMHVLKTQidvplslKGRI--------IVEAIEGMCY 128
Cdd:cd05109    53 NKEILDEAYVMAGVGSPYVCRLLGICLTS-TVQLVTQLMPYGCLLDYVREN-------KDRIgsqdllnwCVQIAKGMSY 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 129 LHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnKQKEVSSTTKKNNGGT--LYYMAPEHLndINAKP 206
Cdd:cd05109   125 LEEVRLVHRDLAARNVLVKSPNHVKITDFGLA--------------RLLDIDETEYHADGGKvpIKWMALESI--LHRRF 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 207 TEKSDVYSFGIVLWAI--FAKKePYENVICTEqFVICIKSGNRPNVEEIleyCPREIISLMERCWQAIPEDRPTFLGIEE 284
Cdd:cd05109   189 THQSDVWSYGVTVWELmtFGAK-PYDGIPARE-IPDLLEKGERLPQPPI---CTIDVYMIMVKCWMIDSECRPRFRELVD 263

                  ..
gi 1333886239 285 EF 286
Cdd:cd05109   264 EF 265
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
11-279 3.53e-18

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 85.76  E-value: 3.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  11 KMASSDLLEKTDLDSGGFGKVSLC----------------YHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSR 74
Cdd:cd05096     1 KFPRGHLLFKEKLGEGQFGEVHLCevvnpqdlptlqfpfnVRKGRPLLVAVKILRPDANKNARNDFLKEVKILSRLKDPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  75 VVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQI----------DVPLSLKGRII---------VEAIEGMCYLHDKGVI 135
Cdd:cd05096    81 IIRLLGVCVDEDPLCMITEYMENGDLNQFLSSHHlddkeengndAVPPAHCLPAIsyssllhvaLQIASGMKYLSSLNFV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 136 HKDLKPENILVDRDFHIKIADLGVasfktwSKLTKEKDNKQKEVSSTTKknnggtLYYMAPEHLndINAKPTEKSDVYSF 215
Cdd:cd05096   161 HRDLATRNCLVGENLTIKIADFGM------SRNLYAGDYYRIQGRAVLP------IRWMAWECI--LMGKFTTASDVWAF 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333886239 216 GIVLWAIFA--KKEPYENVicTEQFVIciksgnrPNVEEILE------------YCPREIISLMERCWQAIPEDRPTF 279
Cdd:cd05096   227 GVTLWEILMlcKEQPYGEL--TDEQVI-------ENAGEFFRdqgrqvylfrppPCPQGLYELMLQCWSRDCRERPSF 295
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
25-228 3.56e-18

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: 84.99  E-value: 3.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVL 104
Cdd:cd06609    11 KGSFGEVYKGIDKRTNQVVAIKVIDLEEAEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIMEYCGGGSVLDLL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 105 KTQIDvPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwskltkekdnkqkEVSSTTK 184
Cdd:cd06609    91 KPGPL-DETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSG----------------QLTSTMS 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1333886239 185 KNNG--GTLYYMAPEHLNdiNAKPTEKSDVYSFGIVlwAI-FAKKEP 228
Cdd:cd06609   154 KRNTfvGTPFWMAPEVIK--QSGYDEKADIWSLGIT--AIeLAKGEP 196
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
23-269 3.82e-18

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: 84.62  E-value: 3.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPN--RAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNL 100
Cdd:cd14116    13 LGKGKFGNVYLAREKQSKFILALKVLFKAQleKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 MHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasfktWSkltkekdnkqKEVS 180
Cdd:cd14116    93 YRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFG------WS----------VHAP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 181 STTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPYENVICTE----------QFVICIKSGNRPNV 250
Cdd:cd14116   157 SSRRTTLCGTLDYLPPEMIE--GRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQEtykrisrvefTFPDFVTEGARDLI 234
                         250       260
                  ....*....|....*....|..
gi 1333886239 251 EEILEYCPREIISL---MERCW 269
Cdd:cd14116   235 SRLLKHNPSQRPMLrevLEHPW 256
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
26-230 4.16e-18

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: 84.49  E-value: 4.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGFVILKKVYtgpNRAEYN----EVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLM 101
Cdd:cd14072    11 GNFAKVKLARHVLTGREVAIKII---DKTQLNpsslQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYASGGEVF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 HVLKTQ---IDVPLSLKGRIIVEAIEgmcYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwskltkekdnkqkE 178
Cdd:cd14072    88 DYLVAHgrmKEKEARAKFRQIVSAVQ---YCHQKRIVHRDLKAENLLLDADMNIKIADFGFSN----------------E 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333886239 179 VSSTTKKNN-GGTLYYMAPEHLNDINAKPTEkSDVYSFGIVLWAIFAKKEPYE 230
Cdd:cd14072   149 FTPGNKLDTfCGSPPYAAPELFQGKKYDGPE-VDVWSLGVILYTLVSGSLPFD 200
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
14-229 4.65e-18

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: 85.11  E-value: 4.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  14 SSDLLEKTDLDSGGFGKVSLCYHRSHGFVI-LKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVM 92
Cdd:cd06616     5 AEDLKDLGEIGRGAFGTVNKMLHKPSGTIMaVKRIRSTVDEKEQKRLLMDLDVVMRSSDCPYIVKFYGALFREGDCWICM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  93 EYM----EKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDK-GVIHKDLKPENILVDRDFHIKIADLGVASfktwsk 167
Cdd:cd06616    85 ELMdislDKFYKYVYEVLDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGNIKLCDFGISG------ 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333886239 168 ltkekdnkqKEVSSTTKKNNGGTLYYMAPEHL--NDINAKPTEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd06616   159 ---------QLVDSIAKTRDAGCRPYMAPERIdpSASRDGYDVRSDVWSLGITLYEVATGKFPY 213
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
58-286 5.34e-18

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer 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: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 84.60  E-value: 5.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  58 EVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSL-----VMEYMEKGNL-MHVLKTQID-----VPLSLKGRIIVEAIEGM 126
Cdd:cd14204    54 EEFLSEAACMKDFNHPNVIRLLGVCLEVGSQRIpkpmvILPFMKYGDLhSFLLRSRLGsgpqhVPLQTLLKFMIDIALGM 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 127 CYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwSKLTKEKDNKQKEVSSTTKKnnggtlyYMAPEHLNDinAKP 206
Cdd:cd14204   134 EYLSSRNFLHRDLAARNCMLRDDMTVCVADFGLS-----KKIYSGDYYRQGRIAKMPVK-------WIAVESLAD--RVY 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 207 TEKSDVYSFGIVLWAIFAK-KEPYENVICTEQFVICIKsGNRPNVEeilEYCPREIISLMERCWQAIPEDRPTFLGIEEE 285
Cdd:cd14204   200 TVKSDVWAFGVTMWEIATRgMTPYPGVQNHEIYDYLLH-GHRLKQP---EDCLDELYDIMYSCWRSDPTDRPTFTQLREN 275

                  .
gi 1333886239 286 F 286
Cdd:cd14204   276 L 276
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
23-229 5.65e-18

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: 84.24  E-value: 5.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEGkMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMH 102
Cdd:cd14192    12 LGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEVKNEIN-IMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGELFD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLK------TQIDVPLSLKgriivEAIEGMCYLHDKGVIHKDLKPENIL-VDRDFH-IKIADLGVA-SFKTWSKLtkekd 173
Cdd:cd14192    91 RITdesyqlTELDAILFTR-----QICEGVHYLHQHYILHLDLKPENILcVNSTGNqIKIIDFGLArRYKPREKL----- 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333886239 174 nkqkevssttkKNNGGTLYYMAPEHLN-DINAKPTeksDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14192   161 -----------KVNFGTPEFLAPEVVNyDFVSFPT---DMWSVGVITYMLLSGLSPF 203
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
23-229 6.28e-18

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: 84.66  E-value: 6.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHG-FVILKKVYTGPnrAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLM 101
Cdd:cd14166    11 LGSGAFSEVYLVKQRSTGkLYALKCIKKSP--LSRDSSLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQLVSGGELF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 -HVLK----TQIDVplslkGRIIVEAIEGMCYLHDKGVIHKDLKPENILV---DRDFHIKIADLGvasfktwskLTKEKD 173
Cdd:cd14166    89 dRILErgvyTEKDA-----SRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFG---------LSKMEQ 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333886239 174 NKqkeVSSTTkknnGGTLYYMAPEHLNDinaKPTEKS-DVYSFGIVLWAIFAKKEPY 229
Cdd:cd14166   155 NG---IMSTA----CGTPGYVAPEVLAQ---KPYSKAvDCWSIGVITYILLCGYPPF 201
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
23-201 6.90e-18

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: 85.10  E-value: 6.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFV----ILKKvytgpnraeynEVLLEEGKMMHRLRHSRVVK------LLGIiieegNYSL-- 90
Cdd:cd05571     3 LGKGTFGKVILCREKATGELyaikILKK-----------EVIIAKDEVAHTLTENRVLQntrhpfLTSL-----KYSFqt 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  91 ------VMEYMEKGNLM-HVLKTQI--DVPLSLKGRIIVEAIEgmcYLHDKGVIHKDLKPENILVDRDFHIKIADLGvas 161
Cdd:cd05571    67 ndrlcfVMEYVNGGELFfHLSRERVfsEDRTRFYGAEIVLALG---YLHSQGIVYRDLKLENLLLDKDGHIKITDFG--- 140
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1333886239 162 fktwskLTKEkdnkqkEVS-STTKKNNGGTLYYMAPEHLND 201
Cdd:cd05571   141 ------LCKE------EISyGATTKTFCGTPEYLAPEVLED 169
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
23-229 7.21e-18

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: 83.92  E-value: 7.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGF-VILKKVYTGPNRAEYNEVL--LE-EGKMMHRLRHSRVVKLLGII--IEEGNYSLVMEYME 96
Cdd:cd06653    10 LGRGAFGEVYLCYDADTGReLAVKQVPFDPDSQETSKEVnaLEcEIQLLKNLRHDRIVQYYGCLrdPEEKKLSIFVEYMP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  97 KGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkeKDNKQ 176
Cdd:cd06653    90 GGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGAS-----------KRIQT 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333886239 177 KEVSSTTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd06653   159 ICMSGTGIKSVTGTPYWMSPEVIS--GEGYGRKADVWSVACTVVEMLTEKPPW 209
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
46-284 9.35e-18

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: 84.34  E-value: 9.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  46 KVYTGPNRAEY-NEVLLEEGKMMHrlrHSRVVKLLGI---IIEEG--NYSLVMEYMEKGNLMHVLKTQ-IDVPLSLkgRI 118
Cdd:cd14054    24 KVFPARHRQNFqNEKDIYELPLME---HSNILRFIGAderPTADGrmEYLLVLEYAPKGSLCSYLRENtLDWMSSC--RM 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 119 IVEAIEGMCYLHDK---------GVIHKDLKPENILVDRDFHIKIADLGVASFKTWSKLTKekdnKQKEVSSTTKKNNGG 189
Cdd:cd14054    99 ALSLTRGLAYLHTDlrrgdqykpAIAHRDLNSRNVLVKADGSCVICDFGLAMVLRGSSLVR----GRPGAAENASISEVG 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 190 TLYYMAPEHLND-INAKPTEKS----DVYSFGIVLWAIFAK-------------KEPYE----NVICTEQFVICIKSGNR 247
Cdd:cd14054   175 TLRYMAPEVLEGaVNLRDCESAlkqvDVYALGLVLWEIAMRcsdlypgesvppyQMPYEaelgNHPTFEDMQLLVSREKA 254
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1333886239 248 ----PNVEEILEYCPREIISLMERCWQAIPEDRPTFLGIEE 284
Cdd:cd14054   255 rpkfPDAWKENSLAVRSLKETIEDCWDQDAEARLTALCVEE 295
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
26-278 1.05e-17

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: 83.27  E-value: 1.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYH-RSHGFVILKKV-YTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYM--EKGNLM 101
Cdd:cd06607    12 GSFGAVYYARNkRTSEVVAIKKMsYSGKQSTEKWQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVMEYClgSASDIV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 HVLKTQI-DVPLSlkgRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFktwskltkeKDNKQKEVs 180
Cdd:cd06607    92 EVHKKPLqEVEIA---AICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSASL---------VCPANSFV- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 181 sttkknngGTLYYMAPEHLNDINAKP-TEKSDVYSFGIVLWAIFAKKEPYENVICTEQfVICIKSGNRPNVEEIlEYcPR 259
Cdd:cd06607   159 --------GTPYWMAPEVILAMDEGQyDGKVDVWSLGITCIELAERKPPLFNMNAMSA-LYHIAQNDSPTLSSG-EW-SD 227
                         250
                  ....*....|....*....
gi 1333886239 260 EIISLMERCWQAIPEDRPT 278
Cdd:cd06607   228 DFRNFVDSCLQKIPQDRPS 246
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
16-300 1.06e-17

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: 83.74  E-value: 1.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  16 DLLEKTD-LDSGGFGKVSLCYHRSHGFVI-LKKVYTGPNRAEYNEVLLEEgKMMHRLRHSRVVKLLGIIIEEGNYSLVME 93
Cdd:cd06622     1 DEIEVLDeLGKGNYGSVYKVLHRPTGVTMaMKEIRLELDESKFNQIIMEL-DILHKAVSPYIVDFYGAFFIEGAVYMCME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  94 YMEKGNLMHVLKTQID---VPLSLKGRIIVEAIEGMCYLHDK-GVIHKDLKPENILVDRDFHIKIADLGVASfktwsklt 169
Cdd:cd06622    80 YMDAGSLDKLYAGGVAtegIPEDVLRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGNGQVKLCDFGVSG-------- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 170 kekdnkqkEVSSTTKKNNGGTLYYMAPEHLNDINAKP----TEKSDVYSFGIVLWAIFAKKEPYENVICTEQF--VICIK 243
Cdd:cd06622   152 --------NLVASLAKTNIGCQSYMAPERIKSGGPNQnptyTVQSDVWSLGLSILEMALGRYPYPPETYANIFaqLSAIV 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333886239 244 SGNRPNVEEilEYCPrEIISLMERCWQAIPEDRPTFLGIEEEfrPFYLS------HFEEYVEE 300
Cdd:cd06622   224 DGDPPTLPS--GYSD-DAQDFVAKCLNKIPNRRPTYAQLLEH--PWLVKyknadvDMAEWVTG 281
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
23-229 1.08e-17

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: 83.55  E-value: 1.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGF-VILKKVYTGPNRAEYNEVL--LE-EGKMMHRLRHSRVVKLLGII--IEEGNYSLVMEYME 96
Cdd:cd06652    10 LGQGAFGRVYLCYDADTGReLAVKQVQFDPESPETSKEVnaLEcEIQLLKNLLHERIVQYYGCLrdPQERTLSIFMEYMP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  97 KGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkeKDNKQ 176
Cdd:cd06652    90 GGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGAS-----------KRLQT 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333886239 177 KEVSSTTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd06652   159 ICLSGTGMKSVTGTPYWMSPEVIS--GEGYGRKADIWSVGCTVVEMLTEKPPW 209
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
24-279 1.30e-17

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: 84.65  E-value: 1.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  24 DSGGFGKVSLCYHrshgfVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVM-EYMEKGNLMH 102
Cdd:cd05103    27 DAFGIDKTATCRT-----VAVKMLKEGATHSEHRALMSELKILIHIGHHLNVVNLLGACTKPGGPLMVIvEFCKFGNLSA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLKTQ---------------------IDVPLSLKGRI-------------IVE--------------------------- 121
Cdd:cd05103   102 YLRSKrsefvpyktkgarfrqgkdyvGDISVDLKRRLdsitssqssassgFVEekslsdveeeeagqedlykdfltledl 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 122 ------AIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwSKLTKEKDNKQKEVSSTTKKnnggtlyYMA 195
Cdd:cd05103   182 icysfqVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLA-----RDIYKDPDYVRKGDARLPLK-------WMA 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 196 PEHLNDinAKPTEKSDVYSFGIVLWAIFA-KKEPYENVICTEQFVICIKSGNRPNVEeilEYCPREIISLMERCWQAIPE 274
Cdd:cd05103   250 PETIFD--RVYTIQSDVWSFGVLLWEIFSlGASPYPGVKIDEEFCRRLKEGTRMRAP---DYTTPEMYQTMLDCWHGEPS 324

                  ....*
gi 1333886239 275 DRPTF 279
Cdd:cd05103   325 QRPTF 329
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
84-219 1.44e-17

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 86.39  E-value: 1.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  84 EEGNYS-LVMEYMEKGNLMHVLKTQidVPLSLKG--RIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVA 160
Cdd:NF033483   77 EDGGIPyIVMEYVDGRTLKDYIREH--GPLSPEEavEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIA 154
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333886239 161 sfktwskltkekdnkqKEVSSTTKKNNG---GTLYYMAPEHLNDINAkpTEKSDVYSFGIVL 219
Cdd:NF033483  155 ----------------RALSSTTMTQTNsvlGTVHYLSPEQARGGTV--DARSDIYSLGIVL 198
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
27-229 1.45e-17

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: 83.11  E-value: 1.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  27 GFGKVSLCYH-RSHG---FVILKKVytgpNRAEYNEVLlEEGKMMHRLRHSRVVKLLGIIiEEGNYS-LVMEYMEKGNLM 101
Cdd:cd14010     9 GRGKHSVVYKgRRKGtieFVAIKCV----DKSKRPEVL-NEVRLTHELKHPNVLKFYEWY-ETSNHLwLVVEYCTGGDLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 HVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVA------SFKTWSKLTKEKDNK 175
Cdd:cd14010    83 TLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLArregeiLKELFGQFSDEGNVN 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1333886239 176 QKEVSSTTKknngGTLYYMAPEHL-NDINAKpteKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14010   163 KVSKKQAKR----GTPYYMAPELFqGGVHSF---ASDLWALGCVLYEMFTGKPPF 210
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
23-229 1.49e-17

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


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 83.65  E-value: 1.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHG-FVILKKVYTGPNRAEYN-EVLLEEGKMMHRLRHSRVVKL------LGIIIEEGNYSLVMEY 94
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTGeYVAIKKCRQELSPSDKNrERWCLEVQIMKKLNHPNVVSArdvppeLEKLSPNDLPLLAMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKGNLMHVLkTQIDVPLSLKG---RIIVEAI-EGMCYLHDKGVIHKDLKPENILV----DRDFHiKIADLGVAsfktws 166
Cdd:cd13989    81 CSGGDLRKVL-NQPENCCGLKEsevRTLLSDIsSAISYLHENRIIHRDLKPENIVLqqggGRVIY-KLIDLGYA------ 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333886239 167 kltKEKDnKQKEVSSTTkknngGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd13989   153 ---KELD-QGSLCTSFV-----GTLQYLAPELFE--SKKYTCTVDYWSFGTLAFECITGYRPF 204
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
26-278 1.53e-17

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: 82.87  E-value: 1.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHG--FVILKKVYTGPNRAEyNEVLLEEGKMMHRLRHSRVVKLL-GIIIEEGNYSLVMEYMEKGNLMH 102
Cdd:cd08223    11 GSYGEVWLVRHKRDRkqYVIKKLNLKNASKRE-RKAAEQEAKLLSKLKHPNIVSYKeSFEGEDGFLYIVMGFCEGGDLYT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLKTQIDVPLSlkGRIIVE-----AIeGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnKQK 177
Cdd:cd08223    90 RLKEQKGVLLE--ERQVVEwfvqiAM-ALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIA--------------RVL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 178 EVSSTTKKNNGGTLYYMAPEHLNDinaKP-TEKSDVYSFGIVLWAIFAKKEPYeNVICTEQFVICIKSGNRPNVEEilEY 256
Cdd:cd08223   153 ESSSDMATTLIGTPYYMSPELFSN---KPyNHKSDVWALGCCVYEMATLKHAF-NAKDMNSLVYKILEGKLPPMPK--QY 226
                         250       260
                  ....*....|....*....|..
gi 1333886239 257 CPrEIISLMERCWQAIPEDRPT 278
Cdd:cd08223   227 SP-ELGELIKAMLHQDPEKRPS 247
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
25-278 1.58e-17

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: 83.71  E-value: 1.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSLCYHRSHGFVI-LKKVYTGP---NRaeynevlleEGKMMHRLRHSRVVKLLG-IIIEEGNYS-----LVMEY 94
Cdd:cd14137    14 SGSFGVVYQAKLLETGEVVaIKKVLQDKrykNR---------ELQIMRRLKHPNIVKLKYfFYSSGEKKDevylnLVMEY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKgNL----MHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHI-KIADLGVAsfktwsklt 169
Cdd:cd14137    85 MPE-TLyrviRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPETGVlKLCDFGSA--------- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 170 KEKDNKQKEVSSTtkknngGTLYYMAPEHLndINAKP-TEKSDVYSFGIVL------WAIFAKKEPyenvicTEQFVICI 242
Cdd:cd14137   155 KRLVPGEPNVSYI------CSRYYRAPELI--FGATDyTTAIDIWSAGCVLaelllgQPLFPGESS------VDQLVEII 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 243 KSGNRPNVEEILE------------------------YCPREIISLMERCWQAIPEDRPT 278
Cdd:cd14137   221 KVLGTPTREQIKAmnpnytefkfpqikphpwekvfpkRTPPDAIDLLSKILVYNPSKRLT 280
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
124-284 1.68e-17

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: 85.08  E-value: 1.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 124 EGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwskltkekdNKQKEVSSTTKKNNGGTLYYMAPEHLNDin 203
Cdd:cd05105   248 RGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLAR------------DIMHDSNYVSKGSTFLPVKWMAPESIFD-- 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 204 AKPTEKSDVYSFGIVLWAIFA-KKEPYENVICTEQFVICIKSGNRPNVEEileYCPREIISLMERCWQAIPEDRPTFLGI 282
Cdd:cd05105   314 NLYTTLSDVWSYGILLWEIFSlGGTPYPGMIVDSTFYNKIKSGYRMAKPD---HATQEVYDIMVKCWNSEPEKRPSFLHL 390

                  ..
gi 1333886239 283 EE 284
Cdd:cd05105   391 SD 392
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
63-278 1.70e-17

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: 82.69  E-value: 1.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  63 EGKMMHRLRHSRVVKLLGIII--EEGNYSLVMEYMeKGNLMHVLKTQID--VPLSLKGRIIVEAIEGMCYLHDKGVIHKD 138
Cdd:cd14119    44 EIQILRRLNHRNVIKLVDVLYneEKQKLYMVMEYC-VGGLQEMLDSAPDkrLPIWQAHGYFVQLIDGLEYLHSQGIIHKD 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 139 LKPENILVDRDFHIKIADLGVAsfktwskltkekDNKQKEVSSTTKKNNGGTLYYMAPEHLNDINAKPTEKSDVYSFGIV 218
Cdd:cd14119   123 IKPGNLLLTTDGTLKISDFGVA------------EALDLFAEDDTCTTSQGSPAFQPPEIANGQDSFSGFKVDIWSAGVT 190
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333886239 219 LWAIFAKKEPYE--------NVICTEQFVIciksgnRPNVEEILEycpreiiSLMERCWQAIPEDRPT 278
Cdd:cd14119   191 LYNMTTGKYPFEgdniyklfENIGKGEYTI------PDDVDPDLQ-------DLLRGMLEKDPEKRFT 245
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
23-229 2.06e-17

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: 82.82  E-value: 2.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVIL-KKVYTGPNRAEYNE---VLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLV--MEYME 96
Cdd:cd06651    15 LGQGAFGRVYLCYDVDTGRELAaKQVQFDPESPETSKevsALECEIQLLKNLQHERIVQYYGCLRDRAEKTLTifMEYMP 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  97 KGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkeKDNKQ 176
Cdd:cd06651    95 GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGAS-----------KRLQT 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333886239 177 KEVSSTTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd06651   164 ICMSGTGIRSVTGTPYWMSPEVIS--GEGYGRKADVWSLGCTVVEMLTEKPPW 214
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
11-228 2.31e-17

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: 83.94  E-value: 2.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  11 KMASSDLLEKTDLDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSL 90
Cdd:cd06649     1 ELKDDDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  91 VMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDK-GVIHKDLKPENILVDRDFHIKIADLGVASfktwsklt 169
Cdd:cd06649    81 CMEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRGEIKLCDFGVSG-------- 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1333886239 170 kekdnkqkEVSSTTKKNNGGTLYYMAPEHLNDINAkpTEKSDVYSFGIVLWAIFAKKEP 228
Cdd:cd06649   153 --------QLIDSMANSFVGTRSYMSPERLQGTHY--SVQSDIWSMGLSLVELAIGRYP 201
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
23-229 2.49e-17

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: 83.01  E-value: 2.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGfvilkKVYTGPN--------RAEYNEVLLEEgKMMHRLrHSRVVKLLGIIIE-EGNYSLVME 93
Cdd:cd05608     9 LGKGGFGEVSACQMRATG-----KLYACKKlnkkrlkkRKGYEGAMVEK-RILAKV-HSRFIVSLAYAFQtKTDLCLVMT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  94 YMEKGNL-MHVLKTQIDVPLSLKGRII---VEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwsklT 169
Cdd:cd05608    82 IMNGGDLrYHIYNVDEENPGFQEPRACfytAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLA--------V 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 170 KEKDNKQKevssttKKNNGGTLYYMAPEHLNDinAKPTEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd05608   154 ELKDGQTK------TKGYAGTPGFMAPELLLG--EEYDYSVDYFTLGVTLYEMIAARGPF 205
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
44-282 2.65e-17

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB 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: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 82.22  E-value: 2.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  44 LKKVYTGPNRAEYnevlLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKtQID---VPLSLKGriIV 120
Cdd:cd05065    40 LKSGYTEKQRRDF----LSEASIMGQFDHPNIIHLEGVVTKSRPVMIITEFMENGALDSFLR-QNDgqfTVIQLVG--ML 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 121 EAI-EGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFktwskltKEKDNKQKEVSSTTkknnGGTL--YYMAPE 197
Cdd:cd05065   113 RGIaAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRF-------LEDDTSDPTYTSSL----GGKIpiRWTAPE 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 198 HLNdiNAKPTEKSDVYSFGIVLWAIFAKKE-PYENVicTEQFVI-CIKSGNR--PNVEeileyCPREIISLMERCWQAIP 273
Cdd:cd05065   182 AIA--YRKFTSASDVWSYGIVMWEVMSYGErPYWDM--SNQDVInAIEQDYRlpPPMD-----CPTALHQLMLDCWQKDR 252

                  ....*....
gi 1333886239 274 EDRPTFLGI 282
Cdd:cd05065   253 NLRPKFGQI 261
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
23-229 2.87e-17

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: 82.17  E-value: 2.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVY---TGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGN 99
Cdd:cd14070    10 LGEGSFAKVREGLHAVTGEKVAIKVIdkkKAKKDSYVTKNLRREGRIQQMIRHPNITQLLDILETENSYYLVMELCPGGN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 100 LMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTWSKLTKEKDNKqkev 179
Cdd:cd14070    90 LMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAGILGYSDPFSTQ---- 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1333886239 180 ssttkknnGGTLYYMAPEHLNDINAKPteKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14070   166 --------CGSPAYAAPELLARKKYGP--KVDVWSIGVNMYAMLTGTLPF 205
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
26-230 2.92e-17

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: 82.37  E-value: 2.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRS-HGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNL---M 101
Cdd:cd14202    13 GAFAVVFKGRHKEkHDLEVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDFQEIANSVYLVMEYCNGGDLadyL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 HVLKTQIDVPLslkgRIIVEAIEG-MCYLHDKGVIHKDLKPENILVD---------RDFHIKIADLGVASFKTwskltke 171
Cdd:cd14202    93 HTMRTLSEDTI----RLFLQQIAGaMKMLHSKGIIHRDLKPQNILLSysggrksnpNNIRIKIADFGFARYLQ------- 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1333886239 172 kdnkqkevSSTTKKNNGGTLYYMAPEHLndINAKPTEKSDVYSFGIVLWAIFAKKEPYE 230
Cdd:cd14202   162 --------NNMMAATLCGSPMYMAPEVI--MSQHYDAKADLWSIGTIIYQCLTGKAPFQ 210
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
124-279 3.08e-17

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 84.13  E-value: 3.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 124 EGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltKEKDNKQKEVsstTKKNNGGTLYYMAPEHLNDin 203
Cdd:cd05106   223 QGMDFLASKNCIHRDVAARNVLLTDGRVAKICDFGLA---------RDIMNDSNYV---VKGNARLPVKWMAPESIFD-- 288
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 204 AKPTEKSDVYSFGIVLWAIFA-KKEPYENVICTEQFVICIKSG---NRPnveeilEYCPREIISLMERCWQAIPEDRPTF 279
Cdd:cd05106   289 CVYTVQSDVWSYGILLWEIFSlGKSPYPGILVNSKFYKMVKRGyqmSRP------DFAPPEIYSIMKMCWNLEPTERPTF 362
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
23-272 3.38e-17

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: 82.00  E-value: 3.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLC-YHRSHGFV----ILKKVYTGPNRAEYNEVlleegKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEK 97
Cdd:cd14167    11 LGTGAFSEVVLAeEKRTQKLVaikcIAKKALEGKETSIENEI-----AVLHKIKHPNIVALDDIYESGGHLYLIMQLVSG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  98 GNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENIL---VDRDFHIKIADLGVasfktwSKLtkekdn 174
Cdd:cd14167    86 GELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGL------SKI------ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 175 kqkEVSSTTKKNNGGTLYYMAPEHLNDinaKPTEKS-DVYSFGIVLWAIFAKKEPYENVICTEQFVICIKSG---NRPNV 250
Cdd:cd14167   154 ---EGSGSVMSTACGTPGYVAPEVLAQ---KPYSKAvDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEyefDSPYW 227
                         250       260
                  ....*....|....*....|....*....
gi 1333886239 251 EEILEYCPREIISLMER-------CWQAI 272
Cdd:cd14167   228 DDISDSAKDFIQHLMEKdpekrftCEQAL 256
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
23-218 3.62e-17

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: 81.50  E-value: 3.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLlEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLM- 101
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKDREDVR-NEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGELFe 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 ------HVLkTQIDVPLSLkgRIIVEAIEgmcYLHDKGVIHKDLKPENIL-VDRD-FHIKIADLGVAsfktwskltkekd 173
Cdd:cd14103    80 rvvdddFEL-TERDCILFM--RQICEGVQ---YMHKQGILHLDLKPENILcVSRTgNQIKIIDFGLA------------- 140
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1333886239 174 nkQKEVSSTTKKNNGGTLYYMAPEHLNDINAKPTekSDVYSFGIV 218
Cdd:cd14103   141 --RKYDPDKKLKVLFGTPEFVAPEVVNYEPISYA--TDMWSVGVI 181
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
22-278 3.74e-17

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: 82.78  E-value: 3.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  22 DLDSGGFGKVSLCYH-RSHGFVILKKV-YTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYM--EK 97
Cdd:cd06633    28 EIGHGSFGAVYFATNsHTNEVVAIKKMsYSGKQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEYClgSA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  98 GNLMHVLKTQI-DVPLSlkgRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFktwskltkekdnkq 176
Cdd:cd06633   108 SDLLEVHKKPLqEVEIA---AITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASI-------------- 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 177 kevsSTTKKNNGGTLYYMAPEHLNDINAKPTE-KSDVYSFGIVLWAIFAKKEPYENVICTEQfVICIKSGNRPNVEEilE 255
Cdd:cd06633   171 ----ASPANSFVGTPYWMAPEVILAMDEGQYDgKVDIWSLGITCIELAERKPPLFNMNAMSA-LYHIAQNDSPTLQS--N 243
                         250       260
                  ....*....|....*....|...
gi 1333886239 256 YCPREIISLMERCWQAIPEDRPT 278
Cdd:cd06633   244 EWTDSFRGFVDYCLQKIPQERPS 266
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
70-284 4.43e-17

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: 82.14  E-value: 4.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  70 LRHSRVVKLLGI-IIEEGNYS---LVMEYMEKGNLMHVLKTQIDVPLSLkGRIIVEAIEGMCYLHDK--------GVIHK 137
Cdd:cd14144    46 MRHENILGFIAAdIKGTGSWTqlyLITDYHENGSLYDFLRGNTLDTQSM-LKLAYSAACGLAHLHTEifgtqgkpAIAHR 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 138 DLKPENILVDRDFHIKIADLGVASfktwskltkeKDNKQKEVSSTTKKNNGGTLYYMAPEHLNDINAK----PTEKSDVY 213
Cdd:cd14144   125 DIKSKNILVKKNGTCCIADLGLAV----------KFISETNEVDLPPNTRVGTKRYMAPEVLDESLNRnhfdAYKMADMY 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 214 SFGIVLWAIFAK----------KEPYENVICTE------QFVICIKsGNRPNV------EEILeycpREIISLMERCWQA 271
Cdd:cd14144   195 SFGLVLWEIARRcisggiveeyQLPYYDAVPSDpsyedmRRVVCVE-RRRPSIpnrwssDEVL----RTMSKLMSECWAH 269
                         250
                  ....*....|...
gi 1333886239 272 IPEDRPTFLGIEE 284
Cdd:cd14144   270 NPAARLTALRVKK 282
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
23-277 4.52e-17

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: 81.77  E-value: 4.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHG-FVILKKVYTGPNRAEynevllEEGKMMHRLRHSRVVKLLG--------IIIEEGNYSLV-- 91
Cdd:cd14047    14 IGSGGFGQVFKAKHRIDGkTYAIKRVKLNNEKAE------REVKALAKLDHPNIVRYNGcwdgfdydPETSSSNSSRSkt 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  92 ------MEYMEKGNLMHVL----KTQIDVPLSLkgRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLG-VA 160
Cdd:cd14047    88 kclfiqMEFCEKGTLESWIekrnGEKLDKVLAL--EIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDFGlVT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 161 SFKTWSKLTKEKdnkqkevssttkknngGTLYYMAPEHLNDINAKptEKSDVYSFGIVLWAIFAKkepYENVICTEQFVI 240
Cdd:cd14047   166 SLKNDGKRTKSK----------------GTLSYMSPEQISSQDYG--KEVDIYALGLILFELLHV---CDSAFEKSKFWT 224
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1333886239 241 CIKSGNRPnveeiLEYCPREII--SLMERCWQAIPEDRP 277
Cdd:cd14047   225 DLRNGILP-----DIFDKRYKIekTIIKKMLSKKPEDRP 258
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
90-278 5.09e-17

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: 81.28  E-value: 5.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  90 LVMEYMEKGNLMHVL----KTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVasfktw 165
Cdd:cd08530    76 IVMEYAPFGDLSKLIskrkKKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGI------ 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 166 SKLTKekdnkqkevsSTTKKNNGGTLYYMAPEHLNDinaKP-TEKSDVYSFGIVLWAIFAKKEPYEnVICTEQFVICIKS 244
Cdd:cd08530   150 SKVLK----------KNLAKTQIGTPLYAAPEVWKG---RPyDYKSDIWSLGCLLYEMATFRPPFE-ARTMQELRYKVCR 215
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1333886239 245 GNRPNVEEILEycpREIISLMERCWQAIPEDRPT 278
Cdd:cd08530   216 GKFPPIPPVYS---QDLQQIIRSLLQVNPKKRPS 246
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
70-284 5.61e-17

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: 81.72  E-value: 5.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  70 LRHSRVvklLGIII----EEGNYS---LVMEYMEKGNLMHVLkTQIDVPLSLKGRIIVEAIEGMCYLHDK--------GV 134
Cdd:cd14143    46 LRHENI---LGFIAadnkDNGTWTqlwLVSDYHEHGSLFDYL-NRYTVTVEGMIKLALSIASGLAHLHMEivgtqgkpAI 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 135 IHKDLKPENILVDRDFHIKIADLGVASfktwskltkekdnKQKEVSSTTKKNNG---GTLYYMAPEHLND-INAKPTE-- 208
Cdd:cd14143   122 AHRDLKSKNILVKKNGTCCIADLGLAV-------------RHDSATDTIDIAPNhrvGTKRYMAPEVLDDtINMKHFEsf 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 209 -KSDVYSFGIVLWAIFAK----------KEPYENVICTE------QFVICIKsGNRPNVEEILEYCP--REIISLMERCW 269
Cdd:cd14143   189 kRADIYALGLVFWEIARRcsiggihedyQLPYYDLVPSDpsieemRKVVCEQ-KLRPNIPNRWQSCEalRVMAKIMRECW 267
                         250
                  ....*....|....*
gi 1333886239 270 QAIPEDRPTFLGIEE 284
Cdd:cd14143   268 YANGAARLTALRIKK 282
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
15-229 5.64e-17

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 82.56  E-value: 5.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  15 SDLLEKTDLDSGGFGKVSLCYHRSHG----FVILKKVYTgpNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSL 90
Cdd:PTZ00263   18 SDFEMGETLGTGSFGRVRIAKHKGTGeyyaIKCLKKREI--LKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  91 VMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltk 170
Cdd:PTZ00263   96 LLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFA---------- 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 171 ekdnkqKEVSSTTkKNNGGTLYYMAPEhlnDINAKPTEKS-DVYSFGIVLWAIFAKKEPY 229
Cdd:PTZ00263  166 ------KKVPDRT-FTLCGTPEYLAPE---VIQSKGHGKAvDWWTMGVLLYEFIAGYPPF 215
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
26-224 6.93e-17

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


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 81.85  E-value: 6.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHG-FVILKKVYTGPnRAEYNE----VLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEkGNL 100
Cdd:cd07841    11 GTYAVVYKARDKETGrIVAIKKIKLGE-RKEAKDginfTALREIKLLQELKHPNIIGLLDVFGHKSNINLVFEFME-TDL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 MHVLKTQIDV--PLSLKGrIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVA-SFktwskltkekdnkqk 177
Cdd:cd07841    89 EKVIKDKSIVltPADIKS-YMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLArSF--------------- 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1333886239 178 eVSSTTK-KNNGGTLYYMAPEHLndINAKpteksdVYSFGIVLWA---IFA 224
Cdd:cd07841   153 -GSPNRKmTHQVVTRWYRAPELL--FGAR------HYGVGVDMWSvgcIFA 194
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
15-278 1.02e-16

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: 81.64  E-value: 1.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  15 SDLLEktdLDSGGFGKVSLCYH-RSHGFVILKKV-YTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVM 92
Cdd:cd06635    28 SDLRE---IGHGSFGAVYFARDvRTSEVVAIKKMsYSGKQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVM 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  93 EYM--EKGNLMHVLKT---QIDVPLSLKGriiveAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFktwsk 167
Cdd:cd06635   105 EYClgSASDLLEVHKKplqEIEIAAITHG-----ALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASI----- 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 168 ltkekdnkqkevsSTTKKNNGGTLYYMAPEHLNDINAKPTE-KSDVYSFGIVLWAIFAKKEPYENVICTEQfVICIKSGN 246
Cdd:cd06635   175 -------------ASPANSFVGTPYWMAPEVILAMDEGQYDgKVDVWSLGITCIELAERKPPLFNMNAMSA-LYHIAQNE 240
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1333886239 247 RPNVE--EILEYcpreIISLMERCWQAIPEDRPT 278
Cdd:cd06635   241 SPTLQsnEWSDY----FRNFVDSCLQKIPQDRPT 270
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
26-276 1.04e-16

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: 80.98  E-value: 1.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSR---VVKLLGIIIEEGNYSLVMEYMEKGNLMH 102
Cdd:cd06917    12 GSYGAVYRGYHVKTGRVVALKVLNLDTDDDDVSDIQKEVALLSQLKLGQpknIIKYYGSYLKGPSLWIIMDYCEGGSIRT 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLKTQidvPLSLK--GRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwskltkekdnkqkEVS 180
Cdd:cd06917    92 LMRAG---PIAERyiAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAA----------------SLN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 181 STTKKNNG--GTLYYMAPEHLNDINAKPTeKSDVYSFGIVLWAIFAKKEPYENVictEQF-VICIKSGNRPNVEEILEYC 257
Cdd:cd06917   153 QNSSKRSTfvGTPYWMAPEVITEGKYYDT-KADIWSLGITTYEMATGNPPYSDV---DALrAVMLIPKSKPPRLEGNGYS 228
                         250       260
                  ....*....|....*....|.
gi 1333886239 258 P--REIISLmerCWQAIPEDR 276
Cdd:cd06917   229 PllKEFVAA---CLDEEPKDR 246
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
71-282 1.33e-16

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 80.81  E-value: 1.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  71 RHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKT----QIDVPLSLKG------------RIIVEAIEGMCYLHDKGV 134
Cdd:cd05089    61 HHPNIINLLGACENRGYLYIAIEYAPYGNLLDFLRKsrvlETDPAFAKEHgtastltsqqllQFASDVAKGMQYLSEKQF 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 135 IHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnKQKEVssTTKKNNGG-TLYYMAPEHLNdiNAKPTEKSDVY 213
Cdd:cd05089   141 IHRDLAARNVLVGENLVSKIADFGLS--------------RGEEV--YVKKTMGRlPVRWMAIESLN--YSVYTTKSDVW 202
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 214 SFGIVLWAIFA-KKEPYENVICTEQFVIcIKSGNRpnvEEILEYCPREIISLMERCWQAIPEDRPTFLGI 282
Cdd:cd05089   203 SFGVLLWEIVSlGGTPYCGMTCAELYEK-LPQGYR---MEKPRNCDDEVYELMRQCWRDRPYERPPFSQI 268
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
50-237 1.33e-16

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


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 80.78  E-value: 1.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  50 GPNRAEYNEVlleegKMMHRLRHSRVVKLLGIIIE--EGNYSLVMEYMEKGNLMHVLKTQidvPLSL-KGRIIVE-AIEG 125
Cdd:cd14199    67 GPIERVYQEI-----AILKKLDHPNVVKLVEVLDDpsEDHLYMVFELVKQGPVMEVPTLK---PLSEdQARFYFQdLIKG 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 126 MCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwskltkekdnkQKEVSSTTKKNNGGTLYYMAPEHLNDINAK 205
Cdd:cd14199   139 IEYLHYQKIIHRDVKPSNLLVGEDGHIKIADFGVSN--------------EFEGSDALLTNTVGTPAFMAPETLSETRKI 204
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1333886239 206 PTEKS-DVYSFGIVLWAIFAKKEPY--ENVICTEQ 237
Cdd:cd14199   205 FSGKAlDVWAMGVTLYCFVFGQCPFmdERILSLHS 239
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
20-229 1.54e-16

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: 79.96  E-value: 1.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  20 KTDLDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEgKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGN 99
Cdd:cd14190     9 KEVLGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKEMVLLEI-QVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 100 LMHVLKTQiDVPLS-LKGRIIVEAI-EGMCYLHDKGVIHKDLKPENIL-VDRDFH-IKIADLGVA-SFKTWSKLtkekdn 174
Cdd:cd14190    88 LFERIVDE-DYHLTeVDAMVFVRQIcEGIQFMHQMRVLHLDLKPENILcVNRTGHqVKIIDFGLArRYNPREKL------ 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333886239 175 kqkevssttkKNNGGTLYYMAPEHLN-DINAKPTeksDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14190   161 ----------KVNFGTPEFLSPEVVNyDQVSFPT---DMWSMGVITYMLLSGLSPF 203
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
22-228 1.56e-16

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: 80.46  E-value: 1.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  22 DLDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEgKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLM 101
Cdd:cd06643    12 ELGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELEDYMVEI-DILASCDHPNIVKLLDAFYYENNLWILIEFCAGGAVD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 HVLkTQIDVPLSLKGRIIV--EAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTwsKLTKEKDNKQkev 179
Cdd:cd06643    91 AVM-LELERPLTEPQIRVVckQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNT--RTLQRRDSFI--- 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333886239 180 ssttkknngGTLYYMAPEHLNDINAK--PTE-KSDVYSFGIVLWAIfAKKEP 228
Cdd:cd06643   165 ---------GTPYWMAPEVVMCETSKdrPYDyKADVWSLGVTLIEM-AQIEP 206
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
23-229 1.59e-16

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: 80.89  E-value: 1.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHG--FVI--LKKvytgpnraeynEVLLE----EGKMMHR------LRHSRVVKLLGIIIEEGNY 88
Cdd:cd05592     3 LGKGSFGKVMLAELKGTNqyFAIkaLKK-----------DVVLEdddvECTMIERrvlalaSQHPFLTHLFCTFQTESHL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  89 SLVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskl 168
Cdd:cd05592    72 FFVMEYLNGGDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMC-------- 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333886239 169 tKEKDNKQKEVSSTTkknngGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd05592   144 -KENIYGENKASTFC-----GTPDYIAPEILK--GQKYNQSVDWWSFGVLLYEMLIGQSPF 196
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
23-219 1.79e-16

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: 79.73  E-value: 1.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHG--FVI--LKKVYTGPnrAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKG 98
Cdd:cd13997     8 IGSGSFSEVFKVRSKVDGclYAVkkSKKPFRGP--KERARALREVEAHAALGQHPNIVRYYSSWEEGGHLYIQMELCENG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  99 NLMHVLKT---QIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTWSKLTKEKDNK 175
Cdd:cd13997    86 SLQDALEElspISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLETSGDVEEGDSR 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1333886239 176 qkevssttkknnggtlyYMAPEHLNDiNAKPTEKSDVYSFGIVL 219
Cdd:cd13997   166 -----------------YLAPELLNE-NYTHLPKADIFSLGVTV 191
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
23-218 1.93e-16

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: 79.23  E-value: 1.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKV--YTGPNRAEynevLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNL 100
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFAAKFipKRDKKKEA----VLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGEL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 MHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVD--RDFHIKIADLGVAsfktwSKLTKEKdnkqke 178
Cdd:cd14006    77 LDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLAdrPSPQIKIIDFGLA-----RKLNPGE------ 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1333886239 179 vsstTKKNNGGTLYYMAPEHLNDINAKPTekSDVYSFGIV 218
Cdd:cd14006   146 ----ELKEIFGTPEFVAPEIVNGEPVSLA--TDMWSIGVL 179
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
23-279 2.06e-16

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: 80.03  E-value: 2.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYH-RSHGFVILKKVyTGPNRAEYNEVLlEEGKMMHRLRHSRVVKLLG-IIIEEGNYS----LVMEYME 96
Cdd:cd13986     8 LGEGGFSFVYLVEDlSTGRLYALKKI-LCHSKEDVKEAM-REIENYRLFNHPNILRLLDsQIVKEAGGKkevyLLLPYYK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  97 KGNLMHVLKTQID----VPLSLKGRIIVEAIEGMCYLHD---KGVIHKDLKPENILVDRDFHIKIADLGVAsfktwSKLT 169
Cdd:cd13986    86 RGSLQDEIERRLVkgtfFPEDRILHIFLGICRGLKAMHEpelVPYAHRDIKPGNVLLSEDDEPILMDLGSM-----NPAR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 170 KEKDNKQKEVSSTTKKNNGGTLYYMAPEHLN-DINAKPTEKSDVYSFGIVLWAIFAKKEPYENVICTEQFV-ICIKSGNR 247
Cdd:cd13986   161 IEIEGRREALALQDWAAEHCTMPYRAPELFDvKSHCTIDEKTDIWSLGCTLYALMYGESPFERIFQKGDSLaLAVLSGNY 240
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1333886239 248 PNVEEilEYCPREIISLMERCWQAIPEDRPTF 279
Cdd:cd13986   241 SFPDN--SRYSEELHQLVKSMLVVNPAERPSI 270
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
17-278 2.47e-16

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: 79.58  E-value: 2.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  17 LLEKTDLDSGGFGKVSLCYHRSHGFV----ILKKVYTGPN-RAE--YNEVLLEEGKmmhrlRHSRVVKLLGIIIEEGNYS 89
Cdd:cd14198    10 ILTSKELGRGKFAVVRQCISKSTGQEyaakFLKKRRRGQDcRAEilHEIAVLELAK-----SNPRVVNLHEVYETTSEII 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  90 LVMEYMEKGNLMHVLKTQID--VPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDF---HIKIADLGVAsfkt 164
Cdd:cd14198    85 LILEYAAGGEIFNLCVPDLAemVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYplgDIKIVDFGMS---- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 165 wskltkekdnkQKEVSSTTKKNNGGTLYYMAPEHLndiNAKP-TEKSDVYSFGIVLWAIFAKKEPYENVICTEQFvICIK 243
Cdd:cd14198   161 -----------RKIGHACELREIMGTPEYLAPEIL---NYDPiTTATDMWNIGVIAYMLLTHESPFVGEDNQETF-LNIS 225
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1333886239 244 SGNRPNVEEILEYCPREIISLMERCWQAIPEDRPT 278
Cdd:cd14198   226 QVNVDYSEETFSSVSQLATDFIQKLLVKNPEKRPT 260
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
16-275 2.66e-16

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: 80.08  E-value: 2.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  16 DLLEKTdLDSGGFGKVSLCYHR----SHGFVILKKVYTGPNRAEYNEVLLEEGkmmhrlrHSRVVKLLGIIIEEGNYSLV 91
Cdd:cd14179     9 DLKDKP-LGEGSFSICRKCLHKktnqEYAVKIVSKRMEANTQREIAALKLCEG-------HPNIVKLHEVYHDQLHTFLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  92 MEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILV---DRDFHIKIADLGVASFKTwskl 168
Cdd:cd14179    81 MELLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDFGFARLKP---- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 169 tkeKDNKqkevsstTKKNNGGTLYYMAPEHLNDINAKptEKSDVYSFGIVLWAIFAKKEPYEnviCTEQFVICIKSgnrp 248
Cdd:cd14179   157 ---PDNQ-------PLKTPCFTLHYAAPELLNYNGYD--ESCDLWSLGVILYTMLSGQVPFQ---CHDKSLTCTSA---- 217
                         250       260
                  ....*....|....*....|....*..
gi 1333886239 249 nvEEILEYCPREIISLMERCWQAIPED 275
Cdd:cd14179   218 --EEIMKKIKQGDFSFEGEAWKNVSQE 242
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
26-162 3.54e-16

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: 79.39  E-value: 3.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHG-FVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVL 104
Cdd:cd07846    12 GSYGMVMKCRHKETGqIVAIKKFLESEDDKMVKKIAMREIKMLKQLRHENLVNLIEVFRRKKRWYLVFEFVDHTVLDDLE 91
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1333886239 105 KTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASF 162
Cdd:cd07846    92 KYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFART 149
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
22-278 3.64e-16

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 79.17  E-value: 3.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  22 DLDSGGFGKVSL---CYHRSHGFVILKKVYTGPNRAEYNEvLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKG 98
Cdd:cd05042     2 EIGNGWFGKVLLgeiYSGTSVAQVVVKELKASANPKEQDT-FLKEGQPYRILQHPNILQCLGQCVEAIPYLLVMEFCDLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  99 NLMHVLKTQ-----IDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwskltkekd 173
Cdd:cd05042    81 DLKAYLRSEreherGDSDTRTLQRMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLAH------------ 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 174 NKQKEVSSTTKKNNGGTLYYMAPE-----HLNDINAKPTEKSDVYSFGIVLWAIFA-KKEPYENVICTEQFVICIKSGN- 246
Cdd:cd05042   149 SRYKEDYIETDDKLWFPLRWTAPElvtefHDRLLVVDQTKYSNIWSLGVTLWELFEnGAQPYSNLSDLDVLAQVVREQDt 228
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1333886239 247 ---RPNVEeiLEYCPReIISLMERCWQAiPEDRPT 278
Cdd:cd05042   229 klpKPQLE--LPYSDR-WYEVLQFCWLS-PEQRPA 259
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
23-282 3.67e-16

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 78.68  E-value: 3.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGF------VILKKVYtGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNySLVMEYME 96
Cdd:cd05037     7 LGQGTFTNIYDGILREVGDgrvqevEVLLKVL-DSDHRDISESFFETASLMSQISHKHLVKLYGVCVADEN-IMVQEYVR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  97 KGNLMHVLKTQ-IDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRD-------FhIKIADLGVaSFKTWSKL 168
Cdd:cd05037    85 YGPLDKYLRRMgNNVPLSWKLQVAKQLASALHYLEDKKLIHGNVRGRNILLAREgldgyppF-IKLSDPGV-PITVLSRE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 169 TKEKDnkqkevssttkknnggtLYYMAPEHLNDINAKPTEKSDVYSFGIVLWAIFAK-KEPYENVICTEQfvicIKSGNR 247
Cdd:cd05037   163 ERVDR-----------------IPWIAPECLRNLQANLTIAADKWSFGTTLWEICSGgEEPLSALSSQEK----LQFYED 221
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1333886239 248 PNVEEILEyCPrEIISLMERCWQAIPEDRPTFLGI 282
Cdd:cd05037   222 QHQLPAPD-CA-ELAELIMQCWTYEPTKRPSFRAI 254
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
25-323 4.48e-16

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: 79.88  E-value: 4.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSLCYHRSHG-FVILKKVytgpNRAEYNEVL----LEEGKMMHRLRHSRVVKLLGIIIEEGNYS-----LVMEY 94
Cdd:cd07834    10 SGAYGVVCSAYDKRTGrKVAIKKI----SNVFDDLIDakriLREIKILRHLKHENIIGLLDILRPPSPEEfndvyIVTEL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKgNLMHVLKTQIdvPLSLK--GRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwsklTKEK 172
Cdd:cd07834    86 MET-DLHKVIKSPQ--PLTDDhiQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLAR-------GVDP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 173 DNKQKEVSS--TTKknnggtlYYMAPEHLNDinakptekSDVYSFGIVLWA---IFAK----------KEPYE--NVIC- 234
Cdd:cd07834   156 DEDKGFLTEyvVTR-------WYRAPELLLS--------SKKYTKAIDIWSvgcIFAElltrkplfpgRDYIDqlNLIVe 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 235 -----TEQFVICIKSGN------------RPNVEEILEYCPREIISLMERCWQAIPEDRPTflgIEEEfrpfyLSH--FE 295
Cdd:cd07834   221 vlgtpSEEDLKFISSEKarnylkslpkkpKKPLSEVFPGASPEAIDLLEKMLVFNPKKRIT---ADEA-----LAHpyLA 292
                         330       340
                  ....*....|....*....|....*...
gi 1333886239 296 EYVEEDVASLKKEYPDQSPVLQRMFSLQ 323
Cdd:cd07834   293 QLHDPEDEPVAKPPFDFPFFDDEELTIE 320
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
23-218 4.69e-16

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: 78.57  E-value: 4.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFV-----ILKKVYTGPNRAEYNEVlleegKMMHRLRHSRVVKLLGIIIEEGNYSLVMEY--- 94
Cdd:cd14083    11 LGTGAFSEVVLAEDKATGKLvaikcIDKKALKGKEDSLENEI-----AVLRKIKHPNIVQLLDIYESKSHLYLVMELvtg 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 -------MEKGNLmhvlkTQIDVplSLKGRIIVEAIEgmcYLHDKGVIHKDLKPENILV---DRDFHIKIADLGvasfkt 164
Cdd:cd14083    86 gelfdriVEKGSY-----TEKDA--SHLIRQVLEAVD---YLHSLGIVHRDLKPENLLYyspDEDSKIMISDFG------ 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1333886239 165 wskLTKEKDNkqkEVSSTTkknnGGTLYYMAPEHLNDinaKPTEKS-DVYSFGIV 218
Cdd:cd14083   150 ---LSKMEDS---GVMSTA----CGTPGYVAPEVLAQ---KPYGKAvDCWSIGVI 191
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
23-232 4.93e-16

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: 78.63  E-value: 4.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSlCYHRSHGFVI-LKKVYTGPN-----RAEYnEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYME 96
Cdd:cd06631     9 LGKGAYGTVY-CGLTSTGQLIaVKQVELDTSdkekaEKEY-EKLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEFVP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  97 KGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTWSKLTKEKDNKQ 176
Cdd:cd06631    87 GGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRLCINLSSGSQSQLL 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333886239 177 KEVSsttkknngGTLYYMAPEHLNDinAKPTEKSDVYSFGIVLWAIFAKKEPYENV 232
Cdd:cd06631   167 KSMR--------GTPYWMAPEVINE--TGHGRKSDIWSIGCTVFEMATGKPPWADM 212
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
23-224 5.04e-16

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 79.80  E-value: 5.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYH-RSHGFVILKKVYT--GPNRAEY----------NEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYS 89
Cdd:PTZ00024   17 LGEGTYGKVEKAYDtLTGKIVAIKKVKIieISNDVTKdrqlvgmcgiHFTTLRELKIMNEIKHENIMGLVDVYVEGDFIN 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  90 LVMEYMEkGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTWS--- 166
Cdd:PTZ00024   97 LVMDIMA-SDLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARRYGYPpys 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1333886239 167 -KLTKEKDNKQKEvSSTTKKNnggTLYYMAPEHLNDINaKPTEKSDVYSFGivlwAIFA 224
Cdd:PTZ00024  176 dTLSKDETMQRRE-EMTSKVV---TLWYRAPELLMGAE-KYHFAVDMWSVG----CIFA 225
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
63-230 5.70e-16

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: 79.37  E-value: 5.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  63 EGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMH-----VLKTQIDVPLSLkgriiVEAIEGMCYLHDKGVIHK 137
Cdd:cd05582    47 ERDILADVNHPFIVKLHYAFQTEGKLYLILDFLRGGDLFTrlskeVMFTEEDVKFYL-----AELALALDHLHSLGIIYR 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 138 DLKPENILVDRDFHIKIADLGvasfktwskLTKEKDNKQKEVSSTTkknngGTLYYMAPEHLNdiNAKPTEKSDVYSFGI 217
Cdd:cd05582   122 DLKPENILLDEDGHIKLTDFG---------LSKESIDHEKKAYSFC-----GTVEYMAPEVVN--RRGHTQSADWWSFGV 185
                         170
                  ....*....|...
gi 1333886239 218 VLWAIFAKKEPYE 230
Cdd:cd05582   186 LMFEMLTGSLPFQ 198
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
60-282 5.71e-16

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The EphA10 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: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 78.43  E-value: 5.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  60 LLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQidvplslKGRIIVEAI--------EGMCYLHD 131
Cdd:cd05064    53 FLAEALTLGQFDHSNIVRLEGVITRGNTMMIVTEYMSNGALDSFLRKH-------EGQLVAGQLmgmlpglaSGMKYLSE 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 132 KGVIHKDLKPENILVDRDFHIKIADLGvasfktwskltKEKDNKQKEVSSTTKKNNggTLYYMAPEHLNDINAKPTekSD 211
Cdd:cd05064   126 MGYVHKGLAAHKVLVNSDLVCKISGFR-----------RLQEDKSEAIYTTMSGKS--PVLWAAPEAIQYHHFSSA--SD 190
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333886239 212 VYSFGIVLWAIFAKKE-PYENVicTEQFVI-CIKSGNR--PNVEeileyCPREIISLMERCWQAIPEDRPTFLGI 282
Cdd:cd05064   191 VWSFGIVMWEVMSYGErPYWDM--SGQDVIkAVEDGFRlpAPRN-----CPNLLHQLMLDCWQKERGERPRFSQI 258
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
49-286 6.61e-16

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 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: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 78.95  E-value: 6.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  49 TGPnraEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEgNYSLVMEYMEKGNLM---HVLKTQIDVPLSLKGriIVEAIEG 125
Cdd:cd05110    48 TGP---KANVEFMDEALIMASMDHPHLVRLLGVCLSP-TIQLVTQLMPHGCLLdyvHEHKDNIGSQLLLNW--CVQIAKG 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 126 MCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFktwskltKEKDNKQKEVssttkknNGGTL--YYMAPEHLNdiN 203
Cdd:cd05110   122 MMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARL-------LEGDEKEYNA-------DGGKMpiKWMALECIH--Y 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 204 AKPTEKSDVYSFGIVLWAIFA-KKEPYENvICTEQFVICIKSGNRPNVEEIleyCPREIISLMERCWQAIPEDRPTFLGI 282
Cdd:cd05110   186 RKFTHQSDVWSYGVTIWELMTfGGKPYDG-IPTREIPDLLEKGERLPQPPI---CTIDVYMVMVKCWMIDADSRPKFKEL 261

                  ....
gi 1333886239 283 EEEF 286
Cdd:cd05110   262 AAEF 265
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
124-284 6.62e-16

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: 79.95  E-value: 6.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 124 EGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltKEKDNKQKEVsstTKKNNGGTLYYMAPEHLndIN 203
Cdd:cd05104   225 KGMEFLASKNCIHRDLAARNILLTHGRITKICDFGLA---------RDIRNDSNYV---VKGNARLPVKWMAPESI--FE 290
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 204 AKPTEKSDVYSFGIVLWAIFA-KKEPYENVICTEQFVICIKSGNRpnvEEILEYCPREIISLMERCWQAIPEDRPTFLGI 282
Cdd:cd05104   291 CVYTFESDVWSYGILLWEIFSlGSSPYPGMPVDSKFYKMIKEGYR---MDSPEFAPSEMYDIMRSCWDADPLKRPTFKQI 367

                  ..
gi 1333886239 283 EE 284
Cdd:cd05104   368 VQ 369
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
15-235 6.72e-16

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: 79.28  E-value: 6.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  15 SDLLEKTDLDSGGFGKVSLCYHRSHGFV----ILKKVYTGpnrAEYNEVLLEEGK-MMHRLRHSRVVKLLGIIIEEGNYS 89
Cdd:cd05601     1 KDFEVKNVIGRGHFGEVQVVKEKATGDIyamkVLKKSETL---AQEEVSFFEEERdIMAKANSPWITKLQYAFQDSENLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  90 LVMEYMEKGNLMHVLKTQIDV-PLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwSKL 168
Cdd:cd05601    78 LVMEYHPGGDLLSLLSRYDDIfEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSA-----AKL 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333886239 169 TKEKDnkqkevssTTKKNNGGTLYYMAPEHLNDINAKPTE----KSDVYSFGIVLWAIFAKKEPY--ENVICT 235
Cdd:cd05601   153 SSDKT--------VTSKMPVGTPDYIAPEVLTSMNGGSKGtygvECDWWSLGIVAYEMLYGKTPFteDTVIKT 217
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
51-219 7.57e-16

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: 78.38  E-value: 7.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  51 PNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIE-----------EGNYSLVMEYMEKGNL---MHVLKTQIDVPLSLKG 116
Cdd:cd14048    42 PNNELAREKVLREVRALAKLDHPGIVRYFNAWLErppegwqekmdEVYLYIQMQLCRKENLkdwMNRRCTMESRELFVCL 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 117 RIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfkTWSKLTKEKDN-KQKEVSSTTKKNNGGTLYYMA 195
Cdd:cd14048   122 NIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFGLV---TAMDQGEPEQTvLTPMPAYAKHTGQVGTRLYMS 198
                         170       180
                  ....*....|....*....|....
gi 1333886239 196 PEHLNDINAkpTEKSDVYSFGIVL 219
Cdd:cd14048   199 PEQIHGNQY--SEKVDIFALGLIL 220
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
110-278 7.79e-16

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: 78.32  E-value: 7.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 110 VPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVD-RDFHIKIADLGVASFKTwskLTKEKDNKQKEVSSTTKKNNG 188
Cdd:cd14049   117 VDVDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHgSDIHVRIGDFGLACPDI---LQDGNDSTTMSRLNGLTHTSG 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 189 -GTLYYMAPEHLNDINAKPteKSDVYSFGIVLWAIFakkEPYENVICTEQFVICIKSGNRPnveEILEYCPREIISLMER 267
Cdd:cd14049   194 vGTCLYAAPEQLEGSHYDF--KSDMYSIGVILLELF---QPFGTEMERAEVLTQLRNGQIP---KSLCKRWPVQAKYIKL 265
                         170
                  ....*....|.
gi 1333886239 268 CWQAIPEDRPT 278
Cdd:cd14049   266 LTSTEPSERPS 276
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
44-288 8.17e-16

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 78.60  E-value: 8.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  44 LKKV---YTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGII-IEEGNYSLVMEYMEKgNLMHVLKTQIDV-----PLSL 114
Cdd:cd14001    33 VKKInskCDKGQRSLYQERLKEEAKILKSLNHPNIVGFRAFTkSEDGSLCLAMEYGGK-SLNDLIEERYEAglgpfPAAT 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 115 KGRIIVEAIEGMCYLH-DKGVIHKDLKPENILVDRDFH-IKIADLGVAsfktwSKLTKEkdnkqKEVSSTTKKNNGGTLY 192
Cdd:cd14001   112 ILKVALSIARALEYLHnEKKILHGDIKSGNVLIKGDFEsVKLCDFGVS-----LPLTEN-----LEVDSDPKAQYVGTEP 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 193 YMAPEHLNDiNAKPTEKSDVYSFGIVLWAIFAKKEPYENVICTEQFVI---CIKS-----------GNRP--NVEEIL-E 255
Cdd:cd14001   182 WKAKEALEE-GGVITDKADIFAYGLVLWEMMTLSVPHLNLLDIEDDDEdesFDEDeedeeayygtlGTRPalNLGELDdS 260
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1333886239 256 YCPreIISLMERCWQAIPEDRPTFLGIEEEFRP 288
Cdd:cd14001   261 YQK--VIELFYACTQEDPKDRPSAAHIVEALEA 291
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
23-278 8.36e-16

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: 77.68  E-value: 8.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVIlkKVYtgpNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEgnYSLVMEYMEKGNLMH 102
Cdd:cd14068     2 LGDGGFGSVYRAVYRGEDVAV--KIF---NKHTSFRLLRQELVVLSHLHHPSLVALLAAGTAP--RMLVMELAPKGSLDA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLKTQ-IDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILV-----DRDFHIKIADLGVASFktwskltkekdnkq 176
Cdd:cd14068    75 LLQQDnASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIAQY-------------- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 177 keVSSTTKKNNGGTLYYMAPEhLNDINAKPTEKSDVYSFGIVLwaifakkepYENVICTEQFVICIKSGNRPNVEEILEY 256
Cdd:cd14068   141 --CCRMGIKTSEGTPGFRAPE-VARGNVIYNQQADVYSFGLLL---------YDILTCGERIVEGLKFPNEFDELAIQGK 208
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1333886239 257 CPR-----------EIISLMERCWQAIPEDRPT 278
Cdd:cd14068   209 LPDpvkeygcapwpGVEALIKDCLKENPQCRPT 241
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
62-287 8.49e-16

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 78.08  E-value: 8.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  62 EEGKMMHRLRHSRVVKLLGIIIEEGNYSLvmEYMEKGNLMHVL----KTQIDVPLS--LKGRIIVEAIEGMCYLHDKGVI 135
Cdd:cd14067    59 QEASMLHSLQHPCIVYLIGISIHPLCFAL--ELAPLGSLNTVLeenhKGSSFMPLGhmLTFKIAYQIAAGLAYLHKKNII 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 136 HKDLKPENILV-----DRDFHIKIADLGVA--SFKTwSKLTKEkdnkqkevssttkknngGTLYYMAPEhlndinAKP-- 206
Cdd:cd14067   137 FCDLKSDNILVwsldvQEHINIKLSDYGISrqSFHE-GALGVE-----------------GTPGYQAPE------IRPri 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 207 --TEKSDVYSFGIVLWAIFAKKEPyenVICTEQFVICIK--SGNRP---NVEEILEYCpreIISLMERCWQAIPEDRPTF 279
Cdd:cd14067   193 vyDEKVDMFSYGMVLYELLSGQRP---SLGHHQLQIAKKlsKGIRPvlgQPEEVQFFR---LQALMMECWDTKPEKRPLA 266

                  ....*...
gi 1333886239 280 LGIEEEFR 287
Cdd:cd14067   267 CSVVEQMK 274
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
58-289 8.54e-16

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: 77.71  E-value: 8.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  58 EVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHK 137
Cdd:cd14121    40 ENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGGDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHM 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 138 DLKPENILVDR--DFHIKIADLGVAsfktwSKLTKEKDNKQKEvssttkknngGTLYYMAPEHLndINAKPTEKSDVYSF 215
Cdd:cd14121   120 DLKPQNLLLSSryNPVLKLADFGFA-----QHLKPNDEAHSLR----------GSPLYMAPEMI--LKKKYDARVDLWSV 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 216 GIVLWAIFAKKEPYENVICTEqFVICIKSgNR----PNVEEILEYCPREIISLMERcwqaIPEDRPTFlgieEEF--RPF 289
Cdd:cd14121   183 GVILYECLFGRAPFASRSFEE-LEEKIRS-SKpieiPTRPELSADCRDLLLRLLQR----DPDRRISF----EEFfaHPF 252
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
26-231 8.75e-16

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: 77.68  E-value: 8.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLK 105
Cdd:cd14185    11 GNFAVVKECRHWNENQEYAMKIIDKSKLKGKEDMIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYVRGGDLFDAII 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 106 TQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILV----DRDFHIKIADLGVASFKTWSKLTKekdnkqkevss 181
Cdd:cd14185    91 ESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhnpDKSTTLKLADFGLAKYVTGPIFTV----------- 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1333886239 182 ttkknnGGTLYYMAPEHLNDINAKptEKSDVYSFGIVLWAIFAKKEPYEN 231
Cdd:cd14185   160 ------CGTPTYVAPEILSEKGYG--LEVDMWAAGVILYILLCGFPPFRS 201
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
56-282 9.73e-16

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: 78.25  E-value: 9.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  56 YNEVLLeegkmmhrlRHSRVVKLLGIIIEEGNYS----LVMEYMEKGNLMHVLKTQ-IDVPLSLkgRIIVEAIEGMCYLH 130
Cdd:cd14142    51 YNTVLL---------RHENILGFIASDMTSRNSCtqlwLITHYHENGSLYDYLQRTtLDHQEML--RLALSAASGLVHLH 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 131 DK--------GVIHKDLKPENILVDRDFHIKIADLGVAsfktwskLTKEKDNKQKEVSSTTKKnngGTLYYMAPEHLND- 201
Cdd:cd14142   120 TEifgtqgkpAIAHRDLKSKNILVKSNGQCCIADLGLA-------VTHSQETNQLDVGNNPRV---GTKRYMAPEVLDEt 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 202 INAKPTE---KSDVYSFGIVLWAIFAK----------KEPYENVICTE------QFVICIkSGNRPNV------EEILEy 256
Cdd:cd14142   190 INTDCFEsykRVDIYAFGLVLWEVARRcvsggiveeyKPPFYDVVPSDpsfedmRKVVCV-DQQRPNIpnrwssDPTLT- 267
                         250       260
                  ....*....|....*....|....*.
gi 1333886239 257 cprEIISLMERCWQAIPEDRPTFLGI 282
Cdd:cd14142   268 ---AMAKLMKECWYQNPSARLTALRI 290
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
67-286 1.00e-15

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 78.07  E-value: 1.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  67 MHRLRHSRVVKLLGIIiEEGNYSLVMEYMEKGNLM-HVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENIL 145
Cdd:cd05111    63 IGSLDHAYIVRLLGIC-PGASLQLVTQLLPLGSLLdHVRQHRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVL 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 146 VDRDFHIKIADLGVASFKTwskltkeKDNKQ---KEVSSTTKknnggtlyYMAPEHLndINAKPTEKSDVYSFGIVLWAI 222
Cdd:cd05111   142 LKSPSQVQVADFGVADLLY-------PDDKKyfySEAKTPIK--------WMALESI--HFGKYTHQSDVWSYGVTVWEM 204
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333886239 223 FA-KKEPYENVICTEQFVIcIKSGNRPNVEEIleyCPREIISLMERCWQAIPEDRPTFLGIEEEF 286
Cdd:cd05111   205 MTfGAEPYAGMRLAEVPDL-LEKGERLAQPQI---CTIDVYMVMVKCWMIDENIRPTFKELANEF 265
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
23-278 1.06e-15

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: 77.49  E-value: 1.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHG-FVILKKVYTGPNRAEYNEVLLEEGKMMHR-------------LRHSRVVKLLGIIIEEGNY 88
Cdd:cd14077     9 IGAGSMGKVKLAKHIRTGeKCAIKIIPRASNAGLKKEREKRLEKEISRdirtireaalsslLNHPHICRLRDFLRTPNHY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  89 SLVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTWSKL 168
Cdd:cd14077    89 YMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGLSNLYDPRRL 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 169 TkekdnkqkevssttkKNNGGTLYYMAPEHLndiNAKP--TEKSDVYSFGIVLWAIFAKKEPY--ENVICTEQfviCIKS 244
Cdd:cd14077   169 L---------------RTFCGSLYFAAPELL---QAQPytGPEVDVWSFGVVLYVLVCGKVPFddENMPALHA---KIKK 227
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1333886239 245 GNrpnveeiLEYC---PREIISLMERCWQAIPEDRPT 278
Cdd:cd14077   228 GK-------VEYPsylSSECKSLISRMLVVDPKKRAT 257
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
61-278 1.10e-15

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: 77.31  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  61 LEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLK--TQIDVPLSLKG--RIIVEAIEGMCYLHDKGVIH 136
Cdd:cd08224    48 LKEIDLLQQLNHPNIIKYLASFIENNELNIVLELADAGDLSRLIKhfKKQKRLIPERTiwKYFVQLCSALEHMHSKRIMH 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 137 KDLKPENILVDRDFHIKIADLGVASFktwskltkekdnkqkeVSSTTKKNNG--GTLYYMAPEHlndINAKPTE-KSDVY 213
Cdd:cd08224   128 RDIKPANVFITANGVVKLGDLGLGRF----------------FSSKTTAAHSlvGTPYYMSPER---IREQGYDfKSDIW 188
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 214 SFGIVLWAIFAKKEPYENvictEQ---FVIC--IKSGNRPNVEEilEYCPREIISLMERCWQAIPEDRPT 278
Cdd:cd08224   189 SLGCLLYEMAALQSPFYG----EKmnlYSLCkkIEKCEYPPLPA--DLYSQELRDLVAACIQPDPEKRPD 252
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
125-279 1.10e-15

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: 79.67  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 125 GMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwskltkekdNKQKEVSSTTKKNNGGTLYYMAPEHLndINA 204
Cdd:cd05107   251 GMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLAR------------DIMRDSNYISKGSTFLPLKWMAPESI--FNN 316
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333886239 205 KPTEKSDVYSFGIVLWAIFA-KKEPYENVICTEQFVICIKSGNRPNVEeilEYCPREIISLMERCWQAIPEDRPTF 279
Cdd:cd05107   317 LYTTLSDVWSFGILLWEIFTlGGTPYPELPMNEQFYNAIKRGYRMAKP---AHASDEIYEIMQKCWEEKFEIRPDF 389
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
23-223 1.27e-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: 77.31  E-value: 1.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCY-HRSHGFVILKKVytgPNRAEYNEVLLEEGKMMHRLR------HSRVVKLLGIIIEEGNYSLVMEYM 95
Cdd:cd14133     7 LGKGTFGQVVKCYdLLTGEEVALKII---KNNKDYLDQSLDEIRLLELLNkkdkadKYHIVRLKDVFYFKNHLCIVFELL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  96 EKgNLMHVLKTQIDVPLSLK--GRIIVEAIEGMCYLHDKGVIHKDLKPENILV--DRDFHIKIADLGVASFKTwskltke 171
Cdd:cd14133    84 SQ-NLYEFLKQNKFQYLSLPriRKIAQQILEALVFLHSLGLIHCDLKPENILLasYSRCQIKIIDFGSSCFLT------- 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333886239 172 kdnkqKEVSSTTKknnggTLYYMAPEHLndINAKPTEKSDVYSFGIVLWAIF 223
Cdd:cd14133   156 -----QRLYSYIQ-----SRYYRAPEVI--LGLPYDEKIDMWSLGCILAELY 195
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
22-278 1.28e-15

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk3, also called lemur tyrosine kinase 3 (Lmtk3) is a receptor kinase containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. The function of Aatyk3 is still unknown. The Aatyk3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 77.68  E-value: 1.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  22 DLDSGGFGKVSLC-----YHRSHGFVILKKVYTGPNRaeyNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYME 96
Cdd:cd14206     4 EIGNGWFGKVILGeifsdYTPAQVVVKELRVSAGPLE---QRKFISEAQPYRSLQHPNILQCLGLCTETIPFLLIMEFCQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  97 KGNLMHVLKTQ-------IDVP---LSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktws 166
Cdd:cd14206    81 LGDLKRYLRAQrkadgmtPDLPtrdLRTLQRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLSH----- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 167 kltkekdNKQKEVSSTTKKNNGGTLYYMAPEHLNDINAK-----PTEKSDVYSFGIVLWAIFA-KKEPYENVICTEQFVI 240
Cdd:cd14206   156 -------NNYKEDYYLTPDRLWIPLRWVAPELLDELHGNlivvdQSKESNVWSLGVTIWELFEfGAQPYRHLSDEEVLTF 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1333886239 241 CIKSgnrpnvEEILEYCPREIIS-------LMERCWQAiPEDRPT 278
Cdd:cd14206   229 VVRE------QQMKLAKPRLKLPyadywyeIMQSCWLP-PSQRPS 266
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
25-229 1.29e-15

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: 77.86  E-value: 1.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSLCYHRSHGFVILKKVYTGPN--RAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMH 102
Cdd:cd05612    11 TGTFGRVHLVRDRISEHYYALKVMAIPEviRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLMEYVPGGELFS 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLKTQIDVPLSLkGRI----IVEAIEgmcYLHDKGVIHKDLKPENILVDRDFHIKIADLGVA---SFKTWSKLtkekdnk 175
Cdd:cd05612    91 YLRNSGRFSNST-GLFyaseIVCALE---YLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAkklRDRTWTLC------- 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1333886239 176 qkevssttkknngGTLYYMAPEhlnDINAKPTEKS-DVYSFGIVLWAIFAKKEPY 229
Cdd:cd05612   160 -------------GTPEYLAPE---VIQSKGHNKAvDWWALGILIYEMLVGYPPF 198
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
18-229 1.33e-15

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: 77.26  E-value: 1.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  18 LEKTDLDSGG-FGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLlEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYME 96
Cdd:cd14193     6 VNKEEILGGGrFGQVHKCEEKSSGLKLAAKIIKARSQKEKEEVK-NEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  97 KGNLMHVL------KTQIDVPLSLKgriivEAIEGMCYLHDKGVIHKDLKPENIL-VDRD-FHIKIADLGVA-SFKTWSK 167
Cdd:cd14193    85 GGELFDRIidenynLTELDTILFIK-----QICEGIQYMHQMYILHLDLKPENILcVSREaNQVKIIDFGLArRYKPREK 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333886239 168 LtkekdnkqkevssttkKNNGGTLYYMAPEHLN-DINAKPTeksDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14193   160 L----------------RVNFGTPEFLAPEVVNyEFVSFPT---DMWSLGVIAYMLLSGLSPF 203
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
18-224 1.33e-15

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: 77.72  E-value: 1.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  18 LEKtdLDSGGFGKVSLCYHRSHG-FVILKKVytgpnRAEYNE-----VLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLV 91
Cdd:cd07835     4 LEK--IGEGTYGVVYKARDKLTGeIVALKKI-----RLETEDegvpsTAIREISLLKELNHPNIVRLLDVVHSENKLYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  92 MEYmekgnLMHVLKTQID-VPLSLKGRIIVEA-----IEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVA-SF-- 162
Cdd:cd07835    77 FEF-----LDLDLKKYMDsSPLTGLDPPLIKSylyqlLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLArAFgv 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333886239 163 --KTWSkltkekdnkqKEVSsttkknnggTLYYMAPEHLndinakptEKSDVYSFGIVLWA---IFA 224
Cdd:cd07835   152 pvRTYT----------HEVV---------TLWYRAPEIL--------LGSKHYSTPVDIWSvgcIFA 191
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
26-230 1.50e-15

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: 78.03  E-value: 1.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGFV----ILKKvytgpnraeynEVLLE----EGKMMHR------LRHSRVVKLLGIIIEEGNYSLV 91
Cdd:cd05570     6 GSFGKVMLAERKKTDELyaikVLKK-----------EVIIEdddvECTMTEKrvlalaNRHPFLTGLHACFQTEDRLYFV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  92 MEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasfktwskLTKE 171
Cdd:cd05570    75 MEYVNGGDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFG---------MCKE 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 172 kDNKQKEVSSTTkknnGGTLYYMAPEHLNDinaKPTEKS-DVYSFGIVLWAIFAKKEPYE 230
Cdd:cd05570   146 -GIWGGNTTSTF----CGTPDYIAPEILRE---QDYGFSvDWWALGVLLYEMLAGQSPFE 197
Death_FADD cd08306
Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in ...
575-641 1.56e-15

Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in FAS-associated via death domain (FADD). FADD is a component of the death-inducing signaling complex (DISC) and serves as an adaptor in the signaling pathway of death receptor proteins. It modulates apoptosis as well as non-apoptotic processes such as cell cycle progression, survival, innate immune signaling, and hematopoiesis. FADD contains an N-terminal DED and a C-terminal DD. Its DD interacts with the DD of the activated death receptor, FAS, and its DED recruits the initiator caspases, caspase-8 and -10, to the DISC complex via a homotypic interaction with the N-terminal DED of the caspase. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes.


Pssm-ID: 260020  Cd Length: 85  Bit Score: 71.94  E-value: 1.56e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333886239 575 IRENLGRQWKNCARKLGFTESQIDEIDHDYERDgLKEKVYQMLQKWLMREGtKGATVGKLAQALHQC 641
Cdd:cd08306     8 ICENLGRDWRQLARKLGLSETKIESISEAHPRN-LREQVRQSLREWKKIKK-AEATVADLIKALRDC 72
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
23-276 1.60e-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: 76.88  E-value: 1.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFV----ILKKVYTGPNRAEynEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKG 98
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTfalkCVKKRHIVQTRQQ--EHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  99 NLMHVLKtqiDVPL--SLKGRI----IVEAIEgmcYLHDKGVIHKDLKPENILVDRDFHIKIADLGVA-----SFKTWSK 167
Cdd:cd05572    79 ELWTILR---DRGLfdEYTARFytacVVLAFE---YLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAkklgsGRKTWTF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 168 LtkekdnkqkevssttkknngGTLYYMAPEHLndINAKPTEKSDVYSFGIVLWAIFAKKEPYENvICTEQFVIC--IKSG 245
Cdd:cd05572   153 C--------------------GTPEYVAPEII--LNKGYDFSVDYWSLGILLYELLTGRPPFGG-DDEDPMKIYniILKG 209
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1333886239 246 NrpnveEILEYCP---REIISLMERCWQAIPEDR 276
Cdd:cd05572   210 I-----DKIEFPKyidKNAKNLIKQLLRRNPEER 238
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
16-231 1.78e-15

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: 76.66  E-value: 1.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  16 DLLEKtdLDSGGFGKVSLCYHRSHG-FVILKKVYTGPNRAEYNEV-LLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVME 93
Cdd:cd14073     4 ELLET--LGKGTYGKVKLAIERATGrEVAIKSIKKDKIEDEQDMVrIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  94 YMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKtwskltkekd 173
Cdd:cd14073    82 YASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLY---------- 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 174 nKQKEVSSTTkknnGGTLYYMAPEhlnDINAKPTE--KSDVYSFGIVLWAIFAKKEPYEN 231
Cdd:cd14073   152 -SKDKLLQTF----CGSPLYASPE---IVNGTPYQgpEVDCWSLGVLLYTLVYGTMPFDG 203
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
15-278 2.07e-15

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: 77.37  E-value: 2.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  15 SDLLEktdLDSGGFGKVSLCYH-RSHGFVILKKV-YTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVM 92
Cdd:cd06634    18 SDLRE---IGHGSFGAVYFARDvRNNEVVAIKKMsYSGKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVM 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  93 EYM--EKGNLMHVLKT---QIDVPLSLKGriiveAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFktwsk 167
Cdd:cd06634    95 EYClgSASDLLEVHKKplqEVEIAAITHG-----ALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASI----- 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 168 ltkekdnkqkevsSTTKKNNGGTLYYMAPEHLNDINAKPTE-KSDVYSFGIVLWAIFAKKEPYENVICTEQfVICIKSGN 246
Cdd:cd06634   165 -------------MAPANSFVGTPYWMAPEVILAMDEGQYDgKVDVWSLGITCIELAERKPPLFNMNAMSA-LYHIAQNE 230
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1333886239 247 RPNVEEilEYCPREIISLMERCWQAIPEDRPT 278
Cdd:cd06634   231 SPALQS--GHWSEYFRNFVDSCLQKIPQDRPT 260
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
58-279 2.49e-15

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: 76.12  E-value: 2.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  58 EVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLK-----TQIDVPLSLKgriivEAIEGMCYLHDK 132
Cdd:cd14189    46 EKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRKSLAHIWKarhtlLEPEVRYYLK-----QIISGLKYLHLK 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 133 GVIHKDLKPENILVDRDFHIKIADLGVASfktwskltkekdnkQKEVSSTTKKNNGGTLYYMAPEHLNDINAKPteKSDV 212
Cdd:cd14189   121 GILHRDLKLGNFFINENMELKVGDFGLAA--------------RLEPPEQRKKTICGTPNYLAPEVLLRQGHGP--ESDV 184
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333886239 213 YSFGIVLWAIFAKKEPYENVICTEQFViCIKsgnrpNVEEILEYC----PREIISLMercWQAIPEDRPTF 279
Cdd:cd14189   185 WSLGCVMYTLLCGNPPFETLDLKETYR-CIK-----QVKYTLPASlslpARHLLAGI---LKRNPGDRLTL 246
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
26-230 2.56e-15

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: 76.31  E-value: 2.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRS-HGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVL 104
Cdd:cd08220    11 GAYGTVYLCRRKDdNKLVIIKQIPVEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEYAPGGTLFEYI 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 105 KTQIDVPLSLKG--RIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHI-KIADLGVAsfktwskltkekdnkqKEVSS 181
Cdd:cd08220    91 QQRKGSLLSEEEilHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVvKIGDFGIS----------------KILSS 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1333886239 182 TTKKNNG-GTLYYMAPEHlndINAKP-TEKSDVYSFGIVLWAIFAKKEPYE 230
Cdd:cd08220   155 KSKAYTVvGTPCYISPEL---CEGKPyNQKSDIWALGCVLYELASLKRAFE 202
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
23-278 2.64e-15

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: 76.31  E-value: 2.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLC----YHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKG 98
Cdd:cd08222     8 LGSGNFGTVYLVsdlkATADEELKVLKEISVGELQPDETVDANREAKLLSKLDHPAIVKFHDSFVEKESFCIVTEYCEGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  99 NLMHVLKTQIDVPLSLKGRIIVE----AIEGMCYLHDKGVIHKDLKPENILVDRDFhIKIADLGVASFktwskLTKEKDn 174
Cdd:cd08222    88 DLDDKISEYKKSGTTIDENQILDwfiqLLLAVQYMHERRILHRDLKAKNIFLKNNV-IKVGDFGISRI-----LMGTSD- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 175 kqkEVSSTTkknngGTLYYMAPEHLNDINAkpTEKSDVYSFGIVLWAIFAKKEPYE--NVIcteQFVICIKSGNRPNVEE 252
Cdd:cd08222   161 ---LATTFT-----GTPYYMSPEVLKHEGY--NSKSDIWSLGCILYEMCCLKHAFDgqNLL---SVMYKIVEGETPSLPD 227
                         250       260
                  ....*....|....*....|....*.
gi 1333886239 253 ILeycPREIISLMERCWQAIPEDRPT 278
Cdd:cd08222   228 KY---SKELNAIYSRMLNKDPALRPS 250
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
11-229 2.68e-15

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: 77.66  E-value: 2.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  11 KMASSDLLEKTDLDSGGFGKVSLCYHRSHG--FVI--LKKvytgpnraeyNEVLLE---EGKMMHR------LRHSRVVK 77
Cdd:cd05619     1 KLTIEDFVLHKMLGKGSFGKVFLAELKGTNqfFAIkaLKK----------DVVLMDddvECTMVEKrvlslaWEHPFLTH 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  78 LLGIIIEEGNYSLVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADL 157
Cdd:cd05619    71 LFCTFQTKENLFFVMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADF 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333886239 158 GVAsfktwskltkeKDNKQKEVSSTTkknNGGTLYYMAPEHLndINAKPTEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd05619   151 GMC-----------KENMLGDAKTST---FCGTPDYIAPEIL--LGQKYNTSVDWWSFGVLLYEMLIGQSPF 206
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
26-229 2.72e-15

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: 76.25  E-value: 2.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHR-SHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVL 104
Cdd:cd14120     4 GAFAVVFKGRHRkKPDLPVAIKCITKKNLSKSQNLLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGDLADYL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 105 ktQIDVPLSLKG-RIIVEAIEG-MCYLHDKGVIHKDLKPENILVDR---------DFHIKIADLGVASFktwskltkekd 173
Cdd:cd14120    84 --QAKGTLSEDTiRVFLQQIAAaMKALHSKGIVHRDLKPQNILLSHnsgrkpspnDIRLKIADFGFARF----------- 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333886239 174 nKQKEVSSTTKknnGGTLYYMAPEHLndINAKPTEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14120   151 -LQDGMMAATL---CGSPMYMAPEVI--MSLQYDAKADLWSIGTIVYQCLTGKAPF 200
pknD PRK13184
serine/threonine-protein kinase PknD;
26-231 3.07e-15

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 79.81  E-value: 3.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGF-VILKKVytgpnRAEY--NEVL----LEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKG 98
Cdd:PRK13184   13 GGMGEVYLAYDPVCSRrVALKKI-----REDLseNPLLkkrfLREAKIAADLIHPGIVPVYSICSDGDPVYYTMPYIEGY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  99 NLMHVLKT--QIDV---PLSLKG------RIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTWSK 167
Cdd:PRK13184   88 TLKSLLKSvwQKESlskELAEKTsvgaflSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAAIFKKLEE 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333886239 168 ---LTKEKDNKQKEVSSTTKKNN-GGTLYYMAPEHLNDINAkpTEKSDVYSFGIVLWAIFAKKEPYEN 231
Cdd:PRK13184  168 edlLDIDVDERNICYSSMTIPGKiVGTPDYMAPERLLGVPA--SESTDIYALGVILYQMLTLSFPYRR 233
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
23-230 3.49e-15

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: 76.60  E-value: 3.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHG-FVILKKVYTGPNRAEYNEVL-LEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNL 100
Cdd:cd05630     8 LGKGGFGEVCACQVRATGkMYACKKLEKKRIKKRKGEAMaLNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGGDL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 ----MHVLKTQIDvplslKGRIIVEAIE---GMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTwskltkekd 173
Cdd:cd05630    88 kfhiYHMGQAGFP-----EARAVFYAAEiccGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVP--------- 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333886239 174 nkqkevSSTTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPYE 230
Cdd:cd05630   154 ------EGQTIKGRVGTVGYMAPEVVK--NERYTFSPDWWALGCLLYEMIAGQSPFQ 202
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
26-199 4.51e-15

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: 76.64  E-value: 4.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHG-FVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEE--------GNYSLVMEYME 96
Cdd:cd07865    23 GTFGEVFKARHRKTGqIVALKKVLMENEKEGFPITALREIKILQLLKHENVVNLIEICRTKatpynrykGSIYLVFEFCE 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  97 KgNLMHVLK-TQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfKTWSKLTKEKDNK 175
Cdd:cd07865   103 H-DLAGLLSnKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLA--RAFSLAKNSQPNR 179
                         170       180
                  ....*....|....*....|....
gi 1333886239 176 QkevssttkKNNGGTLYYMAPEHL 199
Cdd:cd07865   180 Y--------TNRVVTLWYRPPELL 195
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
26-231 4.55e-15

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: 75.63  E-value: 4.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGFVILKKVYtgPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLK 105
Cdd:cd14111    14 GRFGVIRRCRENATGKNFPAKIV--PYQAEEKQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAEFCSGKELLHSLI 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 106 TQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfKTWSKLT-KEKDNKQkevssttk 184
Cdd:cd14111    92 DRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSA--QSFNPLSlRQLGRRT-------- 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1333886239 185 knngGTLYYMAPEHLN-DINAKPTeksDVYSFGIVLWAIFAKKEPYEN 231
Cdd:cd14111   162 ----GTLEYMAPEMVKgEPVGPPA---DIWSIGVLTYIMLSGRSPFED 202
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
16-278 4.82e-15

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: 76.07  E-value: 4.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  16 DLLEKTDLDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYM 95
Cdd:cd06619     2 DIQYQEILGHGNGGTVYKAYHLLTRRILAVKVIPLDITVELQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  96 EKGNLMHVLKtqidVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwskltkekdnk 175
Cdd:cd06619    82 DGGSLDVYRK----IPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVST-------------- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 176 qkEVSSTTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPYENVICTE------QFVICIKSGNRPn 249
Cdd:cd06619   144 --QLVNSIAKTYVGTNAYMAPERIS--GEQYGIHSDVWSLGISFMELALGRFPYPQIQKNQgslmplQLLQCIVDEDPP- 218
                         250       260
                  ....*....|....*....|....*....
gi 1333886239 250 VEEILEYCPReIISLMERCWQAIPEDRPT 278
Cdd:cd06619   219 VLPVGQFSEK-FVHFITQCMRKQPKERPA 246
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
23-230 5.54e-15

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: 75.64  E-value: 5.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHG-FVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIE-EGNYSLVMEYMEKGNL 100
Cdd:cd05577     1 LGRGGFGEVCACQVKATGkMYACKKLDKKRIKKKKGETMALNEKIILEKVSSPFIVSLAYAFEtKDKLCLVLTLMNGGDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 -MHVlkTQIDVPLSLKGRIIVEAIE---GMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwskltkekdnkq 176
Cdd:cd05577    81 kYHI--YNVGTRGFSEARAIFYAAEiicGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAV--------------- 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1333886239 177 kEVSSTTK-KNNGGTLYYMAPEHLNDINAKpTEKSDVYSFGIVLWAIFAKKEPYE 230
Cdd:cd05577   144 -EFKGGKKiKGRVGTHGYMAPEVLQKEVAY-DFSVDWFALGCMLYEMIAGRSPFR 196
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
90-229 5.67e-15

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: 75.47  E-value: 5.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  90 LVMEYMEKGNLMHVLkTQIdVPLSLKG--RIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwSK 167
Cdd:cd14093    86 LVFELCRKGELFDYL-TEV-VTLSEKKtrRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFA-----TR 158
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333886239 168 LTKEKdnKQKEVSsttkknngGTLYYMAPEHL----NDINAKPTEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14093   159 LDEGE--KLRELC--------GTPGYLAPEVLkcsmYDNAPGYGKEVDMWACGVIMYTLLAGCPPF 214
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
72-282 6.22e-15

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 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: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 76.19  E-value: 6.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  72 HSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKT----QIDVPLSLKGR------------IIVEAIEGMCYLHDKGVI 135
Cdd:cd05088    67 HPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLRKsrvlETDPAFAIANStastlssqqllhFAADVARGMDYLSQKQFI 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 136 HKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnKQKEVssTTKKNNGG-TLYYMAPEHLNdiNAKPTEKSDVYS 214
Cdd:cd05088   147 HRDLAARNILVGENYVAKIADFGLS--------------RGQEV--YVKKTMGRlPVRWMAIESLN--YSVYTTNSDVWS 208
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333886239 215 FGIVLWAIFA-KKEPYENVICTEQFVIcIKSGNRpnVEEILEyCPREIISLMERCWQAIPEDRPTFLGI 282
Cdd:cd05088   209 YGVLLWEIVSlGGTPYCGMTCAELYEK-LPQGYR--LEKPLN-CDDEVYDLMRQCWREKPYERPSFAQI 273
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
23-231 7.24e-15

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: 76.20  E-value: 7.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEV--LLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNL 100
Cdd:cd05595     3 LGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVahTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 M-HVLKTQI--DVPLSLKGRIIVEAIEgmcYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnKQK 177
Cdd:cd05595    83 FfHLSRERVftEDRARFYGAEIVSALE---YLHSRDVVYRDIKLENLMLDKDGHIKITDFGLC--------------KEG 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333886239 178 EVSSTTKKNNGGTLYYMAPEHLNDINAKptEKSDVYSFGIVLWAIFAKKEPYEN 231
Cdd:cd05595   146 ITDGATMKTFCGTPEYLAPEVLEDNDYG--RAVDWWGLGVVMYEMMCGRLPFYN 197
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
41-222 7.44e-15

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: 75.43  E-value: 7.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  41 FVILKKVytgpnRAEYNE----VLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEK---------GNLMHVLKTQ 107
Cdd:cd07871    32 LVALKEI-----RLEHEEgapcTAIREVSLLKNLKHANIVTLHDIIHTERCLTLVFEYLDSdlkqyldncGNLMSMHNVK 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 108 IdvplslkgrIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnKQKEVSSTTKKNN 187
Cdd:cd07871   107 I---------FMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLA--------------RAKSVPTKTYSNE 163
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1333886239 188 GGTLYYMAPehlnDINAKPTEksdvYSFGIVLWAI 222
Cdd:cd07871   164 VVTLWYRPP----DVLLGSTE----YSTPIDMWGV 190
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
23-230 8.41e-15

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: 74.63  E-value: 8.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMH 102
Cdd:cd08219     8 VGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYCDGGDLMQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLKTQidvplslKGRI-----IVEAIEGMC----YLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFktwskLTKEKD 173
Cdd:cd08219    88 KIKLQ-------RGKLfpedtILQWFVQMClgvqHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARL-----LTSPGA 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333886239 174 NKQKEVssttkknngGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPYE 230
Cdd:cd08219   156 YACTYV---------GTPYYVPPEIWE--NMPYNNKSDIWSLGCILYELCTLKHPFQ 201
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
23-279 9.89e-15

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: 74.66  E-value: 9.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKvslCYHRSHgfVILKKVYTGP-------NRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYM 95
Cdd:cd14188     9 LGKGGFAK---CYEMTD--LTTNKVYAAKiiphsrvSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  96 EKGNLMHVLK-----TQIDVPLSLKgriivEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwskltk 170
Cdd:cd14188    84 SRRSMAHILKarkvlTEPEVRYYLR-----QIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAA--------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 171 ekdnkQKEVSSTTKKNNGGTLYYMAPEHLNDINAKPteKSDVYSFGIVLWAIFAKKEPYENVICTEQFViCIKSGNRPNV 250
Cdd:cd14188   150 -----RLEPLEHRRRTICGTPNYLSPEVLNKQGHGC--ESDIWALGCVMYTMLLGRPPFETTNLKETYR-CIREARYSLP 221
                         250       260
                  ....*....|....*....|....*....
gi 1333886239 251 EEILEYCPREIISLMERCwqaiPEDRPTF 279
Cdd:cd14188   222 SSLLAPAKHLIASMLSKN----PEDRPSL 246
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
69-231 9.96e-15

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: 74.32  E-value: 9.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  69 RLRHSRVVKLLGIIIEEGNYS------LVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPE 142
Cdd:cd14012    54 KLRHPNLVSYLAFSIERRGRSdgwkvyLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAG 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 143 NILVDRDFHIKIADLgvasfkTWSKLTKEKDNKQKEVSSTTKKNnggtLYYMAPEhLNDINAKPTEKSDVYSFGIVLWAI 222
Cdd:cd14012   134 NVLLDRDAGTGIVKL------TDYSLGKTLLDMCSRGSLDEFKQ----TYWLPPE-LAQGSKSPTRKTDVWDLGLLFLQM 202

                  ....*....
gi 1333886239 223 FAKKEPYEN 231
Cdd:cd14012   203 LFGLDVLEK 211
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
21-284 1.17e-14

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), 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. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b 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 BMPR1b, 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 BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 75.09  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  21 TDLDSGGFGKVSLCYHRSHGfVILKKVYTGPNRAEYNEVLLEEGKMMhrlRHSRVVKLLGIIIE-EGNYS---LVMEYME 96
Cdd:cd14219    11 KQIGKGRYGEVWMGKWRGEK-VAVKVFFTTEEASWFRETEIYQTVLM---RHENILGFIAADIKgTGSWTqlyLITDYHE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  97 KGNLMHVLK-TQIDVPLSLKgrIIVEAIEGMCYLHDK--------GVIHKDLKPENILVDRDFHIKIADLGVAsfktwsk 167
Cdd:cd14219    87 NGSLYDYLKsTTLDTKAMLK--LAYSSVSGLCHLHTEifstqgkpAIAHRDLKSKNILVKKNGTCCIADLGLA------- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 168 LTKEKDNKQKEVSSTTKKnngGTLYYMAPEHLNDINAKPTEKS----DVYSFGIVLWAIFAK----------KEPYENVI 233
Cdd:cd14219   158 VKFISDTNEVDIPPNTRV---GTKRYMPPEVLDESLNRNHFQSyimaDMYSFGLILWEVARRcvsggiveeyQLPYHDLV 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333886239 234 CTE------QFVICIKS-----GNRPNVEEileyCPREIISLMERCWQAIPEDRPTFLGIEE 284
Cdd:cd14219   235 PSDpsyedmREIVCIKRlrpsfPNRWSSDE----CLRQMGKLMTECWAHNPASRLTALRVKK 292
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
23-278 1.24e-14

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: 74.63  E-value: 1.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFV-ILKKVYTgPNRAEYNeVLLEEGKMMHRLR-HSRVVKLLGIII---EEGNYS--LVMEYM 95
Cdd:cd14037    11 LAEGGFAHVYLVKTSNGGNRaALKRVYV-NDEHDLN-VCKREIEIMKRLSgHKNIVGYIDSSAnrsGNGVYEvlLLMEYC 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  96 EKGNLMHVLKTQIDVPLS----LKgrIIVEAIEGMCYLH--DKGVIHKDLKPENILVDRDFHIKIADLGVASFKTWSKLT 169
Cdd:cd14037    89 KGGGVIDLMNQRLQTGLTeseiLK--IFCDVCEAVAAMHylKPPLIHRDLKVENVLISDSGNYKLCDFGSATTKILPPQT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 170 K-EKDNKQKEVSSTTkknnggTLYYMAPEHLNDINAKP-TEKSDVYSFGIVLWAIFAKKEPYENV----ICTEQFVIcik 243
Cdd:cd14037   167 KqGVTYVEEDIKKYT------TLQYRAPEMIDLYRGKPiTEKSDIWALGCLLYKLCFYTTPFEESgqlaILNGNFTF--- 237
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1333886239 244 sgnrPNVEeilEYCPReIISLMERCWQAIPEDRPT 278
Cdd:cd14037   238 ----PDNS---RYSKR-LHKLIRYMLEEDPEKRPN 264
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
23-230 1.27e-14

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: 75.42  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRS----HGFVILKKvytgpnraeynEVLLEEGKMMHRLRHSRVVKLLG----------IIIEEGNY 88
Cdd:cd05616     8 LGKGSFGKVMLAERKGtdelYAVKILKK-----------DVVIQDDDVECTMVEKRVLALSGkppfltqlhsCFQTMDRL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  89 SLVMEYMEKGNLMHVLKtqiDVPLSLKGRIIVEAIE---GMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTW 165
Cdd:cd05616    77 YFVMEYVNGGDLMYHIQ---QVGRFKEPHAVFYAAEiaiGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIW 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333886239 166 skltkekdnkqkevSSTTKKNNGGTLYYMAPEhlnDINAKPTEKS-DVYSFGIVLWAIFAKKEPYE 230
Cdd:cd05616   154 --------------DGVTTKTFCGTPDYIAPE---IIAYQPYGKSvDWWAFGVLLYEMLAGQAPFE 202
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
23-269 1.39e-14

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: 74.52  E-value: 1.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVI-LKKVYTGPNRAEYNE-VLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNL 100
Cdd:cd14117    14 LGKGKFGNVYLAREKQSKFIVaLKVLFKSQIEKEGVEhQLRREIEIQSHLRHPNILRLYNYFHDRKRIYLILEYAPRGEL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 MHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasfktWSkltkekdnkqKEVS 180
Cdd:cd14117    94 YKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFG------WS----------VHAP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 181 STTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPYENVICTE----------QFVICIKSGNRPNV 250
Cdd:cd14117   158 SLRRRTMCGTLDYLPPEMIE--GRTHDEKVDLWCIGVLCYELLVGMPPFESASHTEtyrrivkvdlKFPPFLSDGSRDLI 235
                         250       260
                  ....*....|....*....|..
gi 1333886239 251 EEILEYCPREIISL---MERCW 269
Cdd:cd14117   236 SKLLRYHPSERLPLkgvMEHPW 257
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
15-229 1.41e-14

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: 74.29  E-value: 1.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  15 SDLLEKTDLDSGGFGKV--SLCyHRSHGFVILKKVYTGPNR-AEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLV 91
Cdd:cd08228     2 ANFQIEKKIGRGQFSEVyrATC-LLDRKPVALKKVQIFEMMdAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  92 MEYMEKGNL----MHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTwsk 167
Cdd:cd08228    81 LELADAGDLsqmiKYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFS--- 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333886239 168 ltkekdnkqkevSSTTKKNN-GGTLYYMAPE--HLNDINAkpteKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd08228   158 ------------SKTTAAHSlVGTPYYMSPEriHENGYNF----KSDIWSLGCLLYEMAALQSPF 206
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
69-276 1.44e-14

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 74.67  E-value: 1.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  69 RLRHSRVVKLLGI-IIEEGNYS---LVMEYMEKGNLMHVLKTQIdvpLSLKG--RIIVEAIEGMCYLHD----------K 132
Cdd:cd14053    45 GMKHENILQFIGAeKHGESLEAeywLITEFHERGSLCDYLKGNV---ISWNElcKIAESMARGLAYLHEdipatngghkP 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 133 GVIHKDLKPENILVDRDFHIKIADLGVA-SFKTwsklTKEKDNKQKEVssttkknngGTLYYMAPEHLND-INAKPTE-- 208
Cdd:cd14053   122 SIAHRDFKSKNVLLKSDLTACIADFGLAlKFEP----GKSCGDTHGQV---------GTRRYMAPEVLEGaINFTRDAfl 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 209 KSDVYSFGIVLWAI-----FAKKEPYENVICTEQFViciksGNRPNVEEILEYC------PR------------EIISLM 265
Cdd:cd14053   189 RIDMYAMGLVLWELlsrcsVHDGPVDEYQLPFEEEV-----GQHPTLEDMQECVvhkklrPQirdewrkhpglaQLCETI 263
                         250
                  ....*....|.
gi 1333886239 266 ERCWQAIPEDR 276
Cdd:cd14053   264 EECWDHDAEAR 274
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
54-229 1.65e-14

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: 74.18  E-value: 1.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  54 AEYNEVLLEEGKMMHRLR-HSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDK 132
Cdd:cd14182    50 QELREATLKEIDILRKVSgHPNIIQLKDTYETNTFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKL 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 133 GVIHKDLKPENILVDRDFHIKIADLGVAsfktwskLTKEKDNKQKEVSsttkknngGTLYYMAPE----HLNDINAKPTE 208
Cdd:cd14182   130 NIVHRDLKPENILLDDDMNIKLTDFGFS-------CQLDPGEKLREVC--------GTPGYLAPEiiecSMDDNHPGYGK 194
                         170       180
                  ....*....|....*....|.
gi 1333886239 209 KSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14182   195 EVDMWSTGVIMYTLLAGSPPF 215
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
47-289 1.67e-14

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: 74.65  E-value: 1.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  47 VYTGPNRAEYNEVLLEEGKMMHR----------------LRHSRVVKLLGIIIEEGNYSLVMEYMEK---------GNLM 101
Cdd:cd07873    18 VYKGRSKLTDNLVALKEIRLEHEegapctairevsllkdLKHANIVTLHDIIHTEKSLTLVFEYLDKdlkqylddcGNSI 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 HVLKTQIdvplslkgrIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnKQKEVSS 181
Cdd:cd07873    98 NMHNVKL---------FLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLA--------------RAKSIPT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 182 TTKKNNGGTLYYMAPehlnDINAKPTEksdvYSFGIVLWAifakkepyenvicteqfVICI---KSGNRP-----NVEEI 253
Cdd:cd07873   155 KTYSNEVVTLWYRPP----DILLGSTD----YSTQIDMWG-----------------VGCIfyeMSTGRPlfpgsTVEEQ 209
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1333886239 254 LEYCPREIISLMERCWQAIPEDrptflgieEEFRPF 289
Cdd:cd07873   210 LHFIFRILGTPTEETWPGILSN--------EEFKSY 237
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
26-226 1.82e-14

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: 74.45  E-value: 1.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHG-FVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIII----------EEGNYSLVMEY 94
Cdd:cd07864    18 GTYGQVYKAKDKDTGeLVALKKVRLDNEKEGFPITAIREIKILRQLNHRSVVNLKEIVTdkqdaldfkkDKGAFYLVFEY 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKgNLMHVLKTQ-IDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFktWSKltkekd 173
Cdd:cd07864    98 MDH-DLMGLLESGlVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLARL--YNS------ 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333886239 174 nkqkeVSSTTKKNNGGTLYYMAPEHLNDiNAKPTEKSDVYSFGIVLWAIFAKK 226
Cdd:cd07864   169 -----EESRPYTNKVITLWYRPPELLLG-EERYGPAIDVWSCGCILGELFTKK 215
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
44-219 2.02e-14

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: 74.00  E-value: 2.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  44 LKKVYTGPNRAEYnevLLEEGKMMHRLR---HSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQidvplSLKGR--- 117
Cdd:cd14052    34 LKPNYAGAKDRLR---RLEEVSILRELTldgHDNIVQLIDSWEYHGHLYIQTELCENGSLDVFLSEL-----GLLGRlde 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 118 -----IIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfkTWSkltkekDNKQKEVSsttkknngGTLY 192
Cdd:cd14052   106 frvwkILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMAT--VWP------LIRGIERE--------GDRE 169
                         170       180
                  ....*....|....*....|....*...
gi 1333886239 193 YMAPEHLNDIN-AKPtekSDVYSFGIVL 219
Cdd:cd14052   170 YIAPEILSEHMyDKP---ADIFSLGLIL 194
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
31-229 2.73e-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: 2.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  31 VSLCYHRSHG--FVIlKKVYTGPNR---AEYNEVLLEEGKMMHRLR----HSRVVKLLGIIIEEGNYSLVMEYMEKGNLM 101
Cdd:cd14181    26 VRRCVHRHTGqeFAV-KIIEVTAERlspEQLEEVRSSTLKEIHILRqvsgHPSIITLIDSYESSTFIFLVFDLMRRGELF 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 HVLKTQidVPLSLK-GRIIVEAI-EGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskLTKEKDNKQKEV 179
Cdd:cd14181   105 DYLTEK--VTLSEKeTRSIMRSLlEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFS-------CHLEPGEKLREL 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333886239 180 SsttkknngGTLYYMAPEHL----NDINAKPTEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14181   176 C--------GTPGYLAPEILkcsmDETHPGYGKEVDLWACGVILFTLLAGSPPF 221
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
58-231 2.83e-14

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: 73.42  E-value: 2.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  58 EVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVL-KTQIDvplslKGRIIV---EAIEGMCYLHDKG 133
Cdd:cd06647    49 ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVtETCMD-----EGQIAAvcrECLQALEFLHSNQ 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 134 VIHKDLKPENILVDRDFHIKIADLGVAsfktwSKLTKEKDNKQKEVssttkknngGTLYYMAPEHLNDINAKPteKSDVY 213
Cdd:cd06647   124 VIHRDIKSDNILLGMDGSVKLTDFGFC-----AQITPEQSKRSTMV---------GTPYWMAPEVVTRKAYGP--KVDIW 187
                         170
                  ....*....|....*...
gi 1333886239 214 SFGIVLWAIFAKKEPYEN 231
Cdd:cd06647   188 SLGIMAIEMVEGEPPYLN 205
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
26-219 3.04e-14

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: 73.88  E-value: 3.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHR-SHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKgNLMHVL 104
Cdd:cd07848    12 GAYGVVLKCRHKeTKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVEK-NMLELL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 105 KTQIDVPLSLKGR-IIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwSKLTKEKDNKQKEVSSTT 183
Cdd:cd07848    91 EEMPNGVPPEKVRsYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFA-----RNLSEGSNANYTEYVATR 165
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1333886239 184 kknnggtlYYMAPEHLndINAKPTEKSDVYSFGIVL 219
Cdd:cd07848   166 --------WYRSPELL--LGAPYGKAVDMWSVGCIL 191
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
90-229 3.22e-14

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: 74.21  E-value: 3.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  90 LVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwsklt 169
Cdd:cd05620    73 FVMEFLNGGDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMC--------- 143
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 170 keKDNKQKEVSSTTkknNGGTLYYMAPEHLNDInaKPTEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd05620   144 --KENVFGDNRAST---FCGTPDYIAPEILQGL--KYTFSVDWWSFGVLLYEMLIGQSPF 196
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
47-222 3.25e-14

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: 73.67  E-value: 3.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  47 VYTGPNRAEYNEVLL-------EEG---------KMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGnlmhvLKTQIDV 110
Cdd:cd07836    16 VYKGRNRTTGEIVALkeihldaEEGtpstaireiSLMKELKHENIVRLHDVIHTENKLMLVFEYMDKD-----LKKYMDT 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 111 -------PLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVA-SFKtwskltkekdnkqkeVSST 182
Cdd:cd07836    91 hgvrgalDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLArAFG---------------IPVN 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1333886239 183 TKKNNGGTLYYMAPEHLndinakptEKSDVYSFGIVLWAI 222
Cdd:cd07836   156 TFSNEVVTLWYRAPDVL--------LGSRTYSTSIDIWSV 187
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
15-278 3.29e-14

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 74.47  E-value: 3.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  15 SDLLEKTDLDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEY 94
Cdd:PLN00034   74 SELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTVRRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEF 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKGNL--MHVLKTQIdvpLSLKGRIIveaIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFktwskLTKEK 172
Cdd:PLN00034  154 MDGGSLegTHIADEQF---LADVARQI---LSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRI-----LAQTM 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 173 DNKQKEVssttkknngGTLYYMAPEHLN-DIN--AKPTEKSDVYSFGIVLWAIFAKKEPY--------ENVICTeqfvIC 241
Cdd:PLN00034  223 DPCNSSV---------GTIAYMSPERINtDLNhgAYDGYAGDIWSLGVSILEFYLGRFPFgvgrqgdwASLMCA----IC 289
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1333886239 242 IKSGNRPNVEEILEYcpREIISlmeRCWQAIPEDRPT 278
Cdd:PLN00034  290 MSQPPEAPATASREF--RHFIS---CCLQREPAKRWS 321
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
91-230 3.34e-14

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


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 73.97  E-value: 3.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  91 VMEYMEKGNLMHvlktQIDVPLSLKGRIIV----EAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasfktws 166
Cdd:cd05587    75 VMEYVNGGDLMY----HIQQVGKFKEPVAVfyaaEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFG-------- 142
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333886239 167 kLTKEKDNKQKevsstTKKNNGGTLYYMAPEHlndINAKPTEKS-DVYSFGIVLWAIFAKKEPYE 230
Cdd:cd05587   143 -MCKEGIFGGK-----TTRTFCGTPDYIAPEI---IAYQPYGKSvDWWAYGVLLYEMLAGQPPFD 198
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
90-220 3.47e-14

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: 73.21  E-value: 3.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  90 LVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTWSKLT 169
Cdd:cd05609    77 MVMEYVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKIGLMSLTT 156
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333886239 170 K------EKDNKQ---KEVSsttkknngGTLYYMAPEH-LNDINAKPTeksDVYSFGIVLW 220
Cdd:cd05609   157 NlyeghiEKDTREfldKQVC--------GTPEYIAPEViLRQGYGKPV---DWWAMGIILY 206
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
37-304 3.92e-14

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: 74.13  E-value: 3.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  37 RSHGFVILKKVY------TGPNRAeYNEVLLeegkmMHRLR-HSRVVKLLGIIIEEGN---YsLVMEYMEKgNLMHVLKT 106
Cdd:cd07852    30 KTGEVVALKKIFdafrnaTDAQRT-FREIMF-----LQELNdHPNIIKLLNVIRAENDkdiY-LVFEYMET-DLHAVIRA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 107 QI--DVPlslKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVA-SFKTWSKltKEKDNKQKE-VSst 182
Cdd:cd07852   102 NIleDIH---KQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLArSLSQLEE--DDENPVLTDyVA-- 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 183 tkknnggTLYYMAPEHLndinakptEKSDVYSFGIVLWA---IFAkkepyENVIC-----------------------TE 236
Cdd:cd07852   175 -------TRWYRAPEIL--------LGSTRYTKGVDMWSvgcILG-----EMLLGkplfpgtstlnqlekiievigrpSA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 237 QFVICIKSG------------NRPNVEEILEYCPREIISLMERCWQAIPEDRPTflgIEEEFRPFYLSHFEEYVEEDVAS 304
Cdd:cd07852   235 EDIESIQSPfaatmleslppsRPKSLDELFPKASPDALDLLKKLLVFNPNKRLT---AEEALRHPYVAQFHNPADEPSLP 311
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
60-278 4.42e-14

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 73.10  E-value: 4.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  60 LLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLM------HVLKTQIDVPLSLKgRIIVEAIEGMCYLHDKG 133
Cdd:cd05087    44 FLEEAQPYRALQHTNLLQCLAQCAEVTPYLLVMEFCPLGDLKgylrscRAAESMAPDPLTLQ-RMACEVACGLLHLHRNN 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 134 VIHKDLKPENILVDRDFHIKIADLGVASFktwskltkekdnKQKEVSSTTKKNNGGTLYYMAPE-----HLNDINAKPTE 208
Cdd:cd05087   123 FVHSDLALRNCLLTADLTVKIGDYGLSHC------------KYKEDYFVTADQLWVPLRWIAPElvdevHGNLLVVDQTK 190
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333886239 209 KSDVYSFGIVLWAIFA-KKEPYENVICTEQFVICIKsgnrpnvEEILEYC-PREIISLMER-------CWQAiPEDRPT 278
Cdd:cd05087   191 QSNVWSLGVTIWELFElGNQPYRHYSDRQVLTYTVR-------EQQLKLPkPQLKLSLAERwyevmqfCWLQ-PEQRPT 261
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
51-278 4.80e-14

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: 72.83  E-value: 4.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  51 PNR-AEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQIDvPLSLKGRIIV----EAIEG 125
Cdd:cd06624    42 PERdSREVQPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGGSLSALLRSKWG-PLKDNENTIGyytkQILEG 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 126 MCYLHDKGVIHKDLKPENILVDR-DFHIKIADLGvasfktwsklTKEKDNKQKEVSSTTKknngGTLYYMAPEHLNDINA 204
Cdd:cd06624   121 LKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFG----------TSKRLAGINPCTETFT----GTLQYMAPEVIDKGQR 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 205 KPTEKSDVYSFGivlwaifakkepyenviCTeqfVICIKSGNRPNVE------------------EILEYCPREIISLME 266
Cdd:cd06624   187 GYGPPADIWSLG-----------------CT---IIEMATGKPPFIElgepqaamfkvgmfkihpEIPESLSEEAKSFIL 246
                         250
                  ....*....|..
gi 1333886239 267 RCWQAIPEDRPT 278
Cdd:cd06624   247 RCFEPDPDKRAT 258
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
26-237 4.95e-14

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: 72.33  E-value: 4.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGFVILKKVY---TGPNraEYNEVLL-EEGKMMHRLRHSRVVKLLGII-IEEGNYSLVMEYMEKGNL 100
Cdd:cd14163    11 GTYSKVKEAFSKKHQRKVAIKIIdksGGPE--EFIQRFLpRELQIVERLDHKNIIHVYEMLeSADGKIYLVMELAEDGDV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 MHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVdRDFHIKIADLGVAsfktwskltKEKDNKQKEVS 180
Cdd:cd14163    89 FDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL-QGFTLKLTDFGFA---------KQLPKGGRELS 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333886239 181 STTkknnGGTLYYMAPEHLNDInAKPTEKSDVYSFGIVLWAIFAKKEPYEN-----VICTEQ 237
Cdd:cd14163   159 QTF----CGSTAYAAPEVLQGV-PHDSRKGDIWSMGVVLYVMLCAQLPFDDtdipkMLCQQQ 215
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
90-217 5.80e-14

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: 72.72  E-value: 5.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  90 LVMEYMEKGNLMHVLKTQIDVPLSLK----GRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktw 165
Cdd:cd06608    86 LVMEYCGGGSVTDLVKGLRKKGKRLKeewiAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVSA---- 161
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333886239 166 skltkekdnkqkEVSSTTKKNNG--GTLYYMAPEHLN-DINAKPT--EKSDVYSFGI 217
Cdd:cd06608   162 ------------QLDSTLGRRNTfiGTPYWMAPEVIAcDQQPDASydARCDVWSLGI 206
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
17-229 5.96e-14

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: 72.85  E-value: 5.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  17 LLEKtdLDSGGFGKV--SLCYHRSHGFVILKKVytgpNRAEYNEV---------LLEEGKMMHRLRHSRVVKLLGIIIEE 85
Cdd:cd14096     5 LINK--IGEGAFSNVykAVPLRNTGKPVAIKVV----RKADLSSDnlkgssranILKEVQIMKRLSHPNIVKLLDFQESD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  86 GNYSLVMEYMEKGNLMHvlktQIdVPLS-----LKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDR-DFH-------- 151
Cdd:cd14096    79 EYYYIVLELADGGEIFH----QI-VRLTyfsedLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPiPFIpsivklrk 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 152 ------------------------IKIADLGVAsfktwskltkekdnkqKEVSSTTKKNNGGTLYYMAPEHLNDinAKPT 207
Cdd:cd14096   154 adddetkvdegefipgvggggigiVKLADFGLS----------------KQVWDSNTKTPCGTVGYTAPEVVKD--ERYS 215
                         250       260
                  ....*....|....*....|..
gi 1333886239 208 EKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14096   216 KKVDMWALGCVLYTLLCGFPPF 237
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
23-277 6.29e-14

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: 72.53  E-value: 6.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHG--FVILKKVYT-----GPNRAE----YNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLV 91
Cdd:cd08528     8 LGSGAFGCVYKVRKKSNGqtLLALKEINMtnpafGRTEQErdksVGDIISEVNIIKEQLRHPNIVRYYKTFLENDRLYIV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  92 MEYMEK---GNLMHVLKTQ-IDVPLSLKGRIIVEAIEGMCYLH-DKGVIHKDLKPENILVDRDFHIKIADLGVAsfktws 166
Cdd:cd08528    88 MELIEGaplGEHFSSLKEKnEHFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDKVTITDFGLA------ 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 167 kltkekdnKQKEVSSTTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPYenvicteqFVICIKSGN 246
Cdd:cd08528   162 --------KQKGPESSKMTSVVGTILYSCPEIVQ--NEPYGEKADIWALGCILYQMCTLQPPF--------YSTNMLTLA 223
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1333886239 247 RPNVEEILEYCPR-----EIISLMERCWQAIPEDRP 277
Cdd:cd08528   224 TKIVEAEYEPLPEgmysdDITFVIRSCLTPDPEARP 259
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
22-229 6.38e-14

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: 72.30  E-value: 6.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  22 DLDSGGFGKVSLCYHRSHGF-----VILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYME 96
Cdd:cd14196    12 ELGSGQFAIVKKCREKSTGLeyaakFIKKRQSRASRRGVSREEIEREVSILRQVLHPNIITLHDVYENRTDVVLILELVS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  97 KGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENI-LVDRDF---HIKIADLGVAsfktwskltkek 172
Cdd:cd14196    92 GGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDFGLA------------ 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1333886239 173 dnkQKEVSSTTKKNNGGTLYYMAPEhlnDINAKPTE-KSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14196   160 ---HEIEDGVEFKNIFGTPEFVAPE---IVNYEPLGlEADMWSIGVITYILLSGASPF 211
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
15-232 7.14e-14

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: 72.09  E-value: 7.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  15 SDLLEKTDLDSGGFGKVSLCYHRSHG-FVILKKV-YTGPNRAE--YNEVLLeegkmMHRLRHSRVVKLLGIIIEEGNYSL 90
Cdd:cd06648     7 SDLDNFVKIGEGSTGIVCIATDKSTGrQVAVKKMdLRKQQRREllFNEVVI-----MRDYQHPNIVEMYSSYLVGDELWV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  91 VMEYMEKGNLMHVLkTQidvplslkGRIIVEAIEGMC--------YLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsf 162
Cdd:cd06648    82 VMEFLEGGALTDIV-TH--------TRMNEEQIATVCravlkalsFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFC-- 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333886239 163 ktwSKLTKEKDNKQKEVssttkknngGTLYYMAPEHlndINAKP--TEkSDVYSFGIVLWAIFAKKEPYENV 232
Cdd:cd06648   151 ---AQVSKEVPRRKSLV---------GTPYWMAPEV---ISRLPygTE-VDIWSLGIMVIEMVDGEPPYFNE 206
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
72-246 7.26e-14

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: 72.72  E-value: 7.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  72 HSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILV---DR 148
Cdd:cd14092    58 HPNIVKLHEVFQDELHTYLVMELLRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFtdeDD 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 149 DFHIKIADLGVASFKtwskltkeKDNKQKEVSSTtkknnggTLYYMAPEHLNDINAKP--TEKSDVYSFGIVLWAIFAKK 226
Cdd:cd14092   138 DAEIKIVDFGFARLK--------PENQPLKTPCF-------TLPYAAPEVLKQALSTQgyDESCDLWSLGVILYTMLSGQ 202
                         170       180
                  ....*....|....*....|....*.
gi 1333886239 227 EPY------ENVICTEQfviCIKSGN 246
Cdd:cd14092   203 VPFqspsrnESAAEIMK---RIKSGD 225
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
22-229 8.55e-14

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: 71.97  E-value: 8.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  22 DLDSGGFGKVSLCYHRSHGF-----VILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYME 96
Cdd:cd14194    12 ELGSGQFAVVKKCREKSTGLqyaakFIKKRRTKSSRRGVSREDIEREVSILKEIQHPNVITLHEVYENKTDVILILELVA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  97 KGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENI-LVDRDF---HIKIADLGVAsfktwskltkek 172
Cdd:cd14194    92 GGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENImLLDRNVpkpRIKIIDFGLA------------ 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1333886239 173 dnkQKEVSSTTKKNNGGTLYYMAPEhlnDINAKPTE-KSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14194   160 ---HKIDFGNEFKNIFGTPEFVAPE---IVNYEPLGlEADMWSIGVITYILLSGASPF 211
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
25-301 8.85e-14

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: 72.78  E-value: 8.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSLCYHRSHG-FVILKKV---YTGPNRAEYNevlLEEGKMMHRLRHSRVVKLLGIIIEEGNYS------LVMEY 94
Cdd:cd07855    15 SGAYGVVCSAIDTKSGqKVAIKKIpnaFDVVTTAKRT---LRELKILRHFKHDNIIAIRDILRPKVPYAdfkdvyVVLDL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEkGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltKEKDN 174
Cdd:cd07855    92 ME-SDLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMA---------RGLCT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 175 KQKEvSSTTKKNNGGTLYYMAPEHLNDINaKPTEKSDVYSFGIVLWAIFAKKE--PYENVICTEQFVI------------ 240
Cdd:cd07855   162 SPEE-HKYFMTEYVATRWYRAPELMLSLP-EYTQAIDMWSVGCIFAEMLGRRQlfPGKNYVHQLQLILtvlgtpsqavin 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333886239 241 ---------CIKS-GNRPNV--EEILEYCPREIISLMERCWQAIPEDRPTflgIEEEFR-PFylshFEEYVEED 301
Cdd:cd07855   240 aigadrvrrYIQNlPNKQPVpwETLYPKADQQALDLLSQMLRFDPSERIT---VAEALQhPF----LAKYHDPD 306
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
23-199 9.20e-14

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: 72.82  E-value: 9.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLC-----YHRSHGFV--ILKKVY-------TGPNRAEYNevLLEEgkmmhrLRHSRVVKLLGIIIEEGNY 88
Cdd:cd05584     4 LGKGGYGKVFQVrkttgSDKGKIFAmkVLKKASivrnqkdTAHTKAERN--ILEA------VKHPFIVDLHYAFQTGGKL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  89 SLVMEYMEKGNL-MHVLKTQI---DVPLSLKGRIIVeAIEgmcYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasfkt 164
Cdd:cd05584    76 YLILEYLSGGELfMHLEREGIfmeDTACFYLAEITL-ALG---HLHSLGIIYRDLKPENILLDAQGHVKLTDFG------ 145
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1333886239 165 wskLTKEkdnkqkEVSSTTKKNN-GGTLYYMAPEHL 199
Cdd:cd05584   146 ---LCKE------SIHDGTVTHTfCGTIEYMAPEIL 172
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
23-229 9.38e-14

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


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 72.26  E-value: 9.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIiEEGNYS------LVMEYME 96
Cdd:cd14039     1 LGTGGFGNVCLYQNQETGEKIAIKSCRLELSVKNKDRWCHEIQIMKKLNHPNVVKACDVP-EEMNFLvndvplLAMEYCS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  97 KGNLMHVLKTQIDVpLSLKGRIIVEAI----EGMCYLHDKGVIHKDLKPENILVD----RDFHiKIADLGVAsfktwskl 168
Cdd:cd14039    80 GGDLRKLLNKPENC-CGLKESQVLSLLsdigSGIQYLHENKIIHRDLKPENIVLQeingKIVH-KIIDLGYA-------- 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333886239 169 tkeKDNKQKEVSSTTKknngGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14039   150 ---KDLDQGSLCTSFV----GTLQYLAPELFE--NKSYTVTVDYWSFGTMVFECIAGFRPF 201
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
45-278 9.67e-14

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: 71.49  E-value: 9.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  45 KKVYTGPNRAE-----YNEV------------LLEEGKMMHRLRHSRVVKLLG--IIIEEGNYSLVMEYMEKGNLMHVLK 105
Cdd:cd13983    15 KTVYRAFDTEEgievaWNEIklrklpkaerqrFKQEIEILKSLKHPNIIKFYDswESKSKKEVIFITELMTSGTLKQYLK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 106 --TQIDVPLsLK--GRIIVEAIEgmcYLH--DKGVIHKDLKPENILVD-RDFHIKIADLGVASFKtwskltkeKDNKQKE 178
Cdd:cd13983    95 rfKRLKLKV-IKswCRQILEGLN---YLHtrDPPIIHRDLKCDNIFINgNTGEVKIGDLGLATLL--------RQSFAKS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 179 VSsttkknngGTLYYMAPEHLNDinaKPTEKSDVYSFGIVLWAIFAKKEPYENviCTE--QFVICIKSGNRPN-VEEILE 255
Cdd:cd13983   163 VI--------GTPEFMAPEMYEE---HYDEKVDIYAFGMCLLEMATGEYPYSE--CTNaaQIYKKVTSGIKPEsLSKVKD 229
                         250       260
                  ....*....|....*....|...
gi 1333886239 256 YCPREIIslmERCWqAIPEDRPT 278
Cdd:cd13983   230 PELKDFI---EKCL-KPPDERPS 248
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
25-226 1.45e-13

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: 71.54  E-value: 1.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSLCYHRSHG-FVILKKVYTGPNRAEYNEVLLEEGKMMHRLR---HSRVVKLLGI--IIEEGNY---SLVMEYM 95
Cdd:cd07838     9 EGAYGTVYKARDLQDGrFVALKKVRVPLSEEGIPLSTIREIALLKQLEsfeHPNVVRLLDVchGPRTDRElklTLVFEHV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  96 EK---GNLMHVLKTQIDvPLSLKgRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTW-SKLTke 171
Cdd:cd07838    89 DQdlaTYLDKCPKPGLP-PETIK-DLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLARIYSFeMALT-- 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333886239 172 kdnkqkEVSSttkknnggTLYYMAPEHL-NDINAKPTeksDVYSFGIVLWAIFAKK 226
Cdd:cd07838   165 ------SVVV--------TLWYRAPEVLlQSSYATPV---DMWSVGCIFAELFNRR 203
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
23-229 1.48e-13

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: 71.93  E-value: 1.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVI----LKKVYTGPNRAEynEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKG 98
Cdd:cd05632    10 LGKGGFGEVCACQVRATGKMYackrLEKKRIKKRKGE--SMALNEKQILEKVNSQFVVNLAYAYETKDALCLVLTIMNGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  99 NL-MHVLktQIDVPLSLKGRIIVEAIEGMC---YLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwskLTKEKDN 174
Cdd:cd05632    88 DLkFHIY--NMGNPGFEEERALFYAAEILCgleDLHRENTVYRDLKPENILLDDYGHIRISDLGLAV------KIPEGES 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1333886239 175 KQKEVssttkknngGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd05632   160 IRGRV---------GTVGYMAPEVLN--NQRYTLSPDYWGLGCLIYEMIEGQSPF 203
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
23-220 1.52e-13

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: 71.88  E-value: 1.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHG--F---VILKKVYTgpNRAEYNEVLLEEGkMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEK 97
Cdd:cd05574     9 LGKGDVGRVYLVRLKGTGklFamkVLDKEEMI--KRNKVKRVLTERE-ILATLDHPFLPTLYASFQTSTHLCFVMDYCPG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  98 GNLMHVLKTQidvplslKGRIIVE------AIEGMC---YLHDKGVIHKDLKPENILVDRDFHIKIAD------LGV--- 159
Cdd:cd05574    86 GELFRLLQKQ-------PGKRLPEevarfyAAEVLLaleYLHLLGFVYRDLKPENILLHESGHIMLTDfdlskqSSVtpp 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333886239 160 ----ASFKTWSKLTKEKDNKQKEVSSTTKKNNG--GTLYYMAPE------HLNDInakpteksDVYSFGIVLW 220
Cdd:cd05574   159 pvrkSLRKGSRRSSVKSIEKETFVAEPSARSNSfvGTEEYIAPEvikgdgHGSAV--------DWWTLGILLY 223
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
23-278 1.67e-13

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: 70.92  E-value: 1.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLcYHRS--HGFVILKKVytGPNRAEYNEV--LLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKG 98
Cdd:cd08221     8 LGRGAFGEAVL-YRKTedNSLVVWKEV--NLSRLSEKERrdALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  99 NLMHVLKTQIDVPLSLKGRI--IVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltKEKDNKQ 176
Cdd:cd08221    85 NLHDKIAQQKNQLFPEEVVLwyLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGIS---------KVLDSES 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 177 KEVSSTTkknngGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPYEnviCTEQFVICIK--SGNRpnvEEIL 254
Cdd:cd08221   156 SMAESIV-----GTPYYMSPELVQ--GVKYNFKSDIWAVGCVLYELLTLKRTFD---ATNPLRLAVKivQGEY---EDID 222
                         250       260
                  ....*....|....*....|....
gi 1333886239 255 EYCPREIISLMERCWQAIPEDRPT 278
Cdd:cd08221   223 EQYSEEIIQLVHDCLHQDPEDRPT 246
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
22-278 1.72e-13

Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk2 is a member of the Aatyk subfamily of proteins, which are receptor kinases containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk2 is also called lemur tyrosine kinase 2 (Lmtk2) or brain-enriched kinase (Brek). It is expressed at high levels in early postnatal brain, and has been shown to play a role in nerve growth factor (NGF) signaling. Studies with knockout mice reveal that Aatyk2 is essential for late stage spermatogenesis. Although it is classified as a PTK based on sequence similarity and the phylogenetic tree, Aatyk2 has been functionally characterized as a serine/threonine kinase. The Aatyk2 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: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 71.05  E-value: 1.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  22 DLDSGGFGKVSL--CYHRSHGF-VILKKVYTGPNRAEYNEvLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKG 98
Cdd:cd05086     4 EIGNGWFGKVLLgeIYTGTSVArVVVKELKASANPKEQDD-FLQQGEPYYILQHPNILQCVGQCVEAIPYLLVFEFCDLG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  99 NLMHVLKTQI-----DVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFktwskltkekd 173
Cdd:cd05086    83 DLKTYLANQQeklrgDSQIMLLQRMACEIAAGLAHMHKHNFLHSDLALRNCYLTSDLTVKVGDYGIGFS----------- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 174 nKQKEVSSTTKKNNGGTLYYMAPEHLND-----INAKPTEKSDVYSFGIVLWAIFAK-KEPYENVICTEQFVICIKSGN- 246
Cdd:cd05086   152 -RYKEDYIETDDKKYAPLRWTAPELVTSfqdglLAAEQTKYSNIWSLGVTLWELFENaAQPYSDLSDREVLNHVIKERQv 230
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1333886239 247 ---RPNVEeiLEYCPReIISLMERCWQAiPEDRPT 278
Cdd:cd05086   231 klfKPHLE--QPYSDR-WYEVLQFCWLS-PEKRPT 261
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
17-231 1.83e-13

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 71.04  E-value: 1.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  17 LLEKTDLDSGGFGKVSLCYHRSHGFVILKKVYTGPNraeYNEVLLeegkMMHRL--RHSRVVKLLGIIIEEGNYSLVMEY 94
Cdd:PHA03390   18 IVKKLKLIDGKFGKVSVLKHKPTQKLFVQKIIKAKN---FNAIEP----MVHQLmkDNPNFIKLYYSVTTLKGHVLIMDY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDR-DFHIKIADLGvasfktwskLTKEKD 173
Cdd:PHA03390   91 IKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRaKDRIYLCDYG---------LCKIIG 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1333886239 174 nkqkevsstTKKNNGGTLYYMAPEHLNDINAkpTEKSDVYSFGIVLWAIFAKKEPYEN 231
Cdd:PHA03390  162 ---------TPSCYDGTLDYFSPEKIKGHNY--DVSFDWWAVGVLTYELLTGKHPFKE 208
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
40-224 1.99e-13

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


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 71.55  E-value: 1.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  40 GFVILKKVYTGPNRAEYNEV-LLEEgkmmhrLRHSRVVKLLGIIIEEGNYS--LVMEYMEKgNLMHVLK-----TQIDVP 111
Cdd:cd07842    34 KFKGDKEQYTGISQSACREIaLLRE------LKHENVVSLVEVFLEHADKSvyLLFDYAEH-DLWQIIKfhrqaKRVSIP 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 112 LSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFH----IKIADLGVASFktWSKLTKEKDNKQKEVSsttkknn 187
Cdd:cd07842   107 PSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVMGEGPergvVKIGDLGLARL--FNAPLKPLADLDPVVV------- 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1333886239 188 ggTLYYMAPEHLndINAKPteksdvYSFGIVLWA---IFA 224
Cdd:cd07842   178 --TIWYRAPELL--LGARH------YTKAIDIWAigcIFA 207
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
26-231 2.04e-13

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: 70.64  E-value: 2.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRS----HGFVILKKVYTGpnraeyNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLM 101
Cdd:cd14087    12 GSFSRVVRVEHRVtrqpYAIKMIETKCRG------REVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMELATGGELF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 HVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILV---DRDFHIKIADLGVASFKtwsklTKEKDNKQKE 178
Cdd:cd14087    86 DRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYyhpGPDSKIMITDFGLASTR-----KKGPNCLMKT 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333886239 179 VSsttkknngGTLYYMAPEHLndiNAKP-TEKSDVYSFGIVLWAIFAKKEPYEN 231
Cdd:cd14087   161 TC--------GTPEYIAPEIL---LRKPyTQSVDMWAVGVIAYILLSGTMPFDD 203
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
20-229 2.06e-13

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: 71.30  E-value: 2.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  20 KTDLDSGGFGKVSLCYHRSHGFVILKKVY-TGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKG 98
Cdd:cd14086     6 KEELGKGAFSVVRRCVQKSTGQEFAAKIInTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  99 NLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILV---DRDFHIKIADLGVASfktwskltkekdnk 175
Cdd:cd14086    86 ELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAI-------------- 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333886239 176 qkEVSSTTKKNNG--GTLYYMAPEHLN-DINAKPTeksDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14086   152 --EVQGDQQAWFGfaGTPGYLSPEVLRkDPYGKPV---DIWACGVILYILLVGYPPF 203
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
18-229 2.75e-13

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: 70.83  E-value: 2.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  18 LEKTDLDSGGFGKVSLCYH----RSHGFVILKKvYTGPNRAEynevLLEEGKMMHRLR-HSRVVKLLGIIIEEGNYSLVM 92
Cdd:cd14173     5 LQEEVLGEGAYARVQTCINlitnKEYAVKIIEK-RPGHSRSR----VFREVEMLYQCQgHRNVLELIEFFEEEDKFYLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  93 EYMEKGNLM-HVLKTQIDVplSLKGRIIVEAI-EGMCYLHDKGVIHKDLKPENILVDRDFhiKIADLGVASFKTWSKLTK 170
Cdd:cd14173    80 EKMRGGSILsHIHRRRHFN--ELEASVVVQDIaSALDFLHNKGIAHRDLKPENILCEHPN--QVSPVKICDFDLGSGIKL 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333886239 171 EKDNkqKEVSSTTKKNNGGTLYYMAPEHLNDINAKPT---EKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14173   156 NSDC--SPISTPELLTPCGSAEYMAPEVVEAFNEEASiydKRCDLWSLGVILYIMLSGYPPF 215
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
23-229 2.80e-13

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: 70.79  E-value: 2.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHG-FVILKKVYTGPNRAEYNEVL-LEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNL 100
Cdd:cd05631     8 LGKGGFGEVCACQVRATGkMYACKKLEKKRIKKRKGEAMaLNEKRILEKVNSRFVVSLAYAYETKDALCLVLTIMNGGDL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 -MHVLktQIDVPLSLKGRIIVEAIEGMCYLHD---KGVIHKDLKPENILVDRDFHIKIADLGVASfktwskltkekdnkq 176
Cdd:cd05631    88 kFHIY--NMGNPGFDEQRAIFYAAELCCGLEDlqrERIVYRDLKPENILLDDRGHIRISDLGLAV--------------- 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333886239 177 KEVSSTTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd05631   151 QIPEGETVRGRVGTVGYMAPEVIN--NEKYTFSPDWWGLGCLIYEMIQGQSPF 201
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
26-222 2.96e-13

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


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 70.05  E-value: 2.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGF-----VILKKVYTGPNRAEYNEVLLeegkmMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNL 100
Cdd:cd14095    11 GNFAVVKECRDKATDKeyalkIIDKAKCKGKEHMIENEVAI-----LRRVKHPNIVQLIEEYDTDTELYLVMELVKGGDL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 MHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRD----FHIKIADLGVASfktwskltkekdnKQ 176
Cdd:cd14095    86 FDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHedgsKSLKLADFGLAT-------------EV 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1333886239 177 KEVSSTTkknnGGTLYYMAPEHLNDINakpteksdvYSFGIVLWAI 222
Cdd:cd14095   153 KEPLFTV----CGTPTYVAPEILAETG---------YGLKVDIWAA 185
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
23-278 3.35e-13

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: 70.35  E-value: 3.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKvslCYHRSH--------GFVILKKVYTGPNRAEYNEVLLEegkmMHR-LRHSRVVKLLGIIIEEGNYSLVME 93
Cdd:cd14187    15 LGKGGFAK---CYEITDadtkevfaGKIVPKSLLLKPHQKEKMSMEIA----IHRsLAHQHVVGFHGFFEDNDFVYVVLE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  94 YMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwskltkekd 173
Cdd:cd14187    88 LCRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLAT------------ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 174 nkQKEVSSTTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPYENViCTEQFVICIKSGnrpnveei 253
Cdd:cd14187   156 --KVEYDGERKKTLCGTPNYIAPEVLS--KKGHSFEVDIWSIGCIMYTLLVGKPPFETS-CLKETYLRIKKN-------- 222
                         250       260       270
                  ....*....|....*....|....*....|
gi 1333886239 254 lEYC-PREI----ISLMERCWQAIPEDRPT 278
Cdd:cd14187   223 -EYSiPKHInpvaASLIQKMLQTDPTARPT 251
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
9-229 3.59e-13

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: 71.96  E-value: 3.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239   9 NIKMASSDLLEKTDLDSGGFGKVSLCYHRSHgfvilKKVYTGPNRAEYNEV-------LLEEGKMMHRLRHSRVVKLLGI 81
Cdd:cd05622    67 DLRMKAEDYEVVKVIGRGAFGEVQLVRHKST-----RKVYAMKLLSKFEMIkrsdsafFWEERDIMAFANSPWVVQLFYA 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  82 IIEEGNYSLVMEYMEKGNLMHVLkTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGvas 161
Cdd:cd05622   142 FQDDRYLYMVMEYMPGGDLVNLM-SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFG--- 217
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 162 fktwsklTKEKDNKQKEVSSTTKKnngGTLYYMAPEHLNDINAKP--TEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd05622   218 -------TCMKMNKEGMVRCDTAV---GTPDYISPEVLKSQGGDGyyGRECDWWSVGVFLYEMLVGDTPF 277
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
16-245 3.64e-13

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: 70.52  E-value: 3.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  16 DLLEKTD--LDSGGFGKVSLCY----HRSHGFVILKKVYTGPNRAEYNEVlleegKMMHRLR-HSRVVKLLGIIIEEGNY 88
Cdd:cd14090     1 DLYKLTGelLGEGAYASVQTCInlytGKEYAVKIIEKHPGHSRSRVFREV-----ETLHQCQgHPNILQLIEYFEDDERF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  89 SLVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENIL---VDRDFHIKIADLGVASfktw 165
Cdd:cd14090    76 YLVFEKMRGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILcesMDKVSPVKICDFDLGS---- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 166 skltKEKDNKQKEVSSTTKK--NNGGTLYYMAPEHLNDINAKPT---EKSDVYSFGIVLWAIFAKKEPY----------- 229
Cdd:cd14090   152 ----GIKLSSTSMTPVTTPEllTPVGSAEYMAPEVVDAFVGEALsydKRCDLWSLGVILYIMLCGYPPFygrcgedcgwd 227
                         250
                  ....*....|....*....
gi 1333886239 230 --ENV-ICTEQFVICIKSG 245
Cdd:cd14090   228 rgEACqDCQELLFHSIQEG 246
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
62-259 4.22e-13

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: 69.65  E-value: 4.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  62 EEGKMMHRLRHSRVVKLL----GIIIEEGNYSLVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKG--VI 135
Cdd:cd14033    49 EEVEMLKGLQHPNIVRFYdswkSTVRGHKCIILVTELMTSGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSRCppIL 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 136 HKDLKPENILVD-RDFHIKIADLGVASFKtwskltkekdnkqkevSSTTKKNNGGTLYYMAPEHLNDinaKPTEKSDVYS 214
Cdd:cd14033   129 HRDLKCDNIFITgPTGSVKIGDLGLATLK----------------RASFAKSVIGTPEFMAPEMYEE---KYDEAVDVYA 189
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333886239 215 FGIVLWAIFAKKEPYENVICTEQFVICIKSGNRPN---------VEEILEYCPR 259
Cdd:cd14033   190 FGMCILEMATSEYPYSECQNAAQIYRKVTSGIKPDsfykvkvpeLKEIIEGCIR 243
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
26-222 5.71e-13

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: 69.84  E-value: 5.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHG-FVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGnlmhvL 104
Cdd:cd07860    11 GTYGVVYKARNKLTGeVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQD-----L 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 105 KTQID------VPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnKQKE 178
Cdd:cd07860    86 KKFMDasaltgIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLA--------------RAFG 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1333886239 179 VSSTTKKNNGGTLYYMAPEHLndinakptEKSDVYSFGIVLWAI 222
Cdd:cd07860   152 VPVRTYTHEVVTLWYRAPEIL--------LGCKYYSTAVDIWSL 187
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
23-220 6.28e-13

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: 70.30  E-value: 6.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHR-SHGFVILKKVYTGPnraEYNEVLLEEGKMMHRLRHS--------RVVKLLG---IIIEEGNY-S 89
Cdd:cd14136    18 LGWGHFSTVWLCWDLqNKRFVALKVVKSAQ---HYTEAALDEIKLLKCVREAdpkdpgreHVVQLLDdfkHTGPNGTHvC 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  90 LVMEYMekG-NLMHVLKtQID---VPLSLKGRIIVEAIEGMCYLHDK-GVIHKDLKPENILVD-RDFHIKIADLGVASFk 163
Cdd:cd14136    95 MVFEVL--GpNLLKLIK-RYNyrgIPLPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVLLCiSKIEVKIADLGNACW- 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333886239 164 TWSKLTKEKDNKQkevssttkknnggtlyYMAPEHLndINAKPTEKSDVYSFGIVLW 220
Cdd:cd14136   171 TDKHFTEDIQTRQ----------------YRSPEVI--LGAGYGTPADIWSTACMAF 209
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
16-229 7.98e-13

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: 69.15  E-value: 7.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  16 DLLEktDLDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEyNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYM 95
Cdd:cd14114     5 DILE--ELGTGAFGVVHRCTERATGNNFAAKFIMTPHESD-KETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  96 EKGNLMHVLKTQiDVPLSLKGRI--IVEAIEGMCYLHDKGVIHKDLKPENILVD--RDFHIKIADLGVASfktwskltke 171
Cdd:cd14114    82 SGGELFERIAAE-HYKMSEAEVInyMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLAT---------- 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1333886239 172 KDNKQKEVSSTTkknngGTLYYMAPEhlnDINAKPTE-KSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14114   151 HLDPKESVKVTT-----GTAEFAAPE---IVEREPVGfYTDMWAVGVLSYVLLSGLSPF 201
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
61-228 8.38e-13

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: 69.56  E-value: 8.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  61 LEEGKMMHRLRHSRVVKLLGIIIEEG--NYSLVMEYMEkgnlmHVLKTQIDV---PLSLKGR--IIVEAIEGMCYLHDKG 133
Cdd:cd07843    52 LREINILLKLQHPNIVTVKEVVVGSNldKIYMVMEYVE-----HDLKSLMETmkqPFLQSEVkcLMLQLLSGVAHLHDNW 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 134 VIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnkqKEVSSTTKK--NNGGTLYYMAPEHLNDInAKPTEKSD 211
Cdd:cd07843   127 ILHRDLKTSNLLLNNRGILKICDFGLA----------------REYGSPLKPytQLVVTLWYRAPELLLGA-KEYSTAID 189
                         170       180
                  ....*....|....*....|
gi 1333886239 212 VYSFGivlwAIFAK---KEP 228
Cdd:cd07843   190 MWSVG----CIFAElltKKP 205
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
17-229 8.63e-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: 68.92  E-value: 8.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  17 LLEKTDLDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAE--YNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEY 94
Cdd:cd14106    10 TVESTPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQdcRNEILHEIAVLELCKDCPRVVNLHEVYETRSELILILEL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDF---HIKIADLGVasfktwSKLTKE 171
Cdd:cd14106    90 AAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFplgDIKLCDFGI------SRVIGE 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1333886239 172 KdNKQKEVSsttkknngGTLYYMAPEHLndiNAKP-TEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14106   164 G-EEIREIL--------GTPDYVAPEIL---SYEPiSLATDMWSIGVLTYVLLTGHSPF 210
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
23-230 8.81e-13

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: 69.94  E-value: 8.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTgpnraeyNEVLLEEGKMMHRLRHSRVV----------KLLGIIIEEGNYSLVM 92
Cdd:cd05590     3 LGKGSFGKVMLARLKESGRLYAVKVLK-------KDVILQDDDVECTMTEKRILslarnhpfltQLYCCFQTPDRLFFVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  93 EYMEKGNLM-HVLKTQ-IDVPlslKGRII-VEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwsklt 169
Cdd:cd05590    76 EFVNGGDLMfHIQKSRrFDEA---RARFYaAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMC--------- 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333886239 170 kekdnKQKEVSSTTKKNNGGTLYYMAPEHLNDINAKPTekSDVYSFGIVLWAIFAKKEPYE 230
Cdd:cd05590   144 -----KEGIFNGKTTSTFCGTPDYIAPEILQEMLYGPS--VDWWAMGVLLYEMLCGHAPFE 197
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
10-229 9.66e-13

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: 70.41  E-value: 9.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  10 IKMASSDLLEKTDLDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNE--VLLEEGKMMHRLRHSRVVKLLGIIIEEGN 87
Cdd:cd05621    47 LQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDsaFFWEERDIMAFANSPWVVQLFCAFQDDKY 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  88 YSLVMEYMEKGNLMHVLKTqIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwsk 167
Cdd:cd05621   127 LYMVMEYMPGGDLVNLMSN-YDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCM------ 199
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333886239 168 ltkekdnKQKEVSSTTKKNNGGTLYYMAPEHLNDINAKP--TEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd05621   200 -------KMDETGMVHCDTAVGTPDYISPEVLKSQGGDGyyGRECDWWSVGVFLFEMLVGDTPF 256
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
23-231 1.05e-12

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: 69.72  E-value: 1.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEV--LLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNL 100
Cdd:cd05593    23 LGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVahTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 M-HVLKTQI--DVPLSLKGRIIVEAIEgmcYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnKQK 177
Cdd:cd05593   103 FfHLSRERVfsEDRTRFYGAEIVSALD---YLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC--------------KEG 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333886239 178 EVSSTTKKNNGGTLYYMAPEHLNDINAKptEKSDVYSFGIVLWAIFAKKEPYEN 231
Cdd:cd05593   166 ITDAATMKTFCGTPEYLAPEVLEDNDYG--RAVDWWGLGVVMYEMMCGRLPFYN 217
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
58-219 1.11e-12

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 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: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 68.76  E-value: 1.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  58 EVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVL-KTQIDVPLSLKGR--IIVEAIEGMCYLHDK-- 132
Cdd:cd14160    37 KRFLSELEVLLLFQHPNILELAAYFTETEKFCLVYPYMQNGTLFDRLqCHGVTKPLSWHERinILIGIAKAIHYLHNSqp 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 133 -GVIHKDLKPENILVDRDFHIKIADLGVASFKTWSKltkekdnkqkEVSSTTKKNNGGT--LYYMAPEHLNDinAKPTEK 209
Cdd:cd14160   117 cTVICGNISSANILLDDQMQPKLTDFALAHFRPHLE----------DQSCTINMTTALHkhLWYMPEEYIRQ--GKLSVK 184
                         170
                  ....*....|
gi 1333886239 210 SDVYSFGIVL 219
Cdd:cd14160   185 TDVYSFGIVI 194
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
26-199 1.31e-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: 68.94  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHG-FVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKgNLMHVL 104
Cdd:cd07847    12 GSYGVVFKCRNRETGqIVAIKKFVESEDDPVIKKIALREIRMLKQLKHPNLVNLIEVFRRKRKLHLVFEYCDH-TVLNEL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 105 -KTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFktwskLTKEKDNKQKEVSstt 183
Cdd:cd07847    91 eKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARI-----LTGPGDDYTDYVA--- 162
                         170
                  ....*....|....*.
gi 1333886239 184 kknnggTLYYMAPEHL 199
Cdd:cd07847   163 ------TRWYRAPELL 172
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
16-229 1.31e-12

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: 68.67  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  16 DLLEKtdLDSGGFGKVSLCYHRSHGFV-----ILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSL 90
Cdd:cd14105     8 DIGEE--LGSGQFAVVKKCREKSTGLEyaakfIKKRRSKASRRGVSREDIEREVSILRQVLHPNIITLHDVFENKTDVVL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  91 VMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENI-LVDRDF---HIKIADLGVAsfktws 166
Cdd:cd14105    86 ILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENImLLDKNVpipRIKLIDFGLA------ 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333886239 167 kltkekdnkQKEVSSTTKKNNGGTLYYMAPEhlnDINAKPTE-KSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14105   160 ---------HKIEDGNEFKNIFGTPEFVAPE---IVNYEPLGlEADMWSIGVITYILLSGASPF 211
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
61-277 1.59e-12

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: 68.52  E-value: 1.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  61 LEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNL----MHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIH 136
Cdd:cd08229    72 IKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGDLsrmiKHFKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMH 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 137 KDLKPENILVDRDFHIKIADLGVASFKTwskltkekdnkqkevSSTTKKNN-GGTLYYMAPE--HLNDINAkpteKSDVY 213
Cdd:cd08229   152 RDIKPANVFITATGVVKLGDLGLGRFFS---------------SKTTAAHSlVGTPYYMSPEriHENGYNF----KSDIW 212
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333886239 214 SFGIVLWAIFAKKEP-YENVICTEQFVICIKSGNRPNVEEilEYCPREIISLMERCWQAIPEDRP 277
Cdd:cd08229   213 SLGCLLYEMAALQSPfYGDKMNLYSLCKKIEQCDYPPLPS--DHYSEELRQLVNMCINPDPEKRP 275
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
23-230 1.94e-12

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: 67.67  E-value: 1.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEV-LLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLM 101
Cdd:cd14161    11 LGKGTYGRVKKARDSSGRLVAIKSIRKDRIKDEQDLLhIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEYASRGDLY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 -HVLKTQidvPLSLKG-----RIIVEAIEgmcYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTWSKLTkekdnk 175
Cdd:cd14161    91 dYISERQ---RLSELEarhffRQIVSAVH---YCHANGIVHRDLKLENILLDANGNIKIADFGLSNLYNQDKFL------ 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333886239 176 qkevssttkKNNGGTLYYMAPEhlnDINAKPTEKSDV--YSFGIVLWAIFAKKEPYE 230
Cdd:cd14161   159 ---------QTYCGSPLYASPE---IVNGRPYIGPEVdsWSLGVLLYILVHGTMPFD 203
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
71-278 2.19e-12

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


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 67.33  E-value: 2.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  71 RHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQiDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDF 150
Cdd:cd14050    59 EHPNCVRFIKAWEEKGILYIQTELCDTSLQQYCEETH-SLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDG 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 151 HIKIADLGVAsfktwSKLTKEKDNKQKEvssttkknngGTLYYMAPEHLNDInakPTEKSDVYSFGIVLWAIFAKKEPYE 230
Cdd:cd14050   138 VCKLGDFGLV-----VELDKEDIHDAQE----------GDPRYMAPELLQGS---FTKAADIFSLGITILELACNLELPS 199
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1333886239 231 NVICTEQfvicIKSGNRPnvEEILEYCPREIISLMERCWQAIPEDRPT 278
Cdd:cd14050   200 GGDGWHQ----LRQGYLP--EEFTAGLSPELRSIIKLMMDPDPERRPT 241
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
26-231 2.46e-12

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: 68.13  E-value: 2.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHG-FVILKKVytGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVL 104
Cdd:cd06657    31 GSTGIVCIATVKSSGkLVAVKKM--DLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIV 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 105 kTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwSKLTKEKDNKQKEVssttk 184
Cdd:cd06657   109 -THTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFC-----AQVSKEVPRRKSLV----- 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1333886239 185 knngGTLYYMAPEHLNDINAKPteKSDVYSFGIVLWAIFAKKEPYEN 231
Cdd:cd06657   178 ----GTPYWMAPELISRLPYGP--EVDIWSLGIMVIEMVDGEPPYFN 218
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
58-229 2.57e-12

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: 68.09  E-value: 2.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  58 EVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLkTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHK 137
Cdd:cd06659    63 ELLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGGALTDIV-SQTRLNEEQIATVCEAVLQALAYLHSQGVIHR 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 138 DLKPENILVDRDFHIKIADLGVAsfktwSKLTKEKDNKQKEVssttkknngGTLYYMAPEHLndINAKPTEKSDVYSFGI 217
Cdd:cd06659   142 DIKSDSILLTLDGRVKLSDFGFC-----AQISKDVPKRKSLV---------GTPYWMAPEVI--SRCPYGTEVDIWSLGI 205
                         170
                  ....*....|..
gi 1333886239 218 VLWAIFAKKEPY 229
Cdd:cd06659   206 MVIEMVDGEPPY 217
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
23-229 2.65e-12

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: 67.81  E-value: 2.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHG------------FVILKKVytgpnraeynEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSL 90
Cdd:cd14209     9 LGTGSFGRVMLVRHKETGnyyamkildkqkVVKLKQV----------EHTLNEKRILQAINFPFLVKLEYSFKDNSNLYM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  91 VMEYMEKGNLMHVLKTqidvplslKGRI-----------IVEAIEgmcYLHDKGVIHKDLKPENILVDRDFHIKIADLGV 159
Cdd:cd14209    79 VMEYVPGGEMFSHLRR--------IGRFsepharfyaaqIVLAFE---YLHSLDLIYRDLKPENLLIDQQGYIKVTDFGF 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333886239 160 ASF---KTWSKLtkekdnkqkevssttkknngGTLYYMAPEHlndINAKPTEKS-DVYSFGIVLWAIFAKKEPY 229
Cdd:cd14209   148 AKRvkgRTWTLC--------------------GTPEYLAPEI---ILSKGYNKAvDWWALGVLIYEMAAGYPPF 198
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
25-158 2.80e-12

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: 67.68  E-value: 2.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSLCYHRSHGFVI----LKKVYTGpnRAEYNEvlLEEGKMMHRLR-HSRVVKLLGIIIEE--GNYSLVMEYMEk 97
Cdd:cd07831     9 EGTFSEVLKAQSRKTGKYYaikcMKKHFKS--LEQVNN--LREIQALRRLSpHPNILRLIEVLFDRktGRLALVFELMD- 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333886239  98 GNLMHVLKTQIDvPLSLK--GRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDfHIKIADLG 158
Cdd:cd07831    84 MNLYELIKGRKR-PLPEKrvKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD-ILKLADFG 144
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
22-229 2.92e-12

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: 67.34  E-value: 2.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  22 DLDSGGFGKVSLCYHRSHGF-----VILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYME 96
Cdd:cd14195    12 ELGSGQFAIVRKCREKGTGKeyaakFIKKRRLSSSRRGVSREEIEREVNILREIQHPNIITLHDIFENKTDVVLILELVS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  97 KGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENI-LVDRDF---HIKIADLGVAsfktwskltkek 172
Cdd:cd14195    92 GGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENImLLDKNVpnpRIKLIDFGIA------------ 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1333886239 173 dnkQKEVSSTTKKNNGGTLYYMAPEhlnDINAKPTE-KSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14195   160 ---HKIEAGNEFKNIFGTPEFVAPE---IVNYEPLGlEADMWSIGVITYILLSGASPF 211
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
17-268 3.64e-12

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


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 67.10  E-value: 3.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  17 LLEKtdLDSGGFGKVSLCYH-RSHGFVILKKVytgpNRAEYNEVLLEEGKMMHRLRHSR-VVKLLGIIIEEGNYSLVMEY 94
Cdd:cd14016     4 LVKK--IGSGSFGEVYLGIDlKTGEEVAIKIE----KKDSKHPQLEYEAKVYKLLQGGPgIPRLYWFGQEGDYNVMVMDL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKgNLMHVLKTQIDVpLSLKG--RIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIK---IADLGVASFKtwsklt 169
Cdd:cd14016    78 LGP-SLEDLFNKCGRK-FSLKTvlMLADQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNkvyLIDFGLAKKY------ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 170 keKDNKQKE-VSSTTKKNNGGTLYYMApehlndINA-KPTEKS---DVYSFGIVLwaI-FAK-KEPYENVICTE----QF 238
Cdd:cd14016   150 --RDPRTGKhIPYREGKSLTGTARYAS------INAhLGIEQSrrdDLESLGYVL--IyFLKgSLPWQGLKAQSkkekYE 219
                         250       260       270
                  ....*....|....*....|....*....|
gi 1333886239 239 VICIKSGNRPnVEEILEYCPREIISLMERC 268
Cdd:cd14016   220 KIGEKKMNTS-PEELCKGLPKEFAKYLEYV 248
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
22-278 3.73e-12

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: 66.98  E-value: 3.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  22 DLDSGGFGKVSLCYHR-SHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNL 100
Cdd:cd14075     9 ELGSGNFSQVKLGIHQlTKEKVAIKILDKTKLDQKTQRLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVMEYASGGEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 MHVLKTQIDVPLSLKGRI---IVEAIEGMcylHDKGVIHKDLKPENILVDRDFHIKIADLGvasFKTWSKltkekdnkqk 177
Cdd:cd14075    89 YTKISTEGKLSESEAKPLfaqIVSAVKHM---HENNIIHRDLKAENVFYASNNCVKVGDFG---FSTHAK---------- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 178 evsSTTKKNN-GGTLYYMAPEHLNDINAKpTEKSDVYSFGIVLWAIFAKKEPY--ENVictEQFVICIKSGNRpnveEIL 254
Cdd:cd14075   153 ---RGETLNTfCGSPPYAAPELFKDEHYI-GIYVDIWALGVLLYFMVTGVMPFraETV---AKLKKCILEGTY----TIP 221
                         250       260
                  ....*....|....*....|....
gi 1333886239 255 EYCPREIISLMERCWQAIPEDRPT 278
Cdd:cd14075   222 SYVSEPCQELIRGILQPVPSDRYS 245
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
20-272 3.91e-12

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: 67.22  E-value: 3.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  20 KTDLDSGGFGKVSLCYHR-SHGFVILKKVytgPNRA-EYNEVLLE-EGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYME 96
Cdd:cd14169     8 KEKLGEGAFSEVVLAQERgSQRLVALKCI---PKKAlRGKEAMVEnEIAVLRRINHENIVSLEDIYESPTHLYLAMELVT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  97 KGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFH---IKIADLGVASFktwskltkEKD 173
Cdd:cd14169    85 GGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATPFEdskIMISDFGLSKI--------EAQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 174 NkqkeVSSTTkknnGGTLYYMAPEHLNDinaKPTEKS-DVYSFGIVLWAIFAKKEPYENVICTEQFVICIKSG---NRPN 249
Cdd:cd14169   157 G----MLSTA----CGTPGYVAPELLEQ---KPYGKAvDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEyefDSPY 225
                         250       260       270
                  ....*....|....*....|....*....|
gi 1333886239 250 VEEILEYCPREIISLMER-------CWQAI 272
Cdd:cd14169   226 WDDISESAKDFIRHLLERdpekrftCEQAL 255
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
62-230 4.38e-12

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: 66.81  E-value: 4.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  62 EEGKMMHRLRHSRVVKLLGIIiEEGNYS-LVMEYMEKGNLMHVLKTQIDVPLSLKGR-IIVEAIEGMCYLHDKGVIHKDL 139
Cdd:cd14186    50 NEVEIHCQLKHPSILELYNYF-EDSNYVyLVLEMCHNGEMSRYLKNRKKPFTEDEARhFMHQIVTGMLYLHSHGILHRDL 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 140 KPENILVDRDFHIKIADLGVAsfkTWSKLTKEKDNKQkevssttkknnGGTLYYMAPEhlndINAKPTE--KSDVYSFGI 217
Cdd:cd14186   129 TLSNLLLTRNMNIKIADFGLA---TQLKMPHEKHFTM-----------CGTPNYISPE----IATRSAHglESDVWSLGC 190
                         170
                  ....*....|...
gi 1333886239 218 VLWAIFAKKEPYE 230
Cdd:cd14186   191 MFYTLLVGRPPFD 203
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
6-230 5.30e-12

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: 67.71  E-value: 5.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239   6 SLDNIKMASSDLLekTDLDSGGFGKVSLCYHRS----HGFVILKKvytgpnraeynEVLLEEGKMMHRLRHSRVVKLL-- 79
Cdd:cd05615     3 NLDRVRLTDFNFL--MVLGKGSFGKVMLAERKGsdelYAIKILKK-----------DVVIQDDDVECTMVEKRVLALQdk 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  80 --------GIIIEEGNYSLVMEYMEKGNLMHVLKtqiDVPLSLKGRIIVEAIE---GMCYLHDKGVIHKDLKPENILVDR 148
Cdd:cd05615    70 ppfltqlhSCFQTVDRLYFVMEYVNGGDLMYHIQ---QVGKFKEPQAVFYAAEisvGLFFLHKKGIIYRDLKLDNVMLDS 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 149 DFHIKIADLGVAsfktwskltkekdnKQKEVSSTTKKNNGGTLYYMAPEhlnDINAKPTEKS-DVYSFGIVLWAIFAKKE 227
Cdd:cd05615   147 EGHIKIADFGMC--------------KEHMVEGVTTRTFCGTPDYIAPE---IIAYQPYGRSvDWWAYGVLLYEMLAGQP 209

                  ...
gi 1333886239 228 PYE 230
Cdd:cd05615   210 PFD 212
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
26-160 5.41e-12

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: 67.06  E-value: 5.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHG-FVILKKVytgpnRAEYNE-----VLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEY--MEK 97
Cdd:cd07861    11 GTYGVVYKGRNKKTGqIVAMKKI-----RLESEEegvpsTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFEFlsMDL 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333886239  98 GNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVA 160
Cdd:cd07861    86 KKYLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLA 148
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
26-226 5.56e-12

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


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 67.33  E-value: 5.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGF-VILKKVytGP-NRAEYNEVLLEEGKMMHRLRHSRVVKLLGII----IEEGN--YsLVMEYMEK 97
Cdd:cd07849    16 GAYGMVCSAVHKPTGQkVAIKKI--SPfEHQTYCLRTLREIKILLRFKHENIIGILDIQrpptFESFKdvY-IVQELMET 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  98 gNLMHVLKTQidvPLSlKGRI---IVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdn 174
Cdd:cd07849    93 -DLYKLIKTQ---HLS-NDHIqyfLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLA-------------- 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1333886239 175 kqkEVSSTTKKNNGG------TLYYMAPEHLndINAKPTEKS-DVYSFGIVLWAIFAKK 226
Cdd:cd07849   154 ---RIADPEHDHTGFlteyvaTRWYRAPEIM--LNSKGYTKAiDIWSVGCILAEMLSNR 207
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
23-229 6.18e-12

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


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 66.91  E-value: 6.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYS------LVMEYME 96
Cdd:cd14038     2 LGTGGFGNVLRWINQETGEQVAIKQCRQELSPKNRERWCLEIQIMKRLNHPNVVAARDVPEGLQKLApndlplLAMEYCQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  97 KGNLMHVLkTQIDVPLSLKGRIIVEAIE----GMCYLHDKGVIHKDLKPENILVD----RDFHiKIADLGVAsfktwskl 168
Cdd:cd14038    82 GGDLRKYL-NQFENCCGLREGAILTLLSdissALRYLHENRIIHRDLKPENIVLQqgeqRLIH-KIIDLGYA-------- 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333886239 169 tKEKDnkQKEVSSTTKknngGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14038   152 -KELD--QGSLCTSFV----GTLQYLAPELLE--QQKYTVTVDYWSFGTLAFECITGFRPF 203
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
9-220 6.29e-12

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: 67.40  E-value: 6.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239   9 NIKMASSDLLEKTDLDSGGFGKVSLCYHRSHgfvilKKVYTGPnraeynevLLEEGKMMHR------------LRHSR-- 74
Cdd:cd05596    20 KLRMNAEDFDVIKVIGRGAFGEVQLVRHKST-----KKVYAMK--------LLSKFEMIKRsdsaffweerdiMAHANse 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  75 -VVKLLGIIIEEGNYSLVMEYMEKGNLMHVLkTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIK 153
Cdd:cd05596    87 wIVQLHYAFQDDKYLYMVMDYMPGGDLVNLM-SNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLK 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333886239 154 IADLGvasfktwsklTKEKDNKQKEVSSTTKKnngGTLYYMAPEHLNDIN--AKPTEKSDVYSFGIVLW 220
Cdd:cd05596   166 LADFG----------TCMKMDKDGLVRSDTAV---GTPDYISPEVLKSQGgdGVYGRECDWWSVGVFLY 221
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
23-222 6.62e-12

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: 66.61  E-value: 6.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHG-FVILKKVYTGPnrAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLM 101
Cdd:cd06645    19 IGSGTYGDVYKARNVNTGeLAAIKVIKLEP--GEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEFCGGGSLQ 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 HVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwskltkekdnkqkEVSS 181
Cdd:cd06645    97 DIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSA----------------QITA 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1333886239 182 TTKKNNG--GTLYYMAPEhlndinAKPTEKSDVYSFGIVLWAI 222
Cdd:cd06645   161 TIAKRKSfiGTPYWMAPE------VAAVERKGGYNQLCDIWAV 197
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
53-231 7.06e-12

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: 66.60  E-value: 7.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  53 RAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLkTQIDVPLSLKGRIIVEAIEGMCYLHDK 132
Cdd:cd06658    59 KQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALTDIV-THTRMNEEQIATVCLSVLRALSYLHNQ 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 133 GVIHKDLKPENILVDRDFHIKIADLGVAsfktwSKLTKEKDNKQKEVssttkknngGTLYYMAPEHLNDINAKptEKSDV 212
Cdd:cd06658   138 GVIHRDIKSDSILLTSDGRIKLSDFGFC-----AQVSKEVPKRKSLV---------GTPYWMAPEVISRLPYG--TEVDI 201
                         170
                  ....*....|....*....
gi 1333886239 213 YSFGIVLWAIFAKKEPYEN 231
Cdd:cd06658   202 WSLGIMVIEMIDGEPPYFN 220
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
18-230 7.43e-12

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: 65.88  E-value: 7.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  18 LEKTdLDSGGFGKVSLCYHR-SHGFVILKKVytgpNRAEYNEVLLE----EGKMMHRLRHSRVVKLLGIIIEEGNYSLVM 92
Cdd:cd14071     4 IERT-IGKGNFAVVKLARHRiTKTEVAIKII----DKSQLDEENLKkiyrEVQIMKMLNHPHIIKLYQVMETKDMLYLVT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  93 EYMEKGNLMHVLKTQIDVPLSLKGRI---IVEAIEgmcYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASF------- 162
Cdd:cd14071    79 EYASNGEIFDYLAQHGRMSEKEARKKfwqILSAVE---YCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFfkpgell 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333886239 163 KTWSkltkekdnkqkevssttkknngGTLYYMAPEhLNDINAKPTEKSDVYSFGIVLWAIFAKKEPYE 230
Cdd:cd14071   156 KTWC----------------------GSPPYAAPE-VFEGKEYEGPQLDIWSLGVVLYVLVCGALPFD 200
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
23-276 7.65e-12

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 67.34  E-value: 7.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSL-CYHRSHGFVILKKVYTGP--NRAEYNEVLLEEgKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGN 99
Cdd:cd05626     9 LGIGAFGEVCLaCKVDTHALYAMKTLRKKDvlNRNQVAHVKAER-DILAEADNEWVVKLYYSFQDKDNLYFVMDYIPGGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 100 LMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTWSKLTK--EKDN--- 174
Cdd:cd05626    88 MMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTGFRWTHNSKyyQKGShir 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 175 --------------------KQKEVSSTTKKNNG--------GTLYYMAPEHLndINAKPTEKSDVYSFGIVLWAIFAKK 226
Cdd:cd05626   168 qdsmepsdlwddvsncrcgdRLKTLEQRATKQHQrclahslvGTPNYIAPEVL--LRKGYTQLCDWWSVGVILFEMLVGQ 245
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1333886239 227 EPYENVICTEQFVICIKSGNRPNVEEILEYCPREIISLMERCWQAipEDR 276
Cdd:cd05626   246 PPFLAPTPTETQLKVINWENTLHIPPQVKLSPEAVDLITKLCCSA--EER 293
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
75-220 7.73e-12

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: 66.96  E-value: 7.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  75 VVKLLGIIIEEGNYSLVMEYMEKGNLMHVL-KTQIdVPLSLKGRIIVE---AIEgmcYLHDKGVIHKDLKPENILVDRDF 150
Cdd:cd05598    63 VVKLYYSFQDKENLYFVMDYIPGGDLMSLLiKKGI-FEEDLARFYIAElvcAIE---SVHKMGFIHRDIKPDNILIDRDG 138
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 151 HIKIADLGVASFKTWSkltkeKDNKQKEVSSTTkknngGTLYYMAPEHLNDINAkpTEKSDVYSFGIVLW 220
Cdd:cd05598   139 HIKLTDFGLCTGFRWT-----HDSKYYLAHSLV-----GTPNYIAPEVLLRTGY--TQLCDWWSVGVILY 196
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
61-224 7.74e-12

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 67.21  E-value: 7.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  61 LEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMeKGNLMHVLkTQIDVPLSLKGRIIVE--AIEGMCYLHDKGVIHKD 138
Cdd:PHA03209  105 LIEAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHY-SSDLYTYL-TKRSRPLPIDQALIIEkqILEGLRYLHAQRIIHRD 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 139 LKPENILVDRDFHIKIADLGVASFKtwskltkekdnkqkeVSSTTKKNNGGTLYYMAPEHLndINAKPTEKSDVYSFGIV 218
Cdd:PHA03209  183 VKTENIFINDVDQVCIGDLGAAQFP---------------VVAPAFLGLAGTVETNAPEVL--ARDKYNSKADIWSAGIV 245

                  ....*.
gi 1333886239 219 LWAIFA 224
Cdd:PHA03209  246 LFEMLA 251
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
20-160 7.83e-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: 66.50  E-value: 7.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  20 KTDLDSGGFGKVSLCYHRSHGFV----ILKKVytGPNRAEYNEVLLEEGkmmhrlRHSRVVKLLGIIIEEGNYSLVMEYM 95
Cdd:cd14091     5 KEEIGKGSYSVCKRCIHKATGKEyavkIIDKS--KRDPSEEIEILLRYG------QHPNIITLRDVYDDGNSVYLVTELL 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333886239  96 EKGNLM-HVLKTQIdvpLSLKG-----RIIVEAIEgmcYLHDKGVIHKDLKPENILVDRDFH----IKIADLGVA 160
Cdd:cd14091    77 RGGELLdRILRQKF---FSEREasavmKTLTKTVE---YLHSQGVVHRDLKPSNILYADESGdpesLRICDFGFA 145
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
23-284 8.27e-12

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: 65.72  E-value: 8.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEY------NEVLLEEG--KMMHRLRHSRVVKLLGIIIEEGNYSLVMEY 94
Cdd:cd14005     8 LGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTEWamingpVPVPLEIAllLKASKPGVPGVIRLLDWYERPDGFLLIMER 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 -----------MEKGNLMHVLKTQIdvplslkGRIIVEAIEgMCylHDKGVIHKDLKPENILVDRDFH-IKIADLGVASF 162
Cdd:cd14005    88 pepcqdlfdfiTERGALSENLARII-------FRQVVEAVR-HC--HQRGVLHRDIKDENLLINLRTGeVKLIDFGCGAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 163 ktwskLTKekdnkqkevssTTKKNNGGTLYYMAPEHLND--INAKPtekSDVYSFGIVLWAIFAKKEPYEN--VICTEQF 238
Cdd:cd14005   158 -----LKD-----------SVYTDFDGTRVYSPPEWIRHgrYHGRP---ATVWSLGILLYDMLCGDIPFENdeQILRGNV 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1333886239 239 VIciksgnRPNVEEileycprEIISLMERCWQAIPEDRPTFLGIEE 284
Cdd:cd14005   219 LF------RPRLSK-------ECCDLISRCLQFDPSKRPSLEQILS 251
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
11-160 8.65e-12

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: 66.57  E-value: 8.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  11 KMASSDLLEKtdLDSGGFGKVSLCYHRSHG-FVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEE---- 85
Cdd:cd07866     6 KLRDYEILGK--LGEGTFGEVYKARQIKTGrVVALKKILMHNEKDGFPITALREIKILKKLKHPNVVPLIDMAVERpdks 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  86 ----GNYSLVMEYMEKgNLMHVLKTQiDVPLS---LKGrIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLG 158
Cdd:cd07866    84 krkrGSVYMVTPYMDH-DLSGLLENP-SVKLTesqIKC-YMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFG 160

                  ..
gi 1333886239 159 VA 160
Cdd:cd07866   161 LA 162
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
23-316 1.04e-11

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: 66.56  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHG--FVI--LKK--VYTgpnRAEYnEVLLEEGKMM---HRLRHSRVVKLLGIIIEEGNYSLVME 93
Cdd:cd05589     7 LGRGHFGKVLLAEYKPTGelFAIkaLKKgdIIA---RDEV-ESLMCEKRIFetvNSARHPFLVNLFACFQTPEHVCFVME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  94 YMEKGNLM-HVlktQIDVPLSLKGRIIV-EAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasfktwskLTKE 171
Cdd:cd05589    83 YAAGGDLMmHI---HEDVFSEPRAVFYAaCVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFG---------LCKE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 172 KDNKQKEVSSTTkknngGTLYYMAPEHLNDINAkpTEKSDVYSFGIVLWAIFAKKEPYENVicTEQFVI-CIksgnrpnV 250
Cdd:cd05589   151 GMGFGDRTSTFC-----GTPEFLAPEVLTDTSY--TRAVDWWGLGVLIYEMLVGESPFPGD--DEEEVFdSI-------V 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 251 EEILEYcPR----EIISLMERCWQAIPEDRptfLGIEEE------FRPFYLS-HFEEYVE--------------EDVASL 305
Cdd:cd05589   215 NDEVRY-PRflstEAISIMRRLLRKNPERR---LGASERdaedvkKQPFFRNiDWEALLArkikppfvptikspEDVSNF 290
                         330
                  ....*....|.
gi 1333886239 306 KKEYPDQSPVL 316
Cdd:cd05589   291 DEEFTSEKPVL 301
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
47-222 1.09e-11

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: 66.17  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  47 VYTGPNRAEYNEVLLEEGKMMHR----------------LRHSRVVKLLGIIIEEGNYSLVMEYMEK---------GNLM 101
Cdd:cd07872    22 VFKGRSKLTENLVALKEIRLEHEegapctairevsllkdLKHANIVTLHDIVHTDKSLTLVFEYLDKdlkqymddcGNIM 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 HVLKTQIdvplslkgrIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnKQKEVSS 181
Cdd:cd07872   102 SMHNVKI---------FLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLA--------------RAKSVPT 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1333886239 182 TTKKNNGGTLYYMAPEHLndinakptEKSDVYSFGIVLWAI 222
Cdd:cd07872   159 KTYSNEVVTLWYRPPDVL--------LGSSEYSTQIDMWGV 191
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
57-230 1.20e-11

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: 65.80  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  57 NEVLL-EEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVI 135
Cdd:cd14201    48 SQILLgKEIKILKELQHENIVALYDVQEMPNSVFLVMEYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGII 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 136 HKDLKPENILVD---------RDFHIKIADLGVASFKTwskltkekdnkqkevSSTTKKNNGGTLYYMAPEHLndINAKP 206
Cdd:cd14201   128 HRDLKPQNILLSyasrkkssvSGIRIKIADFGFARYLQ---------------SNMMAATLCGSPMYMAPEVI--MSQHY 190
                         170       180
                  ....*....|....*....|....
gi 1333886239 207 TEKSDVYSFGIVLWAIFAKKEPYE 230
Cdd:cd14201   191 DAKADLWSIGTVIYQCLVGKPPFQ 214
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
26-199 1.22e-11

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: 66.44  E-value: 1.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNevlleegkMMHRLRHSR----------VVKLLGIIIEEGNYSLVMEYM 95
Cdd:cd05610    15 GAFGKVYLGRKKNNSKLYAVKVVKKADMINKN--------MVHQVQAERdalalskspfIVHLYYSLQSANNVYLVMEYL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  96 EKGNLMHVLKT--QIDVPLSLKgrIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVasfktwSKLTKEKD 173
Cdd:cd05610    87 IGGDVKSLLHIygYFDEEMAVK--YISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGL------SKVTLNRE 158
                         170       180
                  ....*....|....*....|....*.
gi 1333886239 174 NKQKEVSSTTKKNNGGTLYYMAPEHL 199
Cdd:cd05610   159 LNMMDILTTPSMAKPKNDYSRTPGQV 184
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
10-222 1.33e-11

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: 66.59  E-value: 1.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  10 IKMASSDLLEKTDLDSGGFGKVSLCYHR-SHGFVILKKVYTGP--NRAEYNEVLLEEgKMMHRLRHSRVVKLLGIIIEEG 86
Cdd:cd05600     6 TRLKLSDFQILTQVGQGGYGSVFLARKKdTGEICALKIMKKKVlfKLNEVNHVLTER-DILTTTNSPWLVKLLYAFQDPE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  87 NYSLVMEYMEKGNlMHVLKTQIDVPLSLKGRI-IVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFK-- 163
Cdd:cd05600    85 NVYLAMEYVPGGD-FRTLLNNSGILSEEHARFyIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASGTls 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 164 ----TWSKLT--------------KEKDNKQKEVSSTTKKNNG---GTLYYMAPEHLNDINakpteksdvYSFGIVLWAI 222
Cdd:cd05600   164 pkkiESMKIRleevkntafleltaKERRNIYRAMRKEDQNYANsvvGSPDYMAPEVLRGEG---------YDLTVDYWSL 234
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
23-220 1.38e-11

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: 65.13  E-value: 1.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTG---PNRAEynEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMeKGN 99
Cdd:cd14082    11 LGSGQFGIVYGGKHRKTGRDVAIKVIDKlrfPTKQE--SQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKL-HGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 100 LMHVLKTqidvplSLKGRI--------IVEAIEGMCYLHDKGVIHKDLKPENILV--DRDF-HIKIADLGVAsfktwsKL 168
Cdd:cd14082    88 MLEMILS------SEKGRLperitkflVTQILVALRYLHSKNIVHCDLKPENVLLasAEPFpQVKLCDFGFA------RI 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333886239 169 TKEKDNKQKEVssttkknngGTLYYMAPEHLNDinaKPTEKS-DVYSFGIVLW 220
Cdd:cd14082   156 IGEKSFRRSVV---------GTPAYLAPEVLRN---KGYNRSlDMWSVGVIIY 196
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
18-278 1.80e-11

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: 65.09  E-value: 1.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  18 LEKtdLDSGGFGKV-SLCYHRSHGFVILKKVYTGPNRAEYNEVLlEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYME 96
Cdd:cd06641     9 LEK--IGKGSFGEVfKGIDNRTQKVVAIKIIDLEEAEDEIEDIQ-QEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  97 KGNLMHVLK------TQIdvplslkGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwskltk 170
Cdd:cd06641    86 GGSALDLLEpgpldeTQI-------ATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAG--------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 171 ekdnkqkEVSSTTKKNNG--GTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIfAKKEPYENVICTEQFVICIKSGNRP 248
Cdd:cd06641   150 -------QLTDTQIKRN*fvGTPFWMAPEVIK--QSAYDSKADIWSLGITAIEL-ARGEPPHSELHPMKVLFLIPKNNPP 219
                         250       260       270
                  ....*....|....*....|....*....|
gi 1333886239 249 NVEEILEYCPREIIslmERCWQAIPEDRPT 278
Cdd:cd06641   220 TLEGNYSKPLKEFV---EACLNKEPSFRPT 246
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
58-231 1.87e-11

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: 65.52  E-value: 1.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  58 EVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLkTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHK 137
Cdd:cd06655    61 ELIINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYLAGGSLTDVV-TETCMDEAQIAAVCRECLQALEFLHANQVIHR 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 138 DLKPENILVDRDFHIKIADLGVAsfktwSKLTKEKDNKQKEVssttkknngGTLYYMAPEHLNDINAKPteKSDVYSFGI 217
Cdd:cd06655   140 DIKSDNVLLGMDGSVKLTDFGFC-----AQITPEQSKRSTMV---------GTPYWMAPEVVTRKAYGP--KVDIWSLGI 203
                         170
                  ....*....|....
gi 1333886239 218 VLWAIFAKKEPYEN 231
Cdd:cd06655   204 MAIEMVEGEPPYLN 217
Death_ank cd08317
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ...
579-651 2.01e-11

Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins are modular proteins comprising three conserved domains, an N-terminal membrane-binding domain containing ANK repeats, a spectrin-binding domain and a C-terminal DD. Ankyrins function as adaptor proteins and they interact, through ANK repeats, with structurally diverse membrane proteins, including ion channels/pumps, calcium release channels, and cell adhesion molecules. They play critical roles in the proper expression and membrane localization of these proteins. In mammals, this family includes ankyrin-R for restricted (or ANK1), ankyrin-B for broadly expressed (or ANK2) and ankyrin-G for general or giant (or ANK3). They are expressed in different combinations in many tissues and play non-overlapping functions. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260029  Cd Length: 84  Bit Score: 60.36  E-value: 2.01e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333886239 579 LGRQWKNCARKLGFTESQIDEIDHDYERDgLKEKVYQMLQKWLMREGTKgATVGKLAQALHQCCRIDLLNHLI 651
Cdd:cd08317    14 LGSDWPELARELGVSEEDIDLIRSENPNS-LAQQAMAMLRLWLEREGEK-ATGNALESALKKIGRDDIVEKCE 84
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
23-229 2.02e-11

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: 64.64  E-value: 2.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEyNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMH 102
Cdd:cd14191    10 LGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKE-KENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMVSGGELFE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLktqIDVPLSLKGRIIV----EAIEGMCYLHDKGVIHKDLKPENIL-VDRD-FHIKIADLGVAsfktwskltkekdnkQ 176
Cdd:cd14191    89 RI---IDEDFELTERECIkymrQISEGVEYIHKQGIVHLDLKPENIMcVNKTgTKIKLIDFGLA---------------R 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333886239 177 KEVSSTTKKNNGGTLYYMAPEHlndINAKPTE-KSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14191   151 RLENAGSLKVLFGTPEFVAPEV---INYEPIGyATDMWSIGVICYILVSGLSPF 201
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
18-159 2.30e-11

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


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 65.24  E-value: 2.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  18 LEKtdLDSGGFGKVSLCYHRSHG-FVILKKvytgpNRAEYNE-----VLLEEGKMMHRLRHS-RVVKLLGI--IIEEG-- 86
Cdd:cd07837     6 LEK--IGEGTYGKVYKARDKNTGkLVALKK-----TRLEMEEegvpsTALREVSLLQMLSQSiYIVRLLDVehVEENGkp 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  87 NYSLVMEYMEKGnlmhvLKTQID---------VPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHI-KIAD 156
Cdd:cd07837    79 LLYLVFEYLDTD-----LKKFIDsygrgphnpLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGLlKIAD 153

                  ...
gi 1333886239 157 LGV 159
Cdd:cd07837   154 LGL 156
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
21-229 2.30e-11

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: 64.55  E-value: 2.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  21 TDLDSGGFGKVSLCYHRSHGFVILKKVYtgPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNL 100
Cdd:cd14110     9 TEINRGRFSVVRQCEEKRSGQMLAAKII--PYKPEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGPEL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 MHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTwskltkekdnkQKEVS 180
Cdd:cd14110    87 LYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFN-----------QGKVL 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1333886239 181 STTKKnnGGTLYYMAPEHLNDINAKPteKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14110   156 MTDKK--GDYVETMAPELLEGQGAGP--QTDIWAIGVTAFIMLSADYPV 200
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
26-226 2.53e-11

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: 64.98  E-value: 2.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHG-FVILKKVYTGPNRAEYNEVLLEEGKMMHRLR---HSRVVKLLGIII-----EEGNYSLVMEYME 96
Cdd:cd07863    11 GAYGTVYKARDPHSGhFVALKSVRVQTNEDGLPLSTVREVALLKRLEafdHPNIVRLMDVCAtsrtdRETKVTLVFEHVD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  97 KGnlmhvLKTQID------VPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTWskltk 170
Cdd:cd07863    91 QD-----LRTYLDkvpppgLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARIYSC----- 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333886239 171 ekdnkQKEVSSTTKknnggTLYYMAPE-HLNDINAKPTeksDVYSFGIVLWAIFAKK 226
Cdd:cd07863   161 -----QMALTPVVV-----TLWYRAPEvLLQSTYATPV---DMWSVGCIFAEMFRRK 204
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
46-199 3.38e-11

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: 64.32  E-value: 3.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  46 KVYTGPNRAEYNEVLLEEGKMMHR----------------LRHSRVVKLLGIIIEEGNYSLVMEYMEK---------GNL 100
Cdd:cd07844    15 TVYKGRSKLTGQLVALKEIRLEHEegapftaireasllkdLKHANIVTLHDIIHTKKTLTLVFEYLDTdlkqymddcGGG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 MHVLKTQIdvplslkgrIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnKQKEVS 180
Cdd:cd07844    95 LSMHNVRL---------FLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLA--------------RAKSVP 151
                         170
                  ....*....|....*....
gi 1333886239 181 STTKKNNGGTLYYMAPEHL 199
Cdd:cd07844   152 SKTYSNEVVTLWYRPPDVL 170
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
58-231 3.68e-11

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: 64.75  E-value: 3.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  58 EVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVL-KTQIDvplslKGRIIV---EAIEGMCYLHDKG 133
Cdd:cd06654    62 ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVtETCMD-----EGQIAAvcrECLQALEFLHSNQ 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 134 VIHKDLKPENILVDRDFHIKIADLGVAsfktwSKLTKEKDNKQKEVssttkknngGTLYYMAPEHLNDINAKPteKSDVY 213
Cdd:cd06654   137 VIHRDIKSDNILLGMDGSVKLTDFGFC-----AQITPEQSKRSTMV---------GTPYWMAPEVVTRKAYGP--KVDIW 200
                         170
                  ....*....|....*...
gi 1333886239 214 SFGIVLWAIFAKKEPYEN 231
Cdd:cd06654   201 SLGIMAIEMIEGEPPYLN 218
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
23-229 4.17e-11

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: 64.30  E-value: 4.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHG-FVILKKVYTGPNRAEYNEVL-LEEGKMMHRLrHSRVVKLLGIIIEEGN-YSLVMEYMEKGN 99
Cdd:cd05605     8 LGKGGFGEVCACQVRATGkMYACKKLEKKRIKKRKGEAMaLNEKQILEKV-NSRFVVSLAYAYETKDaLCLVLTIMNGGD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 100 L-MHVlkTQIDVPLSLKGRIIVEAIE---GMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwsklTKEKDNK 175
Cdd:cd05605    87 LkFHI--YNMGNPGFEEERAVFYAAEitcGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLA--------VEIPEGE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333886239 176 qkevsstTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd05605   157 -------TIRGRVGTVGYMAPEVVK--NERYTFSPDWWGLGCLIYEMIEGQAPF 201
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
58-231 4.31e-11

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: 64.36  E-value: 4.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  58 EVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVL-KTQIDvplslKGRIIV---EAIEGMCYLHDKG 133
Cdd:cd06656    61 ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVtETCMD-----EGQIAAvcrECLQALDFLHSNQ 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 134 VIHKDLKPENILVDRDFHIKIADLGVAsfktwSKLTKEKDNKQKEVssttkknngGTLYYMAPEHLNDINAKPteKSDVY 213
Cdd:cd06656   136 VIHRDIKSDNILLGMDGSVKLTDFGFC-----AQITPEQSKRSTMV---------GTPYWMAPEVVTRKAYGP--KVDIW 199
                         170
                  ....*....|....*...
gi 1333886239 214 SFGIVLWAIFAKKEPYEN 231
Cdd:cd06656   200 SLGIMAIEMVEGEPPYLN 217
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
23-231 4.39e-11

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: 65.05  E-value: 4.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEV--LLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNL 100
Cdd:cd05594    33 LGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVahTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 M-HVLKTQI--DVPLSLKGRIIVEAIEgmcYLH-DKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnKQ 176
Cdd:cd05594   113 FfHLSRERVfsEDRARFYGAEIVSALD---YLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLC--------------KE 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1333886239 177 KEVSSTTKKNNGGTLYYMAPEHLNDINAKptEKSDVYSFGIVLWAIFAKKEPYEN 231
Cdd:cd05594   176 GIKDGATMKTFCGTPEYLAPEVLEDNDYG--RAVDWWGLGVVMYEMMCGRLPFYN 228
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
18-275 4.46e-11

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: 64.51  E-value: 4.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  18 LEKTDLDSGGFGKVSLCYHRSHGFVILKKVYTgpNRAEYNeVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEK 97
Cdd:cd14180     9 LEEPALGEGSFSVCRKCRHRQSGQEYAVKIIS--RRMEAN-TQREVAALRLCQSHPNIVALHEVLHDQYHTYLVMELLRG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  98 GNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFH---IKIADLGVAsfktwskltkekdn 174
Cdd:cd14180    86 GELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFGFA-------------- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 175 KQKEVSSTTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPYEnvicTEQfviciKSGNRPNVEEIL 254
Cdd:cd14180   152 RLRPQGSRPLQTPCFTLQYAAPELFS--NQGYDESCDLWSLGVILYTMLSGQVPFQ----SKR-----GKMFHNHAADIM 220
                         250       260
                  ....*....|....*....|.
gi 1333886239 255 EYCPREIISLMERCWQAIPED 275
Cdd:cd14180   221 HKIKEGDFSLEGEAWKGVSEE 241
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
67-286 4.89e-11

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: 64.32  E-value: 4.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  67 MHRLRHSRVVKLLG----IIIEEGNYSLVMEYMEKGNLMHVLKTQIdvpLSLKG--RIIVEAIEGMCYLH----DKG--- 133
Cdd:cd14055    49 DASLKHENILQFLTaeerGVGLDRQYWLITAYHENGSLQDYLTRHI---LSWEDlcKMAGSLARGLAHLHsdrtPCGrpk 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 134 --VIHKDLKPENILVDRDFHIKIADLGVAsfktwSKLtkekDNKqkeVSSTTKKNNG--GTLYYMAPEHL----NDINAK 205
Cdd:cd14055   126 ipIAHRDLKSSNILVKNDGTCVLADFGLA-----LRL----DPS---LSVDELANSGqvGTARYMAPEALesrvNLEDLE 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 206 PTEKSDVYSFGIVLWAIFAK----------KEPYENVI----CTEQFV-ICIKSGNRPNV-EEILEYCPREIIS-LMERC 268
Cdd:cd14055   194 SFKQIDVYSMALVLWEMASRceasgevkpyELPFGSKVrerpCVESMKdLVLRDRGRPEIpDSWLTHQGMCVLCdTITEC 273
                         250
                  ....*....|....*...
gi 1333886239 269 WQAIPEDRPTFLGIEEEF 286
Cdd:cd14055   274 WDHDPEARLTASCVAERF 291
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
26-231 6.04e-11

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: 64.21  E-value: 6.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGF-----VILKKVYTgpNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNL 100
Cdd:cd05604     7 GSFGKVLLAKRKRDGKyyavkVLQKKVIL--NRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVNGGEL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 MHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnKQKEVS 180
Cdd:cd05604    85 FFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLC--------------KEGISN 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333886239 181 STTKKNNGGTLYYMAPEHlndINAKPTEKS-DVYSFGIVLWAIFAKKEPYEN 231
Cdd:cd05604   151 SDTTTTFCGTPEYLAPEV---IRKQPYDNTvDWWCLGSVLYEMLYGLPPFYC 199
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
20-278 6.39e-11

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: 63.37  E-value: 6.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  20 KTDLDSGGFGKVSLCYHRSHGFVILKKVYtgPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGN 99
Cdd:cd14107     7 KEEIGRGTFGFVKRVTHKGNGECCAAKFI--PLRSSTRARAFQERDILARLSHRRLTCLLDQFETRKTLILILELCSSEE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 100 LM-HVLK----TQIDVPLSLKgriivEAIEGMCYLHDKGVIHKDLKPENILV---DRDfHIKIADLGVAsfktwskltke 171
Cdd:cd14107    85 LLdRLFLkgvvTEAEVKLYIQ-----QVLEGIGYLHGMNILHLDIKPDNILMvspTRE-DIKICDFGFA----------- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 172 kdnkQKEVSSTTKKNNGGTLYYMAPEhlnDINAKP-TEKSDVYSFGIVlwaifakkePYENVICTEQFVICIKSGNRPNV 250
Cdd:cd14107   148 ----QEITPSEHQFSKYGSPEFVAPE---IVHQEPvSAATDIWALGVI---------AYLSLTCHSPFAGENDRATLLNV 211
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1333886239 251 EE-ILEYCPREIISLME-------RCWQAIPEDRPT 278
Cdd:cd14107   212 AEgVVSWDTPEITHLSEdakdfikRVLQPDPEKRPS 247
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
37-226 6.42e-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: 63.93  E-value: 6.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  37 RSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYS--LVMEYMEK--GNLMHVLKTqidvPL 112
Cdd:cd07845    30 TSGEIVALKKVRMDNERDGIPISSLREITLLLNLRHPNIVELKEVVVGKHLDSifLVMEYCEQdlASLLDNMPT----PF 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 113 S---LKGrIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasfktwskLTKEKDNKQKEVSSTTKknngg 189
Cdd:cd07845   106 SesqVKC-LMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFG---------LARTYGLPAKPMTPKVV----- 170
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1333886239 190 TLYYMAPEHLNDINaKPTEKSDVYSFGIVLWAIFAKK 226
Cdd:cd07845   171 TLWYRAPELLLGCT-TYTTAIDMWAVGCILAELLAHK 206
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
22-226 7.14e-11

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: 63.51  E-value: 7.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  22 DLDSGGFGKVSLCYHRSHG--FVILKKVYTGPNRAEYNEVLLEEGKMMHRLR---HSRVVKLLGIII-----EEGNYSLV 91
Cdd:cd07862     8 EIGEGAYGKVFKARDLKNGgrFVALKRVRVQTGEEGMPLSTIREVAVLRHLEtfeHPNVVRLFDVCTvsrtdRETKLTLV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  92 MEYMEKGNLMHVLKT-QIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTWskltk 170
Cdd:cd07862    88 FEHVDQDLTTYLDKVpEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARIYSF----- 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333886239 171 ekdnkQKEVSSTTKknnggTLYYMAPEHLndINAKPTEKSDVYSFGIVLWAIFAKK 226
Cdd:cd07862   163 -----QMALTSVVV-----TLWYRAPEVL--LQSSYATPVDLWSVGCIFAEMFRRK 206
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
26-229 7.32e-11

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: 63.83  E-value: 7.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGF-----VILKKVYTgpNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNL 100
Cdd:cd05603     6 GSFGKVLLAKRKCDGKfyavkVLQKKTIL--KKKEQNHIMAERNVLLKNLKHPFLVGLHYSFQTSEKLYFVLDYVNGGEL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 MHVLKTQiDVPLSLKGRI-IVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasfktwskLTKEkDNKQKEV 179
Cdd:cd05603    84 FFHLQRE-RCFLEPRARFyAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFG---------LCKE-GMEPEET 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1333886239 180 SSTTkknnGGTLYYMAPEHLNDinaKPTEKS-DVYSFGIVLWAIFAKKEPY 229
Cdd:cd05603   153 TSTF----CGTPEYLAPEVLRK---EPYDRTvDWWCLGAVLYEMLYGLPPF 196
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
91-230 8.08e-11

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: 63.67  E-value: 8.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  91 VMEYMEKGNLMHVLKT--QIDVPlslKGRIIV-EAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwsk 167
Cdd:cd05591    74 VMEYVNGGDLMFQIQRarKFDEP---RARFYAaEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMC------- 143
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333886239 168 ltkeKDNKQKEVSSTTkknNGGTLYYMAPEHLNDINAKPTekSDVYSFGIVLWAIFAKKEPYE 230
Cdd:cd05591   144 ----KEGILNGKTTTT---FCGTPDYIAPEILQELEYGPS--VDWWALGVLMYEMMAGQPPFE 197
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
8-160 8.47e-11

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: 63.07  E-value: 8.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239   8 DNIKMASSDLLEktdLDSGGFGKVSLCYHRSHGFVILKKvYTGPNRAEYNEVLLEEGkMMHRLRHSRVVKLLGIIIEEGN 87
Cdd:cd14113     3 DNFDSFYSEVAE---LGRGRFSVVKKCDQRGTKRAVATK-FVNKKLMKRDQVTHELG-VLQSLQHPQLVGLLDTFETPTS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  88 YSLVMEYMEKGNLM-HVLK----TQIDVPLSLKgriivEAIEGMCYLHDKGVIHKDLKPENILVDRDFH---IKIADLGV 159
Cdd:cd14113    78 YILVLEMADQGRLLdYVVRwgnlTEEKIRFYLR-----EILEALQYLHNCRIAHLDLKPENILVDQSLSkptIKLADFGD 152

                  .
gi 1333886239 160 A 160
Cdd:cd14113   153 A 153
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
26-197 8.51e-11

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: 63.79  E-value: 8.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGFV----------ILKKVYTGPNRAEYNevLLEEGKmmhrlrHSRVVKLLGIIIEEGNYSLVMEYM 95
Cdd:cd05599    12 GAFGEVRLVRKKDTGHVyamkklrkseMLEKEQVAHVRAERD--ILAEAD------NPWVVKLYYSFQDEENLYLIMEFL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  96 EKGNLMHVL-KTQIdvpLSLKGR--IIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasfktwskLTKEK 172
Cdd:cd05599    84 PGGDMMTLLmKKDT---LTEEETrfYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFG---------LCTGL 151
                         170       180
                  ....*....|....*....|....*
gi 1333886239 173 DNKQKEVSSTtkknngGTLYYMAPE 197
Cdd:cd05599   152 KKSHLAYSTV------GTPDYIAPE 170
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
26-308 8.68e-11

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: 63.92  E-value: 8.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEV--LLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHV 103
Cdd:cd05627    13 GAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVahIRAERDILVEADGAWVVKMFYSFQDKRNLYLIMEFLPGGDMMTL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 104 LKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAS-------FKTWSKLTKE----- 171
Cdd:cd05627    93 LMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTglkkahrTEFYRNLTHNppsdf 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 172 --KDNKQKEVSSTTKKNNG-------GTLYYMAPEHLndINAKPTEKSDVYSFGIVLWAIFAKKEPYENVICTEQFVICI 242
Cdd:cd05627   173 sfQNMNSKRKAETWKKNRRqlaystvGTPDYIAPEVF--MQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETYRKVM 250
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333886239 243 ksgnrpNVEEILEYCPREIIS------LMERCWQAipEDRPTFLGIEE-EFRPFYLSHFEEYVEEDVASLKKE 308
Cdd:cd05627   251 ------NWKETLVFPPEVPISekakdlILRFCTDA--ENRIGSNGVEEiKSHPFFEGVDWEHIRERPAAIPIE 315
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
23-162 9.02e-11

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: 63.81  E-value: 9.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCY-HRSHGFVILKKVYTGPnrAEYNEVLLEEGkMMHRLR-------HSRVVKLLGIIIEEGNYSLVMEY 94
Cdd:cd14212     7 LGQGTFGQVVKCQdLKTNKLVAVKVLKNKP--AYFRQAMLEIA-ILTLLNtkydpedKHHIVRLLDHFMHHGHLCIVFEL 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333886239  95 MEKgNLMHVLKTQ--IDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRD--FHIKIADLGVASF 162
Cdd:cd14212    84 LGV-NLYELLKQNqfRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLdsPEIKLIDFGSACF 154
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
43-229 1.07e-10

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: 63.33  E-value: 1.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  43 ILKKVYTGPNraeynevlleegkmmhrlrhsrVVKLLGIIIEE--GNYSLVMEYMEKGNLMHVLKTQIDVPLSLKGRIIV 120
Cdd:cd14132    65 ILQNLRGGPN----------------------IVKLLDVVKDPqsKTPSLIFEYVNNTDFKTLYPTLTDYDIRYYMYELL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 121 EAIEgmcYLHDKGVIHKDLKPENILVDRDFH-IKIADLGVASFKTwskltkekdnKQKEVSSTTkknngGTLYYMAPEHL 199
Cdd:cd14132   123 KALD---YCHSKGIMHRDVKPHNIMIDHEKRkLRLIDWGLAEFYH----------PGQEYNVRV-----ASRYYKGPELL 184
                         170       180       190
                  ....*....|....*....|....*....|
gi 1333886239 200 NDINaKPTEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14132   185 VDYQ-YYDYSLDMWSLGCMLASMIFRKEPF 213
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
51-222 1.31e-10

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


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 63.34  E-value: 1.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  51 PNRAEYNEVLLEEGKMMHRLRH-SRVVKLLGIIIE-----------EGNYSL--VMEYMEKGNLMHVLKTQIDVPlSLKG 116
Cdd:cd13977    59 PNVIQLEECVLQRDGLAQRMSHgSSKSDLYLLLVEtslkgercfdpRSACYLwfVMEFCDGGDMNEYLLSRRPDR-QTNT 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 117 RIIVEAIEGMCYLHDKGVIHKDLKPENILV--DRDFHI-KIADLGVASFKTWSKLTKEKD-NKQKEVSSTTkknnGGTLY 192
Cdd:cd13977   138 SFMLQLSSALAFLHRNQIVHRDLKPDNILIshKRGEPIlKVADFGLSKVCSGSGLNPEEPaNVNKHFLSSA----CGSDF 213
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1333886239 193 YMAPE----HLndinakpTEKSDVYSFGIVLWAI 222
Cdd:cd13977   214 YMAPEvwegHY-------TAKADIFALGIIIWAM 240
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
117-278 1.36e-10

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: 62.29  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 117 RIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFH-----IKIADLGvasfktwskLTKEKDNKQKEVSSTTkkNNGGTL 191
Cdd:cd13982   103 RLLRQIASGLAHLHSLNIVHRDLKPQNILISTPNAhgnvrAMISDFG---------LCKKLDVGRSSFSRRS--GVAGTS 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 192 YYMAPEHLN-DINAKPTEKSDVYSFGIVLWAIFAK-KEPY-ENVICTEQfvicIKSGNRPNVEEI-LEYCPREIISLMER 267
Cdd:cd13982   172 GWIAPEMLSgSTKRRQTRAVDIFSLGCVFYYVLSGgSHPFgDKLEREAN----ILKGKYSLDKLLsLGEHGPEAQDLIER 247
                         170
                  ....*....|.
gi 1333886239 268 CWQAIPEDRPT 278
Cdd:cd13982   248 MIDFDPEKRPS 258
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
23-158 1.57e-10

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 59.38  E-value: 1.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRaEYNEVLLEEGKMMHRLRHSR--VVKLLGIIIEEGNYSLVMEYMEKGNL 100
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNN-EEGEDLESEMDILRRLKGLElnIPKVLVTEDVDGPNILLMELVKGGTL 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1333886239 101 MHVLKTQIDVPLSLKgRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLG 158
Cdd:cd13968    80 IAYTQEEELDEKDVE-SIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
25-160 1.58e-10

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: 63.05  E-value: 1.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVslCY---HRSHGFVILKKVYTgPNRAE-YNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGN------YSLVMEY 94
Cdd:cd07880    25 SGAYGTV--CSaldRRTGAKVAIKKLYR-PFQSElFAKRAYRELRLLKHMKHENVIGLLDVFTPDLSldrfhdFYLVMPF 101
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333886239  95 M--EKGNLMHVLKTQIDvplslkgRI---IVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVA 160
Cdd:cd07880   102 MgtDLGKLMKHEKLSED-------RIqflVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLA 165
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
21-160 1.87e-10

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: 62.75  E-value: 1.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  21 TDLDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAE-YNEVLLEEGKMMHRLRHSRVVKLLGII-----IEEGNYSLVMEY 94
Cdd:cd07877    23 SPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIiHAKRTYRELRLLKHMKHENVIGLLDVFtparsLEEFNDVYLVTH 102
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333886239  95 MEKGNLMHVLKTQ--IDVPLSLkgrIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVA 160
Cdd:cd07877   103 LMGADLNNIVKCQklTDDHVQF---LIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLA 167
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
75-292 2.04e-10

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 63.14  E-value: 2.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  75 VVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKI 154
Cdd:cd05625    63 VVRLYYSFQDKDNLYFVMDYIPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKL 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 155 ADLGVASFKTW---SKLTKEKDNKQKEVSSTTKKNNG------------------------------GTLYYMAPEHLnd 201
Cdd:cd05625   143 TDFGLCTGFRWthdSKYYQSGDHLRQDSMDFSNEWGDpencrcgdrlkplerraarqhqrclahslvGTPNYIAPEVL-- 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 202 INAKPTEKSDVYSFGIVLWAIFAKKEPYENVICTEQFVICIKSGNRPNVEEILEYCPREIISLMERCWQaiPEDRPTFLG 281
Cdd:cd05625   221 LRTGYTQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRG--PEDRLGKNG 298
                         250
                  ....*....|..
gi 1333886239 282 IEE-EFRPFYLS 292
Cdd:cd05625   299 ADEiKAHPFFKT 310
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
59-222 2.06e-10

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: 61.97  E-value: 2.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  59 VLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLktQIDVPLS--LKGRIIVEAIEGMCYLHDKGVIH 136
Cdd:cd06646    52 LIQQEIFMVKECKHCNIVAYFGSYLSREKLWICMEYCGGGSLQDIY--HVTGPLSelQIAYVCRETLQGLAYLHSKGKMH 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 137 KDLKPENILVDRDFHIKIADLGVAsfktwSKLTkekdnkqkeVSSTTKKNNGGTLYYMAPEhlndinAKPTEKSDVYSFG 216
Cdd:cd06646   130 RDIKGANILLTDNGDVKLADFGVA-----AKIT---------ATIAKRKSFIGTPYWMAPE------VAAVEKNGGYNQL 189

                  ....*.
gi 1333886239 217 IVLWAI 222
Cdd:cd06646   190 CDIWAV 195
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
21-225 2.30e-10

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: 62.59  E-value: 2.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  21 TDLDSGGFGKVSL-CYHR---SHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIE--EGNYsLVMEY 94
Cdd:cd07856    13 SDLQPVGMGAFGLvCSARdqlTGQNVAVKKIMKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIFISplEDIY-FVTEL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MekGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTwSKLTkekdn 174
Cdd:cd07856    92 L--GTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARIQD-PQMT----- 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1333886239 175 kqKEVSsttkknnggTLYYMAPEHLNDINaKPTEKSDVYSFGivlwAIFAK 225
Cdd:cd07856   164 --GYVS---------TRYYRAPEIMLTWQ-KYDVEVDIWSAG----CIFAE 198
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
26-324 2.33e-10

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: 62.73  E-value: 2.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGFVILKKVYTGP---NRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMH 102
Cdd:cd05602    18 GSFGKVLLARHKSDEKFYAVKVLQKKailKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTTDKLYFVLDYINGGELFY 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLKTQiDVPLSLKGRIIVEAI-EGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltkeKDNKQKEVSS 181
Cdd:cd05602    98 HLQRE-RCFLEPRARFYAAEIaSALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLC-----------KENIEPNGTT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 182 TTkknNGGTLYYMAPEHLNDinaKPTEKS-DVYSFGIVLWAIFAKKEPYENVICTEQF--VICIKSGNRPNVEEILEYcp 258
Cdd:cd05602   166 ST---FCGTPEYLAPEVLHK---QPYDRTvDWWCLGAVLYEMLYGLPPFYSRNTAEMYdnILNKPLQLKPNITNSARH-- 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333886239 259 reiisLMERCWQaipEDRPTFLGIEEEFRPFYLSHFEEYVEEDVASLKKEYPDQSPVLQRMFSLQH 324
Cdd:cd05602   238 -----LLEGLLQ---KDRTKRLGAKDDFTEIKNHIFFSPINWDDLINKKITPPFNPNVSGPNDLRH 295
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
26-229 2.63e-10

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: 62.17  E-value: 2.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHG------FVILKKVYTGPNRAeyNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGN 99
Cdd:cd14094    14 GPFSVVRRCIHRETGqqfavkIVDVAKFTSSPGLS--TEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGAD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 100 LMHVLktqidVPLSLKGRIIVEAI---------EGMCYLHDKGVIHKDLKPENIL---VDRDFHIKIADLGVAsfktwsk 167
Cdd:cd14094    92 LCFEI-----VKRADAGFVYSEAVashymrqilEALRYCHDNNIIHRDVKPHCVLlasKENSAPVKLGGFGVA------- 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333886239 168 ltkekdnkqKEVSSTTKKNNG--GTLYYMAPEHLN-DINAKPtekSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14094   160 ---------IQLGESGLVAGGrvGTPHFMAPEVVKrEPYGKP---VDVWGCGVILFILLSGCLPF 212
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
16-228 2.65e-10

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


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 61.47  E-value: 2.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  16 DLLEKtdLDSGGFGKVSLCYHRSHG--------FVILKKVY--TGPNRAeYNEVlleegKMMHRLR-HSRVVKLLGIIIE 84
Cdd:cd14019     4 RIIEK--IGEGTFSSVYKAEDKLHDlydrnkgrLVALKHIYptSSPSRI-LNEL-----ECLERLGgSNNVSGLITAFRN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  85 EGNYSLVMEYMEKGNLMHVLKTqidvpLSLK-----GRIIVEAIEgmcYLHDKGVIHKDLKPENILVDRDF-HIKIADLG 158
Cdd:cd14019    76 EDQVVAVLPYIEHDDFRDFYRK-----MSLTdiriyLRNLFKALK---HVHSFGIIHRDVKPGNFLYNRETgKGVLVDFG 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 159 VASfktwskltKEKDNKQKevssttKKNNGGTLYYMAPEHLNDINAKpTEKSDVYSFGIVLWAIFAKKEP 228
Cdd:cd14019   148 LAQ--------REEDRPEQ------RAPRAGTRGFRAPEVLFKCPHQ-TTAIDIWSAGVILLSILSGRFP 202
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
23-231 3.49e-10

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: 61.46  E-value: 3.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHG-FVILKKVYTGPNRAEYNEVL-LEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNL 100
Cdd:cd05607    10 LGKGGFGEVCAVQVKNTGqMYACKKLDKKRLKKKSGEKMaLLEKEILEKVNSPFIVSLAYAFETKTHLCLVMSLMNGGDL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 MHVLKTQIDVPLSLKgRIIVEAIE---GMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwskltkekdnKQK 177
Cdd:cd05607    90 KYHIYNVGERGIEME-RVIFYSAQitcGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAV-------------EVK 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333886239 178 EVSSTTKKnnGGTLYYMAPEHLNDINAkpTEKSDVYSFGIVLWAIFAKKEPYEN 231
Cdd:cd05607   156 EGKPITQR--AGTNGYMAPEILKEESY--SYPVDWFAMGCSIYEMVAGRTPFRD 205
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
29-220 3.77e-10

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: 61.15  E-value: 3.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  29 GKVSLCYHRSHGFVILKKVYTGPNRAEyNEVLLEegkmMHRLRHSRVVKLLGIIieEGNYS------LVMEYMEKGNLMH 102
Cdd:cd14089    15 GKVLECFHKKTGEKFALKVLRDNPKAR-REVELH----WRASGCPHIVRIIDVY--ENTYQgrkcllVVMECMEGGELFS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 103 VLKTQIDVPLSLK--GRIIVEAIEGMCYLHDKGVIHKDLKPENIL-VDRDFH--IKIADLGVAsfktwskltKEKDNKqk 177
Cdd:cd14089    88 RIQERADSAFTEReaAEIMRQIGSAVAHLHSMNIAHRDLKPENLLySSKGPNaiLKLTDFGFA---------KETTTK-- 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1333886239 178 eVSSTTKKNnggTLYYMAPEHLndiNAKPTEKS-DVYSFGIVLW 220
Cdd:cd14089   157 -KSLQTPCY---TPYYVAPEVL---GPEKYDKScDMWSLGVIMY 193
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
26-332 4.08e-10

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: 62.33  E-value: 4.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSL----CYHRSHGFVIL------KKVYTGPNRAEYNEVLLEEGKMMHRLRHSrvvkllgiiIEEGNY-SLVMEY 94
Cdd:cd05624    83 GAFGEVAVvkmkNTERIYAMKILnkwemlKRAETACFREERNVLVNGDCQWITTLHYA---------FQDENYlYLVMDY 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKGNLMHVL-KTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasfktwSKLtkeKD 173
Cdd:cd05624   154 YVGGDLLTLLsKFEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFG-------SCL---KM 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 174 NKQKEVSSTTKKnngGTLYYMAPEHLN---DINAKPTEKSDVYSFGIVLWAIFAKKEPYENVICTEQFviciksGNRPNV 250
Cdd:cd05624   224 NDDGTVQSSVAV---GTPDYISPEILQameDGMGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETY------GKIMNH 294
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 251 EEILEYcPREIISLMERCWQAIP------EDRPTFLGIeEEFR--PFylshFEEYVEEDVASLKKEY-PD-QSPVLQRMF 320
Cdd:cd05624   295 EERFQF-PSHVTDVSEEAKDLIQrlicsrERRLGQNGI-EDFKkhAF----FEGLNWENIRNLEAPYiPDvSSPSDTSNF 368
                         330
                  ....*....|....*.
gi 1333886239 321 SLQHDCVP----LPPS 332
Cdd:cd05624   369 DVDDDVLRnpeiLPPS 384
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
16-229 4.25e-10

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: 61.20  E-value: 4.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  16 DLLEKTD--LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVME 93
Cdd:cd14174     1 DLYRLTDelLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  94 YMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVdrDFHIKIADLGVASFKTWSKLtkEKD 173
Cdd:cd14174    81 KLRGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILC--ESPDKVSPVKICDFDLGSGV--KLN 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1333886239 174 NKQKEVSSTTKKNNGGTLYYMAPEHLNDINAKPT---EKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14174   157 SACTPITTPELTTPCGSAEYMAPEVVEVFTDEATfydKRCDLWSLGVILYIMLSGYPPF 215
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
18-230 4.51e-10

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: 60.89  E-value: 4.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  18 LEKTdLDSGGFGKVSLCYHRSHGFVILKKVYtgpNRAEYNEV----LLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVME 93
Cdd:cd14074     7 LEET-LGRGHFAVVKLARHVFTGEKVAVKVI---DKTKLDDVskahLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLILE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  94 YMEKGNLM-HVLKTQIDVPLSLKGRI---IVEAIEgmcYLHDKGVIHKDLKPENILV-DRDFHIKIADLGVA-SFKTWSK 167
Cdd:cd14074    83 LGDGGDMYdYIMKHENGLNEDLARKYfrqIVSAIS---YCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSnKFQPGEK 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333886239 168 LTkekdnkqkevssttkkNNGGTLYYMAPE-HLNDINAKPteKSDVYSFGIVLWAIFAKKEPYE 230
Cdd:cd14074   160 LE----------------TSCGSLAYSAPEiLLGDEYDAP--AVDIWSLGVILYMLVCGQPPFQ 205
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
61-226 4.56e-10

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: 61.65  E-value: 4.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  61 LEEGKMMHRLR-HSRVVKLLGI-IIEEGNYSLVMEYMEkgnLMHVLKTQI---DVPLSLK--GRIIVEAIEGMCYLHDKG 133
Cdd:cd07857    49 LRELKLLRHFRgHKNITCLYDMdIVFPGNFNELYLYEE---LMEADLHQIirsGQPLTDAhfQSFIYQILCGLKYIHSAN 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 134 VIHKDLKPENILVDRDFHIKIADLGVAsfKTWSKLTKEKDNKQKEVSSTTkknnggtlYYMAPEHLndINAKPTEKS-DV 212
Cdd:cd07857   126 VLHRDLKPGNLLVNADCELKICDFGLA--RGFSENPGENAGFMTEYVATR--------WYRAPEIM--LSFQSYTKAiDV 193
                         170
                  ....*....|....
gi 1333886239 213 YSFGIVLWAIFAKK 226
Cdd:cd07857   194 WSVGCILAELLGRK 207
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
20-231 4.58e-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: 4.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  20 KTDLDSGGFGKVSLCYHRSHGFVILKKVYTGPNR--AEYNEVLLEEGKmmhrlrHSRVVKLLGIIiEEGNYS-LVMEYME 96
Cdd:cd14178     8 KEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRdpSEEIEILLRYGQ------HPNIITLKDVY-DDGKFVyLVMELMR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  97 KGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENIL-VDRDFH---IKIADLGVAsfktwskltkek 172
Cdd:cd14178    81 GGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILyMDESGNpesIRICDFGFA------------ 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1333886239 173 dnKQKEVSSTTKKNNGGTLYYMAPEHLNDINAKPTekSDVYSFGIVLWAIFAKKEPYEN 231
Cdd:cd14178   149 --KQLRAENGLLMTPCYTANFVAPEVLKRQGYDAA--CDIWSLGILLYTMLAGFTPFAN 203
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
21-226 4.58e-10

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: 61.60  E-value: 4.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  21 TDLDSGGFGKVSLCYH-RSHGFVILKKVyTGP------NRAEYNEVlleegKMMHRLRHSRVVKLLGII-----IEEGNY 88
Cdd:cd07878    21 TPVGSGAYGSVCSAYDtRLRQKVAVKKL-SRPfqslihARRTYREL-----RLLKHMKHENVIGLLDVFtpatsIENFNE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  89 SLVMEYMEKGNLMHVLKTQ--IDVPLSLkgrIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktws 166
Cdd:cd07878    95 VYLVTNLMGADLNNIVKCQklSDEHVQF---LIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLA------ 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333886239 167 kltKEKDNKQKEVSSTTkknnggtlYYMAPE-HLNDINAKPTekSDVYSFGIVLWAIFAKK 226
Cdd:cd07878   166 ---RQADDEMTGYVATR--------WYRAPEiMLNWMHYNQT--VDIWSVGCIMAELLKGK 213
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
23-229 4.97e-10

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: 61.17  E-value: 4.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRS-------HGFVILKKVyTGPNRAEYNEVLLEEGKMMHRLRHSR-VVKLLGIIIEEGNYSLVMEY 94
Cdd:cd05613     8 LGTGAYGKVFLVRKVSghdagklYAMKVLKKA-TIVQKAKTAEHTRTERQVLEHIRQSPfLVTLHYAFQTDTKLHLILDY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKGNLM-HVLK----TQIDVPLSLkGRIIVeAIEgmcYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasfktwskLT 169
Cdd:cd05613    87 INGGELFtHLSQrerfTENEVQIYI-GEIVL-ALE---HLHKLGIIYRDIKLENILLDSSGHVVLTDFG---------LS 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 170 KEKDNKQKEVSSTTkknnGGTLYYMAPEHLNDINAKPTEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd05613   153 KEFLLDENERAYSF----CGTIEYMAPEIVRGGDSGHDKAVDWWSLGVLMYELLTGASPF 208
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
20-231 5.70e-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: 60.81  E-value: 5.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  20 KTDLDSGGFGKVSLCYHRS----HGFVILKKVYTGPnrAEYNEVLLEEGKmmhrlrHSRVVKLLGIIiEEGNY-SLVMEY 94
Cdd:cd14175     6 KETIGVGSYSVCKRCVHKAtnmeYAVKVIDKSKRDP--SEEIEILLRYGQ------HPNIITLKDVY-DDGKHvYLVTEL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKGNLM-HVLKTQI--DVPLSLKGRIIVEAIEgmcYLHDKGVIHKDLKPENIL-VDRDFH---IKIADLGVAsfktwsk 167
Cdd:cd14175    77 MRGGELLdKILRQKFfsEREASSVLHTICKTVE---YLHSQGVVHRDLKPSNILyVDESGNpesLRICDFGFA------- 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333886239 168 ltkekdnKQKEVSSTTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPYEN 231
Cdd:cd14175   147 -------KQLRAENGLLMTPCYTANFVAPEVLK--RQGYDEGCDIWSLGILLYTMLAGYTPFAN 201
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
16-278 6.04e-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: 60.46  E-value: 6.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  16 DLLEKTD-LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEY 94
Cdd:cd06642     4 ELFTKLErIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKGNLMHVLKTQidvPL--SLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwskltkek 172
Cdd:cd06642    84 LGGGSALDLLKPG---PLeeTYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAG----------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 173 dnkqkEVSSTTKKNNG--GTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIfAKKEPYENVICTEQFVICIKSGNRPNV 250
Cdd:cd06642   150 -----QLTDTQIKRNTfvGTPFWMAPEVIK--QSAYDFKADIWSLGITAIEL-AKGEPPNSDLHPMRVLFLIPKNSPPTL 221
                         250       260
                  ....*....|....*....|....*...
gi 1333886239 251 EEILEYCPREIIslmERCWQAIPEDRPT 278
Cdd:cd06642   222 EGQHSKPFKEFV---EACLNKDPRFRPT 246
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
58-278 6.76e-10

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: 60.45  E-value: 6.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  58 EVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKT----QIDVPLSLKgriivEAIEGMCYLHDKG 133
Cdd:cd06640    47 EDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGGGSALDLLRAgpfdEFQIATMLK-----EILKGLDYLHSEK 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 134 VIHKDLKPENILVDRDFHIKIADLGVAsfktwSKLTKEKDNKQKEVssttkknngGTLYYMAPEHLNdiNAKPTEKSDVY 213
Cdd:cd06640   122 KIHRDIKAANVLLSEQGDVKLADFGVA-----GQLTDTQIKRNTFV---------GTPFWMAPEVIQ--QSAYDSKADIW 185
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333886239 214 SFGIVLWAIfAKKEPYENVICTEQFVICIKSGNRPNVEEILEYCPREIIslmERCWQAIPEDRPT 278
Cdd:cd06640   186 SLGITAIEL-AKGEPPNSDMHPMRVLFLIPKNNPPTLVGDFSKPFKEFI---DACLNKDPSFRPT 246
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
26-220 7.08e-10

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: 7.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGFVILKKVYTGP---NRAEYNEVLLEEGKMMHRLRHSRVVKLlgiiieegNYSL--------VMEY 94
Cdd:cd05575     6 GSFGKVLLARHKAEGKLYAVKVLQKKailKRNEVKHIMAERNVLLKNVKHPFLVGL--------HYSFqtkdklyfVLDY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasfktwskLTKEkDN 174
Cdd:cd05575    78 VNGGELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFG---------LCKE-GI 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1333886239 175 KQKEVSSTTkknnGGTLYYMAPEHLNDinaKPTEKS-DVYSFGIVLW 220
Cdd:cd05575   148 EPSDTTSTF----CGTPEYLAPEVLRK---QPYDRTvDWWCLGAVLY 187
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
22-231 7.76e-10

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: 60.00  E-value: 7.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  22 DLDSGGFGKVSLCYHRSHGFVILKKVYtgpNRAEYNEVLLEEGKMMHR-LRHSRVVKLLGIIIEEGNYSLVMEYMEKGNL 100
Cdd:cd14665     7 DIGSGNFGVARLMRDKQTKELVAVKYI---ERGEKIDENVQREIINHRsLRHPNIVRFKEVILTPTHLAIVMEYAAGGEL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 101 MHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDF--HIKIADLGvasfktWSKltkekdnkqKE 178
Cdd:cd14665    84 FERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPapRLKICDFG------YSK---------SS 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1333886239 179 VSSTTKKNNGGTLYYMAPEHL--NDINAKpteKSDVYSFGIVLWAIFAKKEPYEN 231
Cdd:cd14665   149 VLHSQPKSTVGTPAYIAPEVLlkKEYDGK---IADVWSCGVTLYVMLVGAYPFED 200
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
41-277 9.35e-10

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: 60.03  E-value: 9.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  41 FVILKKV---YTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEE-GNYSLVMEYMeKGNLMHVLKTQIDVPLS--- 113
Cdd:cd14011    27 FVFEKKQleeYSKRDREQILELLKRGVKQLTRLRHPRILTVQHPLEESrESLAFATEPV-FASLANVLGERDNMPSPppe 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 114 LKGRIIVEA---------IEGMCYLH-DKGVIHKDLKPENILVDRDFHIKIADLG----VASFKTWSKLTKEKDNKQKEV 179
Cdd:cd14011   106 LQDYKLYDVeikygllqiSEALSFLHnDVKLVHGNICPESVVINSNGEWKLAGFDfcisSEQATDQFPYFREYDPNLPPL 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 180 SSTtkknnggTLYYMAPEH-LNDINakpTEKSDVYSFGIVLWAIFAK-KEPYENVICTEQFVICIKSGNRPNvEEILEYC 257
Cdd:cd14011   186 AQP-------NLNYLAPEYiLSKTC---DPASDMFSLGVLIYAIYNKgKPLFDCVNNLLSYKKNSNQLRQLS-LSLLEKV 254
                         250       260
                  ....*....|....*....|
gi 1333886239 258 PREIISLMERCWQAIPEDRP 277
Cdd:cd14011   255 PEELRDHVKTLLNVTPEVRP 274
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
11-229 9.50e-10

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 60.76  E-value: 9.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  11 KMASSDLLEKTDLDSGGFGKVSLCYHRSHGF--VILKKVYTGPN-RAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGN 87
Cdd:PTZ00426   26 KMKYEDFNFIRTLGTGSFGRVILATYKNEDFppVAIKRFEKSKIiKQKQVDHVFSERKILNYINHPFCVNLYGSFKDESY 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  88 YSLVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwsk 167
Cdd:PTZ00426  106 LYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFA------- 178
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333886239 168 ltkekdnkqkEVSSTTKKNNGGTLYYMAPEHLndINAKPTEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:PTZ00426  179 ----------KVVDTRTYTLCGTPEYIAPEIL--LNVGHGKAADWWTLGIFIYEILVGCPPF 228
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
20-229 9.74e-10

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: 60.45  E-value: 9.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  20 KTDLDSGGFGKVSLCYHRSHGFV-----ILKKVYTGPNRAEYNEVlleegKMMHRLRHSRVVKLLGIIIEEGNYSLVMEY 94
Cdd:cd14168    15 KEVLGTGAFSEVVLAEERATGKLfavkcIPKKALKGKESSIENEI-----AVLRKIKHENIVALEDIYESPNHLYLVMQL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILV---DRDFHIKIADLGVasfktwSKLTKE 171
Cdd:cd14168    90 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGL------SKMEGK 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1333886239 172 KDnkqkeVSSTTkknnGGTLYYMAPEHLNDinaKPTEKS-DVYSFGIVLWAIFAKKEPY 229
Cdd:cd14168   164 GD-----VMSTA----CGTPGYVAPEVLAQ---KPYSKAvDCWSIGVIAYILLCGYPPF 210
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
23-229 1.05e-09

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: 59.87  E-value: 1.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLE-EGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLM 101
Cdd:cd14097     9 LGQGSFGVVIEATHKETQTKWAIKKINREKAGSSAVKLLErEVDILKHVNHAHIIHLEEVFETPKRMYLVMELCEDGELK 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 HVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRD-------FHIKIADLGVASfktwskltkekdn 174
Cdd:cd14097    89 ELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSiidnndkLNIKVTDFGLSV------------- 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1333886239 175 KQKEVSSTTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14097   156 QKYGLGEDMLQETCGTPIYMAPEVIS--AHGYSQQCDIWSIGVIMYMLLCGEPPF 208
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
23-228 1.13e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 60.63  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHR---SHGFVILKKVYTGPNRAEynevlleEGKMMHRLRHSRVVKLlgiIIEEGNYSLVMEYMEKgn 99
Cdd:PHA03207  100 LTPGSEGEVFVCTKHgdeQRKKVIVKAVTGGKTPGR-------EIDILKTISHRAIINL---IHAYRWKSTVCMVMPK-- 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 100 LMHVLKTQIDV--PLSLKGRIIVEA--IEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwSKLTKEKDNK 175
Cdd:PHA03207  168 YKCDLFTYVDRsgPLPLEQAITIQRrlLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAA-----CKLDAHPDTP 242
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333886239 176 QKEVSSTTKKNNGGTLYYMAPEhlndinakpTEKSDVYSFGIVLWAIFAKKEP 228
Cdd:PHA03207  243 QCYGWSGTLETNSPELLALDPY---------CAKTDIWSAGLVLFEMSVKNVT 286
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
26-236 1.20e-09

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: 60.44  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGFV----------ILKKVYTGPNRAEyNEVLLEEGKMMhrlrhsrVVKLLGIIIEEGNYSLVMEYM 95
Cdd:cd05628    12 GAFGEVRLVQKKDTGHVyamkilrkadMLEKEQVGHIRAE-RDILVEADSLW-------VVKMFYSFQDKLNLYLIMEFL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  96 EKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASFKTWSKLTKEKDN- 174
Cdd:cd05628    84 PGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTGLKKAHRTEFYRNl 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 175 -------------KQKEVSSTTKKNNG-------GTLYYMAPEHLndINAKPTEKSDVYSFGIVLWAIFAKKEPYenviC 234
Cdd:cd05628   164 nhslpsdftfqnmNSKRKAETWKRNRRqlafstvGTPDYIAPEVF--MQTGYNKLCDWWSLGVIMYEMLIGYPPF----C 237

                  ..
gi 1333886239 235 TE 236
Cdd:cd05628   238 SE 239
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
23-229 1.20e-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: 59.71  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRS---HGFV----ILKKVyTGPNRAEYNEVLLEEGKMMHRLRHSR-VVKLLGIIIEEGNYSLVMEY 94
Cdd:cd05583     2 LGTGAYGKVFLVRKVGghdAGKLyamkVLKKA-TIVQKAKTAEHTMTERQVLEAVRQSPfLVTLHYAFQTDAKLHLILDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKGNLMHVLKTQIDVPLSlKGRI----IVEAIEgmcYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasfktwskLTK 170
Cdd:cd05583    81 VNGGELFTHLYQREHFTES-EVRIyigeIVLALE---HLHKLGIIYRDIKLENILLDSEGHVVLTDFG---------LSK 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1333886239 171 EKDNKQKEVSSTTkknnGGTLYYMAPEHLNDINAKPTEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd05583   148 EFLPGENDRAYSF----CGTIEYMAPEVVRGGSDGHDKAVDWWSLGVLTYELLTGASPF 202
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
23-223 1.25e-09

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


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 60.15  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTgpNRAEYNEVLLEEGKMMHRLRHS-----RVVKLLGIIIEEGNYSLVMEYMEK 97
Cdd:cd14211     7 LGRGTFGQVVKCWKRGTNEIVAIKILK--NHPSYARQGQIEVSILSRLSQEnadefNFVRAYECFQHKNHTCLVFEMLEQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  98 gNLMHVLKTQIDVPLSLK--GRIIVEAIEGMCYLHDKGVIHKDLKPENI-LVD---RDFHIKIADLGVASFKTwskltke 171
Cdd:cd14211    85 -NLYDFLKQNKFSPLPLKyiRPILQQVLTALLKLKSLGLIHADLKPENImLVDpvrQPYRVKVIDFGSASHVS------- 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333886239 172 kdnkqKEVSSTTKKNNggtlYYMAPEHLndINAKPTEKSDVYSFGIVLWAIF 223
Cdd:cd14211   157 -----KAVCSTYLQSR----YYRAPEII--LGLPFCEAIDMWSLGCVIAELF 197
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
16-160 1.43e-09

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: 59.37  E-value: 1.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  16 DLLEKtdLDSGGFGKVSLCYHR-SHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEY 94
Cdd:cd07839     3 EKLEK--IGEGTYGTVFKAKNReTHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLYDVLHSDKKLTLVFEY 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333886239  95 MEKGnlmhvLKTQIDvplSLKGRI--------IVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVA 160
Cdd:cd07839    81 CDQD-----LKKYFD---SCNGDIdpeivksfMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLA 146
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
52-231 1.51e-09

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: 59.45  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  52 NRAEYNEVLLEEGKMMHRLR-HSRVVKLLGI--IIEEGNYSLVMEYME-----KGNLMHVLKTQID-VPLSLKG--RIIV 120
Cdd:cd14036    36 NEEEKNKAIIQEINFMKKLSgHPNIVQFCSAasIGKEESDQGQAEYLLltelcKGQLVDFVKKVEApGPFSPDTvlKIFY 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 121 EAIEGMCYLHDKG--VIHKDLKPENILVDRDFHIKIADLGVASFKTWSKLTKEKDNKQKEVSSTTKKNNggTLYYMAPEH 198
Cdd:cd14036   116 QTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGSATTEAHYPDYSWSAQKRSLVEDEITRNT--TPMYRTPEM 193
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1333886239 199 LNDINAKP-TEKSDVYSFGIVLWAIFAKKEPYEN 231
Cdd:cd14036   194 IDLYSNYPiGEKQDIWALGCILYLLCFRKHPFED 227
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
90-188 1.67e-09

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 60.25  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  90 LVMEYMEKGNLMHVL-KTQI---DVPLSLKGRIIVeAIEGmcyLHDKGVIHKDLKPENILVDRDFHIKIADLGVAS--FK 163
Cdd:cd05629    78 LIMEFLPGGDLMTMLiKYDTfseDVTRFYMAECVL-AIEA---VHKLGFIHRDIKPDNILIDRGGHIKLSDFGLSTgfHK 153
                          90       100
                  ....*....|....*....|....*
gi 1333886239 164 TWSKLTKEKDNKQKEVSSTTKKNNG 188
Cdd:cd05629   154 QHDSAYYQKLLQGKSNKNRIDNRNS 178
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
90-230 1.70e-09

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: 60.03  E-value: 1.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  90 LVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwsklt 169
Cdd:cd05617    93 LVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMC--------- 163
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333886239 170 kekdnKQKEVSSTTKKNNGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKKEPYE 230
Cdd:cd05617   164 -----KEGLGPGDTTSTFCGTPNYIAPEILR--GEEYGFSVDWWALGVLMFEMMAGRSPFD 217
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
62-260 1.78e-09

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: 59.35  E-value: 1.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  62 EEGKMMHRLRHSRVVKLL----GIIIEEGNYSLVMEYMEKGNLMHVLKT-QIDVPLSLKGrIIVEAIEGMCYLHDKG--V 134
Cdd:cd14031    58 EEAEMLKGLQHPNIVRFYdsweSVLKGKKCIVLVTELMTSGTLKTYLKRfKVMKPKVLRS-WCRQILKGLQFLHTRTppI 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 135 IHKDLKPENILVDRDF-HIKIADLGVASFktwskltkekdnkqkeVSSTTKKNNGGTLYYMAPEHLNDinaKPTEKSDVY 213
Cdd:cd14031   137 IHRDLKCDNIFITGPTgSVKIGDLGLATL----------------MRTSFAKSVIGTPEFMAPEMYEE---HYDESVDVY 197
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333886239 214 SFGIVLWAIFAKKEPYENVICTEQFVICIKSGNR---------PNVEEILEYCPRE 260
Cdd:cd14031   198 AFGMCMLEMATSEYPYSECQNAAQIYRKVTSGIKpasfnkvtdPEVKEIIEGCIRQ 253
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
58-229 1.95e-09

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: 59.45  E-value: 1.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  58 EVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHK 137
Cdd:cd14085    43 KIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHR 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 138 DLKPENILVDR---DFHIKIADLGVasfktwSKLTKEKdnkqkevssTTKKNNGGTLYYMAPEHLNDINAKPteKSDVYS 214
Cdd:cd14085   123 DLKPENLLYATpapDAPLKIADFGL------SKIVDQQ---------VTMKTVCGTPGYCAPEILRGCAYGP--EVDMWS 185
                         170
                  ....*....|....*
gi 1333886239 215 FGIVLWAIFAKKEPY 229
Cdd:cd14085   186 VGVITYILLCGFEPF 200
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
60-217 2.00e-09

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


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 59.62  E-value: 2.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  60 LLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQIDV--PLSLKGRIIVEAIEGMCYLHDKGVIHK 137
Cdd:cd08216    46 LQQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPLMAYGSCRDLLKTHFPEglPELAIAFILRDVLNALEYIHSKGYIHR 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 138 DLKPENILVDRDFHIKIADLGVA-SFktwskltKEKDNKQKEVSSTTkKNNGGTLYYMAPEHLNDINAKPTEKSDVYSFG 216
Cdd:cd08216   126 SVKASHILISGDGKVVLSGLRYAySM-------VKHGKRQRVVHDFP-KSSEKNLPWLSPEVLQQNLLGYNEKSDIYSVG 197

                  .
gi 1333886239 217 I 217
Cdd:cd08216   198 I 198
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
23-162 2.49e-09

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: 59.12  E-value: 2.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCY-HRSHGFVILKKVytgpnRAE--YNEVLLEEGKMMHRLRH------SRVVKLLGIIIEEGNYSLVME 93
Cdd:cd14134    20 LGEGTFGKVLECWdRKRKRYVAVKII-----RNVekYREAAKIEIDVLETLAEkdpngkSHCVQLRDWFDYRGHMCIVFE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  94 --------YMEKGNLmhvlktqIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENIL-VDRDF-------------- 150
Cdd:cd14134    95 llgpslydFLKKNNY-------GPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILlVDSDYvkvynpkkkrqirv 167
                         170
                  ....*....|....*.
gi 1333886239 151 ----HIKIADLGVASF 162
Cdd:cd14134   168 pkstDIKLIDFGSATF 183
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
63-216 2.50e-09

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: 59.35  E-value: 2.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  63 EGKMMHRLRHSRVVKLLGIIIEEGNYS------LVMEYMEkGNLMHVLKTQIDVP-LSLkgrIIVEAIEGMCYLHDKGVI 135
Cdd:cd07850    49 ELVLMKLVNHKNIIGLLNVFTPQKSLEefqdvyLVMELMD-ANLCQVIQMDLDHErMSY---LLYQMLCGIKHLHSAGII 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 136 HKDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnkQKEVSSTTKKNNGGTLYYMAPEHLNDINAKptEKSDVYSF 215
Cdd:cd07850   125 HRDLKPSNIVVKSDCTLKILDFGLA---------------RTAGTSFMMTPYVVTRYYRAPEVILGMGYK--ENVDIWSV 187

                  .
gi 1333886239 216 G 216
Cdd:cd07850   188 G 188
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
51-282 2.59e-09

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit, common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. Jaks 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 Jak3 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: 271110 [Multi-domain]  Cd Length: 260  Bit Score: 58.38  E-value: 2.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  51 PNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEeGNYSLVMEYMEKGNLMHVLKTQ---IDVPLSLKGRIIVEAIEGMC 127
Cdd:cd14208    40 PTHGNCQESFLEAASIMSQISHKHLVLLHGVCVG-KDSIMVQEFVCHGALDLYLKKQqqkGPVAISWKLQVVKQLAYALN 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 128 YLHDKGVIHKDLKPENILVDRDF------HIKIADLGVASFKTWSKLTKEKdnkqkevssttkknnggtLYYMAPEHLND 201
Cdd:cd14208   119 YLEDKQLVHGNVSAKKVLLSREGdkgsppFIKLSDPGVSIKVLDEELLAER------------------IPWVAPECLSD 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 202 INAKPTEkSDVYSFGIVLWAIF-------AKKEPYENVicteQFVICIKSGNRPNVEeileycprEIISLMERCWQAIPE 274
Cdd:cd14208   181 PQNLALE-ADKWGFGATLWEIFsgghmplSALDPSKKL----QFYNDRKQLPAPHWI--------ELASLIQQCMSYNPL 247

                  ....*...
gi 1333886239 275 DRPTFLGI 282
Cdd:cd14208   248 LRPSFRAI 255
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
69-278 3.22e-09

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 58.10  E-value: 3.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  69 RLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQidVPLSLKGRIIV--EAIEGMCYLHDKGVIHKDLKPENILV 146
Cdd:cd13995    52 CFRHENIAELYGALLWEETVHLFMEAGEGGSVLEKLESC--GPMREFEIIWVtkHVLKGLDFLHSKNIIHHDIKPSNIVF 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 147 DRDFHIkIADLGVaSFKTWSKLTKEKDNKqkevssttkknngGTLYYMAPEHLndINAKPTEKSDVYSFGIVLWAIFAKK 226
Cdd:cd13995   130 MSTKAV-LVDFGL-SVQMTEDVYVPKDLR-------------GTEIYMSPEVI--LCRGHNTKADIYSLGATIIHMQTGS 192
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333886239 227 EPYENVICTEQF--VICIKSGNRPNVEEILEYCPREIISLMERCWQAIPEDRPT 278
Cdd:cd13995   193 PPWVRRYPRSAYpsYLYIIHKQAPPLEDIAQDCSPAMRELLEAALERNPNHRSS 246
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
11-199 3.91e-09

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: 58.55  E-value: 3.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  11 KMASSDLLEKtdLDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSL 90
Cdd:cd07869     3 KADSYEKLEK--LGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  91 VMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwskltk 170
Cdd:cd07869    81 VFEYVHTDLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLA---------- 150
                         170       180
                  ....*....|....*....|....*....
gi 1333886239 171 ekdnKQKEVSSTTKKNNGGTLYYMAPEHL 199
Cdd:cd07869   151 ----RAKSVPSHTYSNEVVTLWYRPPDVL 175
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
60-225 4.09e-09

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: 58.64  E-value: 4.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  60 LLEEGKMMHRLRHSRVVKLLGIII-----EEGNYSLVMEYMEKgNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGV 134
Cdd:cd07859    46 ILREIKLLRLLRHPDIVEIKHIMLppsrrEFKDIYVVFELMES-DLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANV 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 135 IHKDLKPENILVDRDFHIKIADLGVASFKTwskltkekdnkQKEVSSTTKKNNGGTLYYMAPEHLNDINAKPTEKSDVYS 214
Cdd:cd07859   125 FHRDLKPKNILANADCKLKICDFGLARVAF-----------NDTPTAIFWTDYVATRWYRAPELCGSFFSKYTPAIDIWS 193
                         170
                  ....*....|.
gi 1333886239 215 FGivlwAIFAK 225
Cdd:cd07859   194 IG----CIFAE 200
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
121-229 4.23e-09

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: 58.22  E-value: 4.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 121 EAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwskltkekdnkqkEVSSTTKKNNGGTLYYMAPEHLn 200
Cdd:cd05606   106 EVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLAC----------------DFSKKKPHASVGTHGYMAPEVL- 168
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1333886239 201 dinAKPT---EKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd05606   169 ---QKGVaydSSADWFSLGCMLYKLLKGHSPF 197
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
23-223 4.58e-09

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: 58.50  E-value: 4.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHR-SHGFVILKKVYTGPNRAEYNEVlleEGKMMHRLRHSRV-----VKLLGIIIEEGNYSLVMEYME 96
Cdd:cd14229     8 LGRGTFGQVVKCWKRgTNEIVAVKILKNHPSYARQGQI---EVGILARLSNENAdefnfVRAYECFQHRNHTCLVFEMLE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  97 KgNLMHVLKTQIDVPLSLK--GRIIVEAIEGMCYLHDKGVIHKDLKPENI-LVD---RDFHIKIADLGVASFKTwskltk 170
Cdd:cd14229    85 Q-NLYDFLKQNKFSPLPLKviRPILQQVATALKKLKSLGLIHADLKPENImLVDpvrQPYRVKVIDFGSASHVS------ 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333886239 171 ekdnkqKEVSSTTKKNNggtlYYMAPEHLndINAKPTEKSDVYSFGIVLWAIF 223
Cdd:cd14229   158 ------KTVCSTYLQSR----YYRAPEII--LGLPFCEAIDMWSLGCVIAELF 198
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
63-222 4.83e-09

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK2 plays a role in mediating NFkB activation by TLR3, TLR4, and TLR8. It is specifically targeted by the viral protein A52, which is important for virulence, to inhibit all IL-1/TLR pathways, indicating that IRAK2 has a predominant role in NFkB activation. It is redundant with IRAK1 in early signaling but is critical for late and sustained activation. The IRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271059 [Multi-domain]  Cd Length: 289  Bit Score: 57.92  E-value: 4.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  63 EGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQID---VPLSLKGRIIVEAIEGMCYLHDKGVIHKDL 139
Cdd:cd14157    42 EVQICFRCCHPNILPLLGFCVESDCHCLIYPYMPNGSLQDRLQQQGGshpLPWEQRLSISLGLLKAVQHLHNFGILHGNI 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 140 KPENILVDRDFHIKIADLGvASFKTWSKLTKEKDNKQKEVSSttkknnggTLYYMAPEHLNdiNAKPTEKSDVYSFGIVL 219
Cdd:cd14157   122 KSSNVLLDGNLLPKLGHSG-LRLCPVDKKSVYTMMKTKVLQI--------SLAYLPEDFVR--HGQLTEKVDIFSCGVVL 190

                  ...
gi 1333886239 220 WAI 222
Cdd:cd14157   191 AEI 193
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
72-232 5.73e-09

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: 58.51  E-value: 5.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  72 HSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFH 151
Cdd:cd05618    80 HPFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGH 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 152 IKIADLGVAsfktwskltkekdnKQKEVSSTTKKNNGGTLYYMAPEHLNDINAKPTekSDVYSFGIVLWAIFAKKEPYEN 231
Cdd:cd05618   160 IKLTDYGMC--------------KEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFS--VDWWALGVLMFEMMAGRSPFDI 223

                  .
gi 1333886239 232 V 232
Cdd:cd05618   224 V 224
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
90-229 6.78e-09

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: 57.97  E-value: 6.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  90 LVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwSKLT 169
Cdd:cd05586    73 LVTDYMSGGELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSK----ADLT 148
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 170 KEKdnkqkevsstTKKNNGGTLYYMAPEHLNDiNAKPTEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd05586   149 DNK----------TTNTFCGTTEYLAPEVLLD-EKGYTKMVDFWSLGVLVFEMCCGWSPF 197
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
61-223 7.59e-09

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: 57.28  E-value: 7.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  61 LEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKgnlmHVLKTQIDVPLSLKGR----IIVEAIEGMCYLHDKGVIH 136
Cdd:cd07870    46 IREASLLKGLKHANIVLLHDIIHTKETLTFVFEYMHT----DLAQYMIQHPGGLHPYnvrlFMFQLLRGLAYIHGQHILH 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 137 KDLKPENILVDRDFHIKIADLGVAsfktwskltkekdnKQKEVSSTTKKNNGGTLYYMAPehlnDINAKPTEKS---DVY 213
Cdd:cd07870   122 RDLKPQNLLISYLGELKLADFGLA--------------RAKSIPSQTYSSEVVTLWYRPP----DVLLGATDYSsalDIW 183
                         170
                  ....*....|
gi 1333886239 214 SFGIVLWAIF 223
Cdd:cd07870   184 GAGCIFIEML 193
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
26-229 9.10e-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: 56.83  E-value: 9.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGFVILKKVYtgPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLK 105
Cdd:cd14108    13 GAFSYLRRVKEKSSDLSFAAKFI--PVRAKKKTSARRELALLAELDHKSIVRFHDAFEKRRVVIIVTELCHEELLERITK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 106 tQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILV--DRDFHIKIADLGvasfktwskltkekdNKQKEVSSTT 183
Cdd:cd14108    91 -RPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMadQKTDQVRICDFG---------------NAQELTPNEP 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1333886239 184 KKNNGGTLYYMAPEhlnDINAKPTEKS-DVYSFGIVLWAIFAKKEPY 229
Cdd:cd14108   155 QYCKYGTPEFVAPE---IVNQSPVSKVtDIWPVGVIAYLCLTGISPF 198
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
15-217 1.05e-08

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: 56.94  E-value: 1.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  15 SDLLEKTD-LDSGGFGKVSLCYHRSHG----FVILKKVYtgpnraEYNEVLLEEGKMMHRLR-HSRVVKLLGIIIEEGNY 88
Cdd:cd06638    17 SDTWEIIEtIGKGTYGKVFKVLNKKNGskaaVKILDPIH------DIDEEIEAEYNILKALSdHPNVVKFYGMYYKKDVK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  89 S-----LVMEYMEKGNLMHVLKTQIDVPLSLKGRIIV----EAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGV 159
Cdd:cd06638    91 NgdqlwLVLELCNGGSVTDLVKGFLKRGERMEEPIIAyilhEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGV 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333886239 160 AsfktwSKLTKEKDNKQKEVssttkknngGTLYYMAPEHL---NDINAKPTEKSDVYSFGI 217
Cdd:cd06638   171 S-----AQLTSTRLRRNTSV---------GTPFWMAPEVIaceQQLDSTYDARCDVWSLGI 217
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
42-285 1.07e-08

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Jak1 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: 270662 [Multi-domain]  Cd Length: 266  Bit Score: 56.87  E-value: 1.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  42 VILKKVytGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNL---MHVLKTQIDVPLSLKgrI 118
Cdd:cd05077    39 VILKVL--DPSHRDISLAFFETASMMRQVSHKHIVLLYGVCVRDVENIMVEEFVEFGPLdlfMHRKSDVLTTPWKFK--V 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 119 IVEAIEGMCYLHDKGVIHKDLKPENILVDRDF-------HIKIADLGVAsfktwskltkekdnkqkeVSSTTKKNNGGTL 191
Cdd:cd05077   115 AKQLASALSYLEDKDLVHGNVCTKNILLAREGidgecgpFIKLSDPGIP------------------ITVLSRQECVERI 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 192 YYMAPEHLNDiNAKPTEKSDVYSFGIVLWAIFAKKEpyenvicteqfvICIKSGNRPNVEEILEYCPR-------EIISL 264
Cdd:cd05077   177 PWIAPECVED-SKNLSIAADKWSFGTTLWEICYNGE------------IPLKDKTLAEKERFYEGQCMlvtpsckELADL 243
                         250       260
                  ....*....|....*....|.
gi 1333886239 265 MERCWQAIPEDRPTFLGIEEE 285
Cdd:cd05077   244 MTHCMNYDPNQRPFFRAIMRD 264
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
23-160 1.13e-08

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


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 57.12  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIiiEEGNYS----LVMEYMEKG 98
Cdd:cd13988     1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSFMRPLDVQMREFEVLKKLNHKNIVKLFAI--EEELTTrhkvLVMELCPCG 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333886239  99 NLMHVLktqiDVPLSLKG-------RIIVEAIEGMCYLHDKGVIHKDLKPENIL--VDRDFH--IKIADLGVA 160
Cdd:cd13988    79 SLYTVL----EEPSNAYGlpeseflIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDGQsvYKLTDFGAA 147
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
71-298 1.16e-08

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 57.72  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  71 RHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQIDVPLSLK----GRIIVEAIEGMCYLHDKGVIHKDLKPENILV 146
Cdd:PTZ00267  123 DHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQIKQRLKEHLPFQeyevGLLFYQIVLALDEVHSRKMMHRDLKSANIFL 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 147 DRDFHIKIADLGVAsfKTWSkltkekDNKQKEVSSTTkknnGGTLYYMAPEHLNdiNAKPTEKSDVYSFGIVLWAIFAKK 226
Cdd:PTZ00267  203 MPTGIIKLGDFGFS--KQYS------DSVSLDVASSF----CGTPYYLAPELWE--RKRYSKKADMWSLGVILYELLTLH 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 227 EPYENvicteqfviciksgnrPNVEEILEY----------CP--REIISLMERCWQAIPEDRPTFLG-IEEEFRPFYLSH 293
Cdd:PTZ00267  269 RPFKG----------------PSQREIMQQvlygkydpfpCPvsSGMKALLDPLLSKNPALRPTTQQlLHTEFLKYVANL 332

                  ....*
gi 1333886239 294 FEEYV 298
Cdd:PTZ00267  333 FQDIV 337
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
66-282 1.31e-08

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: 57.41  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  66 MMHRLRHSRVVKLLGIII------EEGNYSLVMEYMEkGNLMHVLKTQIDvpLSLKGRIIVEAIEGMCYLHDKGVIHKDL 139
Cdd:cd07874    69 LMKCVNHKNIISLLNVFTpqksleEFQDVYLVMELMD-ANLCQVIQMELD--HERMSYLLYQMLCGIKHLHSAGIIHRDL 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 140 KPENILVDRDFHIKIADLGVAsfktwskltkekdnkQKEVSSTTKKNNGGTLYYMAPEHLNDINAKptEKSDVYSFGIVL 219
Cdd:cd07874   146 KPSNIVVKSDCTLKILDFGLA---------------RTAGTSFMMTPYVVTRYYRAPEVILGMGYK--ENVDIWSVGCIM 208
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333886239 220 WAIFAKKEPYENVICTEQFVICIKSGNRPnveeileyCPrEIISLMERCWQAIPEDRPTFLGI 282
Cdd:cd07874   209 GEMVRHKILFPGRDYIDQWNKVIEQLGTP--------CP-EFMKKLQPTVRNYVENRPKYAGL 262
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
6-217 1.34e-08

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: 56.55  E-value: 1.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239   6 SLDNIKMAS----SDLLEKTDL-DSGGFGKVSLCYHRSHGFVILKKVYTGPNRAEynEVLLEEGKMMHRLRHSR-VVKLL 79
Cdd:cd06636     2 SLDDIDLSAlrdpAGIFELVEVvGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEE--EEIKLEINMLKKYSHHRnIATYY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  80 GIIIEEG------NYSLVMEYMEKGNLMHVLKTQIDVPLSLK--GRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFH 151
Cdd:cd06636    80 GAFIKKSppghddQLWLVMEFCGAGSVTDLVKNTKGNALKEDwiAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAE 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333886239 152 IKIADLGVASfktwskltkekdnkqkEVSSTTKKNNG--GTLYYMAPEHLN-DINAKPT--EKSDVYSFGI 217
Cdd:cd06636   160 VKLVDFGVSA----------------QLDRTVGRRNTfiGTPYWMAPEVIAcDENPDATydYRSDIWSLGI 214
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
26-161 1.35e-08

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: 56.19  E-value: 1.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGFVILKKVyTGPNRAEYNEVLLE-EGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLMHVL 104
Cdd:cd14184    12 GNFAVVKECVERSTGKEFALKI-IDKAKCCGKEHLIEnEVSILRRVKHPNIIMLIEEMDTPAELYLVMELVKGGDLFDAI 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333886239 105 KTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILV----DRDFHIKIADLGVAS 161
Cdd:cd14184    91 TSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLAT 151
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
84-235 1.35e-08

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: 56.97  E-value: 1.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  84 EEGNYSLVMEYMEKGNLMHVL-KTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasf 162
Cdd:cd05597    72 DENYLYLVMDYYCGGDLLTLLsKFEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFG---- 147
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333886239 163 ktwSKLTKEKDNKqkeVSSTTKKnngGTLYYMAPEHL---NDINAKPTEKSDVYSFGIVLWAIFAKKEPY--ENVICT 235
Cdd:cd05597   148 ---SCLKLREDGT---VQSSVAV---GTPDYISPEILqamEDGKGRYGPECDWWSLGVCMYEMLYGETPFyaESLVET 216
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
20-275 1.44e-08

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: 56.95  E-value: 1.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  20 KTDLDSGGFGKVSLCYHRSHGFVILKKVYTGPNR--AEYNEVLLEEGKmmhrlrHSRVVKLLGIIiEEGNYS-LVMEYME 96
Cdd:cd14176    24 KEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRdpTEEIEILLRYGQ------HPNIITLKDVY-DDGKYVyVVTELMK 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  97 KGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENIL-VDRDFH---IKIADLGVAsfktwskltkek 172
Cdd:cd14176    97 GGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFA------------ 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 173 dnKQKEVSSTTKKNNGGTLYYMAPEHLNDINAKPTekSDVYSFGIVLWAIFAKKEPYENvicteqfviciksGNRPNVEE 252
Cdd:cd14176   165 --KQLRAENGLLMTPCYTANFVAPEVLERQGYDAA--CDIWSLGVLLYTMLTGYTPFAN-------------GPDDTPEE 227
                         250       260
                  ....*....|....*....|...
gi 1333886239 253 ILEYCPREIISLMERCWQAIPED 275
Cdd:cd14176   228 ILARIGSGKFSLSGGYWNSVSDT 250
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
15-246 1.56e-08

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: 56.56  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  15 SDLLE-KTDLDSGGFGKVSLCYHRSHGFVILKKVYTGPNR--AEYNEVLLEEGKmmhrlrHSRVVKLLGIIiEEGNYS-L 90
Cdd:cd14177     3 TDVYElKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRdpSEEIEILMRYGQ------HPNIITLKDVY-DDGRYVyL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  91 VMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDF----HIKIADLGVAsfktws 166
Cdd:cd14177    76 VTELMKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSanadSIRICDFGFA------ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 167 kltkekdnKQKEVSSTTKKNNGGTLYYMAPEHLndINAKPTEKSDVYSFGIVLWAIFAKKEPYENVI--CTEQFVICIKS 244
Cdd:cd14177   150 --------KQLRGENGLLLTPCYTANFVAPEVL--MRQGYDAACDIWSLGVLLYTMLAGYTPFANGPndTPEEILLRIGS 219

                  ..
gi 1333886239 245 GN 246
Cdd:cd14177   220 GK 221
Death_TRAILR_DR4_DR5 cd08315
Death domain of Tumor necrosis factor-Related Apoptosis-Inducing Ligand Receptors; Death ...
581-646 1.81e-08

Death domain of Tumor necrosis factor-Related Apoptosis-Inducing Ligand Receptors; Death Domain (DD) found in Tumor necrosis factor-Related Apoptosis-Inducing Ligand (TRAIL) Receptors. In mammals, this family includes TRAILR1 (also called DR4 or TNFRSF10A) and TRAILR2 (also called DR5, TNFRSF10B, or KILLER). They function as receptors for the cytokine TRAIL and are involved in apoptosis signaling pathways. TRAIL preferentially induces apoptosis in cancer cells while exhibiting little toxicity in normal cells. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260027  Cd Length: 88  Bit Score: 51.89  E-value: 1.81e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333886239 581 RQWKNCARKLGFTESQIDEIDhdYERDGLKEKVYQMLQKWLMREGtKGATVGKLAQALHqccRIDL 646
Cdd:cd08315    12 KSWKRLMRALGLSDNEIKLAE--ANDPGSQEPLYQMLNKWLNKTG-RKASVNTLLDALE---DLGL 71
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
25-245 1.98e-08

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 57.82  E-value: 1.98e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239   25 SGGFGKVSLCYH-RSHGFVILKKV-YTGPNRAEYNEVLLEEgKMMHRLRHSRVVKLLGIIIEEGNYSL--VMEYMEKGNL 100
Cdd:PTZ00266    23 NGRFGEVFLVKHkRTQEFFCWKAIsYRGLKEREKSQLVIEV-NVMRELKHKNIVRYIDRFLNKANQKLyiLMEFCDAGDL 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  101 MHVLKTQIDVPLSLKGRIIV----EAIEGMCYLHD-------KGVIHKDLKPENILVDRDF-HIkiadlgvasfktwSKL 168
Cdd:PTZ00266   102 SRNIQKCYKMFGKIEEHAIVditrQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLSTGIrHI-------------GKI 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  169 TKEKDNKQKEVSSTT-----KKNNG---------GTLYYMAPEHLNDINAKPTEKSDVYSFGIVLWAIFAKKEPYENVIC 234
Cdd:PTZ00266   169 TAQANNLNGRPIAKIgdfglSKNIGiesmahscvGTPYYWSPELLLHETKSYDDKSDMWALGCIIYELCSGKTPFHKANN 248
                          250
                   ....*....|.
gi 1333886239  235 TEQFVICIKSG 245
Cdd:PTZ00266   249 FSQLISELKRG 259
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
23-219 2.06e-08

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: 56.40  E-value: 2.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCY-HRSHGFVILKKVYtgpNRAEYNEVLLEEGKMMHRLRH------SRVVKLLGIIIEEGNYSLVMEYM 95
Cdd:cd14210    21 LGKGSFGQVVKCLdHKTGQLVAIKIIR---NKKRFHQQALVEVKILKHLNDndpddkHNIVRYKDSFIFRGHLCIVFELL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  96 EKgNLMHVLKTQIDVPLSLK--GRIIVEAIEGMCYLHDKGVIHKDLKPENILV--DRDFHIKIADLGVASFktwskltke 171
Cdd:cd14210    98 SI-NLYELLKSNNFQGLSLSliRKFAKQILQALQFLHKLNIIHCDLKPENILLkqPSKSSIKVIDFGSSCF--------- 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1333886239 172 kdnkqkevssttkknNGGTLY-------YMAPEHLndINAKPTEKSDVYSFGIVL 219
Cdd:cd14210   168 ---------------EGEKVYtyiqsrfYRAPEVI--LGLPYDTAIDMWSLGCIL 205
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
25-160 2.25e-08

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: 56.53  E-value: 2.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSLCYHRSHG-FVILKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGIIIEEGNYS------LVMEYMEK 97
Cdd:cd07851    25 SGAYGQVCSAFDTKTGrKVAIKKLSRPFQSAIHAKRTYRELRLLKHMKHENVIGLLDVFTPASSLEdfqdvyLVTHLMGA 104
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333886239  98 gNLMHVLKTQidvPLS-LKGRIIVEAI-EGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVA 160
Cdd:cd07851   105 -DLNNIVKCQ---KLSdDHIQFLVYQIlRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLA 165
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
26-217 2.42e-08

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: 55.77  E-value: 2.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRSHGFVILKKVYTGPNraEYNEVLLEEGKMMHRL-RHSRVVKLLGIIIEEGNYS-----LVMEYMEKGN 99
Cdd:cd06639    33 GTYGKVYKVTNKKDGSLAAVKILDPIS--DVDEEIEAEYNILRSLpNHPNVVKFYGMFYKADQYVggqlwLVLELCNGGS 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 100 LMHVLKTQIDVPLSLK----GRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwSKLTKEKDNK 175
Cdd:cd06639   111 VTELVKGLLKCGQRLDeamiSYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS-----AQLTSARLRR 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1333886239 176 QKEVssttkknngGTLYYMAPEHL---NDINAKPTEKSDVYSFGI 217
Cdd:cd06639   186 NTSV---------GTPFWMAPEVIaceQQYDYSYDARCDVWSLGI 221
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
23-214 2.64e-08

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: 55.59  E-value: 2.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRSHGF-VILKKVYTGPNRAEynEVLLEEGkmmhrLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLM 101
Cdd:cd13991    14 IGRGSFGEVHRMEDKQTGFqCAVKKVRLEVFRAE--ELMACAG-----LTSPRVVPLYGAVREGPWVNIFMDLKEGGSLG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 HVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRD-FHIKIADLGVAsfktwskLTKEKDNKQKEVs 180
Cdd:cd13991    87 QLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDgSDAFLCDFGHA-------ECLDPDGLGKSL- 158
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1333886239 181 sTTKKNNGGTLYYMAPEhlnDINAKPTE-KSDVYS 214
Cdd:cd13991   159 -FTGDYIPGTETHMAPE---VVLGKPCDaKVDVWS 189
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
62-260 2.88e-08

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: 55.83  E-value: 2.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  62 EEGKMMHRLRHSRVVKLL----GIIIEEGNYSLVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKG--VI 135
Cdd:cd14030    73 EEAGMLKGLQHPNIVRFYdsweSTVKGKKCIVLVTELMTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppII 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 136 HKDLKPENILVDRDF-HIKIADLGVASFKtwskltkekdnkqkevSSTTKKNNGGTLYYMAPEHLNDinaKPTEKSDVYS 214
Cdd:cd14030   153 HRDLKCDNIFITGPTgSVKIGDLGLATLK----------------RASFAKSVIGTPEFMAPEMYEE---KYDESVDVYA 213
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1333886239 215 FGIVLWAIFAKKEPYENVICTEQFVICIKSGNR---------PNVEEILEYCPRE 260
Cdd:cd14030   214 FGMCMLEMATSEYPYSECQNAAQIYRRVTSGVKpasfdkvaiPEVKEIIEGCIRQ 268
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
26-232 2.89e-08

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: 56.04  E-value: 2.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  26 GGFGKVSLCYHRS----HGFVILKKVYTgPNRAEYNEVLLEEgKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGNLM 101
Cdd:cd05585     5 GSFGKVMQVRKKDtsriYALKTIRKAHI-VSRSEVTHTLAER-TVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGELF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 102 HVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVAsfktwsKLTKEKDNKQKEVSs 181
Cdd:cd05585    83 HHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLC------KLNMKDDDKTNTFC- 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333886239 182 ttkknngGTLYYMAPEHLndINAKPTEKSDVYSFGIVLWAIFAKKEPY--ENV 232
Cdd:cd05585   156 -------GTPEYLAPELL--LGHGYTKAVDWWTLGVLLYEMLTGLPPFydENT 199
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
44-229 3.43e-08

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: 55.45  E-value: 3.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  44 LKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGII-IEEGNYSLVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEA 122
Cdd:cd14041    41 LNKNWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFsLDTDSFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQI 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 123 IEGMCYLHD--KGVIHKDLKPENILVDRDF---HIKIADLGVASFktwskltKEKDNKQKEVSSTTKKNNGGTLYYMAPE 197
Cdd:cd14041   121 VNALKYLNEikPPIIHYDLKPGNILLVNGTacgEIKITDFGLSKI-------MDDDSYNSVDGMELTSQGAGTYWYLPPE 193
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1333886239 198 HLNDINAKP--TEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14041   194 CFVVGKEPPkiSNKVDVWSVGVIFYQCLYGRKPF 227
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
90-222 3.59e-08

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: 55.50  E-value: 3.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  90 LVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasfktwskLT 169
Cdd:cd05588    73 FVIEFVNGGDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYG---------MC 143
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333886239 170 KEkDNKQKEVSSTTkknnGGTLYYMAPEHLndinakpteKSDVYSFGIVLWAI 222
Cdd:cd05588   144 KE-GLRPGDTTSTF----CGTPNYIAPEIL---------RGEDYGFSVDWWAL 182
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
84-229 3.63e-08

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: 56.18  E-value: 3.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  84 EEGNYSLVMEYMEKGNLMHVL-KTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasf 162
Cdd:cd05623   143 DDNNLYLVMDYYVGGDLLTLLsKFEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFG---- 218
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 163 kTWSKLTkEKDNKQKEVSSttkknngGTLYYMAPEHLN---DINAKPTEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd05623   219 -SCLKLM-EDGTVQSSVAV-------GTPDYISPEILQameDGKGKYGPECDWWSLGVCMYEMLYGETPF 279
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
18-229 3.77e-08

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: 55.00  E-value: 3.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  18 LEKTDLDSGGFGKVSLCYHRSHG-FVILKKVYTGPNRAEYNEVLLEEGKMMHrlrhsrVVKLLGII--IEEGNYSL--VM 92
Cdd:cd14172     7 LSKQVLGLGVNGKVLECFHRRTGqKCALKLLYDSPKARREVEHHWRASGGPH------IVHILDVYenMHHGKRCLliIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  93 EYMEKGNLMHVLKTQIDVPLSLKG-----RIIVEAIEgmcYLHDKGVIHKDLKPENILV---DRDFHIKIADLGvasfkt 164
Cdd:cd14172    81 ECMEGGELFSRIQERGDQAFTEREaseimRDIGTAIQ---YLHSMNIAHRDVKPENLLYtskEKDAVLKLTDFG------ 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333886239 165 WSKLTKEKDNKQKEVSsttkknnggTLYYMAPEHLNDinAKPTEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14172   152 FAKETTVQNALQTPCY---------TPYYVAPEVLGP--EKYDKSCDMWSLGVIMYILLCGFPPF 205
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
72-254 3.96e-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: 3.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  72 HSRVVKLLGIIIEEGNYSLVMEYMEKG-NLMHVLKTQIDVPLSLKGRIIVEAIEGMCYLHDKGVIHKDLKPENILVD-RD 149
Cdd:cd14101    66 HRGVIRLLDWFEIPEGFLLVLERPQHCqDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDlRT 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 150 FHIKIADLGVASFKTWSKLTkekdnkqkevssttkkNNGGTLYYMAPEHL--NDINAKPtekSDVYSFGIVLWAIFAKKE 227
Cdd:cd14101   146 GDIKLIDFGSGATLKDSMYT----------------DFDGTRVYSPPEWIlyHQYHALP---ATVWSLGILLYDMVCGDI 206
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1333886239 228 PYE---NVICTE-----------QFVIC----IKSGNRPNVEEIL 254
Cdd:cd14101   207 PFErdtDILKAKpsfnkrvsndcRSLIRsclaYNPSDRPSLEQIL 251
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
25-217 4.42e-08

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: 55.11  E-value: 4.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  25 SGGFGKVSLCYHRSHGFVILKKVYTGPNRAEynEVLLEEGKMMHRLRHSR-VVKLLGIIIEEG------NYSLVMEYMEK 97
Cdd:cd06637    16 NGTYGQVYKGRHVKTGQLAAIKVMDVTGDEE--EEIKQEINMLKKYSHHRnIATYYGAFIKKNppgmddQLWLVMEFCGA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  98 GNLMHVLKTQIDVPLSLK--GRIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDFHIKIADLGVASfktwskltkekdnk 175
Cdd:cd06637    94 GSVTDLIKNTKGNTLKEEwiAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSA-------------- 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1333886239 176 qkEVSSTTKKNNG--GTLYYMAPEHLN-DINAKPTE--KSDVYSFGI 217
Cdd:cd06637   160 --QLDRTVGRRNTfiGTPYWMAPEVIAcDENPDATYdfKSDLWSLGI 204
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
63-164 4.42e-08

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 53.04  E-value: 4.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  63 EGKMMHRLRhsrvvkLLGI------IIEEGNYSLVMEYMEKGNLMHVLKTQIDVPLSLK--GRIIVEaiegmcyLHDKGV 134
Cdd:COG3642     6 EARLLRELR------EAGVpvpkvlDVDPDDADLVMEYIEGETLADLLEEGELPPELLRelGRLLAR-------LHRAGI 72
                          90       100       110
                  ....*....|....*....|....*....|
gi 1333886239 135 IHKDLKPENILVDRDfHIKIADLGVASFKT 164
Cdd:COG3642    73 VHGDLTTSNILVDDG-GVYLIDFGLARYSD 101
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
74-278 4.57e-08

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: 54.94  E-value: 4.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  74 RVVKLLGIIIEEGNYSLVMEYMEKGNLMHVLKTQIDVPLSLKG--RIIVEAIEGMCYLHDKGVIHKDLKPENILVDRDF- 150
Cdd:cd14197    70 WVINLHEVYETASEMILVLEYAAGGEIFNQCVADREEAFKEKDvkRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESp 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 151 --HIKIADLGVasfktwSKLTKekdnkqkevSSTTKKNNGGTLYYMAPEHLndiNAKP-TEKSDVYSFGIVLWAIFAKKE 227
Cdd:cd14197   150 lgDIKIVDFGL------SRILK---------NSEELREIMGTPEYVAPEIL---SYEPiSTATDMWSIGVLAYVMLTGIS 211
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1333886239 228 PYENVICTEQFvICIKSGNRPNVEEILEYCPREIISLMERCWQAIPEDRPT 278
Cdd:cd14197   212 PFLGDDKQETF-LNISQMNVSYSEEEFEHLSESAIDFIKTLLIKKPENRAT 261
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
61-160 4.68e-08

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 55.21  E-value: 4.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  61 LEEGKMMHRLRHSRVVKLLGIIIEEGNYSLVMEYMEKGnlmhvLKTQIDV--PLSLKGRII----VEAIEGMCYLHDKGV 134
Cdd:PLN00009   49 IREISLLKEMQHGNIVRLQDVVHSEKRLYLVFEYLDLD-----LKKHMDSspDFAKNPRLIktylYQILRGIAYCHSHRV 123
                          90       100
                  ....*....|....*....|....*..
gi 1333886239 135 IHKDLKPENILVDRDFH-IKIADLGVA 160
Cdd:PLN00009  124 LHRDLKPQNLLIDRRTNaLKLADFGLA 150
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
22-231 4.94e-08

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: 54.39  E-value: 4.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  22 DLDSGGFGKVSLCYHRSHG-FVILKKVYTGPNRAE--YNEVlleegkMMHR-LRHSRVVKLLGIIIEEGNYSLVMEYMEK 97
Cdd:cd14662     7 DIGSGNFGVARLMRNKETKeLVAVKYIERGLKIDEnvQREI------INHRsLRHPNIIRFKEVVLTPTHLAIVMEYAAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  98 GNLMHvlktqidvPLSLKGRI--------IVEAIEGMCYLHDKGVIHKDLKPENILVDRDF--HIKIADLGvasfktWSK 167
Cdd:cd14662    81 GELFE--------RICNAGRFsedearyfFQQLISGVSYCHSMQICHRDLKLENTLLDGSPapRLKICDFG------YSK 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333886239 168 ltkekdnkqKEVSSTTKKNNGGTLYYMAPEHLN--DINAKpteKSDVYSFGIVLWAIFAKKEPYEN 231
Cdd:cd14662   147 ---------SSVLHSQPKSTVGTPAYIAPEVLSrkEYDGK---VADVWSCGVTLYVMLVGAYPFED 200
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
60-160 5.50e-08

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: 55.17  E-value: 5.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  60 LLEEGKMMHRLRHSRVVKL--------------LGIIIEEGNYSLVMEYMEKgNLMHVLKTQidvPLSLK-GRIIV-EAI 123
Cdd:cd07854    49 ALREIKIIRRLDHDNIVKVyevlgpsgsdltedVGSLTELNSVYIVQEYMET-DLANVLEQG---PLSEEhARLFMyQLL 124
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1333886239 124 EGMCYLHDKGVIHKDLKPENILVD-RDFHIKIADLGVA 160
Cdd:cd07854   125 RGLKYIHSANVLHRDLKPANVFINtEDLVLKIGDFGLA 162
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
23-229 5.63e-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: 54.93  E-value: 5.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  23 LDSGGFGKVSLCYHRS-------HGFVILKKVYTgPNRAEYNEVLLEEGKMMHRLRHSR-VVKLLGIIIEEGNYSLVMEY 94
Cdd:cd05614     8 LGTGAYGKVFLVRKVSghdanklYAMKVLRKAAL-VQKAKTVEHTRTERNVLEHVRQSPfLVTLHYAFQTDAKLHLILDY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  95 MEKGNLM-HVLKTQI---DVPLSLKGRIIVeAIEgmcYLHDKGVIHKDLKPENILVDRDFHIKIADLGvasfktwskLTK 170
Cdd:cd05614    87 VSGGELFtHLYQRDHfseDEVRFYSGEIIL-ALE---HLHKLGIVYRDIKLENILLDSEGHVVLTDFG---------LSK 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1333886239 171 EKDNKQKEVSSTTkknnGGTLYYMAPEHLNDINAKpTEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd05614   154 EFLTEEKERTYSF----CGTIEYMAPEIIRGKSGH-GKAVDWWSLGILMFELLTGASPF 207
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
44-229 5.89e-08

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: 54.68  E-value: 5.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239  44 LKKVYTGPNRAEYNEVLLEEGKMMHRLRHSRVVKLLGII-IEEGNYSLVMEYMEKGNLMHVLKTQIDVPLSLKGRIIVEA 122
Cdd:cd14040    41 LNKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQI 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333886239 123 IEGMCYLHD--KGVIHKDLKPENI-LVDRDF--HIKIADLGvasfktwskLTKEKDNKQKEVSSTTKKNNG-GTLYYMAP 196
Cdd:cd14040   121 VNALRYLNEikPPIIHYDLKPGNIlLVDGTAcgEIKITDFG---------LSKIMDDDSYGVDGMDLTSQGaGTYWYLPP 191
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1333886239 197 EHLNDINAKP--TEKSDVYSFGIVLWAIFAKKEPY 229
Cdd:cd14040   192 ECFVVGKEPPkiSNKVDVWSVGVIFFQCLYGRKPF 226
 
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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