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Conserved domains on  [gi|18408454|ref|NP_566892|]
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Leucine-rich repeat protein kinase family protein [Arabidopsis thaliana]

Protein Classification

leucine-rich repeat domain-containing protein( domain architecture ID 1000136)

leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN00113 super family cl33413
leucine-rich repeat receptor-like protein kinase; Provisional
29-996 7.43e-111

leucine-rich repeat receptor-like protein kinase; Provisional


The actual alignment was detected with superfamily member PLN00113:

Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 366.48  E-value: 7.43e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454    29 LLQFKSQVsEDKRVVLSSWNHSFPLCNWKGVTCgRKNKRVTHLELGRLQLGGVISPSIGNLSFLVSLDLYENFFGGTIPQ 108
Cdd:PLN00113   34 LLSFKSSI-NDPLKYLSNWNSSADVCLWQGITC-NNSSRVVSIDLSGKNISGKISSAIFRLPYIQTINLSNNQLSGPIPD 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   109 EVGQLS-RLEYLDMGINYLRGPIPLGLYNCsrLLNLRLDSNRLGGSVPSELGSLTNLVQLNLYGNNMRGKLPTSLGNLTL 187
Cdd:PLN00113  112 DIFTTSsSLRYLNLSNNNFTGSIPRGSIPN--LETLDLSNNMLSGEIPNDIGSFSSLKVLDLGGNVLVGKIPNSLTNLTS 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   188 LEQLALS------------------------HNNLEGEIPSDVAQLTQIWSLQLVANNFSGVFPPALYNLSSLKLLGIGY 243
Cdd:PLN00113  190 LEFLTLAsnqlvgqiprelgqmkslkwiylgYNNLSGEIPYEIGGLTSLNHLDLVYNNLTGPIPSSLGNLKNLQYLFLYQ 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   244 NHFSGRLRPDLgILLPNLLSFNMGGNYFTGSIPTTLSNISTLERLGMNENNLTGSIP-TFGNVPNLKLLFLHTNSLGSDS 322
Cdd:PLN00113  270 NKLSGPIPPSI-FSLQKLISLDLSDNSLSGEIPELVIQLQNLEILHLFSNNFTGKIPvALTSLPRLQVLQLWSNKFSGEI 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   323 SRDLEFLTSLTnctqleTLGIGRNRLGGDLPISIANlSAKLVTLDLGGTLISGSIPYDIGNLINLQKLILDQNMLSGPLP 402
Cdd:PLN00113  349 PKNLGKHNNLT------VLDLSTNNLTGEIPEGLCS-SGNLFKLILFSNSLEGEIPKSLGACRSLRRVRLQDNSFSGELP 421
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   403 TSLGKLLNLRYLSLFSNRLSGGIPAFIGNMTMLETLDLSNNGFEGIVPTSLGNcSHLLELWIGDNKLNGTIPLEIMKIQQ 482
Cdd:PLN00113  422 SEFTKLPLVYFLDISNNNLQGRINSRKWDMPSLQMLSLARNKFFGGLPDSFGS-KRLENLDLSRNQFSGAVPRKLGSLSE 500
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   483 LLRLDMSGNSLIGSLPQDIGALQNLGTLSLGDNKLSGKLPQTlgncltmeslflegnlfYGDIPDLKGLvgvkevDLSNN 562
Cdd:PLN00113  501 LMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPAS-----------------FSEMPVLSQL------DLSQN 557
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   563 DLSGSIPEYFASFSKLEYLNLSFNNLEGKVPVKGIFENATTVSIVGNNDLCGGIMGFQLKPClsqapSVVKKHSSRLkkV 642
Cdd:PLN00113  558 QLSGEIPKNLGNVESLVQVNISHNHLHGSLPSTGAFLAINASAVAGNIDLCGGDTTSGLPPC-----KRVRKTPSWW--F 630
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   643 VIGVSVGITLLLLLFMASVTLIWLRKRKKNKETNNPTPS-TLEVLHEKISYGdlrNATNGFSSS----NMVGSGSFGTVY 717
Cdd:PLN00113  631 YITCTLGAFLVLALVAFGFVFIRGRNNLELKRVENEDGTwELQFFDSKVSKS---ITINDILSSlkeeNVISRGKKGASY 707
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   718 KALLLTEKKVVAVKVLNmQRRGAMKSFMAEcesLKDIRHRNLVKLLTACSSidfqgNEFRALIYEFMPNGSLDMWLhpee 797
Cdd:PLN00113  708 KGKSIKNGMQFVVKEIN-DVNSIPSSEIAD---MGKLQHPNIVKLIGLCRS-----EKGAYLIHEYIEGKNLSEVL---- 774
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   798 veeihrpsRTLTLLERLNIAIDVASVLDYLHVHCHEPIAHCDLKPSNVLLDDDLTAHVSdFGLArLLLKFDEESFfnqLS 877
Cdd:PLN00113  775 --------RNLSWERRRKIAIGIAKALRFLHCRCSPAVVVGNLSPEKIIIDGKDEPHLR-LSLP-GLLCTDTKCF---IS 841
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   878 SAgvrgtigYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTNELFGGNFTLNSYTKSALPERILDI-VDESILHIGL 956
Cdd:PLN00113  842 SA-------YVAPETRETKDITEKSDIYGFGLILIELLTGKSPADAEFGVHGSIVEWARYCYSDCHLDMwIDPSIRGDVS 914
                         970       980       990      1000
                  ....*....|....*....|....*....|....*....|
gi 18408454   957 RVGFPVVEcltmVFEVGLRCCEESPMNRLATSIVVKELIS 996
Cdd:PLN00113  915 VNQNEIVE----VMNLALHCTATDPTARPCANDVLKTLES 950
 
Name Accession Description Interval E-value
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
29-996 7.43e-111

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 366.48  E-value: 7.43e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454    29 LLQFKSQVsEDKRVVLSSWNHSFPLCNWKGVTCgRKNKRVTHLELGRLQLGGVISPSIGNLSFLVSLDLYENFFGGTIPQ 108
Cdd:PLN00113   34 LLSFKSSI-NDPLKYLSNWNSSADVCLWQGITC-NNSSRVVSIDLSGKNISGKISSAIFRLPYIQTINLSNNQLSGPIPD 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   109 EVGQLS-RLEYLDMGINYLRGPIPLGLYNCsrLLNLRLDSNRLGGSVPSELGSLTNLVQLNLYGNNMRGKLPTSLGNLTL 187
Cdd:PLN00113  112 DIFTTSsSLRYLNLSNNNFTGSIPRGSIPN--LETLDLSNNMLSGEIPNDIGSFSSLKVLDLGGNVLVGKIPNSLTNLTS 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   188 LEQLALS------------------------HNNLEGEIPSDVAQLTQIWSLQLVANNFSGVFPPALYNLSSLKLLGIGY 243
Cdd:PLN00113  190 LEFLTLAsnqlvgqiprelgqmkslkwiylgYNNLSGEIPYEIGGLTSLNHLDLVYNNLTGPIPSSLGNLKNLQYLFLYQ 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   244 NHFSGRLRPDLgILLPNLLSFNMGGNYFTGSIPTTLSNISTLERLGMNENNLTGSIP-TFGNVPNLKLLFLHTNSLGSDS 322
Cdd:PLN00113  270 NKLSGPIPPSI-FSLQKLISLDLSDNSLSGEIPELVIQLQNLEILHLFSNNFTGKIPvALTSLPRLQVLQLWSNKFSGEI 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   323 SRDLEFLTSLTnctqleTLGIGRNRLGGDLPISIANlSAKLVTLDLGGTLISGSIPYDIGNLINLQKLILDQNMLSGPLP 402
Cdd:PLN00113  349 PKNLGKHNNLT------VLDLSTNNLTGEIPEGLCS-SGNLFKLILFSNSLEGEIPKSLGACRSLRRVRLQDNSFSGELP 421
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   403 TSLGKLLNLRYLSLFSNRLSGGIPAFIGNMTMLETLDLSNNGFEGIVPTSLGNcSHLLELWIGDNKLNGTIPLEIMKIQQ 482
Cdd:PLN00113  422 SEFTKLPLVYFLDISNNNLQGRINSRKWDMPSLQMLSLARNKFFGGLPDSFGS-KRLENLDLSRNQFSGAVPRKLGSLSE 500
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   483 LLRLDMSGNSLIGSLPQDIGALQNLGTLSLGDNKLSGKLPQTlgncltmeslflegnlfYGDIPDLKGLvgvkevDLSNN 562
Cdd:PLN00113  501 LMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPAS-----------------FSEMPVLSQL------DLSQN 557
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   563 DLSGSIPEYFASFSKLEYLNLSFNNLEGKVPVKGIFENATTVSIVGNNDLCGGIMGFQLKPClsqapSVVKKHSSRLkkV 642
Cdd:PLN00113  558 QLSGEIPKNLGNVESLVQVNISHNHLHGSLPSTGAFLAINASAVAGNIDLCGGDTTSGLPPC-----KRVRKTPSWW--F 630
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   643 VIGVSVGITLLLLLFMASVTLIWLRKRKKNKETNNPTPS-TLEVLHEKISYGdlrNATNGFSSS----NMVGSGSFGTVY 717
Cdd:PLN00113  631 YITCTLGAFLVLALVAFGFVFIRGRNNLELKRVENEDGTwELQFFDSKVSKS---ITINDILSSlkeeNVISRGKKGASY 707
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   718 KALLLTEKKVVAVKVLNmQRRGAMKSFMAEcesLKDIRHRNLVKLLTACSSidfqgNEFRALIYEFMPNGSLDMWLhpee 797
Cdd:PLN00113  708 KGKSIKNGMQFVVKEIN-DVNSIPSSEIAD---MGKLQHPNIVKLIGLCRS-----EKGAYLIHEYIEGKNLSEVL---- 774
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   798 veeihrpsRTLTLLERLNIAIDVASVLDYLHVHCHEPIAHCDLKPSNVLLDDDLTAHVSdFGLArLLLKFDEESFfnqLS 877
Cdd:PLN00113  775 --------RNLSWERRRKIAIGIAKALRFLHCRCSPAVVVGNLSPEKIIIDGKDEPHLR-LSLP-GLLCTDTKCF---IS 841
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   878 SAgvrgtigYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTNELFGGNFTLNSYTKSALPERILDI-VDESILHIGL 956
Cdd:PLN00113  842 SA-------YVAPETRETKDITEKSDIYGFGLILIELLTGKSPADAEFGVHGSIVEWARYCYSDCHLDMwIDPSIRGDVS 914
                         970       980       990      1000
                  ....*....|....*....|....*....|....*....|
gi 18408454   957 RVGFPVVEcltmVFEVGLRCCEESPMNRLATSIVVKELIS 996
Cdd:PLN00113  915 VNQNEIVE----VMNLALHCTATDPTARPCANDVLKTLES 950
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
708-997 1.00e-76

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: 252.58  E-value: 1.00e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKkVVAVKVLNMQRRGAM-KSFMAECESLKDIRHRNLVKLLTACSsidfqGNEFRALIYEFMPN 786
Cdd:cd14066    1 IGSGGFGTVYKGVLENGT-VVAVKRLNEMNCAASkKEFLTELEMLGRLRHPNLVRLLGYCL-----ESDEKLLVYEYMPN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  787 GSLDMWLHPeeveeiHRPSRTLTLLERLNIAIDVASVLDYLHVHCHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARLLLK 866
Cdd:cd14066   75 GSLEDRLHC------HKGSPPLPWPQRLKIAKGIARGLEYLHEECPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPP 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  867 FDEESffnqlSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTNElFGGNFTLN---SYTKSALPERI 943
Cdd:cd14066  149 SESVS-----KTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDE-NRENASRKdlvEWVESKGKEEL 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18408454  944 LDIVDEsilHIGLRVGFPVVECLTMvFEVGLRCCEESPMNRLATSIVVKELISI 997
Cdd:cd14066  223 EDILDK---RLVDDDGVEEEEVEAL-LRLALLCTRSDPSLRPSMKEVVQMLEKL 272
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
708-920 8.73e-42

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 160.56  E-value: 8.73e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRG---AMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFM 784
Cdd:COG0515   15 LGRGGMGVVYLARDLRLGRPVALKVLRPELAAdpeARERFRREARALARLNHPNIVRVYDV-----GEEDGRPYLVMEYV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLDMWLhpeeveeihRPSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARLL 864
Cdd:COG0515   90 EGESLADLL---------RRRGPLPPAEALRILAQLAEALAAAH---AAGIVHRDIKPANILLTPDGRVKLIDFGIARAL 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  865 lkfDEESffnqLSSAGVR-GTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:COG0515  158 ---GGAT----LTQTGTVvGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPP 207
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
708-920 2.18e-40

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 149.60  E-value: 2.18e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454     708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQR-RGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFMPN 786
Cdd:smart00220    7 LGEGSFGKVYLARDKKTGKLVAIKVIKKKKiKKDRERILREIKILKKLKHPNIVRLYDV-----FEDEDKLYLVMEYCEG 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454     787 GSLDMWLHPEeveeihrpsRTLTLLERLNIAIDVASVLDYLHVHChepIAHCDLKPSNVLLDDDLTAHVSDFGLARLLlk 866
Cdd:smart00220   82 GDLFDLLKKR---------GRLSEDEARFYLRQILSALEYLHSKG---IVHRDLKPENILLDEDGHVKLADFGLARQL-- 147
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454     867 fDEESFFNqlssaGVRGTIGYAAPE------YGvggqPSIngDVYSFGILLLEMFTGKRP 920
Cdd:smart00220  148 -DPGEKLT-----TFVGTPEYMAPEvllgkgYG----KAV--DIWSLGVILYELLTGKPP 195
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
707-920 2.33e-36

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: 138.40  E-value: 2.33e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454    707 MVGSGSFGTVYKALLLTEKKV----VAVKVLNMQ-RRGAMKSFMAECESLKDIRHRNLVKLLTACSsidfqGNEFRALIY 781
Cdd:pfam07714    6 KLGEGAFGEVYKGTLKGEGENtkikVAVKTLKEGaDEEEREDFLEEASIMKKLDHPNIVKLLGVCT-----QGEPLYIVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454    782 EFMPNGSLDMWLHpeeveeihRPSRTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLA 861
Cdd:pfam07714   81 EYMPGGDLLDFLR--------KHKRKLTLKDLLSMALQIAKGMEYLESK---NFVHRDLAARNCLVSENLVVKISDFGLS 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454    862 RLLLKFDEESffnqlSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRP 920
Cdd:pfam07714  150 RDIYDDDYYR-----KRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQP 204
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
707-920 3.00e-15

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 80.22  E-value: 3.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   707 MVGSGSFGTVYKALLLTEKKVVAVKVL--------NMQRRgamksFMAECESLKDIRHRNLVklltacsSI-DfQGnEFR 777
Cdd:NF033483   14 RIGRGGMAEVYLAKDTRLDRDVAVKVLrpdlardpEFVAR-----FRREAQSAASLSHPNIV-------SVyD-VG-EDG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   778 ALIYEFMpngsldmwlhpEEVE-----EIHRPSRTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLT 852
Cdd:NF033483   80 GIPYIVM-----------EYVDgrtlkDYIREHGPLSPEEAVEIMIQILSALEHAHRN---GIVHRDIKPQNILITKDGR 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18408454   853 AHVSDFGLARLLlkfdeesffNQLS---SAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:NF033483  146 VKVTDFGIARAL---------SSTTmtqTNSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPP 207
 
Name Accession Description Interval E-value
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
29-996 7.43e-111

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 366.48  E-value: 7.43e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454    29 LLQFKSQVsEDKRVVLSSWNHSFPLCNWKGVTCgRKNKRVTHLELGRLQLGGVISPSIGNLSFLVSLDLYENFFGGTIPQ 108
Cdd:PLN00113   34 LLSFKSSI-NDPLKYLSNWNSSADVCLWQGITC-NNSSRVVSIDLSGKNISGKISSAIFRLPYIQTINLSNNQLSGPIPD 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   109 EVGQLS-RLEYLDMGINYLRGPIPLGLYNCsrLLNLRLDSNRLGGSVPSELGSLTNLVQLNLYGNNMRGKLPTSLGNLTL 187
Cdd:PLN00113  112 DIFTTSsSLRYLNLSNNNFTGSIPRGSIPN--LETLDLSNNMLSGEIPNDIGSFSSLKVLDLGGNVLVGKIPNSLTNLTS 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   188 LEQLALS------------------------HNNLEGEIPSDVAQLTQIWSLQLVANNFSGVFPPALYNLSSLKLLGIGY 243
Cdd:PLN00113  190 LEFLTLAsnqlvgqiprelgqmkslkwiylgYNNLSGEIPYEIGGLTSLNHLDLVYNNLTGPIPSSLGNLKNLQYLFLYQ 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   244 NHFSGRLRPDLgILLPNLLSFNMGGNYFTGSIPTTLSNISTLERLGMNENNLTGSIP-TFGNVPNLKLLFLHTNSLGSDS 322
Cdd:PLN00113  270 NKLSGPIPPSI-FSLQKLISLDLSDNSLSGEIPELVIQLQNLEILHLFSNNFTGKIPvALTSLPRLQVLQLWSNKFSGEI 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   323 SRDLEFLTSLTnctqleTLGIGRNRLGGDLPISIANlSAKLVTLDLGGTLISGSIPYDIGNLINLQKLILDQNMLSGPLP 402
Cdd:PLN00113  349 PKNLGKHNNLT------VLDLSTNNLTGEIPEGLCS-SGNLFKLILFSNSLEGEIPKSLGACRSLRRVRLQDNSFSGELP 421
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   403 TSLGKLLNLRYLSLFSNRLSGGIPAFIGNMTMLETLDLSNNGFEGIVPTSLGNcSHLLELWIGDNKLNGTIPLEIMKIQQ 482
Cdd:PLN00113  422 SEFTKLPLVYFLDISNNNLQGRINSRKWDMPSLQMLSLARNKFFGGLPDSFGS-KRLENLDLSRNQFSGAVPRKLGSLSE 500
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   483 LLRLDMSGNSLIGSLPQDIGALQNLGTLSLGDNKLSGKLPQTlgncltmeslflegnlfYGDIPDLKGLvgvkevDLSNN 562
Cdd:PLN00113  501 LMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPAS-----------------FSEMPVLSQL------DLSQN 557
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   563 DLSGSIPEYFASFSKLEYLNLSFNNLEGKVPVKGIFENATTVSIVGNNDLCGGIMGFQLKPClsqapSVVKKHSSRLkkV 642
Cdd:PLN00113  558 QLSGEIPKNLGNVESLVQVNISHNHLHGSLPSTGAFLAINASAVAGNIDLCGGDTTSGLPPC-----KRVRKTPSWW--F 630
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   643 VIGVSVGITLLLLLFMASVTLIWLRKRKKNKETNNPTPS-TLEVLHEKISYGdlrNATNGFSSS----NMVGSGSFGTVY 717
Cdd:PLN00113  631 YITCTLGAFLVLALVAFGFVFIRGRNNLELKRVENEDGTwELQFFDSKVSKS---ITINDILSSlkeeNVISRGKKGASY 707
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   718 KALLLTEKKVVAVKVLNmQRRGAMKSFMAEcesLKDIRHRNLVKLLTACSSidfqgNEFRALIYEFMPNGSLDMWLhpee 797
Cdd:PLN00113  708 KGKSIKNGMQFVVKEIN-DVNSIPSSEIAD---MGKLQHPNIVKLIGLCRS-----EKGAYLIHEYIEGKNLSEVL---- 774
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   798 veeihrpsRTLTLLERLNIAIDVASVLDYLHVHCHEPIAHCDLKPSNVLLDDDLTAHVSdFGLArLLLKFDEESFfnqLS 877
Cdd:PLN00113  775 --------RNLSWERRRKIAIGIAKALRFLHCRCSPAVVVGNLSPEKIIIDGKDEPHLR-LSLP-GLLCTDTKCF---IS 841
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   878 SAgvrgtigYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTNELFGGNFTLNSYTKSALPERILDI-VDESILHIGL 956
Cdd:PLN00113  842 SA-------YVAPETRETKDITEKSDIYGFGLILIELLTGKSPADAEFGVHGSIVEWARYCYSDCHLDMwIDPSIRGDVS 914
                         970       980       990      1000
                  ....*....|....*....|....*....|....*....|
gi 18408454   957 RVGFPVVEcltmVFEVGLRCCEESPMNRLATSIVVKELIS 996
Cdd:PLN00113  915 VNQNEIVE----VMNLALHCTATDPTARPCANDVLKTLES 950
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
708-997 1.00e-76

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: 252.58  E-value: 1.00e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKkVVAVKVLNMQRRGAM-KSFMAECESLKDIRHRNLVKLLTACSsidfqGNEFRALIYEFMPN 786
Cdd:cd14066    1 IGSGGFGTVYKGVLENGT-VVAVKRLNEMNCAASkKEFLTELEMLGRLRHPNLVRLLGYCL-----ESDEKLLVYEYMPN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  787 GSLDMWLHPeeveeiHRPSRTLTLLERLNIAIDVASVLDYLHVHCHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARLLLK 866
Cdd:cd14066   75 GSLEDRLHC------HKGSPPLPWPQRLKIAKGIARGLEYLHEECPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPP 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  867 FDEESffnqlSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTNElFGGNFTLN---SYTKSALPERI 943
Cdd:cd14066  149 SESVS-----KTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDE-NRENASRKdlvEWVESKGKEEL 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18408454  944 LDIVDEsilHIGLRVGFPVVECLTMvFEVGLRCCEESPMNRLATSIVVKELISI 997
Cdd:cd14066  223 EDILDK---RLVDDDGVEEEEVEAL-LRLALLCTRSDPSLRPSMKEVVQMLEKL 272
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
708-994 9.27e-59

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: 202.73  E-value: 9.27e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKaLLLTEKKVVAVKVLNMQRRGAMK-SFMAECESLKDIRHRNLVKLLTACSSidfqgNEFRALIYEFMPN 786
Cdd:cd14664    1 IGRGGAGTVYK-GVMPNGTLVAVKRLKGEGTQGGDhGFQAEIQTLGMIRHRNIVRLRGYCSN-----PTTNLLVYEYMPN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  787 GSLDMWLHPEEVEEIHrpsrtLTLLERLNIAIDVASVLDYLHVHCHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARLLLK 866
Cdd:cd14664   75 GSLGELLHSRPESQPP-----LDWETRQRIALGSARGLAYLHHDCSPLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDD 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  867 FDEESffnqlsSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTNELFGGN-FTLNSYTKSALPERIL- 944
Cdd:cd14664  150 KDSHV------MSSVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPFDEAFLDDgVDIVDWVRGLLEEKKVe 223
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 18408454  945 DIVDESIlhiglrVGFPVVECLTMVFEVGLRCCEESPMNRLATSIVVKEL 994
Cdd:cd14664  224 ALVDPDL------QGVYKLEEVEQVFQVALLCTQSSPMERPTMREVVRML 267
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
708-994 1.25e-50

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: 178.89  E-value: 1.25e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLteKKVVAVKVLNMQRRGA--MKSFMAECESLKDIRHRNLVKLLTACSSidfqGNEFrALIYEFMP 785
Cdd:cd13999    1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDNDelLKEFRREVSILSKLRHPNIVQFIGACLS----PPPL-CIVTEYMP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLdmwlhpEEVeeIHRPSRTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLARLLL 865
Cdd:cd13999   74 GGSL------YDL--LHKKKIPLSWSLRLKIALDIARGMNYLHSP---PIIHRDLKSLNILLDENFTVKIADFGLSRIKN 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  866 KfdeesffNQLSSAGVRGTIGYAAPEYgVGGQP-SINGDVYSFGILLLEMFTGKRPTNELFGGNFTLNSYTKSALPErIL 944
Cdd:cd13999  143 S-------TTEKMTGVVGTPRWMAPEV-LRGEPyTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLRPP-IP 213
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 18408454  945 DIVDESILHIglrvgfpvvecltMvfevgLRCCEESPMNRLATSIVVKEL 994
Cdd:cd13999  214 PDCPPELSKL-------------I-----KRCWNEDPEKRPSFSEIVKRL 245
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
708-920 8.73e-42

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 160.56  E-value: 8.73e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRG---AMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFM 784
Cdd:COG0515   15 LGRGGMGVVYLARDLRLGRPVALKVLRPELAAdpeARERFRREARALARLNHPNIVRVYDV-----GEEDGRPYLVMEYV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLDMWLhpeeveeihRPSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARLL 864
Cdd:COG0515   90 EGESLADLL---------RRRGPLPPAEALRILAQLAEALAAAH---AAGIVHRDIKPANILLTPDGRVKLIDFGIARAL 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  865 lkfDEESffnqLSSAGVR-GTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:COG0515  158 ---GGAT----LTQTGTVvGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPP 207
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
708-920 2.18e-40

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 149.60  E-value: 2.18e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454     708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQR-RGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFMPN 786
Cdd:smart00220    7 LGEGSFGKVYLARDKKTGKLVAIKVIKKKKiKKDRERILREIKILKKLKHPNIVRLYDV-----FEDEDKLYLVMEYCEG 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454     787 GSLDMWLHPEeveeihrpsRTLTLLERLNIAIDVASVLDYLHVHChepIAHCDLKPSNVLLDDDLTAHVSDFGLARLLlk 866
Cdd:smart00220   82 GDLFDLLKKR---------GRLSEDEARFYLRQILSALEYLHSKG---IVHRDLKPENILLDEDGHVKLADFGLARQL-- 147
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454     867 fDEESFFNqlssaGVRGTIGYAAPE------YGvggqPSIngDVYSFGILLLEMFTGKRP 920
Cdd:smart00220  148 -DPGEKLT-----TFVGTPEYMAPEvllgkgYG----KAV--DIWSLGVILYELLTGKPP 195
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
708-920 1.32e-39

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: 147.73  E-value: 1.32e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVL---NMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFM 784
Cdd:cd14014    8 LGRGGMGEVYRARDTLLGRPVAIKVLrpeLAEDEEFRERFLREARALARLSHPNIVRVYDV-----GEDDGRPYIVMEYV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLDMWLhpeeveeihRPSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARLL 864
Cdd:cd14014   83 EGGSLADLL---------RERGPLPPREALRILAQIADALAAAH---RAGIVHRDIKPANILLTEDGRVKLTDFGIARAL 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  865 lkfdEESFFNQlsSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14014  151 ----GDSGLTQ--TGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPP 200
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
708-920 2.84e-38

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: 144.97  E-value: 2.84e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLltEKKVVAVKVLNMQRR---GAMK-SFMAECESLKDIRHRNLVKLLTACssidFQGNEFrALIYEF 783
Cdd:cd14159    1 IGEGGFGCVYQAVM--RNTEYAVKRLKEDSEldwSVVKnSFLTEVEKLSRFRHPNIVDLAGYS----AQQGNY-CLIYVY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  784 MPNGSLDMWLHPEEveeihrPSRTLTLLERLNIAIDVASVLDYLHvHCHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARL 863
Cdd:cd14159   74 LPNGSLEDRLHCQV------SCPCLSWSQRLHVLLGTARAIQYLH-SDSPSLIHGDVKSSNILLDAALNPKLGDFGLARF 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  864 LLKFDEESFFNQLS-SAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14159  147 SRRPKQPGMSSTLArTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRA 204
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
709-914 3.16e-38

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: 142.02  E-value: 3.16e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVYKALLLTEKKVVAVKVLN-MQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFMPNG 787
Cdd:cd00180    2 GKGSFGKVYKARDKETGKKVAVKVIPkEKLKKLLEELLREIEILKKLNHPNIVKLYDV-----FETENFLYLVMEYCEGG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 SLdmwlhpeeVEEIHRPSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARLLlkf 867
Cdd:cd00180   77 SL--------KDLLKENKGPLSEEEALSILRQLLSALEYLH---SNGIIHRDLKPENILLDSDGTVKLADFGLAKDL--- 142
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 18408454  868 deESFFNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEM 914
Cdd:cd00180  143 --DSDDSLLKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL 187
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
706-994 1.02e-37

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: 142.29  E-value: 1.02e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTVYKALLLTE---KKVVAVKVLnmqRRGAMKS----FMAECESLKDIRHRNLVKLLTACSSidfQGNEFra 778
Cdd:cd00192    1 KKLGEGAFGEVYKGKLKGGdgkTVDVAVKTL---KEDASESerkdFLKEARVMKKLGHPNVVRLLGVCTE---EEPLY-- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGSLDMWLHPEEVEEIHRPSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDF 858
Cdd:cd00192   73 LVMEYMEGGDLLDFLRKSRPVFPSPEPSTLSLKDLLSFAIQIAKGMEYLA---SKKFVHRDLAARNCLVGEDLVVKISDF 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  859 GLARLLlkfdEESFFNQLSSAG---VRgtigYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRPtnelFGGnftlnsy 934
Cdd:cd00192  150 GLSRDI----YDDDYYRKKTGGklpIR----WMAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATP----YPG------- 210
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  935 tksALPERILDIVDEsilhiGLRVGFPvVECLTMVFEVGLRCCEESPMNRLATSIVVKEL 994
Cdd:cd00192  211 ---LSNEEVLEYLRK-----GYRLPKP-ENCPDELYELMLSCWQLDPEDRPTFSELVERL 261
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
704-920 1.46e-36

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: 139.06  E-value: 1.46e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  704 SSNMVGSGSFGTVYKALLLTEKkvVAVKVLNMQR--RGAMKSFMAECESLKdIRHRNLVKLLTACSSIDFqgNEFRALIY 781
Cdd:cd13979    7 LQEPLGSGGFGSVYKATYKGET--VAVKIVRRRRknRASRQSFWAELNAAR-LRHENIVRVLAAETGTDF--ASLGLIIM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 EFMPNGSLDmwlhpeevEEIHRPSRTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLA 861
Cdd:cd13979   82 EYCGNGTLQ--------QLIYEGSEPLPLAHRILISLDIARALRFCHSH---GIVHLDVKPANILISEQGVCKLCDFGCS 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  862 RLLLKFDEEsffnQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd13979  151 VKLGEGNEV----GTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELP 205
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
707-920 2.33e-36

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: 138.40  E-value: 2.33e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454    707 MVGSGSFGTVYKALLLTEKKV----VAVKVLNMQ-RRGAMKSFMAECESLKDIRHRNLVKLLTACSsidfqGNEFRALIY 781
Cdd:pfam07714    6 KLGEGAFGEVYKGTLKGEGENtkikVAVKTLKEGaDEEEREDFLEEASIMKKLDHPNIVKLLGVCT-----QGEPLYIVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454    782 EFMPNGSLDMWLHpeeveeihRPSRTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLA 861
Cdd:pfam07714   81 EYMPGGDLLDFLR--------KHKRKLTLKDLLSMALQIAKGMEYLESK---NFVHRDLAARNCLVSENLVVKISDFGLS 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454    862 RLLLKFDEESffnqlSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRP 920
Cdd:pfam07714  150 RDIYDDDYYR-----KRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQP 204
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
709-920 1.85e-35

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 135.74  E-value: 1.85e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454     709 GSGSFGTVYKALLLTEKK----VVAVKVLNMQR-RGAMKSFMAECESLKDIRHRNLVKLLTACSSidfQGNEFraLIYEF 783
Cdd:smart00219    8 GEGAFGEVYKGKLKGKGGkkkvEVAVKTLKEDAsEQQIEEFLREARIMRKLDHPNVVKLLGVCTE---EEPLY--IVMEY 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454     784 MPNGSLDMWLHpeeveeihRPSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARL 863
Cdd:smart00219   83 MEGGDLLSYLR--------KNRPKLSLSDLLSFALQIARGMEYLE---SKNFIHRDLAARNCLVGENLVVKISDFGLSRD 151
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454     864 LLKFDeesffnQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRP 920
Cdd:smart00219  152 LYDDD------YYRKRGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEQP 203
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
709-994 2.85e-35

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: 134.98  E-value: 2.85e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454     709 GSGSFGTVYKALLLTEKKV----VAVKVLNMQR-RGAMKSFMAECESLKDIRHRNLVKLLTACSSidfQGNEFraLIYEF 783
Cdd:smart00221    8 GEGAFGEVYKGTLKGKGDGkeveVAVKTLKEDAsEQQIEEFLREARIMRKLDHPNIVKLLGVCTE---EEPLM--IVMEY 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454     784 MPNGSLDMWLHpeeveeIHRPsRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARL 863
Cdd:smart00221   83 MPGGDLLDYLR------KNRP-KELSLSDLLSFALQIARGMEYLE---SKNFIHRDLAARNCLVGENLVVKISDFGLSRD 152
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454     864 LLKFDEesffnqLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRPTNELfggnftlnsytksaLPER 942
Cdd:smart00221  153 LYDDDY------YKVKGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEPYPGM--------------SNAE 212
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|..
gi 18408454     943 ILDIVDEsilhiGLRVGFPvVECLTMVFEVGLRCCEESPMNRLATSIVVKEL 994
Cdd:smart00221  213 VLEYLKK-----GYRLPKP-PNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
708-920 5.93e-34

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: 131.42  E-value: 5.93e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQR--RGAMKSFMAECESLKDIRHRNLVKLLTACssidfQGNEFRALIYEFMP 785
Cdd:cd13978    1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPncIEERKALLKEAEKMERARHSYVLPLLGVC-----VERRSLGLVMEYME 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLdmwlhpEEVEEIHRPSRTLTLleRLNIAIDVASVLDYLHvHCHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARL-- 863
Cdd:cd13978   76 NGSL------KSLLEREIQDVPWSL--RFRIIHEIALGMNFLH-NMDPPLLHHDLKPENILLDNHFHVKISDFGLSKLgm 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  864 -LLKFDEESffnqlSSAGVRGTIGYAAPEY--GVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd13978  147 kSISANRRR-----GTENLGGTPIYMAPEAfdDFNKKPTSKSDVYSFAIVIWAVLTRKEP 201
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
692-997 1.06e-33

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: 131.47  E-value: 1.06e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  692 YGDLRNATNGF------SSSNMVGSGSFGTVYKALLltEKKVVAVKVLN----MQRRGAMKSFMAECESLKDIRHRNLVK 761
Cdd:cd14158    1 FHELKNMTNNFderpisVGGNKLGEGGFGVVFKGYI--NDKNVAVKKLAamvdISTEDLTKQFEQEIQVMAKCQHENLVE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  762 LLtACSSidfQGNEFrALIYEFMPNGSLDMWLHPEEveeiHRPSrtLTLLERLNIAIDVASVLDYLHVHCHepiAHCDLK 841
Cdd:cd14158   79 LL-GYSC---DGPQL-CLVYTYMPNGSLLDRLACLN----DTPP--LSWHMRCKIAQGTANGINYLHENNH---IHRDIK 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  842 PSNVLLDDDLTAHVSDFGLARlllkfDEESFFNQLSSAGVRGTIGYAAPEyGVGGQPSINGDVYSFGILLLEMFTGKRPT 921
Cdd:cd14158  145 SANILLDETFVPKISDFGLAR-----ASEKFSQTIMTERIVGTTAYMAPE-ALRGEITPKSDIFSFGVVLLEIITGLPPV 218
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  922 NELFGGNFTLNsyTKSALPERILDIVDesilHIGLRVGFPVVECLTMVFEVGLRCCEESPMNRLATSIVVKELISI 997
Cdd:cd14158  219 DENRDPQLLLD--IKEEIEDEEKTIED----YVDKKMGDWDSTSIEAMYSVASQCLNDKKNRRPDIAKVQQLLQEL 288
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
707-920 3.83e-31

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: 123.01  E-value: 3.83e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGA--MKSFMAECESLKDIRHRNLVKLLTACSSidfqgNEFRALIYEFM 784
Cdd:cd06606    7 LLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEeeLEALEREIRILSSLKHPNIVRYLGTERT-----ENTLNIFLEYV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLDmwlhpeeveeihrpsrtlTLLER---LNIAI------DVASVLDYLHVHChepIAHCDLKPSNVLLDDDLTAHV 855
Cdd:cd06606   82 PGGSLA------------------SLLKKfgkLPEPVvrkytrQILEGLEYLHSNG---IVHRDIKGANILVDSDGVVKL 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  856 SDFGLARLLlkfDEESFFNQLSSagVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd06606  141 ADFGCAKRL---AEIATGEGTKS--LRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPP 200
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
702-924 1.09e-30

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: 121.54  E-value: 1.09e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIY 781
Cdd:cd05122    2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESILNEIAILKKCKHPNIVKYYGS-----YLKKDELWIVM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 EFMPNGSLDMWLHpeeveeiHRPsRTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLA 861
Cdd:cd05122   77 EFCSGGSLKDLLK-------NTN-KTLTEQQIAYVCKEVLKGLEYLHSH---GIIHRDIKAANILLTSDGEVKLIDFGLS 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  862 rlllkfdeesffNQLSSAGVR----GTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTNEL 924
Cdd:cd05122  146 ------------AQLSDGKTRntfvGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSEL 200
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
707-920 8.89e-30

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: 118.92  E-value: 8.89e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVvAVKVLnmqRRGAMK--SFMAECESLKDIRHRNLVKLLTACSsidfqGNEFRALIYEFM 784
Cdd:cd05034    2 KLGAGQFGEVWMGVWNGTTKV-AVKTL---KPGTMSpeAFLQEAQIMKKLRHDKLVQLYAVCS-----DEEPIYIVTELM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLDMWLHPEEveeihrpSRTLTLLERLNIAIDVASVLDYLHVHCHepiAHCDLKPSNVLLDDDLTAHVSDFGLARLL 864
Cdd:cd05034   73 SKGSLLDYLRTGE-------GRALRLPQLIDMAAQIASGMAYLESRNY---IHRDLAARNILVGENNVCKVADFGLARLI 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  865 lkfdEESFFNqlSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRP 920
Cdd:cd05034  143 ----EDDEYT--AREGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLYEIVTyGRVP 193
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
254-589 1.70e-29

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 122.35  E-value: 1.70e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  254 LGILLPNLLSFNMGGNYFTGSIPTTLSNISTLERLGMNENNLTGSIPTFGNVPNLKLLFLHTNSLGSDSSRDLEFLTSLT 333
Cdd:COG4886   31 LLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELS 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  334 NCTQLETLGIGRNRLGgDLPISIANLSaKLVTLDLGGTLISgSIPYDIGNLINLQKLILDQNMLSGpLPTSLGKLLNLRY 413
Cdd:COG4886  111 NLTNLESLDLSGNQLT-DLPEELANLT-NLKELDLSNNQLT-DLPEPLGNLTNLKSLDLSNNQLTD-LPEELGNLTNLKE 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  414 LSLFSNRLSGgIPAFIGNMTMLETLDLSNNGFEGIvPTSLGNCSHLLELWIGDNKLNgTIPlEIMKIQQLLRLDMSGNSl 493
Cdd:COG4886  187 LDLSNNQITD-LPEPLGNLTNLEELDLSGNQLTDL-PEPLANLTNLETLDLSNNQLT-DLP-ELGNLTNLEELDLSNNQ- 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  494 IGSLPqDIGALQNLGTLSLGDNKLSGKLPQTLGNCLTMESLFLEGNLFYGDIPDLKGLVGVKEVDLSNNDLSGSIPEYFA 573
Cdd:COG4886  262 LTDLP-PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTL 340
                        330
                 ....*....|....*.
gi 18408454  574 SFSKLEYLNLSFNNLE 589
Cdd:COG4886  341 ALSLSLLALLTLLLLL 356
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
708-920 3.41e-29

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: 117.45  E-value: 3.41e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKkvVAVKVLNMQRRGAmKSFMAECESLKDIRHRNLVKLLTACssidFQGNEFRaLIYEFMPNG 787
Cdd:cd05039   14 IGKGEFGDVMLGDYRGQK--VAVKCLKDDSTAA-QAFLAEASVMTTLRHPNLVQLLGVV----LEGNGLY-IVTEYMAKG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 SLDMWLHPeeveeihRPSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARlllkf 867
Cdd:cd05039   86 SLVDYLRS-------RGRAVITRKDQLGFALDVCEGMEYLE---SKKFVHRDLAARNVLVSEDNVAKVSDFGLAK----- 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18408454  868 dEESffnqLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRP 920
Cdd:cd05039  151 -EAS----SNQDGGKLPIKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVP 199
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
702-920 3.43e-28

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: 114.84  E-value: 3.43e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVvAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSsidfqGNEFRALIY 781
Cdd:cd05148    8 FTLERKLGSGYFGEVWEGLWKNRVRV-AIKILKSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCS-----VGEPVYIIT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 EFMPNGSLDMWLH-PEEveeihrpsRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGL 860
Cdd:cd05148   82 ELMEKGSLLAFLRsPEG--------QVLPVASLIDMACQVAEGMAYLE---EQNSIHRDLAARNILVGEDLVCKVADFGL 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18408454  861 ARLLlkfdEESFFnqlSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRP 920
Cdd:cd05148  151 ARLI----KEDVY---LSSDKKIPYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVP 204
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
705-933 4.13e-28

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: 114.50  E-value: 4.13e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  705 SNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQR--RGAMKSFMAECESLKDIRHRNLVKLltacssID-FQGNEFRALIY 781
Cdd:cd05117    5 GKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKlkSEDEEMLRREIEILKRLDHPNIVKL------YEvFEDDKNLYLVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 EFMPNGSLdmwlhpeeVEEIHRpSRTLTLLERLNIAIDVASVLDYLHVHChepIAHCDLKPSNVLLDDDLTAH---VSDF 858
Cdd:cd05117   79 ELCTGGEL--------FDRIVK-KGSFSEREAAKIMKQILSAVAYLHSQG---IVHRDLKPENILLASKDPDSpikIIDF 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  859 GLARlllKFDEESFFNQLSsagvrGTIGYAAPEygVGGQPSIN--GDVYSFGILLLEMFTGKRP-----TNELFG----G 927
Cdd:cd05117  147 GLAK---IFEEGEKLKTVC-----GTPYYVAPE--VLKGKGYGkkCDIWSLGVILYILLCGYPPfygetEQELFEkilkG 216

                 ....*.
gi 18408454  928 NFTLNS 933
Cdd:cd05117  217 KYSFDS 222
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
253-594 9.16e-28

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 117.34  E-value: 9.16e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  253 DLGILLPNLLSFNMGGNYFTGSIPTTLSNISTLERLGMNENNLTGSIPTFGNVPNLKLLFLHTNSLGSDSSRDLEFLTSL 332
Cdd:COG4886    7 SLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  333 TNCTQLETLgIGRNRLGGDLPISIANLSaKLVTLDLGGTLISgSIPYDIGNLINLQKLILDQNMLSgPLPTSLGKLLNLR 412
Cdd:COG4886   87 LGLTDLGDL-TNLTELDLSGNEELSNLT-NLESLDLSGNQLT-DLPEELANLTNLKELDLSNNQLT-DLPEPLGNLTNLK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  413 YLSLFSNRLSGgIPAFIGNMTMLETLDLSNNGFEGIvPTSLGNCSHLLELWIGDNKLNgTIPLEIMKIQQLLRLDMSGNS 492
Cdd:COG4886  163 SLDLSNNQLTD-LPEELGNLTNLKELDLSNNQITDL-PEPLGNLTNLEELDLSGNQLT-DLPEPLANLTNLETLDLSNNQ 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  493 lIGSLPqDIGALQNLGTLSLGDNKLSgklpqtlgncltmeslflegnlfygDIPDLKGLVGVKEVDLSNNDLSGSIPEYF 572
Cdd:COG4886  240 -LTDLP-ELGNLTNLEELDLSNNQLT-------------------------DLPPLANLTNLKTLDLSNNQLTDLKLKEL 292
                        330       340
                 ....*....|....*....|..
gi 18408454  573 ASFSKLEYLNLSFNNLEGKVPV 594
Cdd:COG4886  293 ELLLGLNSLLLLLLLLNLLELL 314
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
708-920 3.08e-26

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: 108.63  E-value: 3.08e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLlteKKVVAVKVLNMQRRGA--MKSFMAECESLKDIRHRNLVKLLTACSSIDFqgnefrALIYEFMP 785
Cdd:cd14062    1 IGSGSFGTVYKGRW---HGDVAVKKLNVTDPTPsqLQAFKNEVAVLRKTRHVNILLFMGYMTKPQL------AIVTQWCE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLDMWLHPEEVEeihrpsrtLTLLERLNIAIDVASVLDYLHVhchEPIAHCDLKPSNVLLDDDLTAHVSDFGLARLLL 865
Cdd:cd14062   72 GSSLYKHLHVLETK--------FEMLQLIDIARQTAQGMDYLHA---KNIIHRDLKSNNIFLHEDLTVKIGDFGLATVKT 140
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  866 KFDEESFFNQLSsagvrGTIGYAAPEY--GVGGQP-SINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14062  141 RWSGSQQFEQPT-----GSILWMAPEVirMQDENPySFQSDVYAFGIVLYELLTGQLP 193
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
708-924 7.83e-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: 107.62  E-value: 7.83e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALllTEKKVVAVKVLNMQRRGAmKS----FMAECESLKDIRHRNLVKLLTACssIDfQGNEFrALIYEF 783
Cdd:cd14064    1 IGSGSFGKVYKGR--CRNKIVAIKRYRANTYCS-KSdvdmFCREVSILCRLNHPCVIQFVGAC--LD-DPSQF-AIVTQY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  784 MPNGSLDMWLHPEEveeihrpsRTLTLLERLNIAIDVASVLDYLHVHCHePIAHCDLKPSNVLLDDDLTAHVSDFGLARL 863
Cdd:cd14064   74 VSGGSLFSLLHEQK--------RVIDLQSKLIIAVDVAKGMEYLHNLTQ-PIIHRDLNSHNILLYEDGHAVVADFGESRF 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  864 LLKFDEESFFNQlssagvRGTIGYAAPE-YGVGGQPSINGDVYSFGILLLEMFTGKRPTNEL 924
Cdd:cd14064  145 LQSLDEDNMTKQ------PGNLRWMAPEvFTQCTRYSIKADVFSYALCLWELLTGEIPFAHL 200
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
709-936 8.07e-26

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: 108.02  E-value: 8.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVYKALLLTEKKVVAVKVLN-----MQRRG---------AMKSFMAECESLKDIRHRNLVKLLTAcssIDFQGN 774
Cdd:cd14008    2 GRGSFGKVKLALDTETGQLYAIKIFNksrlrKRREGkndrgkiknALDDVRREIAIMKKLDHPNIVRLYEV---IDDPES 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  775 EFRALIYEFMPNGSLDMWLHPEEVEeihrpsrTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAH 854
Cdd:cd14008   79 DKLYLVLEYCEGGPVMELDSGDRVP-------PLPEETARKYFRDLVLGLEYLHEN---GIVHRDIKPENLLLTADGTVK 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  855 VSDFGLARLLLKFDEESFFNQlssagvrGTIGYAAPEYGVGGQPSING---DVYSFGILLLEMFTGKRPtnelFGGNFTL 931
Cdd:cd14008  149 ISDFGVSEMFEDGNDTLQKTA-------GTPAFLAPELCDGDSKTYSGkaaDIWALGVTLYCLVFGRLP----FNGDNIL 217

                 ....*
gi 18408454  932 NSYTK 936
Cdd:cd14008  218 ELYEA 222
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
711-916 3.40e-25

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: 106.64  E-value: 3.40e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  711 GSFGTVYKALLLteKKVVAVKVLNMQRRgamKSFMAECE--SLKDIRHRNLVKLLTACSSIDFQGNEFrALIYEFMPNGS 788
Cdd:cd14053    6 GRFGAVWKAQYL--NRLVAVKIFPLQEK---QSWLTEREiySLPGMKHENILQFIGAEKHGESLEAEY-WLITEFHERGS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  789 LDMWLHpeeveeihrpSRTLTLLERLNIAIDVASVLDYLH-----VHCHE--PIAHCDLKPSNVLLDDDLTAHVSDFGLA 861
Cdd:cd14053   80 LCDYLK----------GNVISWNELCKIAESMARGLAYLHedipaTNGGHkpSIAHRDFKSKNVLLKSDLTACIADFGLA 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  862 rllLKFDEESffNQLSSAGVRGTIGYAAPEYGVGgqpSING--------DVYSFGILLLEMFT 916
Cdd:cd14053  150 ---LKFEPGK--SCGDTHGQVGTRRYMAPEVLEG---AINFtrdaflriDMYAMGLVLWELLS 204
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
708-920 4.01e-25

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: 105.29  E-value: 4.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLN---MQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFM 784
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKVLRkkeIIKRKEVEHTLNERNILERVNHPFIVKLHYA-----FQTEEKLYLVLDYV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLDMWLHPEeveeihrpsrtLTLLE---RLNIAiDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLA 861
Cdd:cd05123   76 PGGELFSHLSKE-----------GRFPEeraRFYAA-EIVLALEYLHSL---GIIYRDLKPENILLDSDGHIKLTDFGLA 140
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  862 RlllkfdEESFFNQLSSAGVrGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd05123  141 K------ELSSDGDRTYTFC-GTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPP 192
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
708-920 5.60e-25

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: 105.57  E-value: 5.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVvAVKVLnmqRRGAM--KSFMAECESLKDIRHRNLVKLLTACSSidfqgNEFRALIYEFMP 785
Cdd:cd05068   16 LGSGQFGEVWEGLWNNTTPV-AVKTL---KPGTMdpEDFLREAQIMKKLRHPKLIQLYAVCTL-----EEPIYIITELMK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLdmwlhpeeVEEIHRPSRTLTLLERLNIAIDVASVLDYLHVHCHepiAHCDLKPSNVLLDDDLTAHVSDFGLARLLL 865
Cdd:cd05068   87 HGSL--------LEYLQGKGRSLQLPQLIDMAAQVASGMAYLESQNY---IHRDLAARNVLVGENNICKVADFGLARVIK 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  866 KFDEESffnqlSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRP 920
Cdd:cd05068  156 VEDEYE-----AREGAKFPIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTyGRIP 206
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
708-929 7.89e-25

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: 104.83  E-value: 7.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLltEKKVVAVKVLNMQRRgaMKSFMAECESLKDIRHRNLVKLLTACSSidfqgNEFRALIYEFMPNG 787
Cdd:cd14058    1 VGRGSFGVVCKARW--RNQIVAVKIIESESE--KKAFEVEVRQLSRVDHPNIIKLYGACSN-----QKPVCLVMEYAEGG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 SLDMWLHPEEVEEIHrpsrtlTLLERLNIAIDVASVLDYLHVHCHEPIAHCDLKPSNVLLDDDLTA-HVSDFGLArlllk 866
Cdd:cd14058   72 SLYNVLHGKEPKPIY------TAAHAMSWALQCAKGVAYLHSMKPKALIHRDLKPPNLLLTNGGTVlKICDFGTA----- 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  867 fdeESFFNQLSSAgvRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTNELFGGNF 929
Cdd:cd14058  141 ---CDISTHMTNN--KGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFDHIGGPAF 198
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
708-920 9.69e-25

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: 104.88  E-value: 9.69e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVK---VLNMQRRGAMKsFMAECESLKDIRHRNLVKLLTACSsidfqgnEFRALIYEFM 784
Cdd:cd14025    4 VGSGGFGQVYKVRHKHWKTWLAIKcppSLHVDDSERME-LLEEAKKMEMAKFRHILPVYGICS-------EPVGLVMEYM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLDMWLhpeeveeihrPSRTLTLLERLNIAIDVASVLDYLHVhCHEPIAHCDLKPSNVLLDDDLTAHVSDFGLArll 864
Cdd:cd14025   76 ETGSLEKLL----------ASEPLPWELRFRIIHETAVGMNFLHC-MKPPLLHLDLKPANILLDAHYHVKISDFGLA--- 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  865 lKFDEESFFNQLSSAGVRGTIGYAAPEYGVGGQ--PSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14025  142 -KWNGLSHSHDLSRDGLRGTIAYLPPERFKEKNrcPDTKHDVYSFAIVIWGILTQKKP 198
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
706-924 2.77e-24

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: 103.07  E-value: 2.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRR--GAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEF 783
Cdd:cd06627    6 DLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIpkSDLKSVMGEIDLLKKLNHPNIVKYIGS-----VKTKDSLYIILEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  784 MPNGSLdmwlhpeeveeihrpSRTLTLLERLN---IAIDVASVLD---YLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSD 857
Cdd:cd06627   81 VENGSL---------------ASIIKKFGKFPeslVAVYIYQVLEglaYLH---EQGVIHRDIKGANILTTKDGLVKLAD 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  858 FGLArllLKFDEesffNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTNEL 924
Cdd:cd06627  143 FGVA---TKLNE----VEKDENSVVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDL 202
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
708-996 4.98e-24

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: 103.29  E-value: 4.98e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEkkVVAVKVLNMQRRgamKSFMAECESLKD--IRHRNLVKLLTACSSIDFQGNEFrALIYEFMP 785
Cdd:cd13998    3 IGKGRFGEVWKASLKNE--PVAVKIFSSRDK---QSWFREKEIYRTpmLKHENILQFIAADERDTALRTEL-WLVTAFHP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLDMWLHpeeveeihrpSRTLTLLERLNIAIDVASVLDYLH------VHCHEPIAHCDLKPSNVLLDDDLTAHVSDFG 859
Cdd:cd13998   77 NGSL*DYLS----------LHTIDWVSLCRLALSVARGLAHLHseipgcTQGKPAIAHRDLKSKNILVKNDGTCCIADFG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  860 LArllLKFDEESFFNQLSSAGVRGTIGYAAPEYGVGgqpSIN---------GDVYSFGILLLEMFtgkRPTNELFGG--N 928
Cdd:cd13998  147 LA---VRLSPSTGEEDNANNGQVGTKRYMAPEVLEG---AINlrdfesfkrVDIYAMGLVLWEMA---SRCTDLFGIveE 217
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18408454  929 FTLNSYTKSAL-P--ERILDIVDESILHIGLRVGFPVVECLTMVFEVGLRCCEESPMNRLaTSIVVKELIS 996
Cdd:cd13998  218 YKPPFYSEVPNhPsfEDMQEVVVRDKQRPNIPNRWLSHPGLQSLAETIEECWDHDAEARL-TAQCIEERLS 287
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
210-589 7.53e-24

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 105.40  E-value: 7.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  210 TQIWSLQLVANNFSGVFPPALYNLSSLKLLGIGYNHFSGRLRPDLGILLPNLLSFNMGGNYFTGSIPTTLSNISTLERLG 289
Cdd:COG4886   23 TLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELD 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  290 MNENNltgsipTFGNVPNLKLLFLHTNSLGSdssrdleFLTSLTNCTQLETLGIGRNRLGgDLPISIANLSaKLVTLDLG 369
Cdd:COG4886  103 LSGNE------ELSNLTNLESLDLSGNQLTD-------LPEELANLTNLKELDLSNNQLT-DLPEPLGNLT-NLKSLDLS 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  370 GTLISgSIPYDIGNLINLQKLILDQNMLSgPLPTSLGKLLNLRYLSLFSNRLSGgIPAFIGNMTMLETLDLSNNGFEGIv 449
Cdd:COG4886  168 NNQLT-DLPEELGNLTNLKELDLSNNQIT-DLPEPLGNLTNLEELDLSGNQLTD-LPEPLANLTNLETLDLSNNQLTDL- 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  450 pTSLGNCSHLLELWIGDNKLNgTIPlEIMKIQQLLRLDMSGNSLIGSLPQDIGALQNLGTLSLGDNKLSGKLPQTLGNCL 529
Cdd:COG4886  244 -PELGNLTNLEELDLSNNQLT-DLP-PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLL 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  530 TMESLFLEGNLFYGDIPDLKGLVGVKEVDLSNNDLSGSIPEYFASFSKLEYLNLSFNNLE 589
Cdd:COG4886  321 TTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLL 380
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
702-918 1.14e-23

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: 102.20  E-value: 1.14e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGamKSFmaECESLKDIRHRNLVKLLTACSSIDFQGNE-FRALI 780
Cdd:cd14137    6 YTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQDKRY--KNR--ELQIMRRLKHPNIVKLKYFFYSSGEKKDEvYLNLV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFMPngsldMWLHPEEVEEIHRPSRTLTLLERLnIAIDVASVLDYLHVHChepIAHCDLKPSNVLLDDD-LTAHVSDFG 859
Cdd:cd14137   82 MEYMP-----ETLYRVIRHYSKNKQTIPIIYVKL-YSYQLFRGLAYLHSLG---ICHRDIKPQNLLVDPEtGVLKLCDFG 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  860 LARLLLKfdeesffNQLSSAgvrgTIG---YAAPE-------YGVggqpSIngDVYSFGILLLEMFTGK 918
Cdd:cd14137  153 SAKRLVP-------GEPNVS----YICsryYRAPElifgatdYTT----AI--DIWSAGCVLAELLLGQ 204
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
708-994 1.68e-23

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: 100.98  E-value: 1.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMK-SFMAECESLKDIRHRNLVKLLTACSSidfqgNEFRALIYEFMPN 786
Cdd:cd05041    3 IGRGNFGDVYRGVLKPDNTEVAVKTCRETLPPDLKrKFLQEARILKQYDHPNIVKLIGVCVQ-----KQPIMIVMELVPG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  787 GSLDMWLHpeeveeihRPSRTLTLLERLNIAIDVASVLDYLHVHChepIAHCDLKPSNVLLDDDLTAHVSDFGLARlllk 866
Cdd:cd05041   78 GSLLTFLR--------KKGARLTVKQLLQMCLDAAAGMEYLESKN---CIHRDLAARNCLVGENNVLKISDFGMSR---- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  867 fdEESFFNQLSSAGVRGT-IGYAAPEYGVGGQPSINGDVYSFGILLLEMFTgkrptnelfGGNFTLNSYTKSALPERIld 945
Cdd:cd05041  143 --EEEDGEYTVSDGLKQIpIKWTAPEALNYGRYTSESDVWSFGILLWEIFS---------LGATPYPGMSNQQTREQI-- 209
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 18408454  946 ivdESilhiGLRVGFPVVeCLTMVFEVGLRCCEESPMNRLATSIVVKEL 994
Cdd:cd05041  210 ---ES----GYRMPAPEL-CPEAVYRLMLQCWAYDPENRPSFSEIYNEL 250
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
72-397 2.03e-23

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 104.25  E-value: 2.03e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   72 ELGRLQLGGviSPSIGNLSFLVSLDLYENFFGgTIPQEVGQLSRLEYLDMGINYLRgPIPLGLYNCSRLLNLRLDSNRLg 151
Cdd:COG4886   97 NLTELDLSG--NEELSNLTNLESLDLSGNQLT-DLPEELANLTNLKELDLSNNQLT-DLPEPLGNLTNLKSLDLSNNQL- 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  152 GSVPSELGSLTNLVQLNLYGNNMRgKLPTSLGNLTLLEQLALSHNNLEgEIPSDVAQLTQIWSLQLVANNFSGVfpPALY 231
Cdd:COG4886  172 TDLPEELGNLTNLKELDLSNNQIT-DLPEPLGNLTNLEELDLSGNQLT-DLPEPLANLTNLETLDLSNNQLTDL--PELG 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  232 NLSSLKLLGIGYNHFSGrLRPDLGilLPNLLSFNMGGNYFTGSIPTTLSNISTLERLGMNENNLTGSIPTFGNVPNLKLL 311
Cdd:COG4886  248 NLTNLEELDLSNNQLTD-LPPLAN--LTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLL 324
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  312 FLHTNS--LGSDSSRDLEFLTSLTNCTQLETLGIGRNRLGGDLPISIANLSAKLVTLDLGGTLISGSIPYDIGNLINLQK 389
Cdd:COG4886  325 LLLLLLkgLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLT 404

                 ....*...
gi 18408454  390 LILDQNML 397
Cdd:COG4886  405 LALLDAVN 412
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
708-994 2.46e-23

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: 100.60  E-value: 2.46e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVvAVKvlnMQRRGAM--KSFMAECESLKDIRHRNLVKLLTACSSidfQGNEFraLIYEFMP 785
Cdd:cd05059   12 LGSGQFGVVHLGKWRGKIDV-AIK---MIKEGSMseDDFIEEAKVMMKLSHPKLVQLYGVCTK---QRPIF--IVTEYMA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLDMWLHPEEVEEihrpsRTLTLLErlnIAIDVASVLDYLHVHChepIAHCDLKPSNVLLDDDLTAHVSDFGLARLLL 865
Cdd:cd05059   83 NGCLLNYLRERRGKF-----QTEQLLE---MCKDVCEAMEYLESNG---FIHRDLAARNCLVGEQNVVKVSDFGLARYVL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  866 kfDEEsffnQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRPTnelfgGNFTlNSytksalperil 944
Cdd:cd05059  152 --DDE----YTSSVGTKFPVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSeGKMPY-----ERFS-NS----------- 208
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 18408454  945 DIVDEsiLHIGLRVGFPVVeCLTMVFEVGLRCCEESPMNRLATSIVVKEL 994
Cdd:cd05059  209 EVVEH--ISQGYRLYRPHL-APTEVYTIMYSCWHEKPEERPTFKILLSQL 255
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
706-930 2.60e-23

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: 100.86  E-value: 2.60e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTVYKALLLTEKKVVAVKV--LNMQ-----RRGAMKSFMAECESLKDIRHRNLVKLLTaCSSIDfqGNEFrA 778
Cdd:cd13990    6 NLLGKGGFSEVYKAFDLVEQRYVACKIhqLNKDwseekKQNYIKHALREYEIHKSLDHPRIVKLYD-VFEID--TDSF-C 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGSLDMWLhpeeveeihrpSRTLTLLERLNIAI--DVASVLDYLHVHcHEPIAHCDLKPSNVLLDDDLTA--- 853
Cdd:cd13990   82 TVLEYCDGNDLDFYL-----------KQHKSIPEREARSIimQVVSALKYLNEI-KPPIIHYDLKPGNILLHSGNVSgei 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  854 HVSDFGLARLllkFDEESFFNQ---LSSAGVrGTIGYAAPE-YGVGGQP---SINGDVYSFGILLLEMFTGKRPtnelFG 926
Cdd:cd13990  150 KITDFGLSKI---MDDESYNSDgmeLTSQGA-GTYWYLPPEcFVVGKTPpkiSSKVDVWSVGVIFYQMLYGRKP----FG 221

                 ....
gi 18408454  927 GNFT 930
Cdd:cd13990  222 HNQS 225
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
709-945 2.88e-23

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: 100.06  E-value: 2.88e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVYKALLLTEKK-VVAVKVLNMQR--RGAMKSFMAECESLKDIRHRNLVKLLtacssiDFQGNE-FRALIYEFM 784
Cdd:cd14121    4 GSGTYATVYKAYRKSGAReVVAVKCVSKSSlnKASTENLLTEIELLKKLKHPHIVELK------DFQWDEeHIYLIMEYC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLDMWLH-----PEEVeeihrpsrTLTLLERLniaidvASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAH--VSD 857
Cdd:cd14121   78 SGGDLSRFIRsrrtlPEST--------VRRFLQQL------ASALQFLREH---NISHMDLKPQNLLLSSRYNPVlkLAD 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  858 FGLARLLLKFDEESffnqlssaGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPtnelfggnftLNSYTKS 937
Cdd:cd14121  141 FGFAQHLKPNDEAH--------SLRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAP----------FASRSFE 202

                 ....*...
gi 18408454  938 ALPERILD 945
Cdd:cd14121  203 ELEEKIRS 210
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
706-916 2.95e-23

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: 100.57  E-value: 2.95e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTVYKALLLTEKKVVAVKVLNmQRRGAMKSFMAECESLKDIRHRNLVKLLTACS-SIDFQgnefraLIYEFM 784
Cdd:cd05052   12 HKLGGGQYGEVYEGVWKKYNLTVAVKTLK-EDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTrEPPFY------IITEFM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLdmwlhpeeVEEIHRPSR-TLTLLERLNIAIDVASVLDYLHVHChepIAHCDLKPSNVLLDDDLTAHVSDFGLARL 863
Cdd:cd05052   85 PYGNL--------LDYLRECNReELNAVVLLYMATQIASAMEYLEKKN---FIHRDLAARNCLVGENHLVKVADFGLSRL 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 18408454  864 LlkfDEESFFNQlssAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT 916
Cdd:cd05052  154 M---TGDTYTAH---AGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIAT 200
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
709-926 3.23e-23

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: 99.65  E-value: 3.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVYKALLLTEKKVVAVKVLNmqrrgamkSFMAECESLKDIRHRNLVKLLTACSSIDFQGnefraLIYEFMPNGS 788
Cdd:cd14060    2 GGGSFGSVYRAIWVSQDKEVAVKKLL--------KIEKEAEILSVLSHRNIIQFYGAILEAPNYG-----IVTEYASYGS 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  789 LDMWLHPEEVEEihrpsrtLTLLERLNIAIDVASVLDYLHVHCHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARlllkfd 868
Cdd:cd14060   69 LFDYLNSNESEE-------MDMDQIMTWATDIAKGMHYLHMEAPVKVIHRDLKSRNVVIAADGVLKICDFGASR------ 135
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  869 eesFFNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTNELFG 926
Cdd:cd14060  136 ---FHSHTTHMSLVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEG 190
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
705-984 4.54e-23

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: 100.53  E-value: 4.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  705 SNMVGSGSFGTVYKALLLTEK----KVVAVKVLN-MQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSidfQGNEFRAL 779
Cdd:cd05038    9 IKQLGEGHFGSVELCRYDPLGdntgEQVAVKSLQpSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCES---PGRRSLRL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  780 IYEFMPNGSLDMWLhpeeveEIHRPSRTLTLLerLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFG 859
Cdd:cd05038   86 IMEYLPSGSLRDYL------QRHRDQIDLKRL--LLFASQICKGMEYLG---SQRYIHRDLAARNILVESEDLVKISDFG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  860 LARLLLKFDEESFFNQLSSAGVRgtigYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTNElfggnfTLNSYTKSAL 939
Cdd:cd05038  155 LAKVLPEDKEYYYVKEPGESPIF----WYAPECLRESRFSSASDVWSFGVTLYELFTYGDPSQS------PPALFLRMIG 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 18408454  940 PERILDIVDE--SILHIGLRVGFPvVECLTMVFEVGLRCCEESPMNR 984
Cdd:cd05038  225 IAQGQMIVTRllELLKSGERLPRP-PSCPDEVYDLMKECWEYEPQDR 270
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
141-551 5.21e-23

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 103.09  E-value: 5.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  141 LNLRLDSNRLGGSVPSELGSLTNLVQLNLYGNNMRGKLPTSLGNLTLLEQLALSHNNLEGEIPSDVAQLTQIWSLQLVAN 220
Cdd:COG4886    1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  221 NFSGVF--PPALYNLSSLKLLGIGYNHFSGRLrpdlgillPNLLSFNMGGNYFTgSIPTTLSNISTLERLGMNENNLTGS 298
Cdd:COG4886   81 LLSLLLlgLTDLGDLTNLTELDLSGNEELSNL--------TNLESLDLSGNQLT-DLPEELANLTNLKELDLSNNQLTDL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  299 IPTFGNVPNLKLLFLHTNSLGSDSSrdlefltSLTNCTQLETLGIGRNRLgGDLPISIANLSaKLVTLDLGGTLISgSIP 378
Cdd:COG4886  152 PEPLGNLTNLKSLDLSNNQLTDLPE-------ELGNLTNLKELDLSNNQI-TDLPEPLGNLT-NLEELDLSGNQLT-DLP 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  379 YDIGNLINLQKLILDQNMLSgPLPtSLGKLLNLRYLSLFSNRLSgGIPaFIGNMTMLETLDLSNNGFEGIVPTSLGNCSH 458
Cdd:COG4886  222 EPLANLTNLETLDLSNNQLT-DLP-ELGNLTNLEELDLSNNQLT-DLP-PLANLTNLKTLDLSNNQLTDLKLKELELLLG 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  459 L---LELWIGDNKLNGTIPLEIMKIQQLLRLDMSGNSLIGSLPQDIGALQNLGTLSLGDNKLSGKLPQTLGNCLTMESLF 535
Cdd:COG4886  298 LnslLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEA 377
                        410
                 ....*....|....*.
gi 18408454  536 LEGNLFYGDIPDLKGL 551
Cdd:COG4886  378 TLLTLALLLLTLLLLL 393
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
708-994 8.07e-23

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: 98.87  E-value: 8.07e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVvAVKVLnmqRRGAM--KSFMAECESLKDIRHRNLVKLLTACSSidfqgNEFRALIYEFMP 785
Cdd:cd05112   12 IGSGQFGLVHLGYWLNKDKV-AIKTI---REGAMseEDFIEEAEVMMKLSHPKLVQLYGVCLE-----QAPICLVFEFME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLDMWLhpeeveeihRPSRTL----TLLErlnIAIDVASVLDYLHVHChepIAHCDLKPSNVLLDDDLTAHVSDFGLA 861
Cdd:cd05112   83 HGCLSDYL---------RTQRGLfsaeTLLG---MCLDVCEGMAYLEEAS---VIHRDLAARNCLVGENQVVKVSDFGMT 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  862 RLLLkfDEEsffnQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRPTNELFGGnftlnsytksalp 940
Cdd:cd05112  148 RFVL--DDQ----YTSSTGTKFPVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYENRSNS------------- 208
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18408454  941 erilDIVDEsiLHIGLRVGFPVVeCLTMVFEVGLRCCEESPMNRLATSIVVKEL 994
Cdd:cd05112  209 ----EVVED--INAGFRLYKPRL-ASTHVYEIMNHCWKERPEDRPSFSLLLRQL 255
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
707-996 9.47e-23

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: 98.49  E-value: 9.47e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLltEKKVVAVKVLNmqRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidfqGNEFRALIYEFMPN 786
Cdd:cd14068    1 LLGDGGFGSVYRAVY--RGEDVAVKIFN--KHTSFRLLRQELVVLSHLHHPSLVALLAA-------GTAPRMLVMELAPK 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  787 GSLDMWLHPEeveeihRPSRTLTLLERlnIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLL-----DDDLTAHVSDFGLA 861
Cdd:cd14068   70 GSLDALLQQD------NASLTRTLQHR--IALHVADGLRYLH---SAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIA 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  862 RlllkfdeesffnQLSSAGVR---GTIGYAAPEYGVGGQP-SINGDVYSFGILLLEMFTGKRPTNElfGGNFTlNSYTKS 937
Cdd:cd14068  139 Q------------YCCRMGIKtseGTPGFRAPEVARGNVIyNQQADVYSFGLLLYDILTCGERIVE--GLKFP-NEFDEL 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  938 ALPERILDIVDesilHIGLrVGFPVVECLTMvfevglRCCEESPMNRlATSIVVKELIS 996
Cdd:cd14068  204 AIQGKLPDPVK----EYGC-APWPGVEALIK------DCLKENPQCR-PTSAQVFDILN 250
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
709-920 1.27e-22

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: 98.43  E-value: 1.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAM-KSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFMPNG 787
Cdd:cd06623   10 GQGSSGVVYKVRHKPTGKIYALKKIHVDGDEEFrKQLLRELKTLRSCESPYVVKCYGA-----FYKEGEISIVLEYMDGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 SLDmwlhpeeveEIHRPSRTLTllERL--NIAIDVASVLDYLHVHCHepIAHCDLKPSNVLLDDDLTAHVSDFGLARLLl 865
Cdd:cd06623   85 SLA---------DLLKKVGKIP--EPVlaYIARQILKGLDYLHTKRH--IIHRDIKPSNLLINSKGEVKIADFGISKVL- 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  866 kfdEESFFNQLSSAgvrGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd06623  151 ---ENTLDQCNTFV---GTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFP 199
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
707-925 2.06e-22

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: 97.71  E-value: 2.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGA--MKSFMAECESLKDIRHRNLVKLLTA-------CSSIDF-QGNEF 776
Cdd:cd14002    8 LIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEkeLRNLRQEIEILRKLNHPNIIEMLDSfetkkefVVVTEYaQGELF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  777 RALIYefmpNGSLdmwlhPEEveEIHRpsrtltllerlnIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVS 856
Cdd:cd14002   88 QILED----DGTL-----PEE--EVRS------------IAKQLVSALHYLHSN---RIIHRDMKPQNILIGKGGVVKLC 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  857 DFGLARLLLkfdeesfFNQLSSAGVRGTIGYAAPEYgVGGQP-SINGDVYSFGILLLEMFTGKRP--TNELF 925
Cdd:cd14002  142 DFGFARAMS-------CNTLVLTSIKGTPLYMAPEL-VQEQPyDHTADLWSLGCILYELFVGQPPfyTNSIY 205
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
708-920 2.89e-22

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


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 98.06  E-value: 2.89e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLN---MQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFM 784
Cdd:cd05581    9 LGEGSYSTVVLAKEKETGKEYAIKVLDkrhIIKEKKVKYVTIEKEVLSRLAHPGIVKLYYT-----FQDESKLYFVLEYA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLdmwlhpeeVEEIHRpsrtltlLERLN------IAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDF 858
Cdd:cd05581   84 PNGDL--------LEYIRK-------YGSLDekctrfYTAEIVLALEYLHSK---GIIHRDLKPENILLDEDMHIKITDF 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  859 GLARLL----------LKFDEESFFNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd05581  146 GTAKVLgpdsspestkGDADSQIAYNQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPP 217
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
706-924 7.29e-22

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: 96.22  E-value: 7.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTVYKALLLTEKKVVAVKVLNMQR--RGAMKSFMAECESLKDIRHRNLVKlltacssidFQGNEF-RALIYE 782
Cdd:cd06626    6 NKIGEGTFGKVYTAVNLDTGELMAMKEIRFQDndPKTIKEIADEMKVLEGLDHPNLVR---------YYGVEVhREEVYI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FM---PNGSLDMWLH-----PEEVEEIHrpsrTLTLLERLNiaidvasvldYLHVHchePIAHCDLKPSNVLLDDDLTAH 854
Cdd:cd06626   77 FMeycQEGTLEELLRhgrilDEAVIRVY----TLQLLEGLA----------YLHEN---GIVHRDIKPANIFLDSNGLIK 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  855 VSDFGLARLLLKFDEESFFNQLSSAgvRGTIGYAAPEYGVGGQPSING---DVYSFGILLLEMFTGKRPTNEL 924
Cdd:cd06626  140 LGDFGSAVKLKNNTTTMAPGEVNSL--VGTPAYMAPEVITGNKGEGHGraaDIWSLGCVVLEMATGKRPWSEL 210
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
708-920 1.57e-21

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: 95.45  E-value: 1.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLT--EKKVVAVKVLNM-----QRRGAMKSFMAECESLKDIRHRNLVKLLTACssIDFQGNefRALI 780
Cdd:cd13994    1 IGKGATSVVRIVTKKNprSGVLYAVKEYRRrddesKRKDYVKRLTSEYIISSKLHHPNIVKVLDLC--QDLHGK--WCLV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFMPNGSLDMWLhpeeveeihRPSRTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGL 860
Cdd:cd13994   77 MEYCPGGDLFTLI---------EKADSLSLEEKDCFFKQILRGVAYLHSH---GIAHRDLKPENILLDEDGVLKLTDFGT 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18408454  861 A-RLLLKFDEESffnqLSSAGVRGTIGYAAPEygVGGQPSING---DVYSFGILLLEMFTGKRP 920
Cdd:cd13994  145 AeVFGMPAEKES----PMSAGLCGSEPYMAPE--VFTSGSYDGravDVWSCGIVLFALFTGRFP 202
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
706-916 1.71e-21

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: 96.28  E-value: 1.71e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTVYKALLltEKKVVAVKVLNMQRRgamKSFMAECE--SLKDIRHRNLVKLLTACSSIDFQGNEFRALIYEF 783
Cdd:cd14054    1 QLIGQGRYGTVWKGSL--DERPVAVKVFPARHR---QNFQNEKDiyELPLMEHSNILRFIGADERPTADGRMEYLLVLEY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  784 MPNGSLDMWLHpeeveeihrpSRTLTLLERLNIAIDVASVLDYLH-----VHCHEP-IAHCDLKPSNVLLDDDLTAHVSD 857
Cdd:cd14054   76 APKGSLCSYLR----------ENTLDWMSSCRMALSLTRGLAYLHtdlrrGDQYKPaIAHRDLNSRNVLVKADGSCVICD 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  858 FGLA---RLLLKFDEESFFNQLSSAGVRGTIGYAAPEYGVGgqpSIN----------GDVYSFGILLLEMFT 916
Cdd:cd14054  146 FGLAmvlRGSSLVRGRPGAAENASISEVGTLRYMAPEVLEG---AVNlrdcesalkqVDVYALGLVLWEIAM 214
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
708-918 1.80e-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: 95.71  E-value: 1.80e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQ--RRGAMKSFMAECESLKDIRHRNLVKL---LTACSSIDFQGNEFraLIYE 782
Cdd:cd07840    7 IGEGTYGQVYKARNKKTGELVALKKIRMEneKEGFPITAIREIKLLQKLDHPNVVRLkeiVTSKGSAKYKGSIY--MVFE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMP---NGSLDmwlhpeeveeihRPSRTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFG 859
Cdd:cd07840   85 YMDhdlTGLLD------------NPEVKFTESQIKCYMKQLLEGLQYLHSN---GILHRDIKGSNILINNDGVLKLADFG 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  860 LARLLLKFDEESFFNQLSsagvrgTIGYAAPE-------YGvggqPSIngDVYSFGILLLEMFTGK 918
Cdd:cd07840  150 LARPYTKENNADYTNRVI------TLWYRPPElllgatrYG----PEV--DMWSVGCILAELFTGK 203
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
708-928 1.83e-21

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: 94.98  E-value: 1.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQR--RGAMKSFMAECESLKDIRHRNLVKLltacssIDFQ-GNEFRALIYEFM 784
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKlnKKLQENLESEIAILKSIKHPNIVRL------YDVQkTEDFIYLVLEYC 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLDMWLH-----PEEVeeihrpsrTLTLLERLniaidvASVLDYLHVHchePIAHCDLKPSNVLL---DDDLTAHVS 856
Cdd:cd14009   75 AGGDLSQYIRkrgrlPEAV--------ARHFMQQL------ASGLKFLRSK---NIIHRDLKPQNLLLstsGDDPVLKIA 137
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  857 DFGLARLLLKFDEesffnqlsSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPtnelFGGN 928
Cdd:cd14009  138 DFGFARSLQPASM--------AETLCGSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPP----FRGS 197
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
707-920 1.97e-21

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: 95.56  E-value: 1.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTE----KKVVAVKVL-NMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSIDFQgnefraLIY 781
Cdd:cd05057   14 VLGSGAFGTVYKGVWIPEgekvKIPVAIKVLrEETGPKANEEILDEAYVMASVDHPHLVRLLGICLSSQVQ------LIT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 EFMPNGSLDmwlhpeevEEIHRPSRTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLA 861
Cdd:cd05057   88 QLMPLGCLL--------DYVRNHRDNIGSQLLLNWCVQIAKGMSYLEEK---RLVHRDLAARNVLVKTPNHVKITDFGLA 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  862 RlLLKFDEesffNQLSSAGVRGTIGYAAPE---YGVGGQPSingDVYSFGILLLEMFT-GKRP 920
Cdd:cd05057  157 K-LLDVDE----KEYHAEGGKVPIKWMALEsiqYRIYTHKS---DVWSYGVTVWELMTfGAKP 211
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
708-919 2.13e-21

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: 94.60  E-value: 2.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVvAVKVLnmqRRGAM--KSFMAECESLKDIRHRNLVKLLTACSSidfqgnEFRALIYEFMP 785
Cdd:cd14203    3 LGQGCFGEVWMGTWNGTTKV-AIKTL---KPGTMspEAFLEEAQIMKKLRHDKLVQLYAVVSE------EPIYIVTEFMS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLDMWLHPEEveeihrpSRTLTLLERLNIAIDVASVLDYLHVHCHepiAHCDLKPSNVLLDDDLTAHVSDFGLARLLL 865
Cdd:cd14203   73 KGSLLDFLKDGE-------GKYLKLPQLVDMAAQIASGMAYIERMNY---IHRDLRAANILVGDNLVCKIADFGLARLIE 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18408454  866 kfDEESFFNQlssaGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKR 919
Cdd:cd14203  143 --DNEYTARQ----GAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGR 190
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
708-928 2.36e-21

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: 94.61  E-value: 2.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAmKSFMAECESLK----DIRHRNLVKLLtacSSIDFQGNEFRALIYEF 783
Cdd:cd05118    7 IGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHP-KAALREIKLLKhlndVEGHPNIVKLL---DVFEHRGGNHLCLVFEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  784 MPNGSLDMwlhpeeveeIHRPSRTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTA-HVSDFGLAR 862
Cdd:cd05118   83 MGMNLYEL---------IKDYPRGLPLDLIKSYLYQLLQALDFLHSN---GIIHRDLKPENILINLELGQlKLADFGLAR 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  863 LllkFDEESFFNQLSsagvrgTIGYAAPEYGVGGQPSING-DVYSFGILLLEMFTGKRptneLFGGN 928
Cdd:cd05118  151 S---FTSPPYTPYVA------TRWYRAPEVLLGAKPYGSSiDIWSLGCILAELLTGRP----LFPGD 204
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
709-920 3.35e-21

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: 94.75  E-value: 3.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVYKALLLT-----EKKVVAVKVLNMQRRGAMKS-FMAECESLKDIRHRNLVKLLTACSSidfqgNEFRALIYE 782
Cdd:cd05048   14 GEGAFGKVYKGELLGpsseeSAISVAIKTLKENASPKTQQdFRREAELMSDLQHPNIVCLLGVCTK-----EQPQCMLFE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLDMWL-------HPEEVEEIHRPSRTLTLLERLNIAIDVASVLDYLHVHcHepIAHCDLKPSNVLLDDDLTAHV 855
Cdd:cd05048   89 YMAHGDLHEFLvrhsphsDVGVSSDDDGTASSLDQSDFLHIAIQIAAGMEYLSSH-H--YVHRDLAARNCLVGDGLTVKI 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  856 SDFGLARLLLKFDeesFFNQLSSA--GVRgtigYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRP 920
Cdd:cd05048  166 SDFGLSRDIYSSD---YYRVQSKSllPVR----WMPPEAILYGKFTTESDVWSFGVVLWEIFSyGLQP 226
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
706-920 3.44e-21

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: 94.16  E-value: 3.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTVYKALLLTEKKVVAVKVL---NMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYE 782
Cdd:cd14099    7 KFLGKGGFAKCYEVTDMSTGKVYAGKVVpksSLTKPKQREKLKSEIKIHRSLKHPNIVKFHDC-----FEDEENVYILLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLDmwlhpeeveEIHRPSRTLTLLERLNIAIDVASVLDYLHVHChepIAHCDLKPSNVLLDDDLTAHVSDFGLAR 862
Cdd:cd14099   82 LCSNGSLM---------ELLKRRKALTEPEVRYFMRQILSGVKYLHSNR---IIHRDLKLGNLFLDENMNVKIGDFGLAA 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  863 lLLKFDEESFFNqlssagVRGTIGYAAPE--YGVGGQpSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14099  150 -RLEYDGERKKT------LCGTPNYIAPEvlEKKKGH-SFEVDIWSLGVILYTLLVGKPP 201
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
701-920 3.45e-21

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: 94.25  E-value: 3.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  701 GFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQ---RRGAMKSFMAECESLKDIRHRNLVKLltaCSSidFQGNEFR 777
Cdd:cd05578    1 HFQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQkciEKDSVRNVLNELEILQELEHPFLVNL---WYS--FQDEEDM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  778 ALIYEFMPNGSLDMWLHPEEV--EEIhrpsrtltllERLNIAiDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHV 855
Cdd:cd05578   76 YMVVDLLLGGDLRYHLQQKVKfsEET----------VKFYIC-EIVLALDYLHSK---NIIHRDIKPDNILLDEQGHVHI 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  856 SDFGLARLLLKfdeesffnQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd05578  142 TDFNIATKLTD--------GTLATSTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRP 198
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
708-919 4.57e-21

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: 94.18  E-value: 4.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLltEKKVVAVKVLN----MQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEF 783
Cdd:cd14160    1 IGEGEIFEVYRVRI--GNRSYAVKLFKqekkMQWKKHWKRFLSELEVLLLFQHPNILELAAY-----FTETEKFCLVYPY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  784 MPNGSLDMWLHpeeveeIHRPSRTLTLLERLNIAIDVASVLDYLHVHCHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARL 863
Cdd:cd14160   74 MQNGTLFDRLQ------CHGVTKPLSWHERINILIGIAKAIHYLHNSQPCTVICGNISSANILLDDQMQPKLTDFALAHF 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  864 LLKFDEESFFNQLSSAGvRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKR 919
Cdd:cd14160  148 RPHLEDQSCTINMTTAL-HKHLWYMPEEYIRQGKLSVKTDVYSFGIVIMEVLTGCK 202
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
709-920 5.16e-21

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: 93.69  E-value: 5.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVYKALLLTEKKVVAVKVL---NMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFMP 785
Cdd:cd14007    9 GKGKFGNVYLAREKKSGFIVALKVIsksQLQKSGLEHQLRREIEIQSHLRHPNILRLYGY-----FEDKKRIYLILEYAP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLdmwlhpeeveeihrpsrtLTLLERL---------NIAIDVASVLDYLHVHChepIAHCDLKPSNVLLDDDLTAHVS 856
Cdd:cd14007   84 NGEL------------------YKELKKQkrfdekeaaKYIYQLALALDYLHSKN---IIHRDIKPENILLGSNGELKLA 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  857 DFGLARlllkfdeESFFNQLSSagVRGTIGYAAPEYgVGGQP---SIngDVYSFGILLLEMFTGKRP 920
Cdd:cd14007  143 DFGWSV-------HAPSNRRKT--FCGTLDYLPPEM-VEGKEydyKV--DIWSLGVLCYELLVGKPP 197
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
707-924 7.75e-21

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: 93.13  E-value: 7.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKkvVAVKVLnmqRRGAMKSFMAECESLKD-------IRHRNLVKLLTACSSIdfqgnEFRAL 779
Cdd:cd14148    1 IIGVGGFGKVYKGLWRGEE--VAVKAA---RQDPDEDIAVTAENVRQearlfwmLQHPNIIALRGVCLNP-----PHLCL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  780 IYEFMPNGSLDMWLHPEEVeeihrPSRTLtllerLNIAIDVASVLDYLHVHCHEPIAHCDLKPSNVLL-----DDDL--- 851
Cdd:cd14148   71 VMEYARGGALNRALAGKKV-----PPHVL-----VNWAVQIARGMNYLHNEAIVPIIHRDLKSSNILIlepieNDDLsgk 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  852 TAHVSDFGLARlllkfdEESFFNQLSSAgvrGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTNEL 924
Cdd:cd14148  141 TLKITDFGLAR------EWHKTTKMSAA---GTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREI 204
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
708-920 9.64e-21

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: 92.58  E-value: 9.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKAL-LLTEKKVvAVKVLNMQR--RGAMKSFMAECESLKDIRHRNLVKLLtacSSIDFQGNEFraLIYEFM 784
Cdd:cd14003    8 LGEGSFGKVKLARhKLTGEKV-AIKIIDKSKlkEEIEEKIKREIEIMKLLNHPNIIKLY---EVIETENKIY--LVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLDMWLhpeeveeihRPSRTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLARll 864
Cdd:cd14003   82 SGGELFDYI---------VNNGRLSEDEARRFFQQLISAVDYCHSN---GIVHRDLKLENILLDKNGNLKIIDFGLSN-- 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  865 lKFDEESFFNQLSsagvrGTIGYAAPEYgVGGQPsING---DVYSFGILLLEMFTGKRP 920
Cdd:cd14003  148 -EFRGGSLLKTFC-----GTPAYAAPEV-LLGRK-YDGpkaDVWSLGVILYAMLTGYLP 198
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
708-1004 1.19e-20

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: 93.03  E-value: 1.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVvAVKVLnmqRRGAMK--SFMAECESLKDIRHRNLVKLLTACSsidfqgNEFRALIYEFMP 785
Cdd:cd05067   15 LGAGQFGEVWMGYYNGHTKV-AIKSL---KQGSMSpdAFLAEANLMKQLQHQRLVRLYAVVT------QEPIYIITEYME 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLDMWLHPEEveeihrpSRTLTLLERLNIAIDVASVLDYLHVHCHepiAHCDLKPSNVLLDDDLTAHVSDFGLARLLl 865
Cdd:cd05067   85 NGSLVDFLKTPS-------GIKLTINKLLDMAAQIAEGMAFIEERNY---IHRDLRAANILVSDTLSCKIADFGLARLI- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  866 kfdEESFFNqlSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRPtnelfggnftlnsYTKSALPERIL 944
Cdd:cd05067  154 ---EDNEYT--AREGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVThGRIP-------------YPGMTNPEVIQ 215
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  945 DivdesiLHIGLRVGFPvVECLTMVFEVGLRCCEESPMNRlatsIVVKELISIRERFFKA 1004
Cdd:cd05067  216 N------LERGYRMPRP-DNCPEELYQLMRLCWKERPEDR----PTFEYLRSVLEDFFTA 264
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
708-944 1.24e-20

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: 92.74  E-value: 1.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSfmaECESLKDIRHRNLVKLltacssidFQGNEFRA---LIYEFM 784
Cdd:cd14010    8 IGRGKHSVVYKGRRKGTIEFVAIKCVDKSKRPEVLN---EVRLTHELKHPNVLKF--------YEWYETSNhlwLVVEYC 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSL------DMWLhPEEVeeIHrpsrtltllerlNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDF 858
Cdd:cd14010   77 TGGDLetllrqDGNL-PESS--VR------------KFGRDLVRGLHYIHSK---GIIYCDLKPSNILLDGNGTLKLSDF 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  859 GLARLLLKFDEEsFFNQLSSAG----------VRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPtnelfggn 928
Cdd:cd14010  139 GLARREGEILKE-LFGQFSDEGnvnkvskkqaKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPP-------- 209
                        250
                 ....*....|....*.
gi 18408454  929 FTLNSYTKsaLPERIL 944
Cdd:cd14010  210 FVAESFTE--LVEKIL 223
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
708-923 1.72e-20

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: 92.29  E-value: 1.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVA------VKVLNMQRrgamKSFMAECESLKDIRHRNLVKLLTACSSIDfqGNEFrALIY 781
Cdd:cd13983    9 LGRGSFKTVYRAFDTEEGIEVAwneiklRKLPKAER----QRFKQEIEILKSLKHPNIIKFYDSWESKS--KKEV-IFIT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 EFMPNGSLDMWLhpeeveeihrpsRTLTLLERLNI---AIDVASVLDYLHVHCHePIAHCDLKPSNVLLDddlTAH---- 854
Cdd:cd13983   82 ELMTSGTLKQYL------------KRFKRLKLKVIkswCRQILEGLNYLHTRDP-PIIHRDLKCDNIFIN---GNTgevk 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  855 VSDFGLARLLLKfdeesffNQLSSagVRGTIGYAAPE-YGVGGQPSIngDVYSFGILLLEMFTGKRPTNE 923
Cdd:cd13983  146 IGDLGLATLLRQ-------SFAKS--VIGTPEFMAPEmYEEHYDEKV--DIYAFGMCLLEMATGEYPYSE 204
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
708-984 2.42e-20

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: 91.64  E-value: 2.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKV---VAVKVL-NMQRRGAMKSFMAECESLKDIRHRNLVKLLTACssidfQGNEFrALIYEF 783
Cdd:cd05060    3 LGHGNFGSVRKGVYLMKSGKeveVAVKTLkQEHEKAGKKEFLREASVMAQLDHPCIVRLIGVC-----KGEPL-MLVMEL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  784 MPNGSLDMWLhpeeveeihRPSRTLTLLERLNIAIDVASVLDYLHvHCHepIAHCDLKPSNVLLDDDLTAHVSDFGLARl 863
Cdd:cd05060   77 APLGPLLKYL---------KKRREIPVSDLKELAHQVAMGMAYLE-SKH--FVHRDLAARNVLLVNRHQAKISDFGMSR- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  864 LLKFDEESFfnQLSSAGvRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRPTNELFGGnftlnsytksalper 942
Cdd:cd05060  144 ALGAGSDYY--RATTAG-RWPLKWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKPYGEMKGP--------------- 205
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 18408454  943 ilDIVdeSILHIGLRVGFPvVECLTMVFEVGLRCCEESPMNR 984
Cdd:cd05060  206 --EVI--AMLESGERLPRP-EECPQEIYSIMLSCWKYRPEDR 242
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
71-521 2.57e-20

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 94.62  E-value: 2.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   71 LELGRLQLGGVISPSIGNLSFLVSLDLYENFFGGTIPQEVGQLSRLEYLDMGINYLRGPIPLGLYNCSRLLNLRldsnRL 150
Cdd:COG4886   26 LLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLT----EL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  151 GGSVPSELGSLTNLVQLNLYGNNMRgKLPTSLGNLTLLEQLALSHNNLEgEIPSDVAQLTQIWSLQLVANNFSGVfPPAL 230
Cdd:COG4886  102 DLSGNEELSNLTNLESLDLSGNQLT-DLPEELANLTNLKELDLSNNQLT-DLPEPLGNLTNLKSLDLSNNQLTDL-PEEL 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  231 YNLSSLKLLGIGYNHFSgrlrpdlgillpnllsfnmggnyftgSIPTTLSNISTLERLGMNENNLTgSIPTfgnvpnlkl 310
Cdd:COG4886  179 GNLTNLKELDLSNNQIT--------------------------DLPEPLGNLTNLEELDLSGNQLT-DLPE--------- 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  311 lflhtnslgsdssrdlefltSLTNCTQLETLGIGRNRLGgDLPiSIANLSaKLVTLDLGGTLISgSIPyDIGNLINLQKL 390
Cdd:COG4886  223 --------------------PLANLTNLETLDLSNNQLT-DLP-ELGNLT-NLEELDLSNNQLT-DLP-PLANLTNLKTL 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  391 ILDQNMLSGPLPTSLGKLLNLRYLSLFSNRLSGGIPAFIGNMTMLETLDLSNNGFEGIVPTSLGNCSHLLELWIGDNKLN 470
Cdd:COG4886  278 DLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLN 357
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18408454  471 GTIPLEIMKIQQLLRLDMSGNSLIGSLPQDIGALQNLGTLSLGDNKLSGKL 521
Cdd:COG4886  358 LLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALL 408
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
290-589 3.26e-20

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 94.62  E-value: 3.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  290 MNENNLTGSIPTFGNVPNLKLLFLHTNSLGSDSSRDLEFLTSLTNCTQLETLGIGRNRLGGDLPISIANLSAKLVTLDLG 369
Cdd:COG4886    1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  370 GTLISGSIPYDIGNLINLQKLILDQNmlsgplpTSLGKLLNLRYLSLFSNRLSGgIPAFIGNMTMLETLDLSNNGFEGIv 449
Cdd:COG4886   81 LLSLLLLGLTDLGDLTNLTELDLSGN-------EELSNLTNLESLDLSGNQLTD-LPEELANLTNLKELDLSNNQLTDL- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  450 PTSLGNCSHLLELWIGDNKLNgtipleimkiqqllrldmsgnsligSLPQDIGALQNLGTLSLGDNKLSgKLPQTLGNCL 529
Cdd:COG4886  152 PEPLGNLTNLKSLDLSNNQLT-------------------------DLPEELGNLTNLKELDLSNNQIT-DLPEPLGNLT 205
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  530 TMESLflegnlfygdipdlkglvgvkevDLSNNDLSgSIPEYFASFSKLEYLNLSFNNLE 589
Cdd:COG4886  206 NLEEL-----------------------DLSGNQLT-DLPEPLANLTNLETLDLSNNQLT 241
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
707-920 4.60e-20

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: 91.25  E-value: 4.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKkvVAVKVlnmQRRGAMKSFMAECESLKD-------IRHRNLVKLLTACSSidfQGNefRAL 779
Cdd:cd14146    1 IIGVGGFGKVYRATWKGQE--VAVKA---ARQDPDEDIKATAESVRQeaklfsmLRHPNIIKLEGVCLE---EPN--LCL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  780 IYEFMPNGSLDMWLHPEEVEEIHRPSRTLTLLERLNIAIDVASVLDYLHVHCHEPIAHCDLKPSNVLL-----DDDL--- 851
Cdd:cd14146   71 VMEFARGGTLNRALAAANAAPGPRRARRIPPHILVNWAVQIARGMLYLHEEAVVPILHRDLKSSNILLlekieHDDIcnk 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  852 TAHVSDFGLARlllkfdEESFFNQLSSAgvrGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14146  151 TLKITDFGLAR------EWHRTTKMSAA---GTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVP 210
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
702-920 5.23e-20

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: 91.00  E-value: 5.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQR----RGAMKSFMAECESLKDIRHRNLVKLltacssID-FQGNEF 776
Cdd:cd14098    2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKvagnDKNLQLFQREINILKSLEHPGIVRL------IDwYEDDQH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  777 RALIYEFMPNGSL-DMWLHPEEVEEIHRPSRTLTLLERLniaidvasvldyLHVHcHEPIAHCDLKPSNVLL--DDDLTA 853
Cdd:cd14098   76 IYLVMEYVEGGDLmDFIMAWGAIPEQHARELTKQILEAM------------AYTH-SMGITHRDLKPENILItqDDPVIV 142
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  854 HVSDFGLARLLlkfDEESFFNQLSsagvrGTIGYAAPEYGVGGQPSING------DVYSFGILLLEMFTGKRP 920
Cdd:cd14098  143 KISDFGLAKVI---HTGTFLVTFC-----GTMAYLAPEILMSKEQNLQGgysnlvDMWSVGCLVYVMLTGALP 207
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
707-940 6.09e-20

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: 90.90  E-value: 6.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVLNM----------QRRGAMKSFMAECESLKDIRHRNLVKLLtACSsidfQGNEF 776
Cdd:cd06629    8 LIGKGTYGRVYLAMNATTGEMLAVKQVELpktssdradsRQKTVVDALKSEIDTLKDLDHPNIVQYL-GFE----ETEDY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  777 RALIYEFMPNGSLDmwlhpeevEEIHRPSRTLTLLERlNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVS 856
Cdd:cd06629   83 FSIFLEYVPGGSIG--------SCLRKYGKFEEDLVR-FFTRQILDGLAYLH---SKGILHRDLKADNILVDLEGICKIS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  857 DFGLARlllkfDEESFFNQLSSAGVRGTIGYAAPE----YGVGGQPSIngDVYSFGILLLEMFTGKRP--TNELFGGNFT 930
Cdd:cd06629  151 DFGISK-----KSDDIYGNNGATSMQGSVFWMAPEvihsQGQGYSAKV--DIWSLGCVVLEMLAGRRPwsDDEAIAAMFK 223
                        250
                 ....*....|
gi 18408454  931 LNSyTKSALP 940
Cdd:cd06629  224 LGN-KRSAPP 232
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
711-923 6.13e-20

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: 91.13  E-value: 6.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  711 GSFGTVYKALLLTEKKVVAVKVLNMQ---RRGAMKSFMAECESLKDIRHRNLVKLLTACSSIDFQGnefraLIYEFMPNG 787
Cdd:cd14026    8 GAFGTVSRARHADWRVTVAIKCLKLDspvGDSERNCLLKEAEILHKARFSYILPILGICNEPEFLG-----IVTEYMTNG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 SLDMWLHPEEVeeihRPSRTLTLleRLNIAIDVASVLDYLHvHCHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARLLLKF 867
Cdd:cd14026   83 SLNELLHEKDI----YPDVAWPL--RLRILYEIALGVNYLH-NMSPPLLHHDLKTQNILLDGEFHVKIADFGLSKWRQLS 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  868 DEESffNQLSSAGVRGTIGYAAPEYGVGGQ---PSINGDVYSFGILLLEMFTGKRPTNE 923
Cdd:cd14026  156 ISQS--RSSKSAPEGGTIIYMPPEEYEPSQkrrASVKHDIYSYAIIMWEVLSRKIPFEE 212
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
706-920 1.06e-19

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: 90.17  E-value: 1.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTVYKALLL------TEKKVVAVKVLnmqRRGAM----KSFMAECESLKDIRHRNLVKLLTACssIDfqgNE 775
Cdd:cd05044    1 KFLGSGAFGEVFEGTAKdilgdgSGETKVAVKTL---RKGATdqekAEFLKEAHLMSNFKHPNILKLLGVC--LD---ND 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  776 FRALIYEFMPNGSLDMWLHPEEVEEIHRPSrtLTLLERLNIAIDVASVLDYLH-VHchepIAHCDLKPSNVLLD----DD 850
Cdd:cd05044   73 PQYIILELMEGGDLLSYLRAARPTAFTPPL--LTLKDLLSICVDVAKGCVYLEdMH----FVHRDLAARNCLVSskdyRE 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18408454  851 LTAHVSDFGLARLLLKFDeesfFNQLSSAG---VRgtigYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRP 920
Cdd:cd05044  147 RVVKIGDFGLARDIYKND----YYRKEGEGllpVR----WMAPESLVDGVFTTQSDVWAFGVLMWEILTlGQQP 212
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
708-924 2.52e-19

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: 89.35  E-value: 2.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEkkvVAVKVLNMQ--RRGAMKSFMAECESLKDIRHRNLVKLLTACSSIDFqgnefrALIYEFMP 785
Cdd:cd14151   16 IGSGSFGTVYKGKWHGD---VAVKMLNVTapTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQL------AIVTQWCE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLDMWLHPEEVEeihrpsrtLTLLERLNIAIDVASVLDYLHVhchEPIAHCDLKPSNVLLDDDLTAHVSDFGLARLLL 865
Cdd:cd14151   87 GSSLYHHLHIIETK--------FEMIKLIDIARQTAQGMDYLHA---KSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKS 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  866 KFDEESFFNQLSsagvrGTIGYAAPE---YGVGGQPSINGDVYSFGILLLEMFTGKRPTNEL 924
Cdd:cd14151  156 RWSGSHQFEQLS-----GSILWMAPEvirMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNI 212
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
708-920 2.53e-19

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: 88.60  E-value: 2.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEkkVVAVKVL------NMQRrgAMKSFMAECESLKDIRHRNLVKLLTACssidFQGNEFrALIY 781
Cdd:cd14061    2 IGVGGFGKVYRGIWRGE--EVAVKAArqdpdeDISV--TLENVRQEARLFWMLRHPNIIALRGVC----LQPPNL-CLVM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 EFMPNGSLDMWLHPEEVeeihRPSRTLtllerlNIAIDVASVLDYLHVHCHEPIAHCDLKPSNVLLD-----DDLTAHV- 855
Cdd:cd14061   73 EYARGGALNRVLAGRKI----PPHVLV------DWAIQIARGMNYLHNEAPVPIIHRDLKSSNILILeaienEDLENKTl 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  856 --SDFGLARlllkfdEESFFNQLSSAgvrGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14061  143 kiTDFGLAR------EWHKTTRMSAA---GTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVP 200
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
708-924 3.77e-19

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: 88.68  E-value: 3.77e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTV-----YKALLLTEKKVVAVKVL-NMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSsidfQGNEFrALIY 781
Cdd:cd05049   13 LGEGAFGKVflgecYNLEPEQDKMLVAVKTLkDASSPDARKDFEREAELLTNLQHENIVKFYGVCT----EGDPL-LMVF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 EFMPNGSLDMWLH---PEEVEEIHRPSRT--LTLLERLNIAIDVASVLDYLhvhCHEPIAHCDLKPSNVLLDDDLTAHVS 856
Cdd:cd05049   88 EYMEHGDLNKFLRshgPDAAFLASEDSAPgeLTLSQLLHIAVQIASGMVYL---ASQHFVHRDLATRNCLVGTNLVVKIG 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  857 DFGLARLLLKFDeesFFNqlssagVRGT----IGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRPTNEL 924
Cdd:cd05049  165 DFGMSRDIYSTD---YYR------VGGHtmlpIRWMPPESILYRKFTTESDVWSFGVVLWEIFTyGKQPWFQL 228
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
706-986 4.15e-19

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: 88.78  E-value: 4.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAM-KSFMAECEslkdirhrnlvkLLTACSS---IDFQGNEFR---- 777
Cdd:cd06619    7 EILGHGNGGTVYKAYHLLTRRILAVKVIPLDITVELqKQIMSELE------------ILYKCDSpyiIGFYGAFFVenri 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  778 ALIYEFMPNGSLDM-WLHPEEVeeihrpsrtltlLERlnIAIDVASVLDYLhvhCHEPIAHCDLKPSNVLLDDDLTAHVS 856
Cdd:cd06619   75 SICTEFMDGGSLDVyRKIPEHV------------LGR--IAVAVVKGLTYL---WSLKILHRDVKPSNMLVNTRGQVKLC 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  857 DFGLARLLLkfdeesffNQLSSAGVrGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTNELFGGNFTLnsytk 936
Cdd:cd06619  138 DFGVSTQLV--------NSIAKTYV-GTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYPQIQKNQGSL----- 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 18408454  937 saLPERILD-IVDES--ILHIGLrVGFPVVECLTmvfevglRCCEESPMNRLA 986
Cdd:cd06619  204 --MPLQLLQcIVDEDppVLPVGQ-FSEKFVHFIT-------QCMRKQPKERPA 246
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
706-920 4.62e-19

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: 88.20  E-value: 4.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTVYKALLLTEKK---VVAVKVLNMQRRGAMKS-FMAECESLKDIRHRNLVKLLTACSSidfqgNEFRALIY 781
Cdd:cd05033   10 KVIGGGEFGEVCSGSLKLPGKkeiDVAIKTLKSGYSDKQRLdFLTEASIMGQFDHPNVIRLEGVVTK-----SRPVMIVT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 EFMPNGSLDMWLHPEEVEeihrpsrtLTLLERLNIAIDVASVLDYLHVHCHepiAHCDLKPSNVLLDDDLTAHVSDFGLA 861
Cdd:cd05033   85 EYMENGSLDKFLRENDGK--------FTVTQLVGMLRGIASGMKYLSEMNY---VHRDLAARNILVNSDLVCKVSDFGLS 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  862 RLLLKFDEEsffnqLSSAGVRGTIGYAAPE---YGVGGQPSingDVYSFGILLLE-MFTGKRP 920
Cdd:cd05033  154 RRLEDSEAT-----YTTKGGKIPIRWTAPEaiaYRKFTSAS---DVWSFGIVMWEvMSYGERP 208
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
708-919 4.69e-19

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: 88.59  E-value: 4.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVvAVKVLnmqRRGAM--KSFMAECESLKDIRHRNLVKLLTACSSidfqgnEFRALIYEFMP 785
Cdd:cd05071   17 LGQGCFGEVWMGTWNGTTRV-AIKTL---KPGTMspEAFLQEAQVMKKLRHEKLVQLYAVVSE------EPIYIVTEYMS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLDMWLHPEEveeihrpSRTLTLLERLNIAIDVASVLDYLHVHCHepiAHCDLKPSNVLLDDDLTAHVSDFGLARLLL 865
Cdd:cd05071   87 KGSLLDFLKGEM-------GKYLRLPQLVDMAAQIASGMAYVERMNY---VHRDLRAANILVGENLVCKVADFGLARLIE 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18408454  866 kfDEESFFNQlssaGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKR 919
Cdd:cd05071  157 --DNEYTARQ----GAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGR 204
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
708-920 6.50e-19

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: 87.79  E-value: 6.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVvAVKVLnmqRRGAM--KSFMAECESLKDIRHRNLVKLLTACSSidfqgNEFRALIYEFMP 785
Cdd:cd05072   15 LGAGQFGEVWMGYYNNSTKV-AVKTL---KPGTMsvQAFLEEANLMKTLQHDKLVRLYAVVTK-----EEPIYIITEYMA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLDMWLHPEEVEEIHRPsrtltllERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARLLl 865
Cdd:cd05072   86 KGSLLDFLKSDEGGKVLLP-------KLIDFSAQIAEGMAYIE---RKNYIHRDLRAANVLVSESLMCKIADFGLARVI- 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  866 kfdEESFFNqlSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRP 920
Cdd:cd05072  155 ---EDNEYT--AREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIP 205
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
705-928 6.51e-19

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: 88.10  E-value: 6.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  705 SNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQ--RRGAMKSFMAECESLKDIR---HRNLVKLLTACSSIDFQGNEFRAL 779
Cdd:cd07838    4 VAEIGEGAYGTVYKARDLQDGRFVALKKVRVPlsEEGIPLSTIREIALLKQLEsfeHPNVVRLLDVCHGPRTDRELKLTL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  780 IYEFMpNGSLDMWL--HPE---EVEEIHRPSRTLTllerlniaidvaSVLDYLHVHChepIAHCDLKPSNVLLDDDLTAH 854
Cdd:cd07838   84 VFEHV-DQDLATYLdkCPKpglPPETIKDLMRQLL------------RGLDFLHSHR---IVHRDLKPQNILVTSDGQVK 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  855 VSDFGLARLLlkfdeeSFFNQLSSAGVrgTIGYAAPEygVGGQPSING--DVYSFGILLLEMFTgKRPtneLFGGN 928
Cdd:cd07838  148 LADFGLARIY------SFEMALTSVVV--TLWYRAPE--VLLQSSYATpvDMWSVGCIFAELFN-RRP---LFRGS 209
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
707-920 7.66e-19

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: 87.52  E-value: 7.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVLNM------QRRGAMKsfmaECESLKDIRHRNLVKLLTAcssidFQGNEFRALI 780
Cdd:cd08215    7 VIGKGSFGSAYLVRRKSDGKLYVLKEIDLsnmsekEREEALN----EVKLLSKLKHPNIVKYYES-----FEENGKLCIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFMPNGSLDMWLHPEEVEEIHRPSRTLtllerLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGL 860
Cdd:cd08215   78 MEYADGGDLAQKIKKQKKKGQPFPEEQI-----LDWFVQICLALKYLHSR---KILHRDLKTQNIFLTKDGVVKLGDFGI 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  861 ARLLlkfdeESFFNQLSSagVRGTIGYAAPE------YgvgGQPSingDVYSFGILLLEMFTGKRP 920
Cdd:cd08215  150 SKVL-----ESTTDLAKT--VVGTPYYLSPElcenkpY---NYKS---DIWALGCVLYELCTLKHP 202
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
707-920 8.36e-19

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: 87.70  E-value: 8.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTE----KKVVAVKVLnmQRRGAMKSFMAECE---SLKDIRHRNLVKLLTACSSIDFQgnefraL 779
Cdd:cd05111   14 VLGSGVFGTVHKGIWIPEgdsiKIPVAIKVI--QDRSGRQSFQAVTDhmlAIGSLDHAYIVRLLGICPGASLQ------L 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  780 IYEFMPNGSLdmwlhPEEVEEiHRPSRTLTLLerLNIAIDVASVLDYLHVHChepIAHCDLKPSNVLLDDDLTAHVSDFG 859
Cdd:cd05111   86 VTQLLPLGSL-----LDHVRQ-HRGSLGPQLL--LNWCVQIAKGMYYLEEHR---MVHRNLAARNVLLKSPSQVQVADFG 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  860 LARLLLKFDEESFFNQlssagVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRP 920
Cdd:cd05111  155 VADLLYPDDKKYFYSE-----AKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMTfGAEP 211
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
708-920 1.09e-18

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: 86.86  E-value: 1.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVyKALLLTEKKVVAVKvlnMQRRGAMKS--FMAECESLKDIRHRNLVKLLTACSSidfQGNEFraLIYEFMP 785
Cdd:cd05113   12 LGTGQFGVV-KYGKWRGQYDVAIK---MIKEGSMSEdeFIEEAKVMMNLSHEKLVQLYGVCTK---QRPIF--IITEYMA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLDMWLHpeevEEIHRPsrtlTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLARLLL 865
Cdd:cd05113   83 NGCLLNYLR----EMRKRF----QTQQLLEMCKDVCEAMEYLESK---QFLHRDLAARNCLVNDQGVVKVSDFGLSRYVL 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  866 kfDEEsffnQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRP 920
Cdd:cd05113  152 --DDE----YTSSVGSKFPVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMP 201
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
708-949 1.23e-18

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: 87.49  E-value: 1.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAM-KSFMAECESLKDIRHRNLVKLLTACSSidfQGNEFrALIYEFMPN 786
Cdd:cd06620   13 LGAGNGGSVSKVLHIPTGTIMAKKVIHIDAKSSVrKQILRELQILHECHSPYIVSFYGAFLN---ENNNI-IICMEYMDC 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  787 GSLDmwlhpeeveEIHRPSRTLTLLERLNIAIDVASVLDYLHVHCHepIAHCDLKPSNVLLDDDLTAHVSDFGLARLLLk 866
Cdd:cd06620   89 GSLD---------KILKKKGPFPEEVLGKIAVAVLEGLTYLYNVHR--IIHRDIKPSNILVNSKGQIKLCDFGVSGELI- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  867 fdeesffNQLSSAGVrGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPtnelFGGNFTLNSytKSALPERILD- 945
Cdd:cd06620  157 -------NSIADTFV-GTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFP----FAGSNDDDD--GYNGPMGILDl 222

                 ....*..
gi 18408454  946 ---IVDE 949
Cdd:cd06620  223 lqrIVNE 229
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
706-920 1.24e-18

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 88.73  E-value: 1.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   706 NMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMA-ECESLKDIRHRNLVKlltaCSSIDFQGNEFRALIyEFM 784
Cdd:PLN00034   80 NRIGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTVRRQICrEIEILRDVNHPNVVK----CHDMFDHNGEIQVLL-EFM 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   785 PNGSLdmwlhpeeveEIHRPSRTLTLLErlnIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARLL 864
Cdd:PLN00034  155 DGGSL----------EGTHIADEQFLAD---VARQILSGIAYLH---RRHIVHRDIKPSNLLINSAKNVKIADFGVSRIL 218
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454   865 lkfdeesffNQL-----SSAgvrGTIGYAAPE-----YGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:PLN00034  219 ---------AQTmdpcnSSV---GTIAYMSPErintdLNHGAYDGYAGDIWSLGVSILEFYLGRFP 272
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
707-923 1.55e-18

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: 86.47  E-value: 1.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALL--LTEKKVVAVKVLNmqRRGAMKSFMA-----ECESLKDIRHRNLVKLLtacsSIdFQGNEFRAL 779
Cdd:cd14080    7 TIGEGSYSKVKLAEYtkSGLKEKVACKIID--KKKAPKDFLEkflprELEILRKLRHPNIIQVY----SI-FERGSKVFI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  780 IYEFMPNGSLdmwlhpeeveeihrpsrtLTLLeRLNIAID----------VASVLDYLHVHChepIAHCDLKPSNVLLDD 849
Cdd:cd14080   80 FMEYAEHGDL------------------LEYI-QKRGALSesqariwfrqLALAVQYLHSLD---IAHRDLKCENILLDS 137
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  850 DLTAHVSDFGLARLLLKFDeesffNQLSSAGVRGTIGYAAPEY--GVGGQPSINgDVYSFGILLLEMFTGKRPTNE 923
Cdd:cd14080  138 NNNVKLSDFGFARLCPDDD-----GDVLSKTFCGSAAYAAPEIlqGIPYDPKKY-DIWSLGVILYIMLCGSMPFDD 207
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
708-923 1.59e-18

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: 86.62  E-value: 1.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRrgamksfmAECESLKDIR----------HRNLVKLLTACSSidfqgNEFR 777
Cdd:cd14069    9 LGEGAFGEVFLAVNRNTEEAVAVKFVDMKR--------APGDCPENIKkevciqkmlsHKNVVRFYGHRRE-----GEFQ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  778 ALIYEFMPNGSLDMWLHPE---EVEEIHRPSRTLTllerlniaidvaSVLDYLHVhchEPIAHCDLKPSNVLLDDDLTAH 854
Cdd:cd14069   76 YLFLEYASGGELFDKIEPDvgmPEDVAQFYFQQLM------------AGLKYLHS---CGITHRDIKPENLLLDENDNLK 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  855 VSDFGLARLLLKFDEESFFNQLssagvRGTIGYAAPEygVGGQPSING---DVYSFGILLLEMFTGKRPTNE 923
Cdd:cd14069  141 ISDFGLATVFRYKGKERLLNKM-----CGTLPYVAPE--LLAKKKYRAepvDVWSCGIVLFAMLAGELPWDQ 205
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
708-920 1.80e-18

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: 86.64  E-value: 1.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGA-MKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFMPN 786
Cdd:cd06610    9 IGSGATAVVYAAYCLPKKEKVAIKRIDLEKCQTsMDELRKEIQAMSQCNHPNVVSYYTS-----FVVGDELWLVMPLLSG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  787 GSLdmwLHpeeveeIHRPSRTLTLLERLNIAIDVASVL---DYLHVHCHepiAHCDLKPSNVLLDDDLTAHVSDFGLARL 863
Cdd:cd06610   84 GSL---LD------IMKSSYPRGGLDEAIIATVLKEVLkglEYLHSNGQ---IHRDVKAGNILLGEDGSVKIADFGVSAS 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  864 LLKfdeesffNQLSSAGVR----GTIGYAAPE-------YGVGgqpsinGDVYSFGILLLEMFTGKRP 920
Cdd:cd06610  152 LAT-------GGDRTRKVRktfvGTPCWMAPEvmeqvrgYDFK------ADIWSFGITAIELATGAAP 206
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
694-984 1.86e-18

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: 86.08  E-value: 1.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  694 DLRNATNGfsssNMVGSGSFGTVYKALLLTEKkvVAVKvlNMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssIDFQG 773
Cdd:cd05083    4 NLQKLTLG----EIIGEGEFGAVLQGEYMGQK--VAVK--NIKCDVTAQAFLEETAVMTKLQHKNLVRLLGV---ILHNG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  774 nefRALIYEFMPNGSLDMWLHPeeveeihRPSRTLTLLERLNIAIDVASVLDYLHVhchEPIAHCDLKPSNVLLDDDLTA 853
Cdd:cd05083   73 ---LYIVMELMSKGNLVNFLRS-------RGRALVPVIQLLQFSLDVAEGMEYLES---KKLVHRDLAARNILVSEDGVA 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  854 HVSDFGLARLLLKFDEESffnqlssagvRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFtgkrptnelfggnftlnS 933
Cdd:cd05083  140 KISDFGLAKVGSMGVDNS----------RLPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVF-----------------S 192
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18408454  934 YTKSALPERILDIVDESiLHIGLRVGFPvVECLTMVFEVGLRCCEESPMNR 984
Cdd:cd05083  193 YGRAPYPKMSVKEVKEA-VEKGYRMEPP-EGCPPDVYSIMTSCWEAEPGKR 241
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
707-994 1.89e-18

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: 86.51  E-value: 1.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLltEKKVVAVKVLNMQRRG------------------AMKSFMA---ECESLKDIRHRNLVKLLTA 765
Cdd:cd14000    1 LLGDGGFGSVYRASY--KGEPVAVKIFNKHTSSnfanvpadtmlrhlratdAMKNFRLlrqELTVLSHLHHPSIVYLLGI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  766 CSsidfqgnEFRALIYEFMPNGSLDMWLHPEEVEEIHRpsrTLTLLERlnIAIDVASVLDYLHvhcHEPIAHCDLKPSNV 845
Cdd:cd14000   79 GI-------HPLMLVLELAPLGSLDHLLQQDSRSFASL---GRTLQQR--IALQVADGLRYLH---SAMIIYRDLKSHNV 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  846 LL-----DDDLTAHVSDFGLARlllkfdeESFfnQLSSAGVRGTIGYAAPEYGVGGQP-SINGDVYSFGILLLEMFTGKR 919
Cdd:cd14000  144 LVwtlypNSAIIIKIADYGISR-------QCC--RMGAKGSEGTPGFRAPEIARGNVIyNEKVDVFSFGMLLYEILSGGA 214
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  920 PtnelFGGNFTLNSYTKsaLPERILDIVDESilhigLRVGFPVVECLTMvfevglRCCEESPMNRLATSIVVKEL 994
Cdd:cd14000  215 P----MVGHLKFPNEFD--IHGGLRPPLKQY-----ECAPWPEVEVLMK------KCWKENPQQRPTAVTVVSIL 272
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
708-920 2.24e-18

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: 86.22  E-value: 2.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEkkvVAVKVLNMQRRGA--MKSFMAECESLKDIRHRNLVKLLTACSSIDFqgnefrALIYEFMP 785
Cdd:cd14150    8 IGTGSFGTVFRGKWHGD---VAVKILKVTEPTPeqLQAFKNEMQVLRKTRHVNILLFMGFMTRPNF------AIITQWCE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLDMWLHPEEVEeihrpsrtLTLLERLNIAIDVASVLDYLHVhchEPIAHCDLKPSNVLLDDDLTAHVSDFGLARLLL 865
Cdd:cd14150   79 GSSLYRHLHVTETR--------FDTMQLIDVARQTAQGMDYLHA---KNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKT 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  866 KFDEESFFNQLSsagvrGTIGYAAPEYGVGGQP---SINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14150  148 RWSGSQQVEQPS-----GSILWMAPEVIRMQDTnpySFQSDVYAYGVVLYELMSGTLP 200
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
708-916 4.88e-18

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: 85.47  E-value: 4.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLT-----EKKVVAVKVLN----MQRRgamKSFMAECESLKDIRHRNLVKLLTACSsidfQGNefRA 778
Cdd:cd05032   14 LGQGSFGMVYEGLAKGvvkgePETRVAIKTVNenasMRER---IEFLNEASVMKEFNCHHVVRLLGVVS----TGQ--PT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 L-IYEFMPNGSLDMWLH---PEEveEIHRPSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAH 854
Cdd:cd05032   85 LvVMELMAKGDLKSYLRsrrPEA--ENNPGLGPPTLQKFIQMAAEIADGMAYLA---AKKFVHRDLAARNCMVAEDLTVK 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  855 VSDFGLARLLLkfdeESFFNQLSSAG---VRgtigYAAPEYGVGGQPSINGDVYSFGILLLEMFT 916
Cdd:cd05032  160 IGDFGMTRDIY----ETDYYRKGGKGllpVR----WMAPESLKDGVFTTKSDVWSFGVVLWEMAT 216
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
709-915 5.74e-18

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: 85.04  E-value: 5.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVYKAllltEKKV----VAVKVLNM-QRRGAMKSFMAECESLKDIRHRNLVKLLTACSsidfqgnEFRALI--Y 781
Cdd:cd13996   15 GSGGFGSVYKV----RNKVdgvtYAIKKIRLtEKSSASEKVLREVKALAKLNHPNIVRYYTAWV-------EEPPLYiqM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 EFMPNGSLDMWLHpeevEEIHRPSRTLTLLerLNIAIDVASVLDYLHVHChepIAHCDLKPSNVLLD-DDLTAHVSDFGL 860
Cdd:cd13996   84 ELCEGGTLRDWID----RRNSSSKNDRKLA--LELFKQILKGVSYIHSKG---IVHRDLKPSNIFLDnDDLQVKIGDFGL 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  861 ARLLLKFDEESFFNQLSSAGVR-------GTIGYAAPEYGVGGQPSINGDVYSFGILLLEMF 915
Cdd:cd13996  155 ATSIGNQKRELNNLNNNNNGNTsnnsvgiGTPLYASPEQLDGENYNEKADIYSLGIILFEML 216
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
708-919 5.97e-18

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: 85.12  E-value: 5.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVvAVKVLnmqRRGAM--KSFMAECESLKDIRHRNLVKLLTACSsidfqgNEFRALIYEFMP 785
Cdd:cd05070   17 LGNGQFGEVWMGTWNGNTKV-AIKTL---KPGTMspESFLEEAQIMKKLKHDKLVQLYAVVS------EEPIYIVTEYMS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLDMWLHPEEveeihrpSRTLTLLERLNIAIDVASVLDYLHVHCHepiAHCDLKPSNVLLDDDLTAHVSDFGLARLLL 865
Cdd:cd05070   87 KGSLLDFLKDGE-------GRALKLPNLVDMAAQVAAGMAYIERMNY---IHRDLRSANILVGNGLICKIADFGLARLIE 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18408454  866 kfDEESFFNQlssaGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKR 919
Cdd:cd05070  157 --DNEYTARQ----GAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGR 204
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
707-920 7.38e-18

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: 84.71  E-value: 7.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKkvVAVKVlnmQRRGAMKSFMAECESLKD-------IRHRNLVKLLTACSSidfQGNefRAL 779
Cdd:cd14145   13 IIGIGGFGKVYRAIWIGDE--VAVKA---ARHDPDEDISQTIENVRQeaklfamLKHPNIIALRGVCLK---EPN--LCL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  780 IYEFMPNGSLDMWLHPEEVeeihrPSRTLtllerLNIAIDVASVLDYLHVHCHEPIAHCDLKPSNVLL-----DDDL--- 851
Cdd:cd14145   83 VMEFARGGPLNRVLSGKRI-----PPDIL-----VNWAVQIARGMNYLHCEAIVPVIHRDLKSSNILIlekveNGDLsnk 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  852 TAHVSDFGLARlllkfdEESFFNQLSSAgvrGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14145  153 ILKITDFGLAR------EWHRTTKMSAA---GTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVP 212
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
708-920 8.00e-18

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: 83.70  E-value: 8.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKkvVAVKVLNMQRRGAMKSfmaecesLKDIRHRNLVKLLTACSsidfQGNEFrALIYEFMPNG 787
Cdd:cd14059    1 LGSGAQGAVFLGKFRGEE--VAVKKVRDEKETDIKH-------LRKLNHPNIIKFKGVCT----QAPCY-CILMEYCPYG 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 SLdmwlhpeevEEIHRPSRTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLARLLlkf 867
Cdd:cd14059   67 QL---------YEVLRAGREITPSLLVDWSKQIASGMNYLHLH---KIIHRDLKSPNVLVTYNDVLKISDFGTSKEL--- 131
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18408454  868 DEESffNQLSSAgvrGTIGYAAPEYgVGGQP-SINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14059  132 SEKS--TKMSFA---GTVAWMAPEV-IRNEPcSEKVDIWSFGVVLWELLTGEIP 179
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
707-1001 8.28e-18

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: 85.12  E-value: 8.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALL----LTEKKVVAVKVLNMQRRGAMKSfmaECESLKDI--RHRNLVKLLTAcssiDFQGNEFRA-- 778
Cdd:cd14055    2 LVGKGRFAEVWKAKLkqnaSGQYETVAVKIFPYEEYASWKN---EKDIFTDAslKHENILQFLTA----EERGVGLDRqy 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 -LIYEFMPNGSLDMWLHpeeveeihrpSRTLTLLERLNIAIDVASVLDYLHVHCHE------PIAHCDLKPSNVLLDDDL 851
Cdd:cd14055   75 wLITAYHENGSLQDYLT----------RHILSWEDLCKMAGSLARGLAHLHSDRTPcgrpkiPIAHRDLKSSNILVKNDG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  852 TAHVSDFGLArllLKFDEESFFNQLSSAGVRGTIGYAAPEygvGGQPSIN---------GDVYSFGILLLEM-----FTG 917
Cdd:cd14055  145 TCVLADFGLA---LRLDPSLSVDELANSGQVGTARYMAPE---ALESRVNledlesfkqIDVYSMALVLWEMasrceASG 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  918 -----KRPTNELFGGNFTLNSYTKSALPERIL-DIVDESILHIGLRvgfpvVECLTMVfevglRCCEESPMNRLATSIVV 991
Cdd:cd14055  219 evkpyELPFGSKVRERPCVESMKDLVLRDRGRpEIPDSWLTHQGMC-----VLCDTIT-----ECWDHDPEARLTASCVA 288
                        330
                 ....*....|
gi 18408454  992 kelisirERF 1001
Cdd:cd14055  289 -------ERF 291
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
707-994 8.46e-18

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: 85.16  E-value: 8.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLL------TEKKVVAVKVLNMQR-RGAMKSFMAECESLKDI-RHRNLVKLLTACSSidfQGNEFra 778
Cdd:cd05053   19 PLGEGAFGQVVKAEAVgldnkpNEVVTVAVKMLKDDAtEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQ---DGPLY-- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGSLDMWLH----PEEVEEI---HRPSRTLTLLERLNIAIDVASVLDYLhvhCHEPIAHCDLKPSNVLLDDDL 851
Cdd:cd05053   94 VVVEYASKGNLREFLRarrpPGEEASPddpRVPEEQLTQKDLVSFAYQVARGMEYL---ASKKCIHRDLAARNVLVTEDN 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  852 TAHVSDFGLARLLLKFDeesfFNQLSSAGvRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTgkrptnelFGGnftl 931
Cdd:cd05053  171 VMKIADFGLARDIHHID----YYRKTTNG-RLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFT--------LGG---- 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  932 NSYTKSALPERIldivdeSILHIGLRVGFPvVECLTMVFEVGLRCCEESPMNRLATSIVVKEL 994
Cdd:cd05053  234 SPYPGIPVEELF------KLLKEGHRMEKP-QNCTQELYMLMRDCWHEVPSQRPTFKQLVEDL 289
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
708-914 8.62e-18

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: 84.48  E-value: 8.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLtacsSIDFQGNEFRaLIYEFMPNG 787
Cdd:cd14154    1 LGKGFFGQAIKVTHRETGEVMVMKELIRFDEEAQRNFLKEVKVMRSLDHPNVLKFI----GVLYKDKKLN-LITEYIPGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 SLDmwlhpeevEEIHRPSRTLTLLERLNIAIDVASVLDYLHVHChepIAHCDLKPSNVLLDDDLTAHVSDFGLARLLLkf 867
Cdd:cd14154   76 TLK--------DVLKDMARPLPWAQRVRFAKDIASGMAYLHSMN---IIHRDLNSHNCLVREDKTVVVADFGLARLIV-- 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  868 DEESFFNQLSSAGVRGTIGYAAPE--YGVGGQP------SING-------DVYSFGILLLEM 914
Cdd:cd14154  143 EERLPSGNMSPSETLRHLKSPDRKkrYTVVGNPywmapeMLNGrsydekvDIFSFGIVLCEI 204
Pkinase pfam00069
Protein kinase domain;
708-920 9.90e-18

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 83.06  E-value: 9.90e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454    708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMK--SFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFMP 785
Cdd:pfam00069    7 LGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKdkNILREIKILKKLNHPNIVRLYDA-----FEDKDNLYLVLEYVE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454    786 NGSLDmwlhpeeveeihrpsrtltllerlniaidvasvlDYLHVHChePIAHCDLKpsnvlldddltahvsdFGLARLLL 865
Cdd:pfam00069   82 GGSLF----------------------------------DLLSEKG--AFSEREAK----------------FIMKQILE 109
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454    866 KFDEESFFNQlssagVRGTIGYAAPEYgVGGQP-SINGDVYSFGILLLEMFTGKRP 920
Cdd:pfam00069  110 GLESGSSLTT-----FVGTPWYMAPEV-LGGNPyGPKVDVWSLGCILYELLTGKPP 159
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
707-996 1.95e-17

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: 83.13  E-value: 1.95e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLlTEKKVVAVKVLNMQRRGAMK-SFMAECESLKDIRHRNLVKLLTACSSidfqgnefRALIY---E 782
Cdd:cd05085    3 LLGKGNFGEVYKGTL-KDKTPVAVKTCKEDLPQELKiKFLSEARILKQYDHPNIVKLIGVCTQ--------RQPIYivmE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLDMWLHPEEVEeihrpsrtLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLAR 862
Cdd:cd05085   74 LVPGGDFLSFLRKKKDE--------LKTKQLVKFSLDAAAGMAYLE---SKNCIHRDLAARNCLVGENNALKISDFGMSR 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  863 lllKFDEESFfnqlSSAGVRGT-IGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRPTNELfggnftlnsyTKSALP 940
Cdd:cd05085  143 ---QEDDGVY----SSSGLKQIpIKWTAPEALNYGRYSSESDVWSFGILLWETFSlGVCPYPGM----------TNQQAR 205
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  941 ERIldivdesilHIGLRVGFPvVECLTMVFEVGLRCCEESPMNRLATSIVVKELIS 996
Cdd:cd05085  206 EQV---------EKGYRMSAP-QRCPEDIYKIMQRCWDYNPENRPKFSELQKELAA 251
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
707-916 1.97e-17

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


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 83.91  E-value: 1.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTV----YKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSidfQGNEFRALIYE 782
Cdd:cd14205   11 QLGKGNFGSVemcrYDPLQDNTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYS---AGRRNLRLIME 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLDMWL--HPEEVEEIhrpsrtltllERLNIAIDVASVLDYLHVHCHepiAHCDLKPSNVLLDDDLTAHVSDFGL 860
Cdd:cd14205   88 YLPYGSLRDYLqkHKERIDHI----------KLLQYTSQICKGMEYLGTKRY---IHRDLATRNILVENENRVKIGDFGL 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  861 ARLLLKfDEESFfnQLSSAGvRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT 916
Cdd:cd14205  155 TKVLPQ-DKEYY--KVKEPG-ESPIFWYAPESLTESKFSVASDVWSFGVVLYELFT 206
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
707-943 2.53e-17

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: 82.97  E-value: 2.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKAL------LLTEKKVV--AVKVLNMQRRGAMKSFMA-ECESLKDIRHRNLVKLLTACSSIDFQgNEFr 777
Cdd:cd06628    7 LIGSGSFGSVYLGMnassgeLMAVKQVElpSVSAENKDRKKSMLDALQrEIALLRELQHENIVQYLGSSSDANHL-NIF- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  778 aliYEFMPNGS----LDMWLHPEEveeihrpsrtlTLLErlNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTA 853
Cdd:cd06628   85 ---LEYVPGGSvatlLNNYGAFEE-----------SLVR--NFVRQILKGLNYLH---NRGIIHRDIKGANILVDNKGGI 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  854 HVSDFGLARlLLKFDEESFFNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTNEL--FGGNFTL 931
Cdd:cd06628  146 KISDFGISK-KLEANSLSTKNNGARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCtqMQAIFKI 224
                        250
                 ....*....|..
gi 18408454  932 NSYTKSALPERI 943
Cdd:cd06628  225 GENASPTIPSNI 236
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
707-997 4.37e-17

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: 82.58  E-value: 4.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKV---VAVKVLNMQ--RRGAMKSFMAECESLKDIRHRNLVKLLTAC-SSIDFQGNEFRALI 780
Cdd:cd05035    6 ILGEGEFGSVMEAQLKQDDGSqlkVAVKTMKVDihTYSEIEEFLSEAACMKDFDHPNVMRLIGVCfTASDLNKPPSPMVI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFMPNGSLDMWLHPEEVEE--IHRPSRTLtllerLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDF 858
Cdd:cd05035   86 LPFMKHGDLHSYLLYSRLGGlpEKLPLQTL-----LKFMVDIAKGMEYLS---NRNFIHRDLAARNCMLDENMTVCVADF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  859 GLARlllKFDEESFFNQLSSAgvRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRPTNELfgGNFTLNSYtks 937
Cdd:cd05035  158 GLSR---KIYSGDYYRQGRIS--KMPVKWIALESLADNVYTSKSDVWSFGVTMWEIATrGQTPYPGV--ENHEIYDY--- 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  938 alperildivdesiLHIGLRVGFPvVECLTMVFEVGLRCCEESPMNRLATSIVVKELISI 997
Cdd:cd05035  228 --------------LRNGNRLKQP-EDCLDEVYFLMYFCWTVDPKDRPTFTKLREVLENI 272
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
708-924 4.68e-17

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: 82.71  E-value: 4.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKA-----LLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSidfqgNEFRALIYE 782
Cdd:cd05092   13 LGEGAFGKVFLAechnlLPEQDKMLVAVKALKEATESARQDFQREAELLTVLQHQHIVRFYGVCTE-----GEPLIMVFE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLDMWL--HPEEVEEIH----RPSRTLTLLERLNIAIDVASVLDYL-HVHchepIAHCDLKPSNVLLDDDLTAHV 855
Cdd:cd05092   88 YMRHGDLNRFLrsHGPDAKILDggegQAPGQLTLGQMLQIASQIASGMVYLaSLH----FVHRDLATRNCLVGQGLVVKI 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  856 SDFGLARLLLKFDeesffnqLSSAGVRGT--IGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRPTNEL 924
Cdd:cd05092  164 GDFGMSRDIYSTD-------YYRVGGRTMlpIRWMPPESILYRKFTTESDIWSFGVVLWEIFTyGKQPWYQL 228
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
708-919 5.94e-17

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: 82.43  E-value: 5.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVvAVKVLnmqRRGAM--KSFMAECESLKDIRHRNLVKLLTACSSidfqgnEFRALIYEFMP 785
Cdd:cd05069   20 LGQGCFGEVWMGTWNGTTKV-AIKTL---KPGTMmpEAFLQEAQIMKKLRHDKLVPLYAVVSE------EPIYIVTEFMG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLDMWLHPEEveeihrpSRTLTLLERLNIAIDVASVLDYLHVHCHepiAHCDLKPSNVLLDDDLTAHVSDFGLARLLL 865
Cdd:cd05069   90 KGSLLDFLKEGD-------GKYLKLPQLVDMAAQIADGMAYIERMNY---IHRDLRAANILVGDNLVCKIADFGLARLIE 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18408454  866 kfDEESFFNQlssaGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKR 919
Cdd:cd05069  160 --DNEYTARQ----GAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGR 207
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
700-924 6.02e-17

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: 81.94  E-value: 6.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  700 NGFSSSNMVGSGSFGTVYKALLLTEKK---VVAVKVLN-----MQRrgamKSFMAECESLKDIRHRNLVKLLTACSSIdf 771
Cdd:cd05063    5 SHITKQKVIGAGEFGEVFRGILKMPGRkevAVAIKTLKpgyteKQR----QDFLSEASIMGQFSHHNIIRLEGVVTKF-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  772 qgnEFRALIYEFMPNGSLDMWLHPEEVEeiHRPSRTLTLLERLNIAIDVASVLDYLHVhchepiahcDLKPSNVLLDDDL 851
Cdd:cd05063   79 ---KPAMIITEYMENGALDKYLRDHDGE--FSSYQLVGMLRGIAAGMKYLSDMNYVHR---------DLAARNILVNSNL 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18408454  852 TAHVSDFGLARLLLKFDEESFfnqlSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRPTNEL 924
Cdd:cd05063  145 ECKVSDFGLSRVLEDDPEGTY----TTSGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSfGERPYWDM 214
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
709-924 6.71e-17

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: 82.10  E-value: 6.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACssidFQGNEFRALIyEFMPNGS 788
Cdd:cd06611   14 GDGAFGKVYKAQHKETGLFAAAKIIQIESEEELEDFMVEIDILSECKHPNIVGLYEAY----FYENKLWILI-EFCDGGA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  789 LDmwlhpEEVEEIHRPsrtLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLARLLLKFD 868
Cdd:cd06611   89 LD-----SIMLELERG---LTEPQIRYVCRQMLEALNFLHSH---KVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTL 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  869 E--ESFFnqlssagvrGTIGYAAPEYGVGGQPSIN-----GDVYSFGILLLEMFTGKRPTNEL 924
Cdd:cd06611  158 QkrDTFI---------GTPYWMAPEVVACETFKDNpydykADIWSLGITLIELAQMEPPHHEL 211
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
708-994 7.45e-17

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: 81.38  E-value: 7.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLnmQRRGAMKSFMAECESLKDIRHRNLVKLLTACssidFQGNEFrALIYEFMPNG 787
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVMVMKEL--KRFDEQRSFLKEVKLMRRLSHPNILRFIGVC----VKDNKL-NFITEYVNGG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 SLDmwlhpeevEEIHRPSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLL---DDDLTAHVSDFGLARLL 864
Cdd:cd14065   74 TLE--------ELLKSMDEQLPWSQRVSLAKDIASGMAYLH---SKNIIHRDLNSKNCLVreaNRGRNAVVADFGLAREM 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  865 --LKFDEESFFNQLSsagVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFtGKRPtnelfggnftlnsytksALPER 942
Cdd:cd14065  143 pdEKTKKPDRKKRLT---VVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEII-GRVP-----------------ADPDY 201
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  943 ILDIVDesilhIGLRV-GF---PVVECLTMVFEVGLRCCEESPMNRLATSIVVKEL 994
Cdd:cd14065  202 LPRTMD-----FGLDVrAFrtlYVPDCPPSFLPLAIRCCQLDPEKRPSFVELEHHL 252
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
705-924 8.39e-17

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: 82.00  E-value: 8.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  705 SNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRgAMKSFMAECESLKDIRHRNLVKLLtacssiDFQGNEFRALIYEFM 784
Cdd:cd14149   17 STRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPE-QFQAFRNEVAVLRKTRHVNILLFM------GYMTKDNLAIVTQWC 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLDMWLHPEEVEeihrpsrtLTLLERLNIAIDVASVLDYLHVhchEPIAHCDLKPSNVLLDDDLTAHVSDFGLARLL 864
Cdd:cd14149   90 EGSSLYKHLHVQETK--------FQMFQLIDIARQTAQGMDYLHA---KNIIHRDMKSNNIFLHEGLTVKIGDFGLATVK 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  865 LKFDEESFFNQLSsagvrGTIGYAAPEY--GVGGQP-SINGDVYSFGILLLEMFTGKRPTNEL 924
Cdd:cd14149  159 SRWSGSQQVEQPT-----GSILWMAPEVirMQDNNPfSFQSDVYSYGIVLYELMTGELPYSHI 216
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
708-918 1.02e-16

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


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 81.76  E-value: 1.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKV--LNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSidfqgNEFRALIYEFMp 785
Cdd:cd07829    7 LGEGTYGVVYKAKDKKTGEIVALKKirLDNEEEGIPSTALREISLLKELKHPNIVKLLDVIHT-----ENKLYLVFEYC- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 ngslDMWLHpeevEEIHRPSRTLTLLERLNIAIDVASVLDYLHVHChepIAHCDLKPSNVLLDDDLTAHVSDFGLARL-- 863
Cdd:cd07829   81 ----DQDLK----KYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHR---ILHRDLKPQNLLINRDGVLKLADFGLARAfg 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18408454  864 --LLKFDEESFfnqlssagvrgTIGYAAPE-------YGvggqPSIngDVYSFGILLLEMFTGK 918
Cdd:cd07829  150 ipLRTYTHEVV-----------TLWYRAPEillgskhYS----TAV--DIWSVGCIFAELITGK 196
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
724-920 1.02e-16

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: 81.28  E-value: 1.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  724 EKKVVAVKVLNMQRRgAMKSFMAECESLKDIRHRNLVKLLTACssidFQGNEFrALIYEFMPNGSLDMWLHPEEVEeihr 803
Cdd:cd13992   24 GGRTVAIKHITFSRT-EKRTILQELNQLKELVHDNLNKFIGIC----INPPNI-AVVTEYCTRGSLQDVLLNREIK---- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  804 psrtLTLLERLNIAIDVASVLDYLHVHchePI-AHCDLKPSNVLLDDDLTAHVSDFGLARLLlkfdEESFFNQLSSAGVR 882
Cdd:cd13992   94 ----MDWMFKSSFIKDIVKGMNYLHSS---SIgYHGRLKSSNCLVDSRWVVKLTDFGLRNLL----EEQTNHQLDEDAQH 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 18408454  883 GTIGYAAPE----YGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd13992  163 KKLLWTAPEllrgSLLEVRGTQKGDVYSFAIILYEILFRSDP 204
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
708-928 1.19e-16

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


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 81.55  E-value: 1.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQ--RRGAMKSFMAECESLKDIR---HRNLVKLLTACSSIDFQGNEFRALIYE 782
Cdd:cd07863    8 IGVGAYGTVYKARDPHSGHFVALKSVRVQtnEDGLPLSTVREVALLKRLEafdHPNIVRLMDVCATSRTDRETKVTLVFE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNgslDMWLHPEEVEEIHRPSRTLTLLERlniaiDVASVLDYLHVHChepIAHCDLKPSNVLLDDDLTAHVSDFGLAR 862
Cdd:cd07863   88 HVDQ---DLRTYLDKVPPPGLPAETIKDLMR-----QFLRGLDFLHANC---IVHRDLKPENILVTSGGQVKLADFGLAR 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  863 LllkfdeesFFNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTgKRPtneLFGGN 928
Cdd:cd07863  157 I--------YSCQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFR-RKP---LFCGN 210
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
708-999 1.45e-16

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: 81.21  E-value: 1.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQ----RRGAMKSFMAECESLKDIRHRNLVKLLTAC-SSIDFQGNEFRALIYE 782
Cdd:cd05075    8 LGEGEFGSVMEGQLNQDDSVLKVAVKTMKiaicTRSEMEDFLSEAVCMKEFDHPNVMRLIGVClQNTESEGYPSPVVILP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLDMWLHPEEVEE--IHRPSRTLtllerLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGL 860
Cdd:cd05075   88 FMKHGDLHSFLLYSRLGDcpVYLPTQML-----VKFMTDIASGMEYLS---SKNFIHRDLAARNCMLNENMNVCVADFGL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  861 ARLLLKFDeesFFNQLSSAgvRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRPtnelFGGnfTLNSytksal 939
Cdd:cd05075  160 SKKIYNGD---YYRQGRIS--KMPVKWIAIESLADRVYTTKSDVWSFGVTMWEIATrGQTP----YPG--VENS------ 222
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  940 perilDIVDesILHIGLRVGFPvVECLTMVFEVGLRCCEESPMNRLATSIVVKELISIRE 999
Cdd:cd05075  223 -----EIYD--YLRQGNRLKQP-PDCLDGLYELMSSCWLLNPKDRPSFETLRCELEKILK 274
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
708-920 1.57e-16

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: 80.41  E-value: 1.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVykalLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACssIDFQGNEFraLIYEFMPNG 787
Cdd:cd05082   14 IGKGEFGDV----MLGDYRGNKVAVKCIKNDATAQAFLAEASVMTQLRHSNLVQLLGVI--VEEKGGLY--IVTEYMAKG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 SLdmwlhpeeVEEIHRPSRTLTLLERL-NIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLARlllk 866
Cdd:cd05082   86 SL--------VDYLRSRGRSVLGGDCLlKFSLDVCEAMEYLEGN---NFVHRDLAARNVLVSEDNVAKVSDFGLTK---- 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  867 fdEESFFNQLSSAGVRGTigyaAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRP 920
Cdd:cd05082  151 --EASSTQDTGKLPVKWT----APEALREKKFSTKSDVWSFGILLWEIYSfGRVP 199
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
708-999 1.67e-16

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: 80.68  E-value: 1.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVvAVKVLnmqRRGAM--KSFMAECESLKDIRHRNLVKLLTACSSidfqgnefRALIY---E 782
Cdd:cd05114   12 LGSGLFGVVRLGKWRAQYKV-AIKAI---REGAMseEDFIEEAKVMMKLTHPKLVQLYGVCTQ--------QKPIYivtE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLDMWLHpeevEEIHRPSRTLTLlerlNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLAR 862
Cdd:cd05114   80 FMENGCLLNYLR----QRRGKLSRDMLL----SMCQDVCEGMEYLE---RNNFIHRDLAARNCLVNDTGVVKVSDFGMTR 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  863 LLLkfDEEsffnQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRPtnelfggnftLNSYTKsalpe 941
Cdd:cd05114  149 YVL--DDQ----YTSSSGAKFPVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTeGKMP----------FESKSN----- 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  942 riLDIVDEsiLHIGLRVGFPVVECLTmVFEVGLRCCEESPMNRLATSIVVKELISIRE 999
Cdd:cd05114  208 --YEVVEM--VSRGHRLYRPKLASKS-VYEVMYSCWHEKPEGRPTFADLLRTITEIAE 260
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
706-920 2.23e-16

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: 80.28  E-value: 2.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTVYKALLLTEKKVVAVKVLNMqrrGAMKS-----FMAECESLKDIRHRNLVKLltacssIDFQGNEFRALI 780
Cdd:cd08217    6 ETIGKGSFGTVRKVRRKSDGKILVWKEIDY---GKMSEkekqqLVSEVNILRELKHPNIVRY------YDRIVDRANTTL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 Y---EFMPNGSLDMWlhpeeveeIHRPSRTLTLLER---LNIAIDVASVLDYLH--VHCHEPIAHCDLKPSNVLLDDDLT 852
Cdd:cd08217   77 YivmEYCEGGDLAQL--------IKKCKKENQYIPEefiWKIFTQLLLALYECHnrSVGGGKILHRDLKPANIFLDSDNN 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  853 AHVSDFGLARLLlkfDEESFFnqlSSAGVrGTIGYAAPEYgVGGQP-SINGDVYSFGILLLEMFTGKRP 920
Cdd:cd08217  149 VKLGDFGLARVL---SHDSSF---AKTYV-GTPYYMSPEL-LNEQSyDEKSDIWSLGCLIYELCALHPP 209
PLN03150 PLN03150
hypothetical protein; Provisional
486-672 2.31e-16

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 83.71  E-value: 2.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   486 LDMSGNSLIGSLPQDIGALQNLGTLSLGDNKLSGKLPQTLGNCLTMESLflegnlfygdipdlkglvgvkevDLSNNDLS 565
Cdd:PLN03150  423 LGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVL-----------------------DLSYNSFN 479
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   566 GSIPEYFASFSKLEYLNLSFNNLEGKVP--VKGIFENATTVSIVGNNDLCgGIMGfqLKPCLSQAPSVVKkhssrlkkvv 643
Cdd:PLN03150  480 GSIPESLGQLTSLRILNLNGNSLSGRVPaaLGGRLLHRASFNFTDNAGLC-GIPG--LRACGPHLSVGAK---------- 546
                         170       180
                  ....*....|....*....|....*....
gi 18408454   644 IGVSVGITLLLLLFMASVTLIWlrKRKKN 672
Cdd:PLN03150  547 IGIAFGVSVAFLFLVICAMCWW--KRRQN 573
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
706-941 2.33e-16

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: 80.14  E-value: 2.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTVYKALLLTEKKVVAVKVLNM-----QRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidfQGNEFRALI 780
Cdd:cd06632    6 QLLGSGSFGSVYEGFNGDTGDFFAVKEVSLvdddkKSRESVKQLEQEIALLSKLRHPNIVQYYGT------EREEDNLYI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 Y-EFMPNGSLDMWLH-----PEEVEEIHrpsrTLTLLerlniaidvaSVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAH 854
Cdd:cd06632   80 FlEYVPGGSIHKLLQrygafEEPVIRLY----TRQIL----------SGLAYLH---SRNTVHRDIKGANILVDTNGVVK 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  855 VSDFGLARLLLKFDEESFFnqlssagvRGTIGYAAPEYGVGGQPSIN--GDVYSFGILLLEMFTGKRPTNELFGGNFTLN 932
Cdd:cd06632  143 LADFGMAKHVEAFSFAKSF--------KGSPYWMAPEVIMQKNSGYGlaVDIWSLGCTVLEMATGKPPWSQYEGVAAIFK 214

                 ....*....
gi 18408454  933 SYTKSALPE 941
Cdd:cd06632  215 IGNSGELPP 223
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
708-914 2.94e-16

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: 80.39  E-value: 2.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKkvVAVKVLNMQRrgaMKSFMAECE--SLKDIRHRNLVKLLtACSSIDFQGNEFRALIYEFMP 785
Cdd:cd14056    3 IGKGRYGEVWLGKYRGEK--VAVKIFSSRD---EDSWFRETEiyQTVMLRHENILGFI-AADIKSTGSWTQLWLITEYHE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLDMWLHpeeveeihrpSRTLTLLERLNIAIDVASVLDYLHVHCH-----EPIAHCDLKPSNVLLDDDLTAHVSDFGL 860
Cdd:cd14056   77 HGSLYDYLQ----------RNTLDTEEALRLAYSAASGLAHLHTEIVgtqgkPAIAHRDLKSKNILVKRDGTCCIADLGL 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  861 ArllLKFDEESFFNQLSSAGVRGTIGYAAPEYGVGgqpSING---------DVYSFGILLLEM 914
Cdd:cd14056  147 A---VRYDSDTNTIDIPPNPRVGTKRYMAPEVLDD---SINPksfesfkmaDIYSFGLVLWEI 203
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
708-920 3.40e-16

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: 79.70  E-value: 3.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAM-KSFMAECESLKDIRHRNLVKLLTACssidFQGNEFrALIYEFMPN 786
Cdd:cd06605    9 LGEGNGGVVSKVRHRPSGQIMAVKVIRLEIDEALqKQILRELDVLHKCNSPYIVGFYGAF----YSEGDI-SICMEYMDG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  787 GSLDMWLhpEEVEEIhrPSRTLTllerlNIAIDVASVLDYLHVHCHepIAHCDLKPSNVLLDDDLTAHVSDFGLARLLLk 866
Cdd:cd06605   84 GSLDKIL--KEVGRI--PERILG-----KIAVAVVKGLIYLHEKHK--IIHRDVKPSNILVNSRGQVKLCDFGVSGQLV- 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18408454  867 fdeesffNQLSSAGVrGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd06605  152 -------DSLAKTFV-GTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFP 197
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
708-984 4.74e-16

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: 79.30  E-value: 4.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVvAVKVLnmqRRGAM--KSFMAECESLKDIRHRNLVKLLTACSsidfqgNEFRALIYEFMP 785
Cdd:cd05073   19 LGAGQFGEVWMATYNKHTKV-AVKTM---KPGSMsvEAFLAEANVMKTLQHDKLVKLHAVVT------KEPIYIITEFMA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLDMWLHPEEVEEIHRPsrtltllERLNIAIDVASVLDYLHVHCHepiAHCDLKPSNVLLDDDLTAHVSDFGLARLLl 865
Cdd:cd05073   89 KGSLLDFLKSDEGSKQPLP-------KLIDFSAQIAEGMAFIEQRNY---IHRDLRAANILVSASLVCKIADFGLARVI- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  866 kfdEESFFnqLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRPtnelfggnftlnsYTKSALPERIl 944
Cdd:cd05073  158 ---EDNEY--TAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGRIP-------------YPGMSNPEVI- 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 18408454  945 divdeSILHIGLRVgfPVVE-CLTMVFEVGLRCCEESPMNR 984
Cdd:cd05073  219 -----RALERGYRM--PRPEnCPEELYNIMMRCWKNRPEER 252
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
708-995 5.06e-16

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


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 78.82  E-value: 5.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKS-FMAECESLKDIRHRNLVKLLTACSSidfqgNEFRALIYEFMPN 786
Cdd:cd05084    4 IGRGNFGEVFSGRLRADNTPVAVKSCRETLPPDLKAkFLQEARILKQYSHPNIVRLIGVCTQ-----KQPIYIVMELVQG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  787 GSLDMWLHPEeveeihrpSRTLTLLERLNIAIDVASVLDYLHV-HChepiAHCDLKPSNVLLDDDLTAHVSDFGLARlll 865
Cdd:cd05084   79 GDFLTFLRTE--------GPRLKVKELIRMVENAAAGMEYLESkHC----IHRDLAARNCLVTEKNVLKISDFGMSR--- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  866 kfdEESFFNQLSSAGVRGT-IGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRPTNELfggnftLNSYTKSALPEri 943
Cdd:cd05084  144 ---EEEDGVYAATGGMKQIpVKWTAPEALNYGRYSSESDVWSFGILLWETFSlGAVPYANL------SNQQTREAVEQ-- 212
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18408454  944 ldivdesilhiGLRVGFPvVECLTMVFEVGLRCCEESPMNRLATSIVVKELI 995
Cdd:cd05084  213 -----------GVRLPCP-ENCPDEVYRLMEQCWEYDPRKRPSFSTVHQDLQ 252
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
706-999 5.39e-16

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: 79.31  E-value: 5.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTVYKALLLTE--KKVVAVKVLN-MQRRGAMKSFMAECESLKDI-RHRNLVKLLTACssidfqgnEFRALIY 781
Cdd:cd05047    1 DVIGEGNFGQVLKARIKKDglRMDAAIKRMKeYASKDDHRDFAGELEVLCKLgHHPNIINLLGAC--------EHRGYLY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 ---EFMPNGSLDMWLHPEEVEEI-------HRPSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDL 851
Cdd:cd05047   73 laiEYAPHGNLLDFLRKSRVLETdpafaiaNSTASTLSSQQLLHFAADVARGMDYLS---QKQFIHRDLAARNILVGENY 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  852 TAHVSDFGLARlllkfDEESFFNQLSSagvRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRPtnelFGGNFT 930
Cdd:cd05047  150 VAKIADFGLSR-----GQEVYVKKTMG---RLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTP----YCGMTC 217
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  931 LNSYTKsaLPErildivdesilhiGLRVGFPvVECLTMVFEVGLRCCEESPMNRLATSIVVKELISIRE 999
Cdd:cd05047  218 AELYEK--LPQ-------------GYRLEKP-LNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLE 270
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
708-920 5.98e-16

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: 78.93  E-value: 5.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVL-------NMQRRGAMKSFMAECESLKDI-RHRNLVKLLTAcssidFQGNEFRAL 779
Cdd:cd13993    8 IGEGAYGVVYLAVDLRTGRKYAIKCLyksgpnsKDGNDFQKLPQLREIDLHRRVsRHPNIITLHDV-----FETEVAIYI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  780 IYEFMPNGSLDMWLHpeevEEIHRPSRTLTLLerlNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLD-DDLTAHVSDF 858
Cdd:cd13993   83 VLEYCPNGDLFEAIT----ENRIYVGKTELIK---NVFLQLIDAVKHCHSL---GIYHRDIKPENILLSqDEGTVKLCDF 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  859 GLARlllkfDEEsffnqLSSAGVRGTIGYAAPE----YGVGGQ--PSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd13993  153 GLAT-----TEK-----ISMDFGVGSEFYMAPEcfdeVGRSLKgyPCAAGDIWSLGIILLNLTFGRNP 210
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
708-920 9.93e-16

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


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 78.22  E-value: 9.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLN---MQRRGAMKSFMAECESLKDIRHRNLVKL---LTACSSIDF-----QGNEf 776
Cdd:cd14663    8 LGEGTFAKVKFARNTKTGESVAIKIIDkeqVAREGMVEQIKREIAIMKLLRHPNIVELhevMATKTKIFFvmelvTGGE- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  777 raLIYEFMPNGSLDmwlhpeevEEIHRpsrtlTLLERLniaidvASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVS 856
Cdd:cd14663   87 --LFSKIAKNGRLK--------EDKAR-----KYFQQL------IDAVDYCHSR---GVFHRDLKPENLLLDEDGNLKIS 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  857 DFGLARLLLKFDEESFFNQlssagVRGTIGYAAPEY----GVGGQPSingDVYSFGILLLEMFTGKRP 920
Cdd:cd14663  143 DFGLSALSEQFRQDGLLHT-----TCGTPNYVAPEVlarrGYDGAKA---DIWSCGVILFVLLAGYLP 202
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
710-920 1.23e-15

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: 78.31  E-value: 1.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  710 SGSFGTVYKALLLTEKKVVAVKVLN-MQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssIDFQGNefRALIYEFMPNGS 788
Cdd:cd14027    3 SGGFGKVSLCFHRTQGLVVLKTVYTgPNCIEHNEALLEEGKMMNRLRHSRVVKLLGV---ILEEGK--YSLVMEYMEKGN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  789 LdmwlhpeeveeihrpsrtLTLLERLNIAIDVAS--VLD------YLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGL 860
Cdd:cd14027   78 L------------------MHVLKKVSVPLSVKGriILEiiegmaYLH---GKGVIHKDLKPENILVDNDFHIKIADLGL 136
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  861 A--RLLLKFDEESFFNQL----SSAGVRGTIGYAAPEY--GVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14027  137 AsfKMWSKLTKEEHNEQRevdgTAKKNAGTLYYMAPEHlnDVNAKPTEKSDVYSFAIVLWAIFANKEP 204
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
701-920 1.37e-15

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: 77.72  E-value: 1.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  701 GFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVlnMQRRGAMKSFMA-----ECESLKDIRHRNLVKLLTACSSidfqgnE 775
Cdd:cd14162    1 GYIVGKTLGHGSYAVVKKAYSTKHKCKVAIKI--VSKKKAPEDYLQkflprEIEVIKGLKHPNLICFYEAIET------T 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  776 FRA-LIYEFMPNGSLDMWLH-----PEEveeihrpsRTLTLLERLNIAIDvasvldYLHvhcHEPIAHCDLKPSNVLLDD 849
Cdd:cd14162   73 SRVyIIMELAENGDLLDYIRkngalPEP--------QARRWFRQLVAGVE------YCH---SKGVVHRDLKCENLLLDK 135
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  850 DLTAHVSDFGLARLLLKFDEESFfnQLSSAGVrGTIGYAAPEY--GVGGQPSInGDVYSFGILLLEMFTGKRP 920
Cdd:cd14162  136 NNNLKITDFGFARGVMKTKDGKP--KLSETYC-GSYAYASPEIlrGIPYDPFL-SDIWSMGVVLYTMVYGRLP 204
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
700-999 1.60e-15

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: 78.05  E-value: 1.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  700 NGFSSSNMVGSGSFGTVYKALLLTEKKV---VAVKVLNM----QRRgaMKSFMAECESLKDIRHRNLVKLLTACSSIDFQ 772
Cdd:cd14204    7 NLLSLGKVLGEGEFGSVMEGELQQPDGTnhkVAVKTMKLdnfsQRE--IEEFLSEAACMKDFNHPNVIRLLGVCLEVGSQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  773 GNEFRALIYEFMPNGSLDMWLHPEEVEE--IHRPSRTLtllerLNIAIDVASVLDYLhvhCHEPIAHCDLKPSNVLLDDD 850
Cdd:cd14204   85 RIPKPMVILPFMKYGDLHSFLLRSRLGSgpQHVPLQTL-----LKFMIDIALGMEYL---SSRNFLHRDLAARNCMLRDD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  851 LTAHVSDFGLARLLLKFDeesFFNQLSSAgvRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRPtnelFGG-- 927
Cdd:cd14204  157 MTVCVADFGLSKKIYSGD---YYRQGRIA--KMPVKWIAVESLADRVYTVKSDVWAFGVTMWEIATrGMTP----YPGvq 227
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  928 NFTLNSYtksalperildivdesILHiGLRVGFPvVECLTMVFEVGLRCCEESPMNRLATSIVVKELISIRE 999
Cdd:cd14204  228 NHEIYDY----------------LLH-GHRLKQP-EDCLDELYDIMYSCWRSDPTDRPTFTQLRENLEKLLE 281
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
708-994 1.73e-15

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: 78.08  E-value: 1.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEK-----KVVAVKVLnmqRRGA----MKSFMAECESLKDIRHRNLVKLLTACSSidfqgNEFRA 778
Cdd:cd05045    8 LGEGEFGKVVKATAFRLKgragyTTVAVKML---KENAssseLRDLLSEFNLLKQVNHPHVIKLYGACSQ-----DGPLL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGSLDMWL---------------HPEEVEEIHRPSRTLTLLERLNIAIDVASVLDYLhvhCHEPIAHCDLKPS 843
Cdd:cd05045   80 LIVEYAKYGSLRSFLresrkvgpsylgsdgNRNSSYLDNPDERALTMGDLISFAWQISRGMQYL---AEMKLVHRDLAAR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  844 NVLLDDDLTAHVSDFGLARLLlkFDEESFFNQlsSAGvRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTgkrptne 923
Cdd:cd05045  157 NVLVAEGRKMKISDFGLSRDV--YEEDSYVKR--SKG-RIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVT------- 224
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18408454  924 lFGGnftlNSYTKSAlPERILdivdeSILHIGLRVGFPvVECLTMVFEVGLRCCEESPMNRLATSIVVKEL 994
Cdd:cd05045  225 -LGG----NPYPGIA-PERLF-----NLLKTGYRMERP-ENCSEEMYNLMLTCWKQEPDKRPTFADISKEL 283
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
708-920 1.87e-15

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


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 78.60  E-value: 1.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVY---KALLLTEKKVVAVKVL---NMQRRGAMKSFMaECESLKDIRHRNLVKLLTAcssidFQGNEFRALIY 781
Cdd:cd05582    3 LGQGSFGKVFlvrKITGPDAGTLYAMKVLkkaTLKVRDRVRTKM-ERDILADVNHPFIVKLHYA-----FQTEGKLYLIL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 EFMPNGSLdmwlhpeeveeIHRPSRTLTLLE---RLNIAiDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDF 858
Cdd:cd05582   77 DFLRGGDL-----------FTRLSKEVMFTEedvKFYLA-ELALALDHLHSL---GIIYRDLKPENILLDEDGHIKLTDF 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  859 GLARlllkfdeESFFNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd05582  142 GLSK-------ESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLP 196
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
710-923 1.94e-15

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: 77.64  E-value: 1.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  710 SGSFGTVYKALLLTEKKVVAVKVLN---MQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFMPN 786
Cdd:cd05579    3 RGAYGRVYLAKKKSTGDLYAIKVIKkrdMIRKNQVDSVLAERNILSQAQNPFVVKLYYS-----FQGKKNLYLVMEYLPG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  787 GSLDMWLH-----PEEVEeihrpsrtltlleRLNIAIDVASvLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLA 861
Cdd:cd05579   78 GDLYSLLEnvgalDEDVA-------------RIYIAEIVLA-LEYLHSH---GIIHRDLKPDNILIDANGHLKLTDFGLS 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  862 RLLL-----KFDEESFFNQLSSAGVRGTIG---YAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTNE 923
Cdd:cd05579  141 KVGLvrrqiKLSIQKKSNGAPEKEDRRIVGtpdYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHA 210
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
706-997 1.99e-15

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: 77.51  E-value: 1.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTVYKALLLTE---KKVVAVKVLN-MQRRGAMKSFMAECESLKDIRHRNLVKLLTACssIDFQGNEFRALIY 781
Cdd:cd05058    1 EVIGKGHFGCVYHGTLIDSdgqKIHCAVKSLNrITDIEEVEQFLKEGIIMKDFSHPNVLSLLGIC--LPSEGSPLVVLPY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 efMPNGSLDMWlhpeeveeIHRPSRTLTLLERLNIAIDVASVLDYLhvhCHEPIAHCDLKPSNVLLDDDLTAHVSDFGLA 861
Cdd:cd05058   79 --MKHGDLRNF--------IRSETHNPTVKDLIGFGLQVAKGMEYL---ASKKFVHRDLAARNCMLDESFTVKVADFGLA 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  862 RLLlkFDEEsFFNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFtgkrptnelfggnftlnsyTKSALPE 941
Cdd:cd05058  146 RDI--YDKE-YYSVHNHTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELM-------------------TRGAPPY 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  942 RILDIVDESI-LHIGLRVGFPVVeCLTMVFEVGLRCCEESPMNRLATSIVVKELISI 997
Cdd:cd05058  204 PDVDSFDITVyLLQGRRLLQPEY-CPDPLYEVMLSCWHPKPEMRPTFSELVSRISQI 259
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
708-917 2.21e-15

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: 77.75  E-value: 2.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRR--GAMKSFMAECESLKDIR-HRNLVKLLTAcssidFQGNEFRALIYEFM 784
Cdd:cd07832    8 IGEGAHGIVFKAKDRETGETVALKKVALRKLegGIPNQALREIKALQACQgHPYVVKLRDV-----FPHGTGFVLVFEYM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGsldmwLHpEEVEEIHRPsrtltllerlniaIDVASVLDYLHV------HCHE-PIAHCDLKPSNVLLDDDLTAHVSD 857
Cdd:cd07832   83 LSS-----LS-EVLRDEERP-------------LTEAQVKRYMRMllkgvaYMHAnRIMHRDLKPANLLISSTGVLKIAD 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  858 FGLARLLLKFDEESFFNQLssagvrGTIGYAAPEYGVGGQ---PSIngDVYSFGILLLEMFTG 917
Cdd:cd07832  144 FGLARLFSEEDPRLYSHQV------ATRWYRAPELLYGSRkydEGV--DLWAVGCIFAELLNG 198
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
702-920 2.27e-15

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: 77.21  E-value: 2.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLN---MQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRA 778
Cdd:cd14186    3 FKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDkkaMQKAGMVQRVRNEVEIHCQLKHPSILELYNY-----FEDSNYVY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGSLDMWLhpeevEEIHRPsrtLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDF 858
Cdd:cd14186   78 LVLEMCHNGEMSRYL-----KNRKKP---FTEDEARHFMHQIVTGMLYLHSH---GILHRDLTLSNLLLTRNMNIKIADF 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  859 GLARLLLKFDEESFfnqlssaGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14186  147 GLATQLKMPHEKHF-------TMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPP 201
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
708-924 2.32e-15

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: 76.92  E-value: 2.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQrrGAMKSFMAECESLKDIRHRNLVKlltacssidFQGNEFRA----LIYEF 783
Cdd:cd06612   11 LGEGSYGSVYKAIHKETGQVVAIKVVPVE--EDLQEIIKEISILKQCDSPYIVK---------YYGSYFKNtdlwIVMEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  784 MPNGS-LDMwlhpeeveeIHRPSRTLTLLErlnIAIDVASV---LDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFG 859
Cdd:cd06612   80 CGAGSvSDI---------MKITNKTLTEEE---IAAILYQTlkgLEYLHSN---KKIHRDIKAGNILLNEEGQAKLADFG 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  860 LARLLlkfdEESFFNQLSsagVRGTIGYAAPEygVGGQPSIN--GDVYSFGILLLEMFTGKRPTNEL 924
Cdd:cd06612  145 VSGQL----TDTMAKRNT---VIGTPFWMAPE--VIQEIGYNnkADIWSLGITAIEMAEGKPPYSDI 202
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
702-920 2.57e-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: 2.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKS---FMAECESLKDIRHRNLVKLLtaCSSIDfqgNEFRA 778
Cdd:cd05612    3 FERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLKQeqhVHNEKRVLKEVSHPFIIRLF--WTEHD---QRFLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGSLDMWLhpeeveeihRPSRTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDF 858
Cdd:cd05612   78 MLMEYVPGGELFSYL---------RNSGRFSNSTGLFYASEIVCALEYLHSK---EIVYRDLKPENILLDKEGHIKLTDF 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  859 GLARLLLKfdeesffnqlSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd05612  146 GFAKKLRD----------RTWTLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPP 197
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
702-920 3.00e-15

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: 76.68  E-value: 3.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQR--RGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRAL 779
Cdd:cd08529    2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRmsRKMREEAIDEARVLSKLNSPYVIKYYDS-----FVDKGKLNI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  780 IYEFMPNGSLDMWLHPEEveeihrpSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFG 859
Cdd:cd08529   77 VMEYAENGDLHSLIKSQR-------GRPLPEDQIWKFFIQTLLGLSHLH---SKKILHRDIKSMNIFLDKGDNVKIGDLG 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18408454  860 LARLLlkfDEESFFNQLssagVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd08529  147 VAKIL---SDTTNFAQT----IVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHP 200
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
707-920 3.00e-15

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 80.22  E-value: 3.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   707 MVGSGSFGTVYKALLLTEKKVVAVKVL--------NMQRRgamksFMAECESLKDIRHRNLVklltacsSI-DfQGnEFR 777
Cdd:NF033483   14 RIGRGGMAEVYLAKDTRLDRDVAVKVLrpdlardpEFVAR-----FRREAQSAASLSHPNIV-------SVyD-VG-EDG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   778 ALIYEFMpngsldmwlhpEEVE-----EIHRPSRTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLT 852
Cdd:NF033483   80 GIPYIVM-----------EYVDgrtlkDYIREHGPLSPEEAVEIMIQILSALEHAHRN---GIVHRDIKPQNILITKDGR 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18408454   853 AHVSDFGLARLLlkfdeesffNQLS---SAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:NF033483  146 VKVTDFGIARAL---------SSTTmtqTNSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPP 207
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
707-976 4.24e-15

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: 77.41  E-value: 4.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTE----KKVVAVKVLNmQRRG--AMKSFMAECESLKDIRHRNLVKLLTACSSIDFQgnefraLI 780
Cdd:cd05110   14 VLGSGAFGTVYKGIWVPEgetvKIPVAIKILN-ETTGpkANVEFMDEALIMASMDHPHLVRLLGVCLSPTIQ------LV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFMPNGSLDMWLHPeeveeiHRPSRTLTLLerLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGL 860
Cdd:cd05110   87 TQLMPHGCLLDYVHE------HKDNIGSQLL--LNWCVQIAKGMMYLE---ERRLVHRDLAARNVLVKSPNHVKITDFGL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  861 ARlLLKFDEESFfnqlSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTgkrptnelFGGNftlnsyTKSALP 940
Cdd:cd05110  156 AR-LLEGDEKEY----NADGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMT--------FGGK------PYDGIP 216
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 18408454  941 ERilDIVDesILHIGLRVGFPVVeCLTMVFEVGLRC 976
Cdd:cd05110  217 TR--EIPD--LLEKGERLPQPPI-CTIDVYMVMVKC 247
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
708-920 4.28e-15

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: 76.85  E-value: 4.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKS---FMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFM 784
Cdd:cd05580    9 LGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKLKQvehVLNEKRILSEVRHPFIVNLLGS-----FQDDRNLYMVMEYV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLDMWLhpeeveeihRPSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARll 864
Cdd:cd05580   84 PGGELFSLL---------RRSGRFPNDVAKFYAAEVVLALEYLH---SLDIVYRDLKPENLLLDSDGHIKITDFGFAK-- 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  865 lKFDEESFfnqlssaGVRGTIGYAAPE--YGVG-GQPSingDVYSFGILLLEMFTGKRP 920
Cdd:cd05580  150 -RVKDRTY-------TLCGTPEYLAPEiiLSKGhGKAV---DWWALGILIYEMLAGYPP 197
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
726-950 7.53e-15

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: 76.05  E-value: 7.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  726 KVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSIdfqgnEFRALIYEFMPNGSLDMWLHPEEVeeihrps 805
Cdd:cd14045   31 RTVAIKKIAKKSFTLSKRIRKEVKQVRELDHPNLCKFIGGCIEV-----PNVAIITEYCPKGSLNDVLLNEDI------- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  806 rTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLArlllKFDEESFFNQLSSAGVRGTI 885
Cdd:cd14045   99 -PLNWGFRFSFATDIARGMAYLHQH---KIYHGRLKSSNCVIDDRWVCKIADYGLT----TYRKEDGSENASGYQQRLMQ 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  886 GYAAPEY--GVGGQPSINGDVYSFGILLLEMFTGKRPTNElfgGNFTLNSYTKSALPERILDIVDES 950
Cdd:cd14045  171 VYLPPENhsNTDTEPTQATDVYSYAIILLEIATRNDPVPE---DDYSLDEAWCPPLPELISGKTENS 234
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
708-932 7.62e-15

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: 76.83  E-value: 7.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKvlnmqrrgamKSFMA------------ECESLKDIR-HRNLVKLLtacssidfqgN 774
Cdd:cd07852   15 LGKGAYGIVWKAIDKKTGEVVALK----------KIFDAfrnatdaqrtfrEIMFLQELNdHPNIIKLL----------N 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  775 EFRA-------LIYEFMpngslDMWLHpeEV------EEIHRPSRTLTLLErlniaidvasVLDYLHvhcHEPIAHCDLK 841
Cdd:cd07852   75 VIRAendkdiyLVFEYM-----ETDLH--AViranilEDIHKQYIMYQLLK----------ALKYLH---SGGVIHRDLK 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  842 PSNVLLDDDLTAHVSDFGLARLLLKFDEESFFNQLSS--AgvrgTIGYAAPEYGVGGQPSING-DVYSFGILLLEMFTGK 918
Cdd:cd07852  135 PSNILLNSDCRVKLADFGLARSLSQLEEDDENPVLTDyvA----TRWYRAPEILLGSTRYTKGvDMWSVGCILGEMLLGK 210
                        250
                 ....*....|....
gi 18408454  919 rPtneLFGGNFTLN 932
Cdd:cd07852  211 -P---LFPGTSTLN 220
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
707-924 8.18e-15

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: 75.91  E-value: 8.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSsidfQGNEFRaLIYEFMPN 786
Cdd:cd06624   15 VLGKGTFGVVYAARDLSTQVRIAIKEIPERDSREVQPLHEEIALHSRLSHKNIVQYLGSVS----EDGFFK-IFMEQVPG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  787 GSL-----DMW--LHPEEVEEIHRpsrTLTLLERLNiaidvasvldYLHvhcHEPIAHCDLKPSNVLLDD-DLTAHVSDF 858
Cdd:cd06624   90 GSLsallrSKWgpLKDNENTIGYY---TKQILEGLK----------YLH---DNKIVHRDIKGDNVLVNTySGVVKISDF 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  859 GLARLL--LKFDEESFfnqlssagvRGTIGYAAPEYGVGGQ-----PSingDVYSFGILLLEMFTGKRPTNEL 924
Cdd:cd06624  154 GTSKRLagINPCTETF---------TGTLQYMAPEVIDKGQrgygpPA---DIWSLGCTIIEMATGKPPFIEL 214
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
708-923 8.48e-15

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: 75.42  E-value: 8.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLlTEKKV-VAVKVLNMQR--RGAMKSFMAECESLKDIRHRNLVKLLTACSSIdFQGNEFRALIYEFM 784
Cdd:cd14033    9 IGRGSFKTVYRGLD-TETTVeVAWCELQTRKlsKGERQRFSEEVEMLKGLQHPNIVRFYDSWKST-VRGHKCIILVTELM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLDMWLhpEEVEEIhrpsrTLTLLERLNIAIdvASVLDYLHVHChEPIAHCDLKPSNVLLDDDL-TAHVSDFGLARL 863
Cdd:cd14033   87 TSGTLKTYL--KRFREM-----KLKLLQRWSRQI--LKGLHFLHSRC-PPILHRDLKCDNIFITGPTgSVKIGDLGLATL 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18408454  864 llkfDEESFfnqlsSAGVRGTIGYAAPE-YGVGGQPSIngDVYSFGILLLEMFTGKRPTNE 923
Cdd:cd14033  157 ----KRASF-----AKSVIGTPEFMAPEmYEEKYDEAV--DVYAFGMCILEMATSEYPYSE 206
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
705-944 9.04e-15

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: 75.89  E-value: 9.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  705 SNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQ------RRGAMKSF--MAECESLKDIRHRNLVKLLTAcssidFQGNEF 776
Cdd:cd14084   11 SRTLGSGACGEVKLAYDKSTCKKVAIKIINKRkftigsRREINKPRniETEIEILKKLSHPCIIKIEDF-----FDAEDD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  777 RALIYEFMPNGSLdmwlhpeeveeIHRPSRTLTLLERLN--IAIDVASVLDYLHvhcHEPIAHCDLKPSNVLL---DDDL 851
Cdd:cd14084   86 YYIVLELMEGGEL-----------FDRVVSNKRLKEAICklYFYQMLLAVKYLH---SNGIIHRDLKPENVLLssqEEEC 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  852 TAHVSDFGLARLLlkfDEESFFNQLSsagvrGTIGYAAPEY-----GVGGQPSIngDVYSFGILLLEMFTGKRPTNElfg 926
Cdd:cd14084  152 LIKITDFGLSKIL---GETSLMKTLC-----GTPTYLAPEVlrsfgTEGYTRAV--DCWSLGVILFICLSGYPPFSE--- 218
                        250
                 ....*....|....*...
gi 18408454  927 gnftlnSYTKSALPERIL 944
Cdd:cd14084  219 ------EYTQMSLKEQIL 230
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
706-961 1.10e-14

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: 76.25  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTVYKALLLTEKKVVAVKVLNM-------QRRGAMKSFMAECESLKDIRHRNLVKLLTACSsidFQGNEFrA 778
Cdd:cd14041   12 HLLGRGGFSEVYKAFDLTEQRYVAVKIHQLnknwrdeKKENYHKHACREYRIHKELDHPRIVKLYDYFS---LDTDSF-C 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGSLDMWLhpeeveeihRPSRTLTLLERLNIAIDVASVLDYLHvHCHEPIAHCDLKPSNVLLDDDLTA---HV 855
Cdd:cd14041   88 TVLEYCEGNDLDFYL---------KQHKLMSEKEARSIIMQIVNALKYLN-EIKPPIIHYDLKPGNILLVNGTACgeiKI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  856 SDFGLARLLlkfDEESFFN----QLSSAGVrGTIGYAAPE-YGVGGQP---SINGDVYSFGILLLEMFTGKRPtnelFGG 927
Cdd:cd14041  158 TDFGLSKIM---DDDSYNSvdgmELTSQGA-GTYWYLPPEcFVVGKEPpkiSNKVDVWSVGVIFYQCLYGRKP----FGH 229
                        250       260       270
                 ....*....|....*....|....*....|....
gi 18408454  928 NftlnsytksalpERILDIVDESILHIGLRVGFP 961
Cdd:cd14041  230 N------------QSQQDILQENTILKATEVQFP 251
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
708-997 1.10e-14

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: 75.82  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLT-----EKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSIDFQgnefrALIYE 782
Cdd:cd05094   13 LGEGAFGKVFLAECYNlsptkDKMLVAVKTLKDPTLAARKDFQREAELLTNLQHDHIVKFYGVCGDGDPL-----IMVFE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLDMWLHPEEVEEI----HRPSRT---LTLLERLNIAIDVASVLDYLhvhCHEPIAHCDLKPSNVLLDDDLTAHV 855
Cdd:cd05094   88 YMKHGDLNKFLRAHGPDAMilvdGQPRQAkgeLGLSQMLHIATQIASGMVYL---ASQHFVHRDLATRNCLVGANLLVKI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  856 SDFGLARLLLKFDEESFfnqlsSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRPTNELfGGNFTLNSY 934
Cdd:cd05094  165 GDFGMSRDVYSTDYYRV-----GGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTyGKQPWFQL-SNTEVIECI 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  935 TKSALPERildivdesilhiglrvgfPVVeCLTMVFEVGLRCCEESPMNRLATSIVVKELISI 997
Cdd:cd05094  239 TQGRVLER------------------PRV-CPKEVYDIMLGCWQREPQQRLNIKEIYKILHAL 282
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
709-920 1.10e-14

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: 75.00  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAmKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFMPNGS 788
Cdd:cd14006    2 GRGRFGVVKRCIEKATGREFAAKFIPKRDKKK-EAVLREISILNQLQHPRIIQLHEA-----YESPTELVLILELCSGGE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  789 L-DMWLHPEEVEEihrpSRTLTLLERLNIAidvasvLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVS--DFGLARLLL 865
Cdd:cd14006   76 LlDRLAERGSLSE----EEVRTYMRQLLEG------LQYLHNH---HILHLDLKPENILLADRPSPQIKiiDFGLARKLN 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  866 KfdEESFFNQLssagvrGTIGYAAPEYgVGGQP-SINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14006  143 P--GEELKEIF------GTPEFVAPEI-VNGEPvSLATDMWSIGVLTYVLLSGLSP 189
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
709-920 1.13e-14

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: 75.07  E-value: 1.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVYKALLLTE--KKV-VAVKVL---NMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSIDFQgnefraLIYE 782
Cdd:cd05040    4 GDGSFGVVRRGEWTTPsgKVIqVAVKCLksdVLSQPNAMDDFLKEVNAMHSLDHPNLIRLYGVVLSSPLM------MVTE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLdmwlhpeeVEEIHRPSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLAR 862
Cdd:cd05040   78 LAPLGSL--------LDRLRKDQGHFLISTLCDYAVQIANGMAYLE---SKRFIHRDLAARNILLASKDKVKIGDFGLMR 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  863 LLLKFDEesffNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRP 920
Cdd:cd05040  147 ALPQNED----HYVMQEHRKVPFAWCAPESLKTRKFSHASDVWMFGVTLWEMFTyGEEP 201
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
709-948 1.16e-14

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: 75.00  E-value: 1.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMA---ECESLKDIRHRNLVKLLTAcssIDFQGNEFraLIYEFMP 785
Cdd:cd14079   11 GVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLDMEEKirrEIQILKLFRHPHIIRLYEV---IETPTDIF--MVMEYVS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLdmwlhpeeVEEIHRPSRtLTLLERLNIAIDVASVLDYLHVHChepIAHCDLKPSNVLLDDDLTAHVSDFGLARLLL 865
Cdd:cd14079   86 GGEL--------FDYIVQKGR-LSEDEARRFFQQIISGVEYCHRHM---VVHRDLKPENLLLDSNMNVKIADFGLSNIMR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  866 kfDEEsfFNQLSSagvrGTIGYAAPEYgVGGQ----PSIngDVYSFGILLLEMFTGKRPTNE-----LF----GGNFTLN 932
Cdd:cd14079  154 --DGE--FLKTSC----GSPNYAAPEV-ISGKlyagPEV--DVWSCGVILYALLCGSLPFDDehipnLFkkikSGIYTIP 222
                        250
                 ....*....|....*....
gi 18408454  933 SYTKSA---LPERILdIVD 948
Cdd:cd14079  223 SHLSPGardLIKRML-VVD 240
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
702-913 1.35e-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: 75.15  E-value: 1.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEK-KVVAVKVLNMQRRGA--MKSFMAECESLKDIR---HRNLVKLLtacSSIDFQGNE 775
Cdd:cd14052    2 FANVELIGSGEFSQVYKVSERVPTgKVYAVKKLKPNYAGAkdRLRRLEEVSILRELTldgHDNIVQLI---DSWEYHGHL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  776 FraLIYEFMPNGSLDMWLhpEEVEEIHR--PSRTLTLLerlniaIDVASVLDYLHvHCHepIAHCDLKPSNVLLDDDLTA 853
Cdd:cd14052   79 Y--IQTELCENGSLDVFL--SELGLLGRldEFRVWKIL------VELSLGLRFIH-DHH--FVHLDLKPANVLITFEGTL 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  854 HVSDFGLARLLLkfDEESFFNQlssagvrGTIGYAAPEYGVGGQPSINGDVYSFGILLLE 913
Cdd:cd14052  146 KIGDFGMATVWP--LIRGIERE-------GDREYIAPEILSEHMYDKPADIFSLGLILLE 196
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
709-920 1.70e-14

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: 74.60  E-value: 1.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVYKALLLTEKKVVAVKVLNmqRRGAMKSFMA-----ECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEF 783
Cdd:cd14081   10 GKGQTGLVKLAKHCVTGQKVAIKIVN--KEKLSKESVLmkverEIAIMKLIEHPNVLKLYDV-----YENKKYLYLVLEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  784 MPNGSLDMWLhpeeveeihRPSRTLTLLERLNIAIDVASVLDYLHVHChepIAHCDLKPSNVLLDDDLTAHVSDFGLARL 863
Cdd:cd14081   83 VSGGELFDYL---------VKKGRLTEKEARKFFRQIISALDYCHSHS---ICHRDLKPENLLLDEKNNIKIADFGMASL 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18408454  864 llkfdeesffnQLSSAGVRGTIG---YAAPEYGVG----GQPSingDVYSFGILLLEMFTGKRP 920
Cdd:cd14081  151 -----------QPEGSLLETSCGsphYACPEVIKGekydGRKA---DIWSCGVILYALLVGALP 200
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
701-924 2.13e-14

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: 74.80  E-value: 2.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  701 GFSSSNMVGSGSFGTVYKALLLTEK---KVVAVK-VLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSsidfQGNEF 776
Cdd:cd05043    7 RVTLSDLLQEGTFGRIFHGILRDEKgkeEEVLVKtVKDHASEIQVTMLLQESSLLYGLSHQNLLPILHVCI----EDGEK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  777 RALIYEFMPNGSLDMWLH-PEEVEEihRPSRTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHV 855
Cdd:cd05043   83 PMVLYPYMNWGNLKLFLQqCRLSEA--NNPQALSTQQLVHMALQIACGMSYLHRR---GVIHKDIAARNCVIDDELQVKI 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  856 SDFGLARLLLKFDeesfFNQLSSAGVRgTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRPTNEL 924
Cdd:cd05043  158 TDNALSRDLFPMD----YHCLGDNENR-PIKWMSLESLVNKEYSSASDVWSFGVLLWELMTlGQTPYVEI 222
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
702-920 2.27e-14

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: 74.28  E-value: 2.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKV-VAVKVLNMQRRGAMKSFMA-ECESLKDIRHRNLVKLLtacssiDFQgnEFRAL 779
Cdd:cd14202    4 FSRKDLIGHGAFAVVFKGRHKEKHDLeVAVKCINKKNLAKSQTLLGkEIKILKELKHENIVALY------DFQ--EIANS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  780 IY---EFMPNGSLDMWLHPEeveeihrpsRTLT------LLERLniaidvASVLDYLHvhcHEPIAHCDLKPSNVLLD-- 848
Cdd:cd14202   76 VYlvmEYCNGGDLADYLHTM---------RTLSedtirlFLQQI------AGAMKMLH---SKGIIHRDLKPQNILLSys 137
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  849 -------DDLTAHVSDFGLARLLLkfdeesffNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14202  138 ggrksnpNNIRIKIADFGFARYLQ--------NNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAP 208
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
707-920 2.36e-14

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: 74.52  E-value: 2.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKK---VVAVKVLNM-----QRRgamkSFMAECESLKDIRHRNLVKL---LTACSSIdfqgne 775
Cdd:cd05065   11 VIGAGEFGEVCRGRLKLPGKreiFVAIKTLKSgytekQRR----DFLSEASIMGQFDHPNIIHLegvVTKSRPV------ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  776 frALIYEFMPNGSLDMWLHPEEVEeihrpsrtLTLLERLNIAIDVASVLDYLHVHCHepiAHCDLKPSNVLLDDDLTAHV 855
Cdd:cd05065   81 --MIITEFMENGALDSFLRQNDGQ--------FTVIQLVGMLRGIAAGMKYLSEMNY---VHRDLAARNILVNSNLVCKV 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  856 SDFGLARLLLkfDEESFFNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLE-MFTGKRP 920
Cdd:cd05065  148 SDFGLSRFLE--DDTSDPTYTSSLGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEvMSYGERP 211
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
707-920 2.56e-14

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: 74.30  E-value: 2.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEkkVVAVKVlnmQRRGAMKSFMAECESLKD-------IRHRNLVKLLTACSSidfQGNefRAL 779
Cdd:cd14147   10 VIGIGGFGKVYRGSWRGE--LVAVKA---ARQDPDEDISVTAESVRQearlfamLAHPNIIALKAVCLE---EPN--LCL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  780 IYEFMPNGSLDMWLHPEEVeeihrPSRTLtllerLNIAIDVASVLDYLHVHCHEPIAHCDLKPSNVLL------DD--DL 851
Cdd:cd14147   80 VMEYAAGGPLSRALAGRRV-----PPHVL-----VNWAVQIARGMHYLHCEALVPVIHRDLKSNNILLlqpienDDmeHK 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  852 TAHVSDFGLARlllkfdEESFFNQLSSAGvrgTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14147  150 TLKITDFGLAR------EWHKTTQMSAAG---TYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVP 209
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
709-920 2.74e-14

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: 73.83  E-value: 2.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVYKALLLTEKKVVAVKVLNMQR----RGAMKSFMAECESLKDIRHRNLVKLltacssIDFQGNEFRALIYEFM 784
Cdd:cd14119    2 GEGSYGKVKEVLDTETLCRRAVKILKKRKlrriPNGEANVKREIQILRRLNHRNVIKL------VDVLYNEEKQKLYMVM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 P--NGSLDmwlhpEEVEEihRPSRTLTLLERLNIAIDVASVLDYLHVHChepIAHCDLKPSNVLLDDDLTAHVSDFGLAR 862
Cdd:cd14119   76 EycVGGLQ-----EMLDS--APDKRLPIWQAHGYFVQLIDGLEYLHSQG---IIHKDIKPGNLLLTTDGTLKISDFGVAE 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18408454  863 LLLKFDEESFFNQlssagVRGTIGYAAPEYgVGGQPSING---DVYSFGILLLEMFTGKRP 920
Cdd:cd14119  146 ALDLFAEDDTCTT-----SQGSPAFQPPEI-ANGQDSFSGfkvDIWSAGVTLYNMTTGKYP 200
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
707-924 2.87e-14

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: 74.13  E-value: 2.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTV-YKALLLTEKK--VVAVKVLNM-----QRRgamkSFMAECESLKDIRHRNLVKL---LTACSSIdfqgne 775
Cdd:cd05066   11 VIGAGEFGEVcSGRLKLPGKReiPVAIKTLKAgytekQRR----DFLSEASIMGQFDHPNIIHLegvVTRSKPV------ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  776 frALIYEFMPNGSLDMWLHPEEVEeihrpsrtLTLLERLNIAIDVASVLDYLHVHCHepiAHCDLKPSNVLLDDDLTAHV 855
Cdd:cd05066   81 --MIVTEYMENGSLDAFLRKHDGQ--------FTVIQLVGMLRGIASGMKYLSDMGY---VHRDLAARNILVNSNLVCKV 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  856 SDFGLARlLLKFDEESFFnqlSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLE-MFTGKRPTNEL 924
Cdd:cd05066  148 SDFGLSR-VLEDDPEAAY---TTRGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEvMSYGERPYWEM 213
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
708-947 2.95e-14

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: 74.68  E-value: 2.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEK-KVVAVKVLNMQ--RRGAMKSFMAECESLKDIR---HRNLVKLLTACSSIDFQGNEFRALIY 781
Cdd:cd07862    9 IGEGAYGKVFKARDLKNGgRFVALKRVRVQtgEEGMPLSTIREVAVLRHLEtfeHPNVVRLFDVCTVSRTDRETKLTLVF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 EFMPNgslDMWLHPEEVEEIHRPSRTLTllerlNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLA 861
Cdd:cd07862   89 EHVDQ---DLTTYLDKVPEPGVPTETIK-----DMMFQLLRGLDFLHSH---RVVHRDLKPQNILVTSSGQIKLADFGLA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  862 RLLlkfdeeSFfnQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTgKRPtneLFGGNFTLNSYTKsalpe 941
Cdd:cd07862  158 RIY------SF--QMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFR-RKP---LFRGSSDVDQLGK----- 220

                 ....*.
gi 18408454  942 rILDIV 947
Cdd:cd07862  221 -ILDVI 225
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
702-998 3.00e-14

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: 74.57  E-value: 3.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEK---KVVAVKVL--NMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSIDFQGN-E 775
Cdd:cd05074   11 FTLGRMLGKGEFGSVREAQLKSEDgsfQKVAVKMLkaDIFSSSDIEEFLREAACMKEFDHPNVIKLIGVSLRSRAKGRlP 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  776 FRALIYEFMPNGSLDMWLHPEEV--EEIHRPSRTLtllerLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTA 853
Cdd:cd05074   91 IPMVILPFMKHGDLHTFLLMSRIgeEPFTLPLQTL-----VRFMIDIASGMEYLS---SKNFIHRDLAARNCMLNENMTV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  854 HVSDFGLARLLLKFDeesFFNQLSSAGVrgTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRPtnelFGG--NFT 930
Cdd:cd05074  163 CVADFGLSKKIYSGD---YYRQGCASKL--PVKWLALESLADNVYTTHSDVWAFGVTMWEIMTrGQTP----YAGveNSE 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  931 LNSYtksalperildivdesiLHIGLRVGFPvVECLTMVFEVGLRCCEESPMNRLATSIVVKELISIR 998
Cdd:cd05074  234 IYNY-----------------LIKGNRLKQP-PDCLEDVYELMCQCWSPEPKCRPSFQHLRDQLELIW 283
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
706-977 3.49e-14

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: 74.32  E-value: 3.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTVYKALLLTEKKVVAVKVLNM-------QRRGAMKSFMAECESLKDIRHRNLVKLLTACSsidFQGNEFrA 778
Cdd:cd14040   12 HLLGRGGFSEVYKAFDLYEQRYAAVKIHQLnkswrdeKKENYHKHACREYRIHKELDHPRIVKLYDYFS---LDTDTF-C 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGSLDMWLhpeeveeihRPSRTLTLLERLNIAIDVASVLDYLHvHCHEPIAHCDLKPSNVLLDDDLTA---HV 855
Cdd:cd14040   88 TVLEYCEGNDLDFYL---------KQHKLMSEKEARSIVMQIVNALRYLN-EIKPPIIHYDLKPGNILLVDGTACgeiKI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  856 SDFGLARLLlkfDEESF---FNQLSSAGVrGTIGYAAPE-YGVGGQP---SINGDVYSFGILLLEMFTGKRPtnelFGGN 928
Cdd:cd14040  158 TDFGLSKIM---DDDSYgvdGMDLTSQGA-GTYWYLPPEcFVVGKEPpkiSNKVDVWSVGVIFFQCLYGRKP----FGHN 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 18408454  929 ftlnsytksalpERILDIVDESILHIGLRVGFPVVECLTMVFEVGLRCC 977
Cdd:cd14040  230 ------------QSQQDILQENTILKATEVQFPVKPVVSNEAKAFIRRC 266
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
711-914 3.84e-14

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


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 74.31  E-value: 3.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  711 GSFGTVYKALLLTEkkVVAVKVLNMQRRgamKSFMAECE--SLKDIRHRNLVKLLTA---CSSIDFQgnefRALIYEFMP 785
Cdd:cd14141    6 GRFGCVWKAQLLNE--YVAVKIFPIQDK---LSWQNEYEiySLPGMKHENILQFIGAekrGTNLDVD----LWLITAFHE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLDMWLHpeeveeihrpSRTLTLLERLNIAIDVASVLDYLHVHC------HEP-IAHCDLKPSNVLLDDDLTAHVSDF 858
Cdd:cd14141   77 KGSLTDYLK----------ANVVSWNELCHIAQTMARGLAYLHEDIpglkdgHKPaIAHRDIKSKNVLLKNNLTACIADF 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18408454  859 GLArllLKFdeESFFNQLSSAGVRGTIGYAAPEYGVGG-----QPSINGDVYSFGILLLEM 914
Cdd:cd14141  147 GLA---LKF--EAGKSAGDTHGQVGTRRYMAPEVLEGAinfqrDAFLRIDMYAMGLVLWEL 202
PLN03150 PLN03150
hypothetical protein; Provisional
143-230 3.85e-14

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 76.78  E-value: 3.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   143 LRLDSNRLGGSVPSELGSLTNLVQLNLYGNNMRGKLPTSLGNLTLLEQLALSHNNLEGEIPSDVAQLTQIWSLQLVANNF 222
Cdd:PLN03150  423 LGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSL 502

                  ....*...
gi 18408454   223 SGVFPPAL 230
Cdd:PLN03150  503 SGRVPAAL 510
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
745-891 4.25e-14

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: 73.54  E-value: 4.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  745 MAECESLKDI-RHRNLVKLltacssID-FQGNEFRALIYEFMPNGSLDMWLhpeeveeihrpSRTLTLLERLNIAI--DV 820
Cdd:cd14093   56 RREIEILRQVsGHPNIIEL------HDvFESPTFIFLVFELCRKGELFDYL-----------TEVVTLSEKKTRRImrQL 118
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18408454  821 ASVLDYLHVHChepIAHCDLKPSNVLLDDDLTAHVSDFGLARLLlkfDEESFFNQLSsagvrGTIGYAAPE 891
Cdd:cd14093  119 FEAVEFLHSLN---IVHRDLKPENILLDDNLNVKISDFGFATRL---DEGEKLRELC-----GTPGYLAPE 178
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
708-918 4.55e-14

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: 74.15  E-value: 4.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMK---SFMA--ECESLKDIRHRNLVKLLTACSSIDFQgnefrALIYE 782
Cdd:cd07841    8 LGEGTYAVVYKARDKETGRIVAIKKIKLGERKEAKdgiNFTAlrEIKLLQELKHPNIIGLLDVFGHKSNI-----NLVFE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPnGSLdmwlhpEEVeeIHRPSRTLTLLERLNIAIDVASVLDYLHVHChepIAHCDLKPSNVLLDDDLTAHVSDFGLAR 862
Cdd:cd07841   83 FME-TDL------EKV--IKDKSIVLTPADIKSYMLMTLRGLEYLHSNW---ILHRDLKPNNLLIASDGVLKLADFGLAR 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  863 lllkfdeesffnQLSSAGVRG-----TIGYAAPE-------YGVGgqpsinGDVYSFGILLLEMFTGK 918
Cdd:cd07841  151 ------------SFGSPNRKMthqvvTRWYRAPEllfgarhYGVG------VDMWSVGCIFAELLLRV 200
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
702-920 4.69e-14

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: 73.01  E-value: 4.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRgAMKSFMAECESLKDIRHRNLVKLLtacSSIDFQGNEFraLIY 781
Cdd:cd06614    2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQ-NKELIINEILIMKECKHPNIVDYY---DSYLVGDELW--VVM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 EFMPNGSLdmwlhpeeVEEIHRPSRTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLA 861
Cdd:cd06614   76 EYMDGGSL--------TDIITQNPVRMNESQIAYVCREVLQGLEYLHSQ---NVIHRDIKSDNILLSKDGSVKLADFGFA 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  862 RLLLKfdeesffNQLSSAGVRGTIGYAAPEYgVGGQP-SINGDVYSFGILLLEMFTGKRP 920
Cdd:cd06614  145 AQLTK-------EKSKRNSVVGTPYWMAPEV-IKRKDyGPKVDIWSLGIMCIEMAEGEPP 196
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
702-924 4.72e-14

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: 73.43  E-value: 4.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRrgamksfmAEcESLKDIRHRnlVKLLTACSSI-------DFQGN 774
Cdd:cd06609    3 FTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEE--------AE-DEIEDIQQE--IQFLSQCDSPyitkyygSFLKG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  775 EFRALIYEFMPNGSLDMWLHPEEVEEIHrpsrtltllerlnIAI---DVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDL 851
Cdd:cd06609   72 SKLWIIMEYCGGGSVLDLLKPGPLDETY-------------IAFilrEVLLGLEYLH---SEGKIHRDIKAANILLSEEG 135
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  852 TAHVSDFGLArlllkfdeesffNQLSSAGVR-----GTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTNEL 924
Cdd:cd06609  136 DVKLADFGVS------------GQLTSTMSKrntfvGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDL 201
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
708-924 6.04e-14

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: 73.15  E-value: 6.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEkkvVAVKVLNMQR--RGAMKSFMAECESLKDIRHRNLVKLLTACSSidfqgNEFRALIYEFMP 785
Cdd:cd14063    8 IGKGRFGRVHRGRWHGD---VAIKLLNIDYlnEEQLEAFKEEVAAYKNTRHDNLVLFMGACMD-----PPHLAIVTSLCK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLdmwlhpeeVEEIHRPSRTLTLLERLNIAIDVASVLDYLHVhchEPIAHCDLKPSNVLLDDDlTAHVSDFGLARL-- 863
Cdd:cd14063   80 GRTL--------YSLIHERKEKFDFNKTVQIAQQICQGMGYLHA---KGIIHKDLKSKNIFLENG-RVVITDFGLFSLsg 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18408454  864 LLKFDEESffNQLssAGVRGTIGYAAPEYGVGGQP----------SINGDVYSFGILLLEMFTGKRPTNEL 924
Cdd:cd14063  148 LLQPGRRE--DTL--VIPNGWLCYLAPEIIRALSPdldfeeslpfTKASDVYAFGTVWYELLAGRWPFKEQ 214
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
700-915 6.70e-14

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: 73.31  E-value: 6.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  700 NGFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQ---RRGAMKsFMAECESLKDIRHRNLVKLLTACSSidfqgnEF 776
Cdd:cd14049    6 NEFEEIARLGKGGYGKVYKVRNKLDGQYYAIKKILIKkvtKRDCMK-VLREVKVLAGLQHPNIVGYHTAWME------HV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  777 RALIYEFMP--NGSLDMWL-----HPEEVEEIHRPSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLD- 848
Cdd:cd14049   79 QLMLYIQMQlcELSLWDWIvernkRPCEEEFKSAPYTPVDVDVTTKILQQLLEGVTYIH---SMGIVHRDLKPRNIFLHg 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  849 DDLTAHVSDFGLA-RLLLKFDEESF----FNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMF 915
Cdd:cd14049  156 SDIHVRIGDFGLAcPDILQDGNDSTtmsrLNGLTHTSGVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF 227
PLN03150 PLN03150
hypothetical protein; Provisional
438-556 6.92e-14

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 76.01  E-value: 6.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   438 LDLSNNGFEGIVPTSLGNCSHLLELWIGDNKLNGTIPLEIMKIQQLLRLDMSGNSLIGSLPQDIGALQNLGTLSLGDNKL 517
Cdd:PLN03150  423 LGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSL 502
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 18408454   518 SGKLPQTLGncltmeSLFLEGNLF-YGDIPDLKGLVGVKE 556
Cdd:PLN03150  503 SGRVPAALG------GRLLHRASFnFTDNAGLCGIPGLRA 536
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
708-920 6.96e-14

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


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 74.24  E-value: 6.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLN---MQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFM 784
Cdd:cd05573    9 IGRGAFGEVWLVRDKDTGQVYAMKILRksdMLKREQIAHVRAERDILADADSPWIVRLHYA-----FQDEDHLYLVMEYM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLDMWLhpeeveeihrpSRTLTLLE---RLNIAIDVASvLDYLH-VHChepiAHCDLKPSNVLLDDDltAHV--SDF 858
Cdd:cd05573   84 PGGDLMNLL-----------IKYDVFPEetaRFYIAELVLA-LDSLHkLGF----IHRDIKPDNILLDAD--GHIklADF 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  859 GLARLLLKFDEESFF-----NQLSSAGVR-----------------GTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT 916
Cdd:cd05573  146 GLCTKMNKSGDRESYlndsvNTLFQDNVLarrrphkqrrvraysavGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLY 225

                 ....
gi 18408454  917 GKRP 920
Cdd:cd05573  226 GFPP 229
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
693-918 7.30e-14

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: 73.56  E-value: 7.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  693 GDLRNATNgFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNM--QRRGAMKSFMAECESLKDIRHRNLVKLLTACssid 770
Cdd:cd07845    1 GRCRSVTE-FEKLNRIGEGTYGIVYRARDTTSGEIVALKKVRMdnERDGIPISSLREITLLLNLRHPNIVELKEVV---- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  771 fQGNEFRA--LIYEFMPN--GSLdmwlhpeeVEEIHRPsrtLTLLERLNIAIDVASVLDYLHVHChepIAHCDLKPSNVL 846
Cdd:cd07845   76 -VGKHLDSifLVMEYCEQdlASL--------LDNMPTP---FSESQVKCLMLQLLRGLQYLHENF---IIHRDLKVSNLL 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  847 LDDDLTAHVSDFGLARLLlkfdeESFFNQLSSAGVrgTIGYAAPEYGVGGQ---PSIngDVYSFGILLLEMFTGK 918
Cdd:cd07845  141 LTDKGCLKIADFGLARTY-----GLPAKPMTPKVV--TLWYRAPELLLGCTtytTAI--DMWAVGCILAELLAHK 206
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
707-922 8.09e-14

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: 72.85  E-value: 8.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGA------MKSFMAECESLKDIRHRNLVKLLTACSsidfQGNEFRALI 780
Cdd:cd06630    7 LLGTGAFSSCYQARDVKTGTLMAVKQVSFCRNSSseqeevVEAIREEIRMMARLNHPNIVRMLGATQ----HKSHFNIFV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 yEFMPNGSLDMWLH-----PEEVEeihrpsrtltllerLNIAIDVASVLDYLHVHChepIAHCDLKPSNVLLDDdlTAH- 854
Cdd:cd06630   83 -EWMAGGSVASLLSkygafSENVI--------------INYTLQILRGLAYLHDNQ---IIHRDLKGANLLVDS--TGQr 142
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  855 --VSDFGLARLLLkfdeesffNQLSSAG-----VRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTN 922
Cdd:cd06630  143 lrIADFGAAARLA--------SKGTGAGefqgqLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWN 209
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
708-924 8.35e-14

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: 73.14  E-value: 8.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACssidFQGNEFRALIyEFMPNG 787
Cdd:cd06643   13 LGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVKLLDAF----YYENNLWILI-EFCAGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 SLDMWLHpeeveEIHRPsrtltlLERLNIAIDVASVLDYLHVHCHEPIAHCDLKPSNVLLDDDLTAHVSDFGLA----RL 863
Cdd:cd06643   88 AVDAVML-----ELERP------LTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSakntRT 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  864 LLKFDeeSFFnqlssagvrGTIGYAAPEYGV----GGQP-SINGDVYSFGILLLEMFTGKRPTNEL 924
Cdd:cd06643  157 LQRRD--SFI---------GTPYWMAPEVVMcetsKDRPyDYKADVWSLGVTLIEMAQIEPPHHEL 211
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
708-916 8.97e-14

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 73.04  E-value: 8.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTV----YKALLLTEKKVVAVKVLNMQRRGA-MKSFMAECESLKDIRHRNLVKLLTACSsiDFQGNEFRaLIYE 782
Cdd:cd05079   12 LGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNhIADLKKEIEILRNLYHENIVKYKGICT--EDGGNGIK-LIME 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLDMWLhPEEVEEIHrpsrtltLLERLNIAIDVASVLDYLHVHCHepiAHCDLKPSNVLLDDDLTAHVSDFGLAR 862
Cdd:cd05079   89 FLPSGSLKEYL-PRNKNKIN-------LKQQLKYAVQICKGMDYLGSRQY---VHRDLAARNVLVESEHQVKIGDFGLTK 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  863 lLLKFDEESFF--NQLSSAgvrgtIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT 916
Cdd:cd05079  158 -AIETDKEYYTvkDDLDSP-----VFWYAPECLIQSKFYIASDVWSFGVTLYELLT 207
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
708-927 9.78e-14

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: 72.71  E-value: 9.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKV--LNMQRRGAMKSFMAECESLKDIRHRNLVKLLtacsSIDFQGNEFRaLIYEFmp 785
Cdd:cd07835    7 IGEGTYGVVYKARDKLTGEIVALKKirLETEDEGVPSTAIREISLLKELNHPNIVRLL----DVVHSENKLY-LVFEF-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 ngsLDMWL------HPEeveeihrpsrtltllerlnIAIDVASVLDYLH------VHCH-EPIAHCDLKPSNVLLDDDLT 852
Cdd:cd07835   80 ---LDLDLkkymdsSPL-------------------TGLDPPLIKSYLYqllqgiAFCHsHRVLHRDLKPQNLLIDTEGA 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  853 AHVSDFGLARlllkfdeeSFfnqlsSAGVRG------TIGYAAPEYGVGG-QPSINGDVYSFGILLLEMFTgKRPtneLF 925
Cdd:cd07835  138 LKLADFGLAR--------AF-----GVPVRTythevvTLWYRAPEILLGSkHYSTPVDIWSVGCIFAEMVT-RRP---LF 200

                 ..
gi 18408454  926 GG 927
Cdd:cd07835  201 PG 202
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
702-920 1.01e-13

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: 72.99  E-value: 1.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSF---MAECESLKDIRHRNLVKLLTAcssidFQGNEFRA 778
Cdd:cd05608    3 FLDFRVLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKGYegaMVEKRILAKVHSRFIVSLAYA-----FQTKTDLC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGslDMWLHPEEVEEiHRPSrtLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDF 858
Cdd:cd05608   78 LVMTIMNGG--DLRYHIYNVDE-ENPG--FQEPRACFYTAQIISGLEHLHQR---RIIYRDLKPENVLLDDDGNVRISDL 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  859 GLARLLLKfdeesffNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd05608  150 GLAVELKD-------GQTKTKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGP 204
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
702-922 1.08e-13

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: 72.03  E-value: 1.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKvlnmqrrGAMKSFMAECESLKDIR----------HRNLVKLLTAcssidF 771
Cdd:cd13997    2 FHELEQIGSGSFSEVFKVRSKVDGCLYAVK-------KSKKPFRGPKERARALReveahaalgqHPNIVRYYSS-----W 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  772 QGNEFRALIYEFMPNGSLDMwlHPEEVEEIHRpsrtLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDL 851
Cdd:cd13997   70 EEGGHLYIQMELCENGSLQD--ALEELSPISK----LSEAEVWDLLLQVALGLAFIH---SKGIVHLDIKPDNIFISNKG 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18408454  852 TAHVSDFGLA-RLLLKFDEEsffnqlssagvRGTIGYAAPEYGVG-GQPSINGDVYSFGILLLEMFTG-KRPTN 922
Cdd:cd13997  141 TCKIGDFGLAtRLETSGDVE-----------EGDSRYLAPELLNEnYTHLPKADIFSLGVTVYEAATGePLPRN 203
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
727-916 1.08e-13

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: 73.09  E-value: 1.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  727 VVAVKVLNMQ-RRGAMKSFMAECESLKDIRHRNLVKLLTACSSIDFQgnefrALIYEFMPNGSLDMWLHPEEVEEIHRPS 805
Cdd:cd05097   46 LVAVKMLRADvTKTARNDFLKEIKIMSRLKNPNIIRLLGVCVSDDPL-----CMITEYMENGDLNQFLSQREIESTFTHA 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  806 RTLTLLERLNI---AIDVASVLDYLhvhCHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARLLLKFDeesfFNQLSSAGVR 882
Cdd:cd05097  121 NNIPSVSIANLlymAVQIASGMKYL---ASLNFVHRDLATRNCLVGNHYTIKIADFGMSRNLYSGD----YYRIQGRAVL 193
                        170       180       190
                 ....*....|....*....|....*....|....
gi 18408454  883 gTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT 916
Cdd:cd05097  194 -PIRWMAWESILLGKFTTASDVWAFGVTLWEMFT 226
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
708-920 1.15e-13

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


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 72.74  E-value: 1.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALL----LTEKKVVAVKVL-NMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSidfqgNEFRALIYE 782
Cdd:cd05090   13 LGECAFGKIYKGHLylpgMDHAQLVAIKTLkDYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQ-----EQPVCMLFE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLDMWL-----HPE---EVEEIHRPSRTLTLLERLNIAIDVASVLDYLHVHCHepiAHCDLKPSNVLLDDDLTAH 854
Cdd:cd05090   88 FMNQGDLHEFLimrspHSDvgcSSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFF---VHKDLAARNILVGEQLHVK 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  855 VSDFGLARLLLKFDeesfFNQLSSAGVRgTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRP 920
Cdd:cd05090  165 ISDLGLSREIYSSD----YYRVQNKSLL-PIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQP 226
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
700-920 1.28e-13

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: 72.46  E-value: 1.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  700 NGFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAM-KSFMAECESLKDIRHRNLVK-----LLTACSSIdfqg 773
Cdd:cd06621    1 DKIVELSSLGEGAGGSVTKCRLRNTKTIFALKTITTDPNPDVqKQILRELEINKSCASPYIVKyygafLDEQDSSI---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  774 nefrALIYEFMPNGSLDMWLhpEEVEeihrpSRTLTLLER--LNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDL 851
Cdd:cd06621   77 ----GIAMEYCEGGSLDSIY--KKVK-----KKGGRIGEKvlGKIAESVLKGLSYLH---SRKIIHRDIKPSNILLTRKG 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  852 TAHVSDFGLArlllkfdeESFFNQLSSAGVrGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd06621  143 QVKLCDFGVS--------GELVNSLAGTFT-GTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFP 202
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
702-924 1.29e-13

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: 72.40  E-value: 1.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRrgamksfmAECEsLKDIRHRnlVKLLTACSS---IDFQGNEFRA 778
Cdd:cd06642    6 FTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEE--------AEDE-IEDIQQE--ITVLSQCDSpyiTRYYGSYLKG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 ----LIYEFMPNGSLDMWLHPEEVEEIHrpsrTLTLLErlniaiDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAH 854
Cdd:cd06642   75 tklwIIMEYLGGGSALDLLKPGPLEETY----IATILR------EILKGLDYLH---SERKIHRDIKAANVLLSEQGDVK 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  855 VSDFGLARLLLKfdeesffNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTNEL 924
Cdd:cd06642  142 LADFGVAGQLTD-------TQIKRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDL 204
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
702-915 1.34e-13

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: 72.14  E-value: 1.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKsfmaECESLKDIRHRNLVKLLTA------CSSIDFQGNE 775
Cdd:cd14047    8 FKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVKLNNEKAER----EVKALAKLDHPNIVRYNGCwdgfdyDPETSSSNSS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  776 FRALIY-----EFMPNGSLDMWlhpeeVEEihRPSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDD 850
Cdd:cd14047   84 RSKTKClfiqmEFCEKGTLESW-----IEK--RNGEKLDKVLALEIFEQITKGVEYIH---SKKLIHRDLKPSNIFLVDT 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  851 LTAHVSDFGLArlllkfdeESFFNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMF 915
Cdd:cd14047  154 GKVKIGDFGLV--------TSLKNDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFELL 210
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
702-928 1.35e-13

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: 72.53  E-value: 1.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKV--LNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACS----SIDF---Q 772
Cdd:cd07864    9 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKvrLDNEKEGFPITAIREIKILRQLNHRSVVNLKEIVTdkqdALDFkkdK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  773 GNEFraLIYEFMPN---GSLDMWLhpEEVEEIHRPSRTLTLLERLNiaidvasvldylhvHCHEP-IAHCDLKPSNVLLD 848
Cdd:cd07864   89 GAFY--LVFEYMDHdlmGLLESGL--VHFSEDHIKSFMKQLLEGLN--------------YCHKKnFLHRDIKCSNILLN 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  849 DDLTAHVSDFGLARLLLKFDEESFFNQLSsagvrgTIGYAAPEYGVGGQ---PSIngDVYSFGILLLEMFTgKRPtneLF 925
Cdd:cd07864  151 NKGQIKLADFGLARLYNSEESRPYTNKVI------TLWYRPPELLLGEErygPAI--DVWSCGCILGELFT-KKP---IF 218

                 ...
gi 18408454  926 GGN 928
Cdd:cd07864  219 QAN 221
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
700-914 1.55e-13

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: 72.21  E-value: 1.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  700 NGFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNM-QRRGAMKSFMAECESLKDIRHRNLVKLLTACSSI---DFQGNE 775
Cdd:cd14048    6 TDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLpNNELAREKVLREVRALAKLDHPGIVRYFNAWLERppeGWQEKM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  776 FRALIYEFMP---NGSLDMWLhpeeveeihrpSRTLTLLER-----LNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLL 847
Cdd:cd14048   86 DEVYLYIQMQlcrKENLKDWM-----------NRRCTMESRelfvcLNIFKQIASAVEYLH---SKGLIHRDLKPSNVFF 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  848 DDDLTAHVSDFGLARLLLKFDEESFFNQLSSAGVR-----GTIGYAAPEYGVGGQPSINGDVYSFGILLLEM 914
Cdd:cd14048  152 SLDDVVKVGDFGLVTAMDQGEPEQTVLTPMPAYAKhtgqvGTRLYMSPEQIHGNQYSEKVDIFALGLILFEL 223
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
701-920 1.69e-13

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


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 71.74  E-value: 1.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  701 GFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNmqRRGAMKSFMA-----ECESLKDIRHRNLVKLLTACSSIDfqGNE 775
Cdd:cd14165    2 GYILGINLGEGSYAKVKSAYSERLKCNVAIKIID--KKKAPDDFVEkflprELEILARLNHKSIIKTYEIFETSD--GKV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  776 FraLIYEFMPNGSLDMWLHPEEVEEIHRPSRtltLLERLNIAIDvasvldylhvHCHE-PIAHCDLKPSNVLLDDDLTAH 854
Cdd:cd14165   78 Y--IVMELGVQGDLLEFIKLRGALPEDVARK---MFHQLSSAIK----------YCHElDIVHRDLKCENLLLDKDFNIK 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  855 VSDFGLARLLLKfDEESffNQLSSAGVRGTIGYAAPEY--GVGGQPSINgDVYSFGILLLEMFTGKRP 920
Cdd:cd14165  143 LTDFGFSKRCLR-DENG--RIVLSKTFCGSAAYAAPEVlqGIPYDPRIY-DIWSLGVILYIMVCGSMP 206
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
709-920 1.79e-13

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: 71.94  E-value: 1.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSIDFQGNEFRALIYEFMPNGS 788
Cdd:cd13986    9 GEGGFSFVYLVEDLSTGRLYALKKILCHSKEDVKEAMREIENYRLFNHPNILRLLDSQIVKEAGGKKEVYLLLPYYKRGS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  789 LDMWLHPEEVEEIHRPSRTLtllerLNIAIDVASVLDYLHVHCHEPIAHCDLKPSNVLLDDDLTAHVSDFG---LARLLL 865
Cdd:cd13986   89 LQDEIERRLVKGTFFPEDRI-----LHIFLGICRGLKAMHEPELVPYAHRDIKPGNVLLSEDDEPILMDLGsmnPARIEI 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  866 KFDEESFFNQlSSAGVRGTIGYAAPE-YGVGGQPSIN--GDVYSFGILLLEMFTGKRP 920
Cdd:cd13986  164 EGRREALALQ-DWAAEHCTMPYRAPElFDVKSHCTIDekTDIWSLGCTLYALMYGESP 220
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
708-925 1.89e-13

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: 72.35  E-value: 1.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVY--KALLLTEKK-----VVAVKVLNMQ-RRGAMKSFMAECESLKDI-RHRNLVKLLTACSSidfQGNEFra 778
Cdd:cd05098   21 LGEGCFGQVVlaEAIGLDKDKpnrvtKVAVKMLKSDaTEKDLSDLISEMEMMKMIgKHKNIINLLGACTQ---DGPLY-- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGSLDMWLH---PEEVEEIHRPS----RTLTLLERLNIAIDVASVLDYLhvhCHEPIAHCDLKPSNVLLDDDL 851
Cdd:cd05098   96 VIVEYASKGNLREYLQarrPPGMEYCYNPShnpeEQLSSKDLVSCAYQVARGMEYL---ASKKCIHRDLAARNVLVTEDN 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  852 TAHVSDFGLARLLLKFDeesFFNQLSSAgvRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT------GKRPTNELF 925
Cdd:cd05098  173 VMKIADFGLARDIHHID---YYKKTTNG--RLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTlggspyPGVPVEELF 247
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
706-916 1.97e-13

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: 72.34  E-value: 1.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTVYKALLLTE--KKVVAVKVLN-MQRRGAMKSFMAECESLKDI-RHRNLVKLLTACssidfqgnEFRALIY 781
Cdd:cd05089    8 DVIGEGNFGQVIKAMIKKDglKMNAAIKMLKeFASENDHRDFAGELEVLCKLgHHPNIINLLGAC--------ENRGYLY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 ---EFMPNGSLDMWLHPEEVEEI-------HRPSRTLTLLERLNIAIDVASVLDYLhvhCHEPIAHCDLKPSNVLLDDDL 851
Cdd:cd05089   80 iaiEYAPYGNLLDFLRKSRVLETdpafakeHGTASTLTSQQLLQFASDVAKGMQYL---SEKQFIHRDLAARNVLVGENL 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  852 TAHVSDFGLARlllkfDEESFFNQLSSagvRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT 916
Cdd:cd05089  157 VSKIADFGLSR-----GEEVYVKKTMG---RLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVS 213
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
711-916 2.03e-13

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


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 71.99  E-value: 2.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  711 GSFGTVYKALLLTEkkVVAVKVLNMQRRgamKSFMAECE--SLKDIRHRNLVKLLTAcssiDFQGNEFRA---LIYEFMP 785
Cdd:cd14140    6 GRFGCVWKAQLMNE--YVAVKIFPIQDK---QSWQSEREifSTPGMKHENLLQFIAA----EKRGSNLEMelwLITAFHD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLDMWLHpeeveeihrpSRTLTLLERLNIAIDVASVLDYLHVHC-------HEP-IAHCDLKPSNVLLDDDLTAHVSD 857
Cdd:cd14140   77 KGSLTDYLK----------GNIVSWNELCHIAETMARGLSYLHEDVprckgegHKPaIAHRDFKSKNVLLKNDLTAVLAD 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  858 FGLArllLKFdeESFFNQLSSAGVRGTIGYAAPEYGVGgqpSING--------DVYSFGILLLEMFT 916
Cdd:cd14140  147 FGLA---VRF--EPGKPPGDTHGQVGTRRYMAPEVLEG---AINFqrdsflriDMYAMGLVLWELVS 205
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
708-1005 2.36e-13

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: 71.61  E-value: 2.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLT-----EKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSIDfqgneFRALIYE 782
Cdd:cd05093   13 LGEGAFGKVFLAECYNlcpeqDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGD-----PLIMVFE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLDMWLHPEEVEEI----HRPSRTLTLLERLNIAIDVASVLDYLhvhCHEPIAHCDLKPSNVLLDDDLTAHVSDF 858
Cdd:cd05093   88 YMKHGDLNKFLRAHGPDAVlmaeGNRPAELTQSQMLHIAQQIAAGMVYL---ASQHFVHRDLATRNCLVGENLLVKIGDF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  859 GLARLLLKFDEESFfnqlsSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRPTNELfGGNFTLNSYTKS 937
Cdd:cd05093  165 GMSRDVYSTDYYRV-----GGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQL-SNNEVIECITQG 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  938 ALPERildivdesilhiglrvgfPVVeCLTMVFEVGLRCCEESPMNRLAtsivVKELISIRERFFKAS 1005
Cdd:cd05093  239 RVLQR------------------PRT-CPKEVYDLMLGCWQREPHMRLN----IKEIHSLLQNLAKAS 283
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
69-327 2.62e-13

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 73.04  E-value: 2.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   69 THLELGRLQLGGvISPSIGNLSFLVSLDLYENFFGgTIPQEVGQLSRLEYLDMGINYLRgPIPLGLYNCSRLLNLRLDSN 148
Cdd:COG4886  162 KSLDLSNNQLTD-LPEELGNLTNLKELDLSNNQIT-DLPEPLGNLTNLEELDLSGNQLT-DLPEPLANLTNLETLDLSNN 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  149 RLggSVPSELGSLTNLVQLNLYGNNMRGkLPtSLGNLTLLEQLALSHNNLEGEIPSDVAQLTQIWSLQLVANNFSGVFPP 228
Cdd:COG4886  239 QL--TDLPELGNLTNLEELDLSNNQLTD-LP-PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELL 314
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  229 ALYNLSSLKLLGIGYNHFSGRLRPDLGILLPNLLSFNMGGNYFTGSIPTTLSNISTLERLGMNENNLTGSIPTFGNVPNL 308
Cdd:COG4886  315 ILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLL 394
                        250
                 ....*....|....*....
gi 18408454  309 KLLFLHTNSLGSDSSRDLE 327
Cdd:COG4886  395 TTTAGVLLLTLALLDAVNT 413
PLN03150 PLN03150
hypothetical protein; Provisional
390-474 2.72e-13

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 74.08  E-value: 2.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   390 LILDQNMLSGPLPTSLGKLLNLRYLSLFSNRLSGGIPAFIGNMTMLETLDLSNNGFEGIVPTSLGNCSHLLELWIGDNKL 469
Cdd:PLN03150  423 LGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSL 502

                  ....*
gi 18408454   470 NGTIP 474
Cdd:PLN03150  503 SGRVP 507
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
708-917 2.85e-13

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: 71.41  E-value: 2.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALllTEKKVVAVKVLNMQRRGAMKS----FMAECESLKDIRHRNLVKLLTACSSidfqgNEFRALIYEF 783
Cdd:cd14157    1 ISEGTFADIYKGY--RHGKQYVIKRLKETECESPKSterfFQTEVQICFRCCHPNILPLLGFCVE-----SDCHCLIYPY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  784 MPNGSLDMWLHPEEVEEIhrpsrtLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLArl 863
Cdd:cd14157   74 MPNGSLQDRLQQQGGSHP------LPWEQRLSISLGLLKAVQHLH---NFGILHGNIKSSNVLLDGNLLPKLGHSGLR-- 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18408454  864 LLKFDEESFFNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTG 917
Cdd:cd14157  143 LCPVDKKSVYTMMKTKVLQISLAYLPEDFVRHGQLTEKVDIFSCGVVLAEILTG 196
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
708-916 3.08e-13

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: 71.75  E-value: 3.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKV-----VAVKVLnmqRRGAM----KSFMAECESLKDI-RHRNLVKLLTACSSidfQGNEFr 777
Cdd:cd05054   15 LGRGAFGKVIQASAFGIDKSatcrtVAVKML---KEGATasehKALMTELKILIHIgHHLNVVNLLGACTK---PGGPL- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  778 ALIYEFMPNGSLDMWLH-------------PEEVEEIHRPS----RTLTLLERLNIAIDVASVLDYLhvhCHEPIAHCDL 840
Cdd:cd05054   88 MVIVEFCKFGNLSNYLRskreefvpyrdkgARDVEEEEDDDelykEPLTLEDLICYSFQVARGMEFL---ASRKCIHRDL 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  841 KPSNVLLDDDLTAHVSDFGLARLLLKfDEEsffnQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT 916
Cdd:cd05054  165 AARNILLSENNVVKICDFGLARDIYK-DPD----YVRKGDARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFS 235
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
708-932 3.08e-13

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


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 72.17  E-value: 3.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNM--------QR--RgamksfmaECESLKDIRHRNLVKLLTAcsSIDFQGNEFR 777
Cdd:cd07834    8 IGSGAYGVVCSAYDKRTGRKVAIKKISNvfddlidaKRilR--------EIKILRHLKHENIIGLLDI--LRPPSPEEFN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  778 AL--IYEFMpngslDMWLH-----PEEVEEIHRPSRTLTLLerlniaidvaSVLDYLHvHCHepIAHCDLKPSNVLLDDD 850
Cdd:cd07834   78 DVyiVTELM-----ETDLHkviksPQPLTDDHIQYFLYQIL----------RGLKYLH-SAG--VIHRDLKPSNILVNSN 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  851 LTAHVSDFGLARlllKFDEESFFNQLSSAGVrgTIGYAAPE-------YGvggqPSIngDVYSFGILLLEMFTGKrPtne 923
Cdd:cd07834  140 CDLKICDFGLAR---GVDPDEDKGFLTEYVV--TRWYRAPElllsskkYT----KAI--DIWSVGCIFAELLTRK-P--- 204

                 ....*....
gi 18408454  924 LFGGNFTLN 932
Cdd:cd07834  205 LFPGRDYID 213
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
708-953 3.09e-13

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: 71.63  E-value: 3.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMA--ECESLKDIRHRNLVKLLTACSSIDFQGNEFRA---LIYE 782
Cdd:cd07865   20 IGQGTFGEVFKARHRKTGQIVALKKVLMENEKEGFPITAlrEIKILQLLKHENVVNLIEICRTKATPYNRYKGsiyLVFE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 F--------MPNGSLDMWLhpEEVEEIHRpsrtlTLLERLNiaidvasvldYLHVHchePIAHCDLKPSNVLLDDDLTAH 854
Cdd:cd07865  100 FcehdlaglLSNKNVKFTL--SEIKKVMK-----MLLNGLY----------YIHRN---KILHRDMKAANILITKDGVLK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  855 VSDFGLARlLLKFDEESFFNQLSSAGVrgTIGYAAPE-------YGvggqPSIngDVYSFGILLLEMFT------GKRPT 921
Cdd:cd07865  160 LADFGLAR-AFSLAKNSQPNRYTNRVV--TLWYRPPElllgerdYG----PPI--DMWGAGCIMAEMWTrspimqGNTEQ 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 18408454  922 NEL-----FGGNFT---------LNSYTKSALPERILDIVDESILH 953
Cdd:cd07865  231 HQLtlisqLCGSITpevwpgvdkLELFKKMELPQGQKRKVKERLKP 276
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
708-925 3.34e-13

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


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 71.98  E-value: 3.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKK-------VVAVKVLNMQRRGA-MKSFMAECESLKDI-RHRNLVKLLTACSsidfQGNEFRA 778
Cdd:cd05100   20 LGEGCFGQVVMAEAIGIDKdkpnkpvTVAVKMLKDDATDKdLSDLVSEMEMMKMIgKHKNIINLLGACT----QDGPLYV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIyEFMPNGSLDMWLHPEE-------VEEIHRPSRTLTLLERLNIAIDVASVLDYLhvhCHEPIAHCDLKPSNVLLDDDL 851
Cdd:cd05100   96 LV-EYASKGNLREYLRARRppgmdysFDTCKLPEEQLTFKDLVSCAYQVARGMEYL---ASQKCIHRDLAARNVLVTEDN 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  852 TAHVSDFGLARLLLKFDeesFFNQLSSAgvRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKR-----PTNELF 925
Cdd:cd05100  172 VMKIADFGLARDVHNID---YYKKTTNG--RLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSpypgiPVEELF 246
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
708-924 3.43e-13

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: 70.80  E-value: 3.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFMPNG 787
Cdd:cd06613    8 IGSGTYGDVYKARNIATGELAAVKVIKLEPGDDFEIIQQEISMLKECRHPNIVAYFGS-----YLRRDKLWIVMEYCGGG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 SLDMWLHpeeveeIHRPsrtltlLERLNIAI---DVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARLL 864
Cdd:cd06613   83 SLQDIYQ------VTGP------LSELQIAYvcrETLKGLAYLH---STGKIHRDIKGANILLTEDGDVKLADFGVSAQL 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  865 LK--FDEESFFnqlssagvrGTIGYAAPEygVGGQPSING-----DVYSFGILLLEMFTGKRPTNEL 924
Cdd:cd06613  148 TAtiAKRKSFI---------GTPYWMAPE--VAAVERKGGydgkcDIWALGITAIELAELQPPMFDL 203
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
702-924 3.81e-13

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: 70.87  E-value: 3.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRrgamksfmAECEsLKDIRHRnlVKLLTACSS---IDFQGNEFRA 778
Cdd:cd06641    6 FTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEE--------AEDE-IEDIQQE--ITVLSQCDSpyvTKYYGSYLKD 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 ----LIYEFMPNGSLDMWLHPEEVEEihrpSRTLTLLErlniaiDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAH 854
Cdd:cd06641   75 tklwIIMEYLGGGSALDLLEPGPLDE----TQIATILR------EILKGLDYLH---SEKKIHRDIKAANVLLSEHGEVK 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  855 VSDFGLARLLLKfdeesffNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTNEL 924
Cdd:cd06641  142 LADFGVAGQLTD-------TQIKRN*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSEL 204
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
708-916 3.84e-13

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


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 71.02  E-value: 3.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKA----LLLTEKK-VVAVKVLNMQRRGAMKS-FMAECESLKDIRHRNLVKLLTACSSidfqgNEFRALIY 781
Cdd:cd05050   13 IGQGAFGRVFQArapgLLPYEPFtMVAVKMLKEEASADMQAdFQREAALMAEFDHPNIVKLLGVCAV-----GKPMCLLF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 EFMPNGSLDMWLH---PEEVEEIHRPSRT----------LTLLERLNIAIDVASVLDYLhvhCHEPIAHCDLKPSNVLLD 848
Cdd:cd05050   88 EYMAYGDLNEFLRhrsPRAQCSLSHSTSSarkcglnplpLSCTEQLCIAKQVAAGMAYL---SERKFVHRDLATRNCLVG 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  849 DDLTAHVSDFGLARLLL-----KFDEESFFnqlssagvrgTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT 916
Cdd:cd05050  165 ENMVVKIADFGLSRNIYsadyyKASENDAI----------PIRWMPPESIFYNRYTTESDVWAYGVVLWEIFS 227
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
708-925 4.14e-13

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: 71.58  E-value: 4.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLL-------TEKKVVAVKVL-NMQRRGAMKSFMAECESLKDI-RHRNLVKLLTACSsidfQGNEFRa 778
Cdd:cd05101   32 LGEGCFGQVVMAEAVgidkdkpKEAVTVAVKMLkDDATEKDLSDLVSEMEMMKMIgKHKNIINLLGACT----QDGPLY- 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGSLDMWLH---PEEVE---EIHR-PSRTLTLLERLNIAIDVASVLDYLhvhCHEPIAHCDLKPSNVLLDDDL 851
Cdd:cd05101  107 VIVEYASKGNLREYLRarrPPGMEysyDINRvPEEQMTFKDLVSCTYQLARGMEYL---ASQKCIHRDLAARNVLVTENN 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  852 TAHVSDFGLARLLLKFDeesFFNQLSSAgvRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKR-----PTNELF 925
Cdd:cd05101  184 VMKIADFGLARDINNID---YYKKTTNG--RLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTlGGSpypgiPVEELF 258
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
708-935 4.14e-13

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: 70.38  E-value: 4.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVK---VLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFM 784
Cdd:cd08224    8 IGKGQFSVVYRARCLLDGRLVALKkvqIFEMMDAKARQDCLKEIDLLQQLNHPNIIKYLAS-----FIENNELNIVLELA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLDMWLHpeeveeiHRPSRTLTLLERL--NIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLAR 862
Cdd:cd08224   83 DAGDLSRLIK-------HFKKQKRLIPERTiwKYFVQLCSALEHMHSK---RIMHRDIKPANVFITANGVVKLGDLGLGR 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  863 lllkfdeesFFNQLSSAG--VRGTIGYAAPEYgVGGQP-SINGDVYSFGILLLEMFTGKRPtnelFGGNfTLNSYT 935
Cdd:cd08224  153 ---------FFSSKTTAAhsLVGTPYYMSPER-IREQGyDFKSDIWSLGCLLYEMAALQSP----FYGE-KMNLYS 213
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
702-928 4.17e-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: 71.00  E-value: 4.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKV--LNMQRRGAMKSFMAECESLKDIRHRNLVKLLtacssiDFQGNEFRA- 778
Cdd:cd07860    2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKirLDTETEGVPSTAIREISLLKELNHPNIVKLL------DVIHTENKLy 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMpNGSLDMWLHPEEVEEIHRP---SRTLTLLERLNiaidvasvldYLHVHchePIAHCDLKPSNVLLDDDLTAHV 855
Cdd:cd07860   76 LVFEFL-HQDLKKFMDASALTGIPLPlikSYLFQLLQGLA----------FCHSH---RVLHRDLKPQNLLINTEGAIKL 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  856 SDFGLARL----LLKFDEESFfnqlssagvrgTIGYAAPEYGVGGQ-PSINGDVYSFGILLLEMFTGKrptnELFGGN 928
Cdd:cd07860  142 ADFGLARAfgvpVRTYTHEVV-----------TLWYRAPEILLGCKyYSTAVDIWSLGCIFAEMVTRR----ALFPGD 204
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
708-862 4.33e-13

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: 71.03  E-value: 4.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVlnMQRRgaMKSFmAECESLKDIR-------HRNLVKLLTAcssidFQGNEFRALI 780
Cdd:cd07830    7 LGDGTFGSVYLARNKETGELVAIKK--MKKK--FYSW-EECMNLREVKslrklneHPNIVKLKEV-----FRENDELYFV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFMPNGSLDMWLHpeeveeihRPSRTLTLLERLNIAIDVASVLDYLHVHCHepiAHCDLKPSNVLLDDDLTAHVSDFGL 860
Cdd:cd07830   77 FEYMEGNLYQLMKD--------RKGKPFSESVIRSIIYQILQGLAHIHKHGF---FHRDLKPENLLVSGPEVVKIADFGL 145

                 ..
gi 18408454  861 AR 862
Cdd:cd07830  146 AR 147
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
706-927 4.42e-13

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: 71.42  E-value: 4.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMaECESLKDIRHR------NLVKLLtacSSIDFQGneFRAL 779
Cdd:cd14210   19 SVLGKGSFGQVVKCLDHKTGQLVAIKIIRNKKRFHQQALV-EVKILKHLNDNdpddkhNIVRYK---DSFIFRG--HLCI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  780 IYEFmpngsLDMWLHpEEVEEIHRPSRTLTLLERlnIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVS--D 857
Cdd:cd14210   93 VFEL-----LSINLY-ELLKSNNFQGLSLSLIRK--FAKQILQALQFLHKL---NIIHCDLKPENILLKQPSKSSIKviD 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  858 FGLArlllKFDEESFFNQLSSagvRgtiGYAAPE------YGvggqPSIngDVYSFGILLLEMFTGkRPtneLFGG 927
Cdd:cd14210  162 FGSS----CFEGEKVYTYIQS---R---FYRAPEvilglpYD----TAI--DMWSLGCILAELYTG-YP---LFPG 217
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
708-924 4.85e-13

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


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 70.83  E-value: 4.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACssidFQGNEFRALIyEFMPNG 787
Cdd:cd06644   20 LGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYMVEIEILATCNHPYIVKLLGAF----YWDGKLWIMI-EFCPGG 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 SLDMWLHpeEVEeihrpsRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARLLLKF 867
Cdd:cd06644   95 AVDAIML--ELD------RGLTEPQIQVICRQMLEALQYLH---SMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKT 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18408454  868 --DEESFFnqlssagvrGTIGYAAPEY----GVGGQP-SINGDVYSFGILLLEMFTGKRPTNEL 924
Cdd:cd06644  164 lqRRDSFI---------GTPYWMAPEVvmceTMKDTPyDYKADIWSLGITLIEMAQIEPPHHEL 218
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
704-923 5.10e-13

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: 70.13  E-value: 5.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  704 SSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMK--SFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIY 781
Cdd:cd14082    7 PDEVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQesQLRNEVAILQQLSHPGVVNLECM-----FETPERVFVVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 EFMPNGSLDMWLHPEEVEEIHRPSRTLTLlerlniAIDVAsvLDYLHvhcHEPIAHCDLKPSNVLL--DDDLTA-HVSDF 858
Cdd:cd14082   82 EKLHGDMLEMILSSEKGRLPERITKFLVT------QILVA--LRYLH---SKNIVHCDLKPENVLLasAEPFPQvKLCDF 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  859 GLARLLlkfDEESFfnqlsSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTNE 923
Cdd:cd14082  151 GFARII---GEKSF-----RRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNE 207
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
727-984 5.15e-13

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: 70.70  E-value: 5.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  727 VVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACssIDfQGNEFraLIYEFMPNGSLDMWLhpeEVEEIHrpsr 806
Cdd:cd14042   32 LVAIKKVNKKRIDLTREVLKELKHMRDLQHDNLTRFIGAC--VD-PPNIC--ILTEYCPKGSLQDIL---ENEDIK---- 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  807 tLTLLERLNIAIDVASVLDYLHvhCHEPIAHCDLKPSNVLLDDDLTAHVSDFGLArlllKFDEESFFNQLSSAGVRGTIg 886
Cdd:cd14042  100 -LDWMFRYSLIHDIVKGMHYLH--DSEIKSHGNLKSSNCVVDSRFVLKITDFGLH----SFRSGQEPPDDSHAYYAKLL- 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  887 YAAPEY----GVGGQPSINGDVYSFGILLLEMFTGKRPtnelfggnFTLNSYTKSalPERILDIVDESILHIGLRvgfPV 962
Cdd:cd14042  172 WTAPELlrdpNPPPPGTQKGDVYSFGIILQEIATRQGP--------FYEEGPDLS--PKEIIKKKVRNGEKPPFR---PS 238
                        250       260
                 ....*....|....*....|....*
gi 18408454  963 VECLTMVFEVGL---RCCEESPMNR 984
Cdd:cd14042  239 LDELECPDEVLSlmqRCWAEDPEER 263
PLN03150 PLN03150
hypothetical protein; Provisional
91-187 5.66e-13

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 72.93  E-value: 5.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454    91 FLVSLDLYENFFGGTIPQEVGQLSRLEYLDMGINYLRGPIPLGLYNCSRLLNLRLDSNRLGGSVPSELGSLTNLVQLNLY 170
Cdd:PLN03150  419 FIDGLGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLN 498
                          90
                  ....*....|....*..
gi 18408454   171 GNNMRGKLPTSLGNLTL 187
Cdd:PLN03150  499 GNSLSGRVPAALGGRLL 515
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
707-927 5.84e-13

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: 70.42  E-value: 5.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVLnMQRRGA---MKSFMAECESLKDIRHRNLVKLLTACSSidfQGNEFraLIYEF 783
Cdd:cd07833    8 VVGEGAYGVVLKCRNKATGEIVAIKKF-KESEDDedvKKTALREVKVLRQLRHENIVNLKEAFRR---KGRLY--LVFEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  784 MPNGSLDMW------LHPEEVEEIhrpsrTLTLLERLNiaidvasvldYLHVHchePIAHCDLKPSNVLLDDDLTAHVSD 857
Cdd:cd07833   82 VERTLLELLeaspggLPPDAVRSY-----IWQLLQAIA----------YCHSH---NIIHRDIKPENILVSESGVLKLCD 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  858 FGLARlllkfdeesffnQLSSAGVR------GTIGYAAPEYGVG----GQPSingDVYSFGILLLEMFTGkRPtneLFGG 927
Cdd:cd07833  144 FGFAR------------ALTARPASpltdyvATRWYRAPELLVGdtnyGKPV---DVWAIGCIMAELLDG-EP---LFPG 204
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
706-946 6.11e-13

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


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 70.06  E-value: 6.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDI-RHRNLVKLLtACSSIDFQGNEFRALIYEFM 784
Cdd:cd13985    6 KQLGEGGFSYVYLAHDVNTGRRYALKRMYFNDEEQLRVAIKEIEIMKRLcGHPNIVQYY-DSAILSSEGRKEVLLLMEYC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PnGSLdmwlhpeeVEEIH-RPSRTLTLLERLNIAIDVASVLDYLHvHCHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARL 863
Cdd:cd13985   85 P-GSL--------VDILEkSPPSPLSEEEVLRIFYQICQAVGHLH-SQSPPIIHRDIKIENILFSNTGRFKLCDFGSATT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  864 LLKFDE--ESFFNQLSSAGVRGTIGYAAPE-------YGVGGQpsinGDVYSFGILLLEMFTGKRPTNE-----LFGGNF 929
Cdd:cd13985  155 EHYPLEraEEVNIIEEEIQKNTTPMYRAPEmidlyskKPIGEK----ADIWALGCLLYKLCFFKLPFDEssklaIVAGKY 230
                        250       260
                 ....*....|....*....|..
gi 18408454  930 TL---NSYTKS--ALPERILDI 946
Cdd:cd13985  231 SIpeqPRYSPElhDLIRHMLTP 252
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
708-916 7.32e-13

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: 70.31  E-value: 7.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTV----YKALLLTEKKVVAVKVLNMQRRGAMKS-FMAECESLKDIRHRNLVKLLTACSSidfQGNEFRALIYE 782
Cdd:cd05080   12 LGEGHFGKVslycYDPTNDGTGEMVAVKALKADCGPQHRSgWKQEIDILKTLYHENIVKYKGCCSE---QGGKSLQLIME 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLDMWLhpeeveeihrPSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLAR 862
Cdd:cd05080   89 YVPLGSLRDYL----------PKHSIGLAQLLLFAQQICEGMAYLH---SQHYIHRDLAARNVLLDNDRLVKIGDFGLAK 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18408454  863 LLlkfDEESFFNQLSSAGVRGTIGYaAPEYGVGGQPSINGDVYSFGILLLEMFT 916
Cdd:cd05080  156 AV---PEGHEYYRVREDGDSPVFWY-APECLKEYKFYYASDVWSFGVTLYELLT 205
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
701-922 7.35e-13

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: 69.73  E-value: 7.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  701 GFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNM------QRRGAMKsfmaECESLKDIRHRNLVKLLTAcsSIDfqGN 774
Cdd:cd08530    1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLgslsqkEREDSVN----EIRLLASVNHPNIIRYKEA--FLD--GN 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  775 EFrALIYEFMPNGSLdmwlhpeeVEEIHRPSRTLTLLER---LNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDL 851
Cdd:cd08530   73 RL-CIVMEYAPFGDL--------SKLISKRKKKRRLFPEddiWRIFIQMLRGLKALH---DQKILHRDLKSANILLSAGD 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18408454  852 TAHVSDFGLARLLLKfdeesffnQLSSAGVrGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTN 922
Cdd:cd08530  141 LVKIGDLGISKVLKK--------NLAKTQI-GTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFE 202
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
706-920 7.96e-13

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: 69.94  E-value: 7.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTVYKALLlTEKKVVAVKVLNMQRRG--AMKSFMAECESLKDIRHR-NLVKLltacssIDFQGNEFRALIYE 782
Cdd:cd14131    7 KQLGKGGSSKVYKVLN-PKKKIYALKRVDLEGADeqTLQSYKNEIELLKKLKGSdRIIQL------YDYEVTDEDDYLYM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLDM--WLHpeeveeihrpsrtltllERLNIAIDVASVLDY-----LHVH-CHEP-IAHCDLKPSNVLLdddlta 853
Cdd:cd14131   80 VMECGEIDLatILK-----------------KKRPKPIDPNFIRYYwkqmlEAVHtIHEEgIVHSDLKPANFLL------ 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  854 hVS------DFGLARLLLKfDEESF--FNQLssagvrGTIGYAAPE------YGVGGQPSIN----GDVYSFGILLLEMF 915
Cdd:cd14131  137 -VKgrlkliDFGIAKAIQN-DTTSIvrDSQV------GTLNYMSPEaikdtsASGEGKPKSKigrpSDVWSLGCILYQMV 208

                 ....*
gi 18408454  916 TGKRP 920
Cdd:cd14131  209 YGKTP 213
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
706-984 8.22e-13

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: 69.92  E-value: 8.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTV----YKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSidfQGNEFRALIY 781
Cdd:cd05081   10 SQLGKGNFGSVelcrYDPLGDNTGALVAVKQLQHSGPDQQRDFQREIQILKALHSDFIVKYRGVSYG---PGRRSLRLVM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 EFMPNGSLDMWLHPEEveeiHRPSRTLTLLerlnIAIDVASVLDYLHVhchEPIAHCDLKPSNVLLDDDLTAHVSDFGLA 861
Cdd:cd05081   87 EYLPSGCLRDFLQRHR----ARLDASRLLL----YSSQICKGMEYLGS---RRCVHRDLAARNILVESEAHVKIADFGLA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  862 RLLLKfDEESFFNQLSSagvRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT----GKRPTNElfggnftlnsYTKS 937
Cdd:cd05081  156 KLLPL-DKDYYVVREPG---QSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFTycdkSCSPSAE----------FLRM 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 18408454  938 ALPERILDIVDE--SILHIGLRVGFPvVECLTMVFEVGLRCCEESPMNR 984
Cdd:cd05081  222 MGCERDVPALCRllELLEEGQRLPAP-PACPAEVHELMKLCWAPSPQDR 269
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
708-920 8.92e-13

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: 69.32  E-value: 8.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLL-TEKKVVAVKVLNMQRRGAMKSFMA-ECESLKDIRHRNLVKLLtacssiDFQ-GNEFRALIYEFM 784
Cdd:cd14120    1 IGHGAFAVVFKGRHRkKPDLPVAIKCITKKNLSKSQNLLGkEIKILKELSHENVVALL------DCQeTSSSVYLVMEYC 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLDMWLHPEeveeihrpsRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLD---------DDLTAHV 855
Cdd:cd14120   75 NGGDLADYLQAK---------GTLSEDTIRVFLQQIAAAMKALH---SKGIVHRDLKPQNILLShnsgrkpspNDIRLKI 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  856 SDFGLARLLLkfdeesffNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14120  143 ADFGFARFLQ--------DGMMAATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAP 199
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
708-914 1.16e-12

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


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 69.04  E-value: 1.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKV--LNMQRRGAMKsfmaECESLKDIRHRNLVKLLTACssidFQGNEFRALIyEFMP 785
Cdd:cd14155    1 IGSGFFSEVYKVRHRTSGQVMALKMntLSSNRANMLR----EVQLMNRLSHPNILRFMGVC----VHQGQLHALT-EYIN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLDMWLHPEEVeeihrpsrtLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLL---DDDLTAHVSDFGLAR 862
Cdd:cd14155   72 GGNLEQLLDSNEP---------LSWTVRVKLALDIARGLSYLH---SKGIFHRDLTSKNCLIkrdENGYTAVVGDFGLAE 139
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18408454  863 LLLKFDEESffnqlSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEM 914
Cdd:cd14155  140 KIPDYSDGK-----EKLAVVGSPYWMAPEVLRGEPYNEKADVFSYGIILCEI 186
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
707-920 1.31e-12

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: 69.37  E-value: 1.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKA---LLLTEKKVVAVKVLNMQRRGAMKS-FMAECESLKDIRHRNLVKLLTACSsidfqgNEFRALIYE 782
Cdd:cd05056   13 CIGEGQFGDVYQGvymSPENEKIAVAVKTCKNCTSPSVREkFLQEAYIMRQFDHPHIVKLIGVIT------ENPVWIVME 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLDMWLhpeEVEEIHRPSRTLTLLerlniAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLAR 862
Cdd:cd05056   87 LAPLGELRSYL---QVNKYSLDLASLILY-----AYQLSTALAYLE---SKRFVHRDIAARNVLVSSPDCVKLGDFGLSR 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  863 LLlkfDEESFFNqlSSAGvRGTIGYAAPEygvggqpSIN-------GDVYSFGILLLEMFT-GKRP 920
Cdd:cd05056  156 YM---EDESYYK--ASKG-KLPIKWMAPE-------SINfrrftsaSDVWMFGVCMWEILMlGVKP 208
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
708-920 1.36e-12

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: 69.48  E-value: 1.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQR---RGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFM 784
Cdd:cd05577    1 LGRGGFGEVCACQVKATGKMYACKKLDKKRikkKKGETMALNEKIILEKVSSPFIVSLAYA-----FETKDKLCLVLTLM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGslDMWLHPEEVEEihrpsRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLArll 864
Cdd:cd05577   76 NGG--DLKYHIYNVGT-----RGFSEARAIFYAAEIICGLEHLH---NRFIVYRDLKPENILLDDHGHVRISDLGLA--- 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  865 lkfdeESFFNQLSSAGVRGTIGYAAPEYGVGGQP-SINGDVYSFGILLLEMFTGKRP 920
Cdd:cd05577  143 -----VEFKGGKKIKGRVGTHGYMAPEVLQKEVAyDFSVDWFALGCMLYEMIAGRSP 194
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
708-999 1.41e-12

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: 68.70  E-value: 1.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVlnMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSidfqgNEFRALIYEFMPNG 787
Cdd:cd14156    1 IGSGFFSKVYKVTHGATGKVMVVKI--YKNDVDQHKIVREISLLQKLSHPNIVRYLGICVK-----DEKLHPILEYVSGG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 SLDMWLHPEEVeeihrpsrTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLL---DDDLTAHVSDFGLARLL 864
Cdd:cd14156   74 CLEELLAREEL--------PLSWREKVELACDISRGMVYLH---SKNIYHRDLNSKNCLIrvtPRGREAVVTDFGLAREV 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  865 LKFDEESFFNQLSsagVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFtGKRPTN-------ELFGGNFTLNSYTKS 937
Cdd:cd14156  143 GEMPANDPERKLS---LVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEIL-ARIPADpevlprtGDFGLDVQAFKEMVP 218
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  938 ALPERILDIVDEsilhiglrvgfpvvecltmvfevglrCCEESPMNRLATSIVVKELISIRE 999
Cdd:cd14156  219 GCPEPFLDLAAS--------------------------CCRMDAFKRPSFAELLDELEDIAE 254
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
708-923 1.51e-12

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: 68.98  E-value: 1.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALllTEKKVVAVKVLNMQRRGAMKS----FMAECESLKDIRHRNLVKLLTACSSIdFQGNEFRALIYEF 783
Cdd:cd14031   18 LGRGAFKTVYKGL--DTETWVEVAWCELQDRKLTKAeqqrFKEEAEMLKGLQHPNIVRFYDSWESV-LKGKKCIVLVTEL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  784 MPNGSLDMWLHPEEVeeiHRPSRTLTLLERlniaidVASVLDYLHVHChEPIAHCDLKPSNVLLDDDL-TAHVSDFGLAR 862
Cdd:cd14031   95 MTSGTLKTYLKRFKV---MKPKVLRSWCRQ------ILKGLQFLHTRT-PPIIHRDLKCDNIFITGPTgSVKIGDLGLAT 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  863 LLlkfdEESFfnqlsSAGVRGTIGYAAPE-YGVGGQPSIngDVYSFGILLLEMFTGKRPTNE 923
Cdd:cd14031  165 LM----RTSF-----AKSVIGTPEFMAPEmYEEHYDESV--DVYAFGMCMLEMATSEYPYSE 215
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
708-920 1.54e-12

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: 69.28  E-value: 1.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLL-----TEKKVVAVKVLNMQRRGAMKS-FMAECESLKDIRHRNLVKLLTACSSidfqgNEFRALIY 781
Cdd:cd05091   14 LGEDRFGKVYKGHLFgtapgEQTQAVAIKTLKDKAEGPLREeFRHEAMLRSRLQHPNIVCLLGVVTK-----EQPMSMIF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 EFMPNGSLDMWL-----HPE--EVEEIHRPSRTLTLLERLNIAIDVASVLDYLHVHcHepIAHCDLKPSNVLLDDDLTAH 854
Cdd:cd05091   89 SYCSHGDLHEFLvmrspHSDvgSTDDDKTVKSTLEPADFLHIVTQIAAGMEYLSSH-H--VVHKDLATRNVLVFDKLNVK 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  855 VSDFGLARLLLKFDeesFFNQLSSAGVrgTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRP 920
Cdd:cd05091  166 ISDLGLFREVYAAD---YYKLMGNSLL--PIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSyGLQP 227
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
708-920 1.79e-12

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: 69.44  E-value: 1.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKV---LNMQRRGAMKsfMAECESLKDIRHRNLVKLLTACSSIDFQGnefRALIYEFM 784
Cdd:cd13988    1 LGQGATANVFRGRHKKTGDLYAVKVfnnLSFMRPLDVQ--MREFEVLKKLNHKNIVKLFAIEEELTTRH---KVLVMELC 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSL-DMWLHPEEveeihrpSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVL--LDDDLTA--HVSDFG 859
Cdd:cd13988   76 PCGSLyTVLEEPSN-------AYGLPESEFLIVLRDVVAGMNHLR---ENGIVHRDIKPGNIMrvIGEDGQSvyKLTDFG 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  860 LARLLLkfDEESFfnqlssAGVRGTIGYAAP---EYGV-----GGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd13988  146 AARELE--DDEQF------VSLYGTEEYLHPdmyERAVlrkdhQKKYGATVDLWSIGVTFYHAATGSLP 206
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
708-925 2.15e-12

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: 69.22  E-value: 2.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKK-------VVAVKVLNMQRRGA-MKSFMAECESLKDI-RHRNLVKLLTACSSidfQGNEFra 778
Cdd:cd05099   20 LGEGCFGQVVRAEAYGIDKsrpdqtvTVAVKMLKDNATDKdLADLISEMELMKLIgKHKNIINLLGVCTQ---EGPLY-- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGSLDMWLH------PEEVEEIHR-PSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDL 851
Cdd:cd05099   95 VIVEYAAKGNLREFLRarrppgPDYTFDITKvPEEQLSFKDLVSCAYQVARGMEYLE---SRRCIHRDLAARNVLVTEDN 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  852 TAHVSDFGLARLLLKFDeesFFNQLSSAgvRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKR-----PTNELF 925
Cdd:cd05099  172 VMKIADFGLARGVHDID---YYKKTSNG--RLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTlGGSpypgiPVEELF 246
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
708-920 2.31e-12

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: 68.12  E-value: 2.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGtvyKALLLTEKKV---VAVKVLNMQRRgAMKSFMAE-CESLKDIRHRNLVKLLtacsSIDFQGNEFRALIYEF 783
Cdd:cd13987    1 LGEGTYG---KVLLAVHKGSgtkMALKFVPKPST-KLKDFLREyNISLELSVHPHIIKTY----DVAFETEDYYVFAQEY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  784 MPNGSLDMWLHPEE-VEEiHRPSRtltllerlnIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLL-DDDLT-AHVSDFGL 860
Cdd:cd13987   73 APYGDLFSIIPPQVgLPE-ERVKR---------CAAQLASALDFMH---SKNLVHRDIKPENVLLfDKDCRrVKLCDFGL 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  861 AR---LLLKFdeesffnqlssagVRGTIGYAAPEY-------GVGGQPSIngDVYSFGILLLEMFTGKRP 920
Cdd:cd13987  140 TRrvgSTVKR-------------VSGTIPYTAPEVceakkneGFVVDPSI--DVWAFGVLLFCCLTGNFP 194
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
708-930 2.38e-12

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: 68.07  E-value: 2.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEK--KVVAVKVL-NMQRRGAMK-SFMAECESLKDIRHRNLVKLLTACSSidfqgnEFRALIYEF 783
Cdd:cd05116    3 LGSGNFGTVKKGYYQMKKvvKTVAVKILkNEANDPALKdELLREANVMQQLDNPYIVRMIGICEA------ESWMLVMEM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  784 MPNGSLDMWLHPEE-------VEEIHRPSRTLTLLERLNIAidvasvldylhvhchepiaHCDLKPSNVLLDDDLTAHVS 856
Cdd:cd05116   77 AELGPLNKFLQKNRhvtekniTELVHQVSMGMKYLEESNFV-------------------HRDLAARNVLLVTQHYAKIS 137
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  857 DFGLARLLLKfdEESFFnQLSSAGvRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRPTNELFGGNFT 930
Cdd:cd05116  138 DFGLSKALRA--DENYY-KAQTHG-KWPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKPYKGMKGNEVT 208
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
709-920 2.47e-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: 68.58  E-value: 2.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVykaLLLTEK---KVVAVKVLNMQRRGAMKSF---MAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYE 782
Cdd:cd14209   10 GTGSFGRV---MLVRHKetgNYYAMKILDKQKVVKLKQVehtLNEKRILQAINFPFLVKLEYS-----FKDNSNLYMVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGslDMWLHpeeveeiHRPSRTLTLLERLNIAIDVASVLDYLHvHCHepIAHCDLKPSNVLLDDDLTAHVSDFGLAR 862
Cdd:cd14209   82 YVPGG--EMFSH-------LRRIGRFSEPHARFYAAQIVLAFEYLH-SLD--LIYRDLKPENLLIDQQGYIKVTDFGFAK 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  863 LLlkfdeesffnQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14209  150 RV----------KGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPP 197
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
707-928 2.97e-12

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: 68.60  E-value: 2.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAM--KSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFM 784
Cdd:cd07846    8 LVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMvkKIAMREIKMLKQLRHENLVNLIEV-----FRRKKRWYLVFEFV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLDmwlhpeeveEIHRPSRTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLARLL 864
Cdd:cd07846   83 DHTVLD---------DLEKYPNGLDESRVRKYLFQILRGIDFCHSH---NIIHRDIKPENILVSQSGVVKLCDFGFARTL 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  865 LKfDEESFFNQLSsagvrgTIGYAAPEYGVG----GQPSingDVYSFGILLLEMFTGkrptNELFGGN 928
Cdd:cd07846  151 AA-PGEVYTDYVA------TRWYRAPELLVGdtkyGKAV---DVWAVGCLVTEMLTG----EPLFPGD 204
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
702-920 3.48e-12

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: 68.80  E-value: 3.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLnmQRRGAMKSFMAECESLKD------IRHRNLVKLLtaCSsidFQGNE 775
Cdd:cd05619    7 FVLHKMLGKGSFGKVFLAELKGTNQFFAIKAL--KKDVVLMDDDVECTMVEKrvlslaWEHPFLTHLF--CT---FQTKE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  776 FRALIYEFMPNGslDMWLHPEEVEEIHRPSRTLtllerlnIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHV 855
Cdd:cd05619   80 NLFFVMEYLNGG--DLMFHIQSCHKFDLPRATF-------YAAEIICGLQFLH---SKGIVYRDLKLDNILLDKDGHIKI 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  856 SDFGLARlllkfdeESFFNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd05619  148 ADFGMCK-------ENMLGDAKTSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSP 205
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
706-994 3.51e-12

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: 68.49  E-value: 3.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAM---KSFMAECESLKDI-RHRNLVKLLTACssidfqgnEFRALIY 781
Cdd:cd05088   13 DVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKddhRDFAGELEVLCKLgHHPNIINLLGAC--------EHRGYLY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 ---EFMPNGSLDMWLHPEEVEEI-------HRPSRTLTLLERLNIAIDVASVLDYLhvhCHEPIAHCDLKPSNVLLDDDL 851
Cdd:cd05088   85 laiEYAPHGNLLDFLRKSRVLETdpafaiaNSTASTLSSQQLLHFAADVARGMDYL---SQKQFIHRDLAARNILVGENY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  852 TAHVSDFGLARlllkfDEESFFNQLSSagvRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRPtnelFGGNFT 930
Cdd:cd05088  162 VAKIADFGLSR-----GQEVYVKKTMG---RLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTP----YCGMTC 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18408454  931 LNSYTKsalperildivdesiLHIGLRVGFPvVECLTMVFEVGLRCCEESPMNRLATSIVVKEL 994
Cdd:cd05088  230 AELYEK---------------LPQGYRLEKP-LNCDDEVYDLMRQCWREKPYERPSFAQILVSL 277
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
708-927 3.61e-12

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


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 68.28  E-value: 3.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQ-RRGAMKSFMAECESLKDIRHRNLVKLLtacssiDFQGNEFR-ALIYEFMp 785
Cdd:cd07836    8 LGEGTYATVYKGRNRTTGEIVALKEIHLDaEEGTPSTAIREISLMKELKHENIVRLH------DVIHTENKlMLVFEYM- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLDMWLhpeeveEIHRPSRTLTLLERLNIAIDVASVLDYlhvhCHE-PIAHCDLKPSNVLLDDDLTAHVSDFGLARll 864
Cdd:cd07836   81 DKDLKKYM------DTHGVRGALDPNTVKSFTYQLLKGIAF----CHEnRVLHRDLKPQNLLINKRGELKLADFGLAR-- 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  865 lkfdeeSF---FNQLSSAGVrgTIGYAAPEYGVGGQP-SINGDVYSFGILLLEMFTGkRPtneLFGG 927
Cdd:cd07836  149 ------AFgipVNTFSNEVV--TLWYRAPDVLLGSRTySTSIDIWSVGCIMAEMITG-RP---LFPG 203
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
707-920 3.99e-12

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: 68.45  E-value: 3.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVLNMQ---RRGAMKSFMAECESL-KDIRHRNLVKLltacsSIDFQGNEFRALIYE 782
Cdd:cd05604    3 VIGKGSFGKVLLAKRKRDGKYYAVKVLQKKvilNRKEQKHIMAERNVLlKNVKHPFLVGL-----HYSFQTTDKLYFVLD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLDMWLHPEeveeihrpsRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLAR 862
Cdd:cd05604   78 FVNGGELFFHLQRE---------RSFPEPRARFYAAEIASALGYLH---SINIVYRDLKPENILLDSQGHIVLTDFGLCK 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  863 lllkfdeESFFNQLSSAGVRGTIGYAAPEYgVGGQPSING-DVYSFGILLLEMFTGKRP 920
Cdd:cd05604  146 -------EGISNSDTTTTFCGTPEYLAPEV-IRKQPYDNTvDWWCLGSVLYEMLYGLPP 196
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
708-924 4.15e-12

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


Pssm-ID: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 67.61  E-value: 4.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMK---SFMAECESLKDIRHRNLVKLLTAC-SSIDFqgnefrALIYEF 783
Cdd:cd05042    3 IGNGWFGKVLLGEIYSGTSVAQVVVKELKASANPKeqdTFLKEGQPYRILQHPNILQCLGQCvEAIPY------LLVMEF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  784 MPNGSLDMWLHPEEVEEihRPSRTLTLLERLniAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLARl 863
Cdd:cd05042   77 CDLGDLKAYLRSEREHE--RGDSDTRTLQRM--ACEVAAGLAHLHKL---NFVHSDLALRNCLLTSDLTVKIGDYGLAH- 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  864 lLKFDEESFfnqLSSAGVRGTIGYAAPE--------YGVGGQpSINGDVYSFGILLLEMFT-GKRPTNEL 924
Cdd:cd05042  149 -SRYKEDYI---ETDDKLWFPLRWTAPElvtefhdrLLVVDQ-TKYSNIWSLGVTLWELFEnGAQPYSNL 213
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
734-921 4.26e-12

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: 67.68  E-value: 4.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  734 NMQRRGAMKSFM---AECESLKDIRHRNLVKLLtacssidfqGNEFRALIY--EFMPNGSLDMWLhpeevEEIHRPSRTL 808
Cdd:cd14067   44 HLRAADAMKNFSefrQEASMLHSLQHPCIVYLI---------GISIHPLCFalELAPLGSLNTVL-----EENHKGSSFM 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  809 TLLERLN--IAIDVASVLDYLHvhcHEPIAHCDLKPSNVLL-DDDLTAHV----SDFGLARlllkfdeESFFNqlSSAGV 881
Cdd:cd14067  110 PLGHMLTfkIAYQIAAGLAYLH---KKNIIFCDLKSDNILVwSLDVQEHIniklSDYGISR-------QSFHE--GALGV 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 18408454  882 RGTIGYAAPEYgvggQPSI----NGDVYSFGILLLEMFTGKRPT 921
Cdd:cd14067  178 EGTPGYQAPEI----RPRIvydeKVDMFSYGMVLYELLSGQRPS 217
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
702-920 5.08e-12

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: 68.13  E-value: 5.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTE----KKVVAVKVL-NMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSIDFQgnef 776
Cdd:cd05108    9 FKKIKVLGSGAFGTVYKGLWIPEgekvKIPVAIKELrEATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQ---- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  777 raLIYEFMPNGSLDMWLHpEEVEEIhrPSRTLtllerLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVS 856
Cdd:cd05108   85 --LITQLMPFGCLLDYVR-EHKDNI--GSQYL-----LNWCVQIAKGMNYLE---DRRLVHRDLAARNVLVKTPQHVKIT 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  857 DFGLARLLLKfDEESFfnqlSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRP 920
Cdd:cd05108  152 DFGLAKLLGA-EEKEY----HAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTfGSKP 211
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
708-920 5.37e-12

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: 67.02  E-value: 5.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKAL-LLTEKKVvAVKVLNMQRRGA-MKSFMAECESLKDIRHRNLVKLltacssidFQGNEFRALIY---E 782
Cdd:cd14078   11 IGSGGFAKVKLAThILTGEKV-AIKIMDKKALGDdLPRVKTEIEALKNLSHQHICRL--------YHVIETDNKIFmvlE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLdmwlhpeeVEEIHRPSRtLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLA- 861
Cdd:cd14078   82 YCPGGEL--------FDYIVAKDR-LSEDEARVFFRQIVSAVAYVH---SQGYAHRDLKPENLLLDEDQNLKLIDFGLCa 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  862 --RLLLKFdeesffnQLSSAGvrGTIGYAAPEYgVGGQPSI--NGDVYSFGILLLEMFTGKRP 920
Cdd:cd14078  150 kpKGGMDH-------HLETCC--GSPAYAAPEL-IQGKPYIgsEADVWSMGVLLYALLCGFLP 202
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
701-923 6.16e-12

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


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 66.81  E-value: 6.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  701 GFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNmQRRGA----MKSFMAECESLKDIRHRNLVKLLtacSSIDFQGnef 776
Cdd:cd14164    1 GYTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVD-RRRASpdfvQKFLPRELSILRRVNHPNIVQMF---ECIEVAN--- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  777 rALIYEFMPNGSLDM--WLHpeeveEIHRPSRTLTllerLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLD-DDLTA 853
Cdd:cd14164   74 -GRLYIVMEAAATDLlqKIQ-----EVHHIPKDLA----RDMFAQMVGAVNYLHDM---NIVHRDLKCENILLSaDDRKI 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  854 HVSDFGLARlllkfdEESFFNQLSSAGVrGTIGYAAPEY--GVGGQPSiNGDVYSFGILLLEMFTGKRPTNE 923
Cdd:cd14164  141 KIADFGFAR------FVEDYPELSTTFC-GSRAYTPPEVilGTPYDPK-KYDVWSLGVVLYVMVTGTMPFDE 204
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
707-924 7.68e-12

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: 66.61  E-value: 7.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVLNMQR-----RGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIY 781
Cdd:cd06625    7 LLGQGAFGQVYLCYDADTGRELAVKQVEIDPinteaSKEVKALECEIQLLKNLQHERIVQYYGC-----LQDEKSLSIFM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 EFMPNGSLDmwlhpEEVEEIHRPSRTLT------LLERLNiaidvasvldYLHVHchePIAHCDLKPSNVLLDDDLTAHV 855
Cdd:cd06625   82 EYMPGGSVK-----DEIKAYGALTENVTrkytrqILEGLA----------YLHSN---MIVHRDIKGANILRDSNGNVKL 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  856 SDFGLARLLlkfdeESFFNQLSSAGVRGTIGYAAPEYgvggqpsING-------DVYSFGILLLEMFTGKRPTNEL 924
Cdd:cd06625  144 GDFGASKRL-----QTICSSTGMKSVTGTPYWMSPEV-------INGegygrkaDIWSVGCTVVEMLTTKPPWAEF 207
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
701-923 7.69e-12

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: 66.55  E-value: 7.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  701 GFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNmqRRGAMKSFMA-----ECESLKDIRHRNLVKLLTACSSIDfqGNE 775
Cdd:cd14163    1 GYQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIID--KSGGPEEFIQrflprELQIVERLDHKNIIHVYEMLESAD--GKI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  776 FraLIYEFMPNGSL-DMWLHPEEVEEihrpSRTLTLLERLNIAIDvasvldylhvHCHE-PIAHCDLKPSNVLLdDDLTA 853
Cdd:cd14163   77 Y--LVMELAEDGDVfDCVLHGGPLPE----HRAKALFRQLVEAIR----------YCHGcGVAHRDLKCENALL-QGFTL 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  854 HVSDFGLARLLLKFDEEsffnqlSSAGVRGTIGYAAPEYgVGGQP--SINGDVYSFGILLLEMFTGKRPTNE 923
Cdd:cd14163  140 KLTDFGFAKQLPKGGRE------LSQTFCGSTAYAAPEV-LQGVPhdSRKGDIWSMGVVLYVMLCAQLPFDD 204
PLN03150 PLN03150
hypothetical protein; Provisional
167-290 7.73e-12

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 69.07  E-value: 7.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   167 LNLYGNNMRGKLPTSLGNLTLLEQLALSHNNLEGEIPSDVAQLTQIWSLQLVANNFSGVFPPALYNLSSLKLLGIGYNHF 246
Cdd:PLN03150  423 LGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSL 502
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 18408454   247 SGRLRPDLGILLPNLLSFNMGGNYFTGSIP---TTLSNISTLERLGM 290
Cdd:PLN03150  503 SGRVPAALGGRLLHRASFNFTDNAGLCGIPglrACGPHLSVGAKIGI 549
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
702-913 8.40e-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: 66.56  E-value: 8.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRG--AMKSFMAECESLKDI-RHRNLVKLLTACSSIDfqgnefRA 778
Cdd:cd14050    3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGekDRKRKLEEVERHEKLgEHPNCVRFIKAWEEKG------IL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGSLDMWLhpeevEEIHR-PSRTLtllerLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSD 857
Cdd:cd14050   77 YIQTELCDTSLQQYC-----EETHSlPESEV-----WNILLDLLKGLKHLHDH---GLIHLDIKPANIFLSKDGVCKLGD 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  858 FGlarLLLKFDEESFFNQLSsagvrGTIGYAAPEYgVGGQPSINGDVYSFGILLLE 913
Cdd:cd14050  144 FG---LVVELDKEDIHDAQE-----GDPRYMAPEL-LQGSFTKAADIFSLGITILE 190
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
709-918 8.49e-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: 67.34  E-value: 8.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVYKALLLTEKKVVAVKVLNM--QRRGAMKSFMAECESLKDIRHRNLVKLLTACSSIDFQGNEFRALIYEFMPN 786
Cdd:cd07866   17 GEGTFGEVYKARQIKTGRVVALKKILMhnEKDGFPITALREIKILKKLKHPNVVPLIDMAVERPDKSKRKRGSVYMVTPY 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  787 GSLDM--WLHPEEV--EEIHRPSRTLTLLERLNiaidvasvldYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLAR 862
Cdd:cd07866   97 MDHDLsgLLENPSVklTESQIKCYMLQLLEGIN----------YLH---ENHILHRDIKAANILIDNQGILKIADFGLAR 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  863 LllkFDEESFFNQLSSAGVRG-------TIGYAAPEYGVGGQ---PSIngDVYSFGILLLEMFTGK 918
Cdd:cd07866  164 P---YDGPPPNPKGGGGGGTRkytnlvvTRWYRPPELLLGERrytTAV--DIWGIGCVFAEMFTRR 224
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
708-928 8.49e-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: 8.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKV--LNMQRRGAMKSFMAECESLKDIRHRNLVKLLtacsSIDFQGNEFRaLIYEFMp 785
Cdd:cd07861    8 IGEGTYGVVYKGRNKKTGQIVAMKKirLESEEEGVPSTAIREISLLKELQHPNIVCLE----DVLMQENRLY-LVFEFL- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 ngSLDMWLHPEEVeeihrpsrtltlleRLNIAIDVASVLDYLH------VHCHEP-IAHCDLKPSNVLLDDDLTAHVSDF 858
Cdd:cd07861   82 --SMDLKKYLDSL--------------PKGKYMDAELVKSYLYqilqgiLFCHSRrVLHRDLKPQNLLIDNKGVIKLADF 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  859 GLARlllkfdeeSFfnqlsSAGVRG------TIGYAAPEYGVGGQP-SINGDVYSFGILLLEMFTgKRPtneLFGGN 928
Cdd:cd07861  146 GLAR--------AF-----GIPVRVythevvTLWYRAPEVLLGSPRySTPVDIWSIGTIFAEMAT-KKP---LFHGD 205
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
708-928 9.59e-12

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: 66.61  E-value: 9.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAmksfmaecESLKDIRHRnlVKLLTACSSID--------FQGNEFRAL 779
Cdd:cd14106   16 LGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQ--------DCRNEILHE--IAVLELCKDCPrvvnlhevYETRSELIL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  780 IYEFMPNGSLDMWLHPEEVeeihrpsrtltLLERlniaiDVA----SVLDYLHvHCHE-PIAHCDLKPSNVLL-----DD 849
Cdd:cd14106   86 ILELAAGGELQTLLDEEEC-----------LTEA-----DVRrlmrQILEGVQ-YLHErNIVHLDLKPQNILLtsefpLG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  850 DLTahVSDFGLARLLLKfdeesffnqlsSAGVR---GTIGYAAPE---YgvggQP-SINGDVYSFGILLLEMFTGKRPtn 922
Cdd:cd14106  149 DIK--LCDFGISRVIGE-----------GEEIReilGTPDYVAPEilsY----EPiSLATDMWSIGVLTYVLLTGHSP-- 209

                 ....*.
gi 18408454  923 elFGGN 928
Cdd:cd14106  210 --FGGD 213
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
709-924 1.03e-11

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: 66.98  E-value: 1.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVY--KALLLTEKKV--------------VAVKVLnmqRRGAMKS----FMAECESLKDIRHRNLVKLLTACSS 768
Cdd:cd05051   14 GEGQFGEVHlcEANGLSDLTSddfigndnkdepvlVAVKML---RPDASKNaredFLKEVKIMSQLKDPNIVRLLGVCTR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  769 idfqgNEFRALIYEFMPNGSLDMWLH---PEEVEEIHRPSRTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNV 845
Cdd:cd05051   91 -----DEPLCMIVEYMENGDLNQFLQkheAETQGASATNSKTLSYGTLLYMATQIASGMKYLESL---NFVHRDLATRNC 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  846 LLDDDLTAHVSDFGLARLLLKFDeesFFNqlssagVRGT----IGYAAPEYGVGGQPSINGDVYSFGILLLEMFT--GKR 919
Cdd:cd05051  163 LVGPNYTIKIADFGMSRNLYSGD---YYR------IEGRavlpIRWMAWESILLGKFTTKSDVWAFGVTLWEILTlcKEQ 233

                 ....*
gi 18408454  920 PTNEL 924
Cdd:cd05051  234 PYEHL 238
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
702-920 1.05e-11

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: 66.59  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVK---VLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRA 778
Cdd:cd08228    4 FQIEKKIGRGQFSEVYRATCLLDRKPVALKkvqIFEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDS-----FIEDNELN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGSLDMWLHPEEVEEIHRPSRTLtllerLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDF 858
Cdd:cd08228   79 IVLELADAGDLSQMIKYFKKQKRLIPERTV-----WKYFVQLCSAVEHMH---SRRVMHRDIKPANVFITATGVVKLGDL 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18408454  859 GLARlllkfdeesFFNQLSSAG--VRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd08228  151 GLGR---------FFSSKTTAAhsLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSP 205
PLN03150 PLN03150
hypothetical protein; Provisional
341-430 1.10e-11

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 68.69  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   341 LGIGRNRLGGDLPISIANLSaKLVTLDLGGTLISGSIPYDIGNLINLQKLILDQNMLSGPLPTSLGKLLNLRYLSLFSNR 420
Cdd:PLN03150  423 LGLDNQGLRGFIPNDISKLR-HLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNS 501
                          90
                  ....*....|
gi 18408454   421 LSGGIPAFIG 430
Cdd:PLN03150  502 LSGRVPAALG 511
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
702-920 1.12e-11

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: 66.73  E-value: 1.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNM----------QRRGAMKSfmaeceSLKDIRHRNLVKLLTACssidF 771
Cdd:cd06917    3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNLdtddddvsdiQKEVALLS------QLKLGQPKNIIKYYGSY----L 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  772 QGNEFrALIYEFMPNGSLDMWLHPEEVEEIHrpsrtLTLLERlniaiDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDL 851
Cdd:cd06917   73 KGPSL-WIIMDYCEGGSIRTLMRAGPIAERY-----IAVIMR-----EVLVALKFIH---KDGIIHRDIKAANILVTNTG 138
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  852 TAHVSDFGLARLLLKfdeesffNQLSSAGVRGTIGYAAPEYGVGGQP-SINGDVYSFGILLLEMFTGKRP 920
Cdd:cd06917  139 NVKLCDFGVAASLNQ-------NSSKRSTFVGTPYWMAPEVITEGKYyDTKADIWSLGITTYEMATGNPP 201
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
708-914 1.20e-11

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: 66.73  E-value: 1.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKkvVAVKVLNMQRRgamKSFMAECESLKDI--RHRNLVKLLTAcssiDFQGNEFRA---LIYE 782
Cdd:cd14144    3 VGKGRYGEVWKGKWRGEK--VAVKIFFTTEE---ASWFRETEIYQTVlmRHENILGFIAA----DIKGTGSWTqlyLITD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLDMWLHpeeveeihrpSRTLTLLERLNIAIDVASVLDYLHVHCH----EP-IAHCDLKPSNVLLDDDLTAHVSD 857
Cdd:cd14144   74 YHENGSLYDFLR----------GNTLDTQSMLKLAYSAACGLAHLHTEIFgtqgKPaIAHRDIKSKNILVKKNGTCCIAD 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  858 FGLArllLKFDEESFFNQLSSAGVRGTIGYAAPEYGVGG------QPSINGDVYSFGILLLEM 914
Cdd:cd14144  144 LGLA---VKFISETNEVDLPPNTRVGTKRYMAPEVLDESlnrnhfDAYKMADMYSFGLVLWEI 203
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
708-923 1.21e-11

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 66.61  E-value: 1.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALllTEKKVVAVKVLNMQRRGAMKS----FMAECESLKDIRHRNLVKLLTACSSiDFQGNEFRALIYEF 783
Cdd:cd14030   33 IGRGSFKTVYKGL--DTETTVEVAWCELQDRKLSKSerqrFKEEAGMLKGLQHPNIVRFYDSWES-TVKGKKCIVLVTEL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  784 MPNGSLDMWLHPEEVEEIhrpsRTLTLLERlniaiDVASVLDYLHVHChEPIAHCDLKPSNVLLDDDL-TAHVSDFGLAR 862
Cdd:cd14030  110 MTSGTLKTYLKRFKVMKI----KVLRSWCR-----QILKGLQFLHTRT-PPIIHRDLKCDNIFITGPTgSVKIGDLGLAT 179
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  863 LllkfDEESFfnqlsSAGVRGTIGYAAPE-YGVGGQPSIngDVYSFGILLLEMFTGKRPTNE 923
Cdd:cd14030  180 L----KRASF-----AKSVIGTPEFMAPEmYEEKYDESV--DVYAFGMCMLEMATSEYPYSE 230
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
696-924 1.21e-11

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 68.14  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   696 RNATNGFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAecesLKDIRHRNLVKLLTACSSIDFQGNE 775
Cdd:PTZ00036   62 RSPNKSYKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVLQDPQYKNRELLI----MKNLNHINIIFLKDYYYTECFKKNE 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   776 ---FRALIYEFMPNGsldmwLHpEEVEEIHRPSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDL- 851
Cdd:PTZ00036  138 kniFLNVVMEFIPQT-----VH-KYMKHYARNNHALPLFLVKLYSYQLCRALAYIH---SKFICHRDLKPQNLLIDPNTh 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   852 TAHVSDFGLARLLLKfdeesffNQLSSAGVRGTIgYAAPEYGVGGQP-SINGDVYSFGILLLEM------FTGKRPTNEL 924
Cdd:PTZ00036  209 TLKLCDFGSAKNLLA-------GQRSVSYICSRF-YRAPELMLGATNyTTHIDLWSLGCIIAEMilgypiFSGQSSVDQL 280
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
702-920 1.46e-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: 66.15  E-value: 1.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLN---MQRrgamKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRA 778
Cdd:cd14113    9 YSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNkklMKR----DQVTHELGVLQSLQHPQLVGLLDT-----FETPTSYI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGSL----DMW--LHPEEVEEIHRpsrtltllerlniaiDVASVLDYLHvHCHepIAHCDLKPSNVLLDDDL- 851
Cdd:cd14113   80 LVLEMADQGRLldyvVRWgnLTEEKIRFYLR---------------EILEALQYLH-NCR--IAHLDLKPENILVDQSLs 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18408454  852 --TAHVSDFGLArllLKFDEESFFNQLssagvRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14113  142 kpTIKLADFGDA---VQLNTTYYIHQL-----LGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSP 204
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
702-920 1.47e-11

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: 66.20  E-value: 1.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQR---RGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRA 778
Cdd:cd05630    2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRikkRKGEAMALNEKQILEKVNSRFVVSLAYA-----YETKDALC 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGslDMWLHPEEVEEIHRPSRTLTLLerlniAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDF 858
Cdd:cd05630   77 LVLTLMNGG--DLKFHIYHMGQAGFPEARAVFY-----AAEICCGLEDLH---RERIVYRDLKPENILLDDHGHIRISDL 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  859 GLArllLKFDEESffnqlSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd05630  147 GLA---VHVPEGQ-----TIKGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSP 200
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
683-920 1.49e-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: 66.67  E-value: 1.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  683 LEVLHEKISYGDLRNATNGFSSsnmVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKL 762
Cdd:cd06656    5 LEKLRSIVSVGDPKKKYTRFEK---IGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  763 LTACssidFQGNEFrALIYEFMPNGSLDmwlhpEEVEEihrpsrtlTLLERLNIAI---DVASVLDYLHVHchePIAHCD 839
Cdd:cd06656   82 LDSY----LVGDEL-WVVMEYLAGGSLT-----DVVTE--------TCMDEGQIAAvcrECLQALDFLHSN---QVIHRD 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  840 LKPSNVLLDDDLTAHVSDFGLARLLLKfdeesffNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKR 919
Cdd:cd06656  141 IKSDNILLGMDGSVKLTDFGFCAQITP-------EQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEP 213

                 .
gi 18408454  920 P 920
Cdd:cd06656  214 P 214
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
709-930 1.52e-11

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: 65.87  E-value: 1.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVYKALLLTEKKVVAVKVLNMQR---RGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFMP 785
Cdd:cd14073   10 GKGTYGKVKLAIERATGREVAIKSIKKDKiedEQDMVRIRREIEIMSSLNHPHIIRIYEV-----FENKDKIVIVMEYAS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLdmwlhPEEVEEIHRpsrtLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLARLll 865
Cdd:cd14073   85 GGEL-----YDYISERRR----LPEREARRIFRQIVSAVHYCHKN---GVVHRDLKLENILLDQNGNAKIADFGLSNL-- 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  866 kFDEESFFNQLSsagvrGTIGYAAPEYgVGGQPSINGDV--YSFGILLLEMFTGKRPtnelFGG-NFT 930
Cdd:cd14073  151 -YSKDKLLQTFC-----GSPLYASPEI-VNGTPYQGPEVdcWSLGVLLYTLVYGTMP----FDGsDFK 207
PLN03150 PLN03150
hypothetical protein; Provisional
366-454 1.55e-11

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 68.30  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   366 LDLGGTLISGSIPYDIGNLINLQKLILDQNMLSGPLPTSLGKLLNLRYLSLFSNRLSGGIPAFIGNMTMLETLDLSNNGF 445
Cdd:PLN03150  423 LGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSL 502

                  ....*....
gi 18408454   446 EGIVPTSLG 454
Cdd:PLN03150  503 SGRVPAALG 511
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
702-925 1.57e-11

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: 66.23  E-value: 1.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNM-----VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRG-AMKSFMAECESLKdiRHRNlvklltaCSSI-DFQGN 774
Cdd:cd06616    3 FTAEDLkdlgeIGRGAFGTVNKMLHKPSGTIMAVKRIRSTVDEkEQKRLLMDLDVVM--RSSD-------CPYIvKFYGA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  775 EFR---ALI-YEFMpNGSLD---MWLHpeEVEEIHRPSRTLTllerlNIAIDVASVLDYLHVHCHepIAHCDLKPSNVLL 847
Cdd:cd06616   74 LFRegdCWIcMELM-DISLDkfyKYVY--EVLDSVIPEEILG-----KIAVATVKALNYLKEELK--IIHRDVKPSNILL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  848 DDDLTAHVSDFGLARLLlkfdEESfFNQLSSAGVRgtiGYAAPEYgvgGQPS-------INGDVYSFGILLLEMFTGKRP 920
Cdd:cd06616  144 DRNGNIKLCDFGISGQL----VDS-IAKTRDAGCR---PYMAPER---IDPSasrdgydVRSDVWSLGITLYEVATGKFP 212

                 ....*...
gi 18408454  921 T---NELF 925
Cdd:cd06616  213 YpkwNSVF 220
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
709-920 1.71e-11

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: 66.28  E-value: 1.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIR-HRNLVKLLTAcssidFQGNEFRALIYEFMPNG 787
Cdd:cd14090   11 GEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRSRVFREVETLHQCQgHPNILQLIEY-----FEDDERFYLVFEKMRGG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 SLdmwlhpeeVEEIHRpSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVL---LDDDLTAHVSDFGLA--- 861
Cdd:cd14090   86 PL--------LSHIEK-RVHFTEQEASLVVRDIASALDFLH---DKGIAHRDLKPENILcesMDKVSPVKICDFDLGsgi 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18408454  862 RLLLKFDEESFFNQLSSAgvRGTIGYAAPEY--GVGGQPSI---NGDVYSFGILLLEMFTGKRP 920
Cdd:cd14090  154 KLSSTSMTPVTTPELLTP--VGSAEYMAPEVvdAFVGEALSydkRCDLWSLGVILYIMLCGYPP 215
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
708-920 1.75e-11

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: 66.09  E-value: 1.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTV--YKALLLTEKkvVAVKVLNMQRRGAMKS-FMAECESLKDIRHRNLVKLLTACSSIDFQGNEFRALIYEFM 784
Cdd:cd14039    1 LGTGGFGNVclYQNQETGEK--IAIKSCRLELSVKNKDrWCHEIQIMKKLNHPNVVKACDVPEEMNFLVNDVPLLAMEYC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLDMWLHPEEVEEIHRPSRTLTLLErlniaiDVASVLDYLHvhcHEPIAHCDLKPSNVLLDD---DLTAHVSDFGLA 861
Cdd:cd14039   79 SGGDLRKLLNKPENCCGLKESQVLSLLS------DIGSGIQYLH---ENKIIHRDLKPENIVLQEingKIVHKIIDLGYA 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  862 RLLlkfDEESffnqLSSAGVrGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14039  150 KDL---DQGS----LCTSFV-GTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRP 200
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
709-924 2.12e-11

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: 65.58  E-value: 2.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVYKALL------LTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSIDFQgnefraLIYE 782
Cdd:cd05037    8 GQGTFTNIYDGILrevgdgRVQEVEVLLKVLDSDHRDISESFFETASLMSQISHKHLVKLYGVCVADENI------MVQE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLDMWLhpeeveeiHRPSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLldddltahvsdfgLAR 862
Cdd:cd05037   82 YVRYGPLDKYL--------RRMGNNVPLSWKLQVAKQLASALHYLE---DKKLIHGNVRGRNIL-------------LAR 137
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  863 LLLkfDEESFFNQLSSAGVRGTIG----------YAAPEYGVGGQ--PSINGDVYSFGILLLEMFT-GKRPTNEL 924
Cdd:cd05037  138 EGL--DGYPPFIKLSDPGVPITVLsreervdripWIAPECLRNLQanLTIAADKWSFGTTLWEICSgGEEPLSAL 210
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
708-916 2.15e-11

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: 65.97  E-value: 2.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKAL---LLTEKKV--VAVKVLN-MQRRGAMKSFMAECESLKDI-RHRNLVKLLTACSSidfQGNEFraLI 780
Cdd:cd05055   43 LGAGAFGKVVEATaygLSKSDAVmkVAVKMLKpTAHSSEREALMSELKIMSHLgNHENIVNLLGACTI---GGPIL--VI 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFMPNGSLdmwlhpeeVEEIHRPSRT-LTLLERLNIAIDVASVLDYLHV-HChepiAHCDLKPSNVLLDDDLTAHVSDF 858
Cdd:cd05055  118 TEYCCYGDL--------LNFLRRKRESfLTLEDLLSFSYQVAKGMAFLASkNC----IHRDLAARNVLLTHGKIVKICDF 185
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  859 GLARlllkfDEESFFNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT 916
Cdd:cd05055  186 GLAR-----DIMNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGILLWEIFS 238
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
708-926 2.39e-11

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


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 65.35  E-value: 2.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKV--VAVKVLNMQRRGAMK-SFMAECESLKDIRHRNLVKLLTACSSidfqgnEFRALIYEFM 784
Cdd:cd05115   12 LGSGNFGCVKKGVYKMRKKQidVAIKVLKQGNEKAVRdEMMREAQIMHQLDNPYIVRMIGVCEA------EALMLVMEMA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLDMWLHPEE--------VEEIHRPSRTLTLLERLNIAidvasvldylhvhchepiaHCDLKPSNVLLDDDLTAHVS 856
Cdd:cd05115   86 SGGPLNKFLSGKKdeitvsnvVELMHQVSMGMKYLEEKNFV-------------------HRDLAARNVLLVNQHYAKIS 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18408454  857 DFGLARLLLKFDEesfFNQLSSAGvRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRPTNELFG 926
Cdd:cd05115  147 DFGLSKALGADDS---YYKARSAG-KWPLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSyGQKPYKKMKG 213
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
711-922 2.50e-11

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: 65.19  E-value: 2.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  711 GSFGTVYKALLLTEKKVVAVKVL---NMQRRGAMKSFMAECESLKDIRHR-NLVKLLTAcssidFQGNEFRALIYEFMPN 786
Cdd:cd05611    7 GAFGSVYLAKKRSTGDYFAIKVLkksDMIAKNQVTNVKAERAIMMIQGESpYVAKLYYS-----FQSKDYLYLVMEYLNG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  787 GSLDmwlhpeeveeihrpsrtlTLLERL---------NIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDdlTAHV-- 855
Cdd:cd05611   82 GDCA------------------SLIKTLgglpedwakQYIAEVVLGVEDLH---QRGIIHRDIKPENLLIDQ--TGHLkl 138
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  856 SDFGLARL-LLKFDEESFFnqlssagvrGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTN 922
Cdd:cd05611  139 TDFGLSRNgLEKRHNKKFV---------GTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFH 197
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
707-920 2.74e-11

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: 65.22  E-value: 2.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLT-EKKVVAVKVLNM----------QRRGAMKSFMAECESLKD-IRHRNLVKLLTAcssidFQGN 774
Cdd:cd08528    7 LLGSGAFGCVYKVRKKSnGQTLLALKEINMtnpafgrteqERDKSVGDIISEVNIIKEqLRHPNIVRYYKT-----FLEN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  775 EFRALIYEFMPNGSLDMWLHPEEVEEIHRPSrtltllERL-NIAIDVASVLDYLHVHchEPIAHCDLKPSNVLLDDDLTA 853
Cdd:cd08528   82 DRLYIVMELIEGAPLGEHFSSLKEKNEHFTE------DRIwNIFVQMVLALRYLHKE--KQIVHRDLKPNNIMLGEDDKV 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  854 HVSDFGLARllLKFDEESffnQLSSagVRGTIGYAAPEYgVGGQPSING-DVYSFGILLLEMFTGKRP 920
Cdd:cd08528  154 TITDFGLAK--QKGPESS---KMTS--VVGTILYSCPEI-VQNEPYGEKaDIWALGCILYQMCTLQPP 213
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
708-914 3.10e-11

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: 65.54  E-value: 3.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKkvVAVKVLNMQRRgamKSFMAECESLKDI--RHRNLVKLLTAcssiDFQGNEFRA---LIYE 782
Cdd:cd14143    3 IGKGRFGEVWRGRWRGED--VAVKIFSSREE---RSWFREAEIYQTVmlRHENILGFIAA----DNKDNGTWTqlwLVSD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLDMWLHpeeveeihrpSRTLTLLERLNIAIDVASVLDYLHVHC-----HEPIAHCDLKPSNVLLDDDLTAHVSD 857
Cdd:cd14143   74 YHEHGSLFDYLN----------RYTVTVEGMIKLALSIASGLAHLHMEIvgtqgKPAIAHRDLKSKNILVKKNGTCCIAD 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  858 FGLArllLKFDEESFFNQLSSAGVRGTIGYAAPEYgvgGQPSIN---------GDVYSFGILLLEM 914
Cdd:cd14143  144 LGLA---VRHDSATDTIDIAPNHRVGTKRYMAPEV---LDDTINmkhfesfkrADIYALGLVFWEI 203
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
708-914 3.13e-11

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: 64.97  E-value: 3.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSiDFQGNefraLIYEFMPNG 787
Cdd:cd14222    1 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYK-DKRLN----LLTEFIEGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 SLDMWLhpeeveeihRPSRTLTLLERLNIAIDVASVLDYLHVHChepIAHCDLKPSNVLLDDDLTAHVSDFGLARLLLK- 866
Cdd:cd14222   76 TLKDFL---------RADDPFPWQQKVSFAKGIASGMAYLHSMS---IIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEe 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  867 ---------FDEESFF---NQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEM 914
Cdd:cd14222  144 kkkpppdkpTTKKRTLrknDRKKRYTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEI 203
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
702-920 3.21e-11

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: 64.88  E-value: 3.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECES--LKDIRHRNLVKLLTAcssidFQGNEFRAL 779
Cdd:cd14097    3 YTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSSAVKLLEREVdiLKHVNHAHIIHLEEV-----FETPKRMYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  780 IYEFMPNGSLDMWLHPEEVeeiHRPSRTLTLLERLniaidvASVLDYLHvhcHEPIAHCDLKPSNVLL-------DDDLT 852
Cdd:cd14097   78 VMELCEDGELKELLLRKGF---FSENETRHIIQSL------ASAVAYLH---KNDIVHRDLKLENILVkssiidnNDKLN 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  853 AHVSDFGLARLLLKFDEESFFNQLssagvrGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14097  146 IKVTDFGLSVQKYGLGEDMLQETC------GTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPP 207
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
707-996 3.24e-11

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: 65.45  E-value: 3.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKkvVAVKVLNMQRRGamkSFMAECESLKDI--RHRNLVKLLTAcssiDFQGNEFRA---LIY 781
Cdd:cd14220    2 QIGKGRYGEVWMGKWRGEK--VAVKVFFTTEEA---SWFRETEIYQTVlmRHENILGFIAA----DIKGTGSWTqlyLIT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 EFMPNGSLDMWLHpeeveeihrpSRTLTLLERLNIAIDVASVLDYLHVHCH----EP-IAHCDLKPSNVLLDDDLTAHVS 856
Cdd:cd14220   73 DYHENGSLYDFLK----------CTTLDTRALLKLAYSAACGLCHLHTEIYgtqgKPaIAHRDLKSKNILIKKNGTCCIA 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  857 DFGLArllLKFDEESFFNQLSSAGVRGTIGYAAPEY------GVGGQPSINGDVYSFGILLLEMftGKRPTNELFGGNFT 930
Cdd:cd14220  143 DLGLA---VKFNSDTNEVDVPLNTRVGTKRYMAPEVldeslnKNHFQAYIMADIYSFGLIIWEM--ARRCVTGGIVEEYQ 217
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  931 LNSYTKSALPERILDIVdESILHIGLRvgfPVV-------ECLTMVFEVGLRCCEESPMNRLaTSIVVKELIS 996
Cdd:cd14220  218 LPYYDMVPSDPSYEDMR-EVVCVKRLR---PTVsnrwnsdECLRAVLKLMSECWAHNPASRL-TALRIKKTLA 285
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
708-928 3.76e-11

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: 64.78  E-value: 3.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSF---MAECESLKDIRHRNlvklltacsSIDFQGNEFRA----LI 780
Cdd:cd06607    9 IGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTEKWqdiIKEVKFLRQLRHPN---------TIEYKGCYLREhtawLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFMPNGSLDMWlhpeeveEIHRpsRTLTLLERLNIAIDVASVLDYLHVHCHepiAHCDLKPSNVLLDDDLTAHVSDFGL 860
Cdd:cd06607   80 MEYCLGSASDIV-------EVHK--KPLQEVEIAAICHGALQGLAYLHSHNR---IHRDVKAGNILLTEPGTVKLADFGS 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18408454  861 ARllLKFDEESFFnqlssagvrGTIGYAAPEYGVG---GQPSINGDVYSFGILLLEMFTGKRPtneLFGGN 928
Cdd:cd06607  148 AS--LVCPANSFV---------GTPYWMAPEVILAmdeGQYDGKVDVWSLGITCIELAERKPP---LFNMN 204
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
702-924 3.91e-11

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: 64.79  E-value: 3.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNM-----VGSGSFGTVYKA-----LLLTEKKVVAVKVLNMQR-RGAMKSFMAECESLKDIRHRNLVKLLTACSSid 770
Cdd:cd05046    2 FPRSNLqeittLGRGEFGEVFLAkakgiEEEGGETLVLVKALQKTKdENLQSEFRRELDMFRKLSHKNVVRLLGLCRE-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  771 fqgNEFRALIYEFMPNGSLDMWLHPEEVEEIHRPSRTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDD 850
Cdd:cd05046   80 ---AEPHYMILEYTDLGDLKQFLRATKSKDEKLKPPPLSTKQKVALCTQIALGMDHLSNA---RFVHRDLAARNCLVSSQ 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  851 LTAHVSDFGLARLLLKFDEESFFNQLssAGVRgtigYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRPTNEL 924
Cdd:cd05046  154 REVKVSLLSLSKDVYNSEYYKLRNAL--IPLR----WLAPEAVQEDDFSTKSDVWSFGVLMWEVFTqGELPFYGL 222
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
702-920 4.65e-11

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: 64.33  E-value: 4.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQR-----------RGAMKSFMAECESLKDIRHRNLVKLLTAcssid 770
Cdd:cd14004    2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERilvdtwvrdrkLGTVPLEIHILDTLNKRSHPNIVKLLDF----- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  771 FQGNEFRALIYEfmPNGS-LDMW----LHPEEVEEIHRpsrtltllerlNIAIDVASVLDYLHVhchEPIAHCDLKPSNV 845
Cdd:cd14004   77 FEDDEFYYLVME--KHGSgMDLFdfieRKPNMDEKEAK-----------YIFRQVADAVKHLHD---QGIVHRDIKDENV 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  846 LLDDDLTAHVSDFGLARLLL--KFDeeSFfnqlssagvRGTIGYAAPEYGVG----GQPSingDVYSFGILLLEMFTGKR 919
Cdd:cd14004  141 ILDGNGTIKLIDFGSAAYIKsgPFD--TF---------VGTIDYAAPEVLRGnpygGKEQ---DIWALGVLLYTLVFKEN 206

                 .
gi 18408454  920 P 920
Cdd:cd14004  207 P 207
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
707-920 5.22e-11

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: 64.93  E-value: 5.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVLNMQR---RGAMKSFMAECESL-KDIRHRNLVKLLtACssidFQGNEFRALIYE 782
Cdd:cd05570    2 VLGKGSFGKVMLAERKKTDELYAIKVLKKEViieDDDVECTMTEKRVLaLANRHPFLTGLH-AC----FQTEDRLYFVME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGslDMWLHpeeveeIHRPSRTLTLLERLNIAiDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLAR 862
Cdd:cd05570   77 YVNGG--DLMFH------IQRARRFTEERARFYAA-EICLALQFLHER---GIIYRDLKLDNVLLDAEGHIKIADFGMCK 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18408454  863 lllkfdeESFFNQLSSAGVRGTIGYAAPE------YGvggqPSIngDVYSFGILLLEMFTGKRP 920
Cdd:cd05570  145 -------EGIWGGNTTSTFCGTPDYIAPEilreqdYG----FSV--DWWALGVLLYEMLAGQSP 195
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
708-946 5.26e-11

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: 64.60  E-value: 5.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQ-RRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFM-- 784
Cdd:cd07870    8 LGEGSYATVYKGISRINGQLVALKVISMKtEEGVPFTAIREASLLKGLKHANIVLLHDI-----IHTKETLTFVFEYMht 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 ---------PNGsldmwLHPEEVEeihrpsrtLTLLERLNiaidvasVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHV 855
Cdd:cd07870   83 dlaqymiqhPGG-----LHPYNVR--------LFMFQLLR-------GLAYIH---GQHILHRDLKPQNLLISYLGELKL 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  856 SDFGLARlllkfdEESFFNQLSSAGVRgTIGYAAPEYGVGGQP-SINGDVYSFGILLLEMFTGKrptnELFGGNftlnsy 934
Cdd:cd07870  140 ADFGLAR------AKSIPSQTYSSEVV-TLWYRPPDVLLGATDySSALDIWGAGCIFIEMLQGQ----PAFPGV------ 202
                        250
                 ....*....|..
gi 18408454  935 tkSALPERILDI 946
Cdd:cd07870  203 --SDVFEQLEKI 212
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
708-920 5.32e-11

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: 64.18  E-value: 5.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACssidFQGNEFrALIYEFMPNG 787
Cdd:cd06647   15 IGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSY----LVGDEL-WVVMEYLAGG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 SLDmwlhpEEVEEihrpsrtlTLLERLNIAI---DVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLARLL 864
Cdd:cd06647   90 SLT-----DVVTE--------TCMDEGQIAAvcrECLQALEFLHSN---QVIHRDIKSDNILLGMDGSVKLTDFGFCAQI 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  865 LKfdeesffNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd06647  154 TP-------EQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPP 202
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
707-920 6.17e-11

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: 64.93  E-value: 6.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVLN---MQRRGAMKSFMAECESLKDIRHRNLVKLLTACssidFQGNEFRALIYEF 783
Cdd:cd05590    2 VLGKGSFGKVMLARLKESGRLYAVKVLKkdvILQDDDVECTMTEKRILSLARNHPFLTQLYCC----FQTPDRLFFVMEF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  784 MPNGslDMWLHPEEVEEIHRPSRTLtllerlnIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARl 863
Cdd:cd05590   78 VNGG--DLMFHIQKSRRFDEARARF-------YAAEITSALMFLH---DKGIIYRDLKLDNVLLDHEGHCKLADFGMCK- 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  864 llkfdeESFFNQLSSAGVRGTIGYAAPE------YGvggqPSIngDVYSFGILLLEMFTGKRP 920
Cdd:cd05590  145 ------EGIFNGKTTSTFCGTPDYIAPEilqemlYG----PSV--DWWAMGVLLYEMLCGHAP 195
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
702-920 6.47e-11

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 64.84  E-value: 6.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKS---FMAECESLKDIRHRNLVKLLtaCSsidFQGNEFRA 778
Cdd:PTZ00263   20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQvqhVAQEKSILMELSHPFIVNMM--CS---FQDENRVY 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   779 LIYEFMPNGslDMWLH-------PEEVEEIHrpsrtltllerlniAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDL 851
Cdd:PTZ00263   95 FLLEFVVGG--ELFTHlrkagrfPNDVAKFY--------------HAELVLAFEYLH---SKDIIYRDLKPENLLLDNKG 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18408454   852 TAHVSDFGLARlllKFDEESFfnqlssaGVRGTIGYAAPEY--GVGGQPSIngDVYSFGILLLEMFTGKRP 920
Cdd:PTZ00263  156 HVKVTDFGFAK---KVPDRTF-------TLCGTPEYLAPEViqSKGHGKAV--DWWTMGVLLYEFIAGYPP 214
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
707-920 7.30e-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: 64.63  E-value: 7.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVLNMQ---RRGAMKSFMAE---CESLKDIRHRNLVKLLtACssidFQGNEFRALI 780
Cdd:cd05589    6 VLGRGHFGKVLLAEYKPTGELFAIKALKKGdiiARDEVESLMCEkriFETVNSARHPFLVNLF-AC----FQTPEHVCFV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFMPNGSLDMWLHpeevEEIHRPSRTLTLlerlniAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGL 860
Cdd:cd05589   81 MEYAAGGDLMMHIH----EDVFSEPRAVFY------AACVVLGLQFLHEH---KIVYRDLKLDNLLLDTEGYVKIADFGL 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  861 ARLLLKF-DEESFFNqlssagvrGTIGYAAPEygVGGQPSING--DVYSFGILLLEMFTGKRP 920
Cdd:cd05589  148 CKEGMGFgDRTSTFC--------GTPEFLAPE--VLTDTSYTRavDWWGLGVLIYEMLVGESP 200
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
700-920 7.35e-11

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: 64.61  E-value: 7.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  700 NGFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQR---RGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEF 776
Cdd:cd05632    2 NTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRikkRKGESMALNEKQILEKVNSQFVVNLAYA-----YETKDA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  777 RALIYEFMPNGSLDMWLH----PEEVEEihrpsrtltllERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLT 852
Cdd:cd05632   77 LCLVLTIMNGGDLKFHIYnmgnPGFEEE-----------RALFYAAEILCGLEDLH---RENTVYRDLKPENILLDDYGH 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  853 AHVSDFGLArllLKFDEESFFNqlssaGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd05632  143 IRISDLGLA---VKIPEGESIR-----GRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSP 202
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
707-920 7.73e-11

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


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 64.73  E-value: 7.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEK---KVVAVKVL-------NMQRRGAMKsfmAECESLKDIRHRNLVKLLTAcssidFQGNEF 776
Cdd:cd05584    3 VLGKGGYGKVFQVRKTTGSdkgKIFAMKVLkkasivrNQKDTAHTK---AERNILEAVKHPFIVDLHYA-----FQTGGK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  777 RALIYEFMPNGSLDMWLhpeEVEEIHRPSRTLTLLERLNIAIDvasvldylHVHChEPIAHCDLKPSNVLLDDDltAHV- 855
Cdd:cd05584   75 LYLILEYLSGGELFMHL---EREGIFMEDTACFYLAEITLALG--------HLHS-LGIIYRDLKPENILLDAQ--GHVk 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  856 -SDFGLARlllkfdeESFFNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd05584  141 lTDFGLCK-------ESIHDGTVTHTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPP 199
PLN03150 PLN03150
hypothetical protein; Provisional
126-206 8.57e-11

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 65.99  E-value: 8.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   126 LRGPIPLGLYNCSRLLNLRLDSNRLGGSVPSELGSLTNLVQLNLYGNNMRGKLPTSLGNLTLLEQLALSHNNLEGEIPSD 205
Cdd:PLN03150  430 LRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSLSGRVPAA 509

                  .
gi 18408454   206 V 206
Cdd:PLN03150  510 L 510
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
707-920 8.65e-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: 64.61  E-value: 8.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVLNMQ---RRGAMKSFMAECESL-KDIRHRNLVKLltacsSIDFQGNEFRALIYE 782
Cdd:cd05603    2 VIGKGSFGKVLLAKRKCDGKFYAVKVLQKKtilKKKEQNHIMAERNVLlKNLKHPFLVGL-----HYSFQTSEKLYFVLD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLdmWLHpeeveeIHRPSRTLTLLERLNIAiDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLAR 862
Cdd:cd05603   77 YVNGGEL--FFH------LQRERCFLEPRARFYAA-EVASAIGYLH---SLNIIYRDLKPENILLDCQGHVVLTDFGLCK 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  863 lllkfdeESFFNQLSSAGVRGTIGYAAPEYgVGGQPSING-DVYSFGILLLEMFTGKRP 920
Cdd:cd05603  145 -------EGMEPEETTSTFCGTPEYLAPEV-LRKEPYDRTvDWWCLGAVLYEMLYGLPP 195
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
708-924 8.92e-11

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: 63.82  E-value: 8.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGA---MKSFMAECESLKDIRHRNLVKLLTACS-SIDFqgnefrALIYEF 783
Cdd:cd14206    5 IGNGWFGKVILGEIFSDYTPAQVVVKELRVSAGpleQRKFISEAQPYRSLQHPNILQCLGLCTeTIPF------LLIMEF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  784 MPNGSLDMWLHPEEVEEIHRP---SRTLTLLERLNIAIdvasVLDYLHVHCHEPIaHCDLKPSNVLLDDDLTAHVSDFGL 860
Cdd:cd14206   79 CQLGDLKRYLRAQRKADGMTPdlpTRDLRTLQRMAYEI----TLGLLHLHKNNYI-HSDLALRNCLLTSDLTVRIGDYGL 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  861 ARLLLKfdeESFFnqLSSAGVRGTIGYAAPE--------YGVGGQpSINGDVYSFGILLLEMFT-GKRPTNEL 924
Cdd:cd14206  154 SHNNYK---EDYY--LTPDRLWIPLRWVAPElldelhgnLIVVDQ-SKESNVWSLGVTIWELFEfGAQPYRHL 220
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
707-920 9.28e-11

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: 63.79  E-value: 9.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALL-LTEKK--VVAVKVL-----NMQRRGamksFMAECESLKDIRHRNLVKLltacSSIDFQGNEFrA 778
Cdd:cd05064   12 ILGTGRFGELCRGCLkLPSKRelPVAIHTLragcsDKQRRG----FLAEALTLGQFDHSNIVRL----EGVITRGNTM-M 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGSLDMWLHPEEVEeihrpsrtLTLLERLNIAIDVASVLDYLhvhCHEPIAHCDLKPSNVLLDDDLTAHVSDF 858
Cdd:cd05064   83 IVTEYMSNGALDSFLRKHEGQ--------LVAGQLMGMLPGLASGMKYL---SEMGYVHKGLAAHKVLVNSDLVCKISGF 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  859 glaRLLLKFDEESFFNQLSSagvRGTIGYAAPEYGVGGQPSINGDVYSFGILLLE-MFTGKRP 920
Cdd:cd05064  152 ---RRLQEDKSEAIYTTMSG---KSPVLWAAPEAIQYHHFSSASDVWSFGIVMWEvMSYGERP 208
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
707-994 1.02e-10

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: 63.89  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTE----KKVVAVKVLNMQRR-GAMKSFMAECESLKDIRHRNLVKLLTACSSIDFQgnefraLIY 781
Cdd:cd05109   14 VLGSGAFGTVYKGIWIPDgenvKIPVAIKVLRENTSpKANKEILDEAYVMAGVGSPYVCRLLGICLTSTVQ------LVT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 EFMPNGSLdmwlhpeeVEEIHRPSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLA 861
Cdd:cd05109   88 QLMPYGCL--------LDYVRENKDRIGSQDLLNWCVQIAKGMSYLE---EVRLVHRDLAARNVLVKSPNHVKITDFGLA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  862 RlLLKFDEESFfnqlSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRPTNelfggnftlnsytksALP 940
Cdd:cd05109  157 R-LLDIDETEY----HADGGKVPIKWMALESILHRRFTHQSDVWSYGVTVWELMTfGAKPYD---------------GIP 216
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18408454  941 ERilDIVDesILHIGLRVGFPVVeCLTMVFEVGLRCCEESPMNRLATSIVVKEL 994
Cdd:cd05109  217 AR--EIPD--LLEKGERLPQPPI-CTIDVYMIMVKCWMIDSECRPRFRELVDEF 265
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
706-920 1.34e-10

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


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 63.22  E-value: 1.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTVYKALLlTEKKVVAVK--VLNMQRRGAMK----SFMAECESLKDIRHRNLVKLLTACSSiDFQGNEFral 779
Cdd:cd06631    7 NVLGKGAYGTVYCGLT-STGQLIAVKqvELDTSDKEKAEkeyeKLQEEVDLLKTLKHVNIVGYLGTCLE-DNVVSIF--- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  780 iYEFMPNGSLDMWLH-----PEEVeeIHRPSRtltllerlNIAIDVAsvldYLHVHChepIAHCDLKPSNVLLDDDLTAH 854
Cdd:cd06631   82 -MEFVPGGSIASILArfgalEEPV--FCRYTK--------QILEGVA----YLHNNN---VIHRDIKGNNIMLMPNGVIK 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  855 VSDFGLA-RLLLKFDEESFFNQLSSagVRGTIGYAAPE------YGVggqpsiNGDVYSFGILLLEMFTGKRP 920
Cdd:cd06631  144 LIDFGCAkRLCINLSSGSQSQLLKS--MRGTPYWMAPEvinetgHGR------KSDIWSIGCTVFEMATGKPP 208
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
707-945 1.55e-10

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: 62.67  E-value: 1.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSfMAECESLKDIR------HRNLVKLLTAcssidFQGNEFRALI 780
Cdd:cd14133    6 VLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLDQS-LDEIRLLELLNkkdkadKYHIVRLKDV-----FYFKNHLCIV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFmpngsLDMWLHpEEVEEIHRPSRTLTLLERlnIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLL--DDDLTAHVSDF 858
Cdd:cd14133   80 FEL-----LSQNLY-EFLKQNKFQYLSLPRIRK--IAQQILEALVFLH---SLGLIHCDLKPENILLasYSRCQIKIIDF 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  859 GLArlllkfdeeSFFNQLSSAGVRgTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKrptnELFGGNFTLN-----S 933
Cdd:cd14133  149 GSS---------CFLTQRLYSYIQ-SRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGE----PLFPGASEVDqlariI 214
                        250
                 ....*....|..
gi 18408454  934 YTKSALPERILD 945
Cdd:cd14133  215 GTIGIPPAHMLD 226
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
708-920 1.61e-10

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: 62.85  E-value: 1.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssiDFQGNEFrALIYEFMPNG 787
Cdd:cd06648   15 IGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQRRELLFNEVVIMRDYQHPNIVEMYSS----YLVGDEL-WVVMEFLEGG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 SL-DMWLHPEEVEEihrpsrtltllERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGlarlllk 866
Cdd:cd06648   90 ALtDIVTHTRMNEE-----------QIATVCRAVLKALSFLHSQ---GVIHRDIKSDSILLTSDGRVKLSDFG------- 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  867 fdeesFFNQLSSAGVR-----GTIGYAAPE------YGVggqpsiNGDVYSFGILLLEMFTGKRP 920
Cdd:cd06648  149 -----FCAQVSKEVPRrkslvGTPYWMAPEvisrlpYGT------EVDIWSLGIMVIEMVDGEPP 202
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
702-920 1.80e-10

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: 62.67  E-value: 1.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVL---NMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRA 778
Cdd:cd14116    7 FEIGRPLGKGKFGNVYLAREKQSKFILALKVLfkaQLEKAGVEHQLRREVEIQSHLRHPNILRLYGY-----FHDATRVY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGsldmwlhpeeveEIHRPSRTLTLLERLNIAIDVASVLDYLhVHCH-EPIAHCDLKPSNVLLDDDLTAHVSD 857
Cdd:cd14116   82 LILEYAPLG------------TVYRELQKLSKFDEQRTATYITELANAL-SYCHsKRVIHRDIKPENLLLGSAGELKIAD 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  858 FGLArlllkfdeesfFNQLSS--AGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14116  149 FGWS-----------VHAPSSrrTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPP 202
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
683-920 1.91e-10

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: 63.20  E-value: 1.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  683 LEVLHEKISYGDLRNATNGFSSsnmVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKL 762
Cdd:cd06654    6 LEKLRSIVSVGDPKKKYTRFEK---IGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKELIINEILVMRENKNPNIVNY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  763 LTACssidFQGNEFrALIYEFMPNGSLDmwlhpEEVEEihrpsrtlTLLERLNIAI---DVASVLDYLHVHchePIAHCD 839
Cdd:cd06654   83 LDSY----LVGDEL-WVVMEYLAGGSLT-----DVVTE--------TCMDEGQIAAvcrECLQALEFLHSN---QVIHRD 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  840 LKPSNVLLDDDLTAHVSDFGLARLLLKfdeesffNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKR 919
Cdd:cd06654  142 IKSDNILLGMDGSVKLTDFGFCAQITP-------EQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEP 214

                 .
gi 18408454  920 P 920
Cdd:cd06654  215 P 215
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
707-919 2.01e-10

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: 62.44  E-value: 2.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVLNMQR--RGAMKSFMAECESLKDIRHRNLvklltacssIDFQGNEF--RAL--I 780
Cdd:cd08220    7 VVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQmtKEERQAALNEVKVLSMLHHPNI---------IEYYESFLedKALmiV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFMPNGSLDMWLHpeeveeihrpSRTLTLLERLNIAIDVASVLDYL-HVHCHEpIAHCDLKPSNVLLDDDLT-AHVSDF 858
Cdd:cd08220   78 MEYAPGGTLFEYIQ----------QRKGSLLSEEEILHFFVQILLALhHVHSKQ-ILHRDLKTQNILLNKKRTvVKIGDF 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  859 GLARLLlkfdeesffNQLSSA-GVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKR 919
Cdd:cd08220  147 GISKIL---------SSKSKAyTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKR 199
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
709-944 2.10e-10

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: 62.41  E-value: 2.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVY---KALLLTEKKVVAVKVLN----MQRRGAMKSFMAECESLKDIRHRN-LVKLLTAcssidFQGNEFRALI 780
Cdd:cd05583    3 GTGAYGKVFlvrKVGGHDAGKLYAMKVLKkatiVQKAKTAEHTMTERQVLEAVRQSPfLVTLHYA-----FQTDAKLHLI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFMPNGSLDMWLHPEEveeihrpsrTLTLLE-RLNIA-IDVAsvLDYLHvhcHEPIAHCDLKPSNVLLDDDltAHV--S 856
Cdd:cd05583   78 LDYVNGGELFTHLYQRE---------HFTESEvRIYIGeIVLA--LEHLH---KLGIIYRDIKLENILLDSE--GHVvlT 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  857 DFGLARLLLKFDEE---SFFnqlssagvrGTIGYAAPEYGVGGQPSING--DVYSFGILLLEMFTGKRPtnelfggnFTL 931
Cdd:cd05583  142 DFGLSKEFLPGENDraySFC---------GTIEYMAPEVVRGGSDGHDKavDWWSLGVLTYELLTGASP--------FTV 204
                        250
                 ....*....|....*..
gi 18408454  932 ----NSytKSALPERIL 944
Cdd:cd05583  205 dgerNS--QSEISKRIL 219
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
747-949 2.25e-10

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: 62.38  E-value: 2.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  747 ECESLKDIRHRNLVKLLtaCSSIDFQGNEFRALIY---EFMPNGSLdmwlhpEEVEEIHRPSRtltlLERLNI-AIDVAS 822
Cdd:cd14012   48 ELESLKKLRHPNLVSYL--AFSIERRGRSDGWKVYlltEYAPGGSL------SELLDSVGSVP----LDTARRwTLQLLE 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  823 VLDYLHVHchePIAHCDLKPSNVLLDDDL---TAHVSDFGLARLLLKFDEESFFNQLSSAGVRgtigyaAPEYGVGG-QP 898
Cdd:cd14012  116 ALEYLHRN---GVVHKSLHAGNVLLDRDAgtgIVKLTDYSLGKTLLDMCSRGSLDEFKQTYWL------PPELAQGSkSP 186
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18408454  899 SINGDVYSFGILLLEMFTGKRPTNELFGGNFTLNSytkSALPERILDIVDE 949
Cdd:cd14012  187 TRKTDVWDLGLLFLQMLFGLDVLEKYTSPNPVLVS---LDLSASLQDFLSK 234
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
702-924 2.40e-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: 62.38  E-value: 2.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRrgamksfmAECEsLKDIRHRnlVKLLTACSS---IDFQGNEFRA 778
Cdd:cd06640    6 FTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEE--------AEDE-IEDIQQE--ITVLSQCDSpyvTKYYGSYLKG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 ----LIYEFMPNGSLDMWLHPEEVEEIhrpsRTLTLLErlniaiDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAH 854
Cdd:cd06640   75 tklwIIMEYLGGGSALDLLRAGPFDEF----QIATMLK------EILKGLDYLH---SEKKIHRDIKAANVLLSEQGDVK 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  855 VSDFGLARLLLKfdeesffNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTNEL 924
Cdd:cd06640  142 LADFGVAGQLTD-------TQIKRNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDM 204
PLN03150 PLN03150
hypothetical protein; Provisional
56-161 2.42e-10

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 64.45  E-value: 2.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454    56 WKGVTCGRKNKR----VTHLELGRLQLGGVISPSIGNLSFLVSLDLYENFFGGTIPQEVGQLSRLEYLDMGINYLRGPIP 131
Cdd:PLN03150  404 WSGADCQFDSTKgkwfIDGLGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIP 483
                          90       100       110
                  ....*....|....*....|....*....|
gi 18408454   132 LGLYNCSRLLNLRLDSNRLGGSVPSELGSL 161
Cdd:PLN03150  484 ESLGQLTSLRILNLNGNSLSGRVPAALGGR 513
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
708-920 2.72e-10

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: 62.31  E-value: 2.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKS---FMAECESLKDIRHRNLVKLLTACSSIDFQgnefrALIYEFM 784
Cdd:cd05087    5 IGHGWFGKVFLGEVNSGLSSTQVVVKELKASASVQDqmqFLEEAQPYRALQHTNLLQCLAQCAEVTPY-----LLVMEFC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLDMWLHPEEVEEIHRPSrTLTLLErlnIAIDVASVLdyLHVHCHEPIaHCDLKPSNVLLDDDLTAHVSDFGLARll 864
Cdd:cd05087   80 PLGDLKGYLRSCRAAESMAPD-PLTLQR---MACEVACGL--LHLHRNNFV-HSDLALRNCLLTADLTVKIGDYGLSH-- 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18408454  865 LKFDEESFfnqLSSAGVRGTIGYAAPEY--GVGGQPSI-----NGDVYSFGILLLEMFT-GKRP 920
Cdd:cd05087  151 CKYKEDYF---VTADQLWVPLRWIAPELvdEVHGNLLVvdqtkQSNVWSLGVTIWELFElGNQP 211
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
696-920 2.85e-10

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: 63.18  E-value: 2.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  696 RNATNGFSSSNMVGSGSFGtvyKALLLTEK---KVVAVKVLNMQ---RRGAMKSFMAECESLKDIRHRNLVKLltacsSI 769
Cdd:cd05593   11 RKTMNDFDYLKLLGKGTFG---KVILVREKasgKYYAMKILKKEviiAKDEVAHTLTESRVLKNTRHPFLTSL-----KY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  770 DFQGNEFRALIYEFMPNGSLDMWLHPEEVEEIHRpsrtltllERLNIAiDVASVLDYLHvhcHEPIAHCDLKPSNVLLDD 849
Cdd:cd05593   83 SFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDR--------TRFYGA-EIVSALDYLH---SGKIVYRDLKLENLMLDK 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18408454  850 DLTAHVSDFGLARlllkfdeESFFNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd05593  151 DGHIKITDFGLCK-------EGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLP 214
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
683-920 3.15e-10

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: 62.43  E-value: 3.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  683 LEVLHEKISYGDLRNAtngFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKL 762
Cdd:cd06655    5 MEKLRTIVSIGDPKKK---YTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  763 LTACssidFQGNEFrALIYEFMPNGSLDmwlhpEEVEEihrpsrtlTLLERLNIAI---DVASVLDYLHVHchePIAHCD 839
Cdd:cd06655   82 LDSF----LVGDEL-FVVMEYLAGGSLT-----DVVTE--------TCMDEAQIAAvcrECLQALEFLHAN---QVIHRD 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  840 LKPSNVLLDDDLTAHVSDFGLARLLLKfdeesffNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKR 919
Cdd:cd06655  141 IKSDNVLLGMDGSVKLTDFGFCAQITP-------EQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEP 213

                 .
gi 18408454  920 P 920
Cdd:cd06655  214 P 214
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
708-947 3.18e-10

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: 63.08  E-value: 3.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLN--MQRRGAMKSFMAECESLKDIRHRNLVKLL---TACSSIdfqgNEFRA--LI 780
Cdd:cd07851   23 VGSGAYGQVCSAFDTKTGRKVAIKKLSrpFQSAIHAKRTYRELRLLKHMKHENVIGLLdvfTPASSL----EDFQDvyLV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFMpnGSldmwlhpeeveEIHRPSRTltllERLN------IAIDVASVLDYLHvHCHepIAHCDLKPSNVLLDDDLTAH 854
Cdd:cd07851   99 THLM--GA-----------DLNNIVKC----QKLSddhiqfLVYQILRGLKYIH-SAG--IIHRDLKPSNLAVNEDCELK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  855 VSDFGLARLLlkfDEEsffnqlsSAGVRGTIGYAAPE-------YgvggqpSINGDVYSFGILLLEMFTGKrptnELFGG 927
Cdd:cd07851  159 ILDFGLARHT---DDE-------MTGYVATRWYRAPEimlnwmhY------NQTVDIWSVGCIMAELLTGK----TLFPG 218
                        250       260
                 ....*....|....*....|
gi 18408454  928 NFTLNSYTksalpeRILDIV 947
Cdd:cd07851  219 SDHIDQLK------RIMNLV 232
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
708-917 3.21e-10

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: 62.39  E-value: 3.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVK--VLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFMP 785
Cdd:cd07847    9 IGEGSYGVVFKCRNRETGQIVAIKkfVESEDDPVIKKIALREIRMLKQLKHPNLVNLIEV-----FRRKRKLHLVFEYCD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLD-MWLHPEEVEEIHRPSRTLTLLERLNIAidvasvldylhvHCHEPIaHCDLKPSNVLLDDDLTAHVSDFGLARLL 864
Cdd:cd07847   84 HTVLNeLEKNPRGVPEHLIKKIIWQTLQAVNFC------------HKHNCI-HRDVKPENILITKQGQIKLCDFGFARIL 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  865 LKFDEEsffnqlsSAGVRGTIGYAAPEYGVG----GQPSingDVYSFGILLLEMFTG 917
Cdd:cd07847  151 TGPGDD-------YTDYVATRWYRAPELLVGdtqyGPPV---DVWAIGCVFAELLTG 197
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
702-920 3.43e-10

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: 62.76  E-value: 3.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSfmaeceslKDIRHrnlVKLLTACSS---IDFQGNEFR- 777
Cdd:cd06650    7 FEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRN--------QIIRE---LQVLHECNSpyiVGFYGAFYSd 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  778 ---ALIYEFMPNGSLDMWLH-----PEEVeeihrpsrtltlLERLNIAidVASVLDYLHVHchEPIAHCDLKPSNVLLDD 849
Cdd:cd06650   76 geiSICMEHMDGGSLDQVLKkagriPEQI------------LGKVSIA--VIKGLTYLREK--HKIMHRDVKPSNILVNS 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18408454  850 DLTAHVSDFGLARLLLKFDEESFFnqlssagvrGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd06650  140 RGEIKLCDFGVSGQLIDSMANSFV---------GTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYP 201
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
708-860 3.45e-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: 62.72  E-value: 3.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQ---RRGAMKSFMAECESL-KDIRHRNLVKLltacsSIDFQGNEFRALIYEF 783
Cdd:cd05575    3 IGKGSFGKVLLARHKAEGKLYAVKVLQKKailKRNEVKHIMAERNVLlKNVKHPFLVGL-----HYSFQTKDKLYFVLDY 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  784 MPNGSLDMWLHPEEVEEIHRpSRTLtllerlniAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDltAHV--SDFGL 860
Cdd:cd05575   78 VNGGELFFHLQRERHFPEPR-ARFY--------AAEIASALGYLH---SLNIIYRDLKPENILLDSQ--GHVvlTDFGL 142
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
708-925 3.52e-10

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 62.14  E-value: 3.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRR--GAMKSFMAECESLKDIRHRNLVKLLtacssiDFQGNEFRA-LIYEFM 784
Cdd:PLN00009   10 IGEGTYGVVYKARDRVTNETIALKKIRLEQEdeGVPSTAIREISLLKEMQHGNIVRLQ------DVVHSEKRLyLVFEYL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   785 pngSLDMWLHPEEVEEIHRPSRTL-TLLERlniaidVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTA-HVSDFGLAR 862
Cdd:PLN00009   84 ---DLDLKKHMDSSPDFAKNPRLIkTYLYQ------ILRGIAYCHSH---RVLHRDLKPQNLLIDRRTNAlKLADFGLAR 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   863 lLLKFDEESFFNQLSsagvrgTIGYAAPEYGVGG-QPSINGDVYSFGILLLEM------FTGKRPTNELF 925
Cdd:PLN00009  152 -AFGIPVRTFTHEVV------TLWYRAPEILLGSrHYSTPVDIWSVGCIFAEMvnqkplFPGDSEIDELF 214
PLN03150 PLN03150
hypothetical protein; Provisional
191-300 3.66e-10

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 63.68  E-value: 3.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   191 LALSHNNLEGEIPSDVAQLTQIWSLQLVANNFSGVFPPALYNLSSLKLLGIGYNHFSGrlrpdlgillpnllsfnmggny 270
Cdd:PLN03150  423 LGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNG---------------------- 480
                          90       100       110
                  ....*....|....*....|....*....|
gi 18408454   271 ftgSIPTTLSNISTLERLGMNENNLTGSIP 300
Cdd:PLN03150  481 ---SIPESLGQLTSLRILNLNGNSLSGRVP 507
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
708-916 3.79e-10

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: 62.29  E-value: 3.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVY----KALLLTEKKV-VAVKVLN----MQRRgamKSFMAECESLKDIRHRNLVKLLTACSSidfqgNEFRA 778
Cdd:cd05061   14 LGQGSFGMVYegnaRDIIKGEAETrVAVKTVNesasLRER---IEFLNEASVMKGFTCHHVVRLLGVVSK-----GQPTL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGSLDMWLHPEEVEEIHRPSRTL-TLLERLNIAIDVASVLDYLHVhchEPIAHCDLKPSNVLLDDDLTAHVSD 857
Cdd:cd05061   86 VVMELMAHGDLKSYLRSLRPEAENNPGRPPpTLQEMIQMAAEIADGMAYLNA---KKFVHRDLAARNCMVAHDFTVKIGD 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18408454  858 FGLARLLLKFDeesffnqLSSAGVRG--TIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT 916
Cdd:cd05061  163 FGMTRDIYETD-------YYRKGGKGllPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITS 216
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
702-925 3.83e-10

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


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 61.50  E-value: 3.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQR-RGAMKSFMAECESLKDIRHRNLVKLLTacssiDFQGNEFRALI 780
Cdd:cd14185    2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKlKGKEDMIESEILIIKSLSHPNIVKLFE-----VYETEKEIYLI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFMPNGSLdmwlHPEEVEEIHRPSRTLTLLerlniAIDVASVLDYLHvhcHEPIAHCDLKPSNVLL----DDDLTAHVS 856
Cdd:cd14185   77 LEYVRGGDL----FDAIIESVKFTEHDAALM-----IIDLCEALVYIH---SKHIVHRDLKPENLLVqhnpDKSTTLKLA 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  857 DFGLARLLLKfdeeSFFNqlssagVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTG-------KRPTNELF 925
Cdd:cd14185  145 DFGLAKYVTG----PIFT------VCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGfppfrspERDQEELF 210
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
708-916 3.95e-10

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: 61.97  E-value: 3.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVY----KALLLTEKKV-VAVKVLNmqRRGAMKS---FMAECESLKDIRHRNLVKLLTACSsidfQGNEfRAL 779
Cdd:cd05062   14 LGQGSFGMVYegiaKGVVKDEPETrVAIKTVN--EAASMRErieFLNEASVMKEFNCHHVVRLLGVVS----QGQP-TLV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  780 IYEFMPNGSLDMWLHPEEVEEIHRPSRTLTLLERL-NIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDF 858
Cdd:cd05062   87 IMELMTRGDLKSYLRSLRPEMENNPVQAPPSLKKMiQMAGEIADGMAYLNAN---KFVHRDLAARNCMVAEDFTVKIGDF 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  859 GLARLLLKFDeesffnqLSSAGVRG--TIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT 916
Cdd:cd05062  164 GMTRDIYETD-------YYRKGGKGllPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIAT 216
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
700-920 4.04e-10

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: 61.80  E-value: 4.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  700 NGFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVL---NMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEF 776
Cdd:cd14117    6 DDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLfksQIEKEGVEHQLRREIEIQSHLRHPNILRLYNY-----FHDRKR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  777 RALIYEFMPNGSLdmwlhPEEVEEIHR--PSRTLTLLERLniaidvASVLDYlhvhCHE-PIAHCDLKPSNVLLDDDLTA 853
Cdd:cd14117   81 IYLILEYAPRGEL-----YKELQKHGRfdEQRTATFMEEL------ADALHY----CHEkKVIHRDIKPENLLMGYKGEL 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  854 HVSDFGLArlllkfdeeSFFNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14117  146 KIADFGWS---------VHAPSLRRRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPP 203
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
798-1000 4.38e-10

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: 61.35  E-value: 4.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  798 VEEIHRP-----SRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARlllkfdEESf 872
Cdd:cd13975   84 MERLHRDlytgiKAGLSLEERLQIALDVVEGIRFLH---SQGLVHRDIKLKNVLLDKKNRAKITDLGFCK------PEA- 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  873 fnqLSSAGVRGTIGYAAPEYGVGGQPSiNGDVYSFGILLLEMFTG--KRP-TNELFGGNFTLNSYTKSALPERILDIVDE 949
Cdd:cd13975  154 ---MMSGSIVGTPIHMAPELFSGKYDN-SVDVYAFGILFWYLCAGhvKLPeAFEQCASKDHLWNNVRKGVRPERLPVFDE 229
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18408454  950 silhiglrvgfpvvECLTMVFEvglrCCEESPMNRLATSIVVKELISIRER 1000
Cdd:cd13975  230 --------------ECWNLMEA----CWSGDPSQRPLLGIVQPKLQGIMDR 262
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
709-916 4.82e-10

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: 61.64  E-value: 4.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVYKALLLTEKKV-----VAVKVL-NMQRRGAMKSFMAECESLKDIRHRNLVKLLTACssidFQGNEfRALIYE 782
Cdd:cd05036   15 GQGAFGEVYEGTVSGMPGDpsplqVAVKTLpELCSEQDEMDFLMEALIMSKFNHPNIVRCIGVC----FQRLP-RFILLE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLDMWLHpEEVEEIHRPSRtLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLL---DDDLTAHVSDFG 859
Cdd:cd05036   90 LMAGGDLKSFLR-ENRPRPEQPSS-LTMLDLLQLAQDVAKGCRYLE---ENHFIHRDIAARNCLLtckGPGRVAKIGDFG 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  860 LARLLLKfdeESFFNQLSSAGVrgTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT 916
Cdd:cd05036  165 MARDIYR---ADYYRKGGKAML--PVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFS 216
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
708-920 4.91e-10

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: 62.01  E-value: 4.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKvlNMQRRGamksfmaECESLKDIrhrnLVKLLTACSSID--FQGNEFRALIYEFmp 785
Cdd:cd06618   23 IGSGTCGQVYKMRHKKTGHVMAVK--QMRRSG-------NKEENKRI----LMDLDVVLKSHDcpYIVKCYGYFITDS-- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 ngslDMWLHPEEVEeihrpsrtlTLLERL--------------NIAIDVASVLDYLHVHcHEpIAHCDLKPSNVLLDDDL 851
Cdd:cd06618   88 ----DVFICMELMS---------TCLDKLlkriqgpipedilgKMTVSIVKALHYLKEK-HG-VIHRDVKPSNILLDESG 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18408454  852 TAHVSDFGLARLLLKfdeesffnqlSSAGVR--GTIGYAAPE-YGVGGQPS--INGDVYSFGILLLEMFTGKRP 920
Cdd:cd06618  153 NVKLCDFGISGRLVD----------SKAKTRsaGCAAYMAPErIDPPDNPKydIRADVWSLGISLVELATGQFP 216
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
709-920 5.31e-10

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 61.12  E-value: 5.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVYKALLLTEKKVVAVKV-LNMQRRGAMKSFMAECESLKDIRHrnlvklltACSSIDFqGNEFRaliYEFMPng 787
Cdd:cd14017    9 GGGGFGEIYKVRDVVDGEEVAMKVeSKSQPKQVLKMEVAVLKKLQGKPH--------FCRLIGC-GRTER---YNYIV-- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 sldMWLHPEEVEEIHR--PSRTLTLLERLNIAIdvaSVLDYLHVhCHEP-IAHCDLKPSNVLL----DDDLTAHVSDFGL 860
Cdd:cd14017   75 ---MTLLGPNLAELRRsqPRGKFSVSTTLRLGI---QILKAIED-IHEVgFLHRDVKPSNFAIgrgpSDERTVYILDFGL 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  861 ARLLLKFDEESFFNQLSSAGVRGTIGYAapeygvggqpSING----------DVYSFGILLLEMFTGKRP 920
Cdd:cd14017  148 ARQYTNKDGEVERPPRNAAGFRGTVRYA----------SVNAhrnkeqgrrdDLWSWFYMLIEFVTGQLP 207
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
708-920 6.01e-10

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: 61.52  E-value: 6.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKV----LNMQRRGamkSFMAECESLKDIRHRNLVKLLTACSSI-DFQGNEFRALIYE 782
Cdd:cd14038    2 LGTGGFGNVLRWINQETGEQVAIKQcrqeLSPKNRE---RWCLEIQIMKRLNHPNVVAARDVPEGLqKLAPNDLPLLAME 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLDMWLHPEEVEEIHRPSRTLTLLErlniaiDVASVLDYLHvhcHEPIAHCDLKPSNVLL---DDDLTAHVSDFG 859
Cdd:cd14038   79 YCQGGDLRKYLNQFENCCGLREGAILTLLS------DISSALRYLH---ENRIIHRDLKPENIVLqqgEQRLIHKIIDLG 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18408454  860 LARLLlkfDEESffnqLSSAGVrGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14038  150 YAKEL---DQGS----LCTSFV-GTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRP 202
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
708-985 6.22e-10

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: 61.09  E-value: 6.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVL---NMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFM 784
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTFALKCVkkrHIVQTRQQEHIFSEKEILEECNSPFIVKLYRT-----FKDKKYLYMLMEYC 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLDMWLhpeeveeihrpsRTLTLLERLNIAIDVASV---LDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLA 861
Cdd:cd05572   76 LGGELWTIL------------RDRGLFDEYTARFYTACVvlaFEYLHSR---GIIYRDLKPENLLLDSNGYVKLVDFGFA 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  862 RLLlkfdeesffnqlsSAGVR-----GTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPtnelFGGNFT--LNSY 934
Cdd:cd05572  141 KKL-------------GSGRKtwtfcGTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPP----FGGDDEdpMKIY 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18408454  935 tksalpERILDIVDesilhiglRVGFPvvECLTMVFE-VGLRCCEESPMNRL 985
Cdd:cd05572  204 ------NIILKGID--------KIEFP--KYIDKNAKnLIKQLLRRNPEERL 239
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
708-923 6.76e-10

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


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 60.86  E-value: 6.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALllTEKKVVAVKVLNMQRRGAMK----SFMAECESLKDIRHRNLVKLLTACSSiDFQGNEFRALIYEF 783
Cdd:cd14032    9 LGRGSFKTVYKGL--DTETWVEVAWCELQDRKLTKverqRFKEEAEMLKGLQHPNIVRFYDFWES-CAKGKRCIVLVTEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  784 MPNGSLDMWLHPEEVeeiHRPSRTLTLLERlniaidVASVLDYLHVHChEPIAHCDLKPSNVLLDDDL-TAHVSDFGLAR 862
Cdd:cd14032   86 MTSGTLKTYLKRFKV---MKPKVLRSWCRQ------ILKGLLFLHTRT-PPIIHRDLKCDNIFITGPTgSVKIGDLGLAT 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  863 LllkfDEESFfnqlsSAGVRGTIGYAAPE-YGVGGQPSIngDVYSFGILLLEMFTGKRPTNE 923
Cdd:cd14032  156 L----KRASF-----AKSVIGTPEFMAPEmYEEHYDESV--DVYAFGMCMLEMATSEYPYSE 206
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
708-918 6.79e-10

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: 60.90  E-value: 6.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYkalLLTEKKVVA---VKVLNMQRRGAMK-----SFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRAL 779
Cdd:cd08222    8 LGSGNFGTVY---LVSDLKATAdeeLKVLKEISVGELQpdetvDANREAKLLSKLDHPAIVKFHDS-----FVEKESFCI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  780 IYEFMPNGSLDmwlhpEEVEEIHRPSRTLTLLERLNIAIDVASVLDYLHVhchEPIAHCDLKPSNVLLDDDLTaHVSDFG 859
Cdd:cd08222   80 VTEYCEGGDLD-----DKISEYKKSGTTIDENQILDWFIQLLLAVQYMHE---RRILHRDLKAKNIFLKNNVI-KVGDFG 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  860 LARLLL-KFDEESFFNqlssagvrGTIGYAAPEYGVGGQPSINGDVYSFGILLLEM------FTGK 918
Cdd:cd08222  151 ISRILMgTSDLATTFT--------GTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMcclkhaFDGQ 208
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
709-920 7.19e-10

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: 61.30  E-value: 7.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSfmaeceslKDIRHrnlVKLLTACSS---IDFQG-----NEFrALI 780
Cdd:cd06615   10 GAGNGGVVTKVLHRPSGLIMARKLIHLEIKPAIRN--------QIIRE---LKVLHECNSpyiVGFYGafysdGEI-SIC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFMPNGSLDMWLH-----PEEVeeihrpsrtltlLERLNIAidVASVLDYLH-VHchePIAHCDLKPSNVLLDDDLTAH 854
Cdd:cd06615   78 MEHMDGGSLDQVLKkagriPENI------------LGKISIA--VLRGLTYLReKH---KIMHRDVKPSNILVNSRGEIK 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  855 VSDFGLARLLLKFDEESFFnqlssagvrGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd06615  141 LCDFGVSGQLIDSMANSFV---------GTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYP 197
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
707-945 7.38e-10

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: 60.99  E-value: 7.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRG----AMKSFMAECESLKDIRHRNLVKLLTACSSidfqGNEFRaLIYE 782
Cdd:cd14070    9 KLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKkdsyVTKNLRREGRIQQMIRHPNITQLLDILET----ENSYY-LVME 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLdmwlhpeeVEEIHRPSRtLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGL-- 860
Cdd:cd14070   84 LCPGGNL--------MHRIYDKKR-LEEREARRYIRQLVSAVEHLHRA---GVVHRDLKIENLLLDENDNIKLIDFGLsn 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  861 -ARLLLKFDEesFFNQLssagvrGTIGYAAPE------YGvggqPSIngDVYSFGILLLEMFTGKRPtnelfggnFTLNS 933
Cdd:cd14070  152 cAGILGYSDP--FSTQC------GSPAYAAPEllarkkYG----PKV--DVWSIGVNMYAMLTGTLP--------FTVEP 209
                        250
                 ....*....|..
gi 18408454  934 YTKSALPERILD 945
Cdd:cd14070  210 FSLRALHQKMVD 221
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
693-920 7.94e-10

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: 61.19  E-value: 7.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  693 GDLRNATNGFSSsnmVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACssidFQ 772
Cdd:cd06657   16 GDPRTYLDNFIK---IGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSY----LV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  773 GNEFrALIYEFMPNGSL-DMWLHPEEVEEihrpsrtltllerlNIAIDVASVLDYLHVHCHEPIAHCDLKPSNVLLDDDL 851
Cdd:cd06657   89 GDEL-WVVMEFLEGGALtDIVTHTRMNEE--------------QIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  852 TAHVSDFGlarlllkfdeesFFNQLSSAGVR-----GTIGYAAPE------YGvggqPSIngDVYSFGILLLEMFTGKRP 920
Cdd:cd06657  154 RVKLSDFG------------FCAQVSKEVPRrkslvGTPYWMAPElisrlpYG----PEV--DIWSLGIMVIEMVDGEPP 215
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
708-920 8.11e-10

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: 60.84  E-value: 8.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVL-----------------------NMQRRGAMKSFMAECESLKDIRHRNLVKLLT 764
Cdd:cd14118    2 IGKGSYGIVKLAYNEEDNTLYAMKILskkkllkqagffrrppprrkpgaLGKPLDPLDRVYREIAILKKLDHPNVVKLVE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  765 AcssIDFQGNEFRALIYEFMPNGsldmwlhpeEVEEIhrPSrTLTLLERL--NIAIDVASVLDYLHvhcHEPIAHCDLKP 842
Cdd:cd14118   82 V---LDDPNEDNLYMVFELVDKG---------AVMEV--PT-DNPLSEETarSYFRDIVLGIEYLH---YQKIIHRDIKP 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  843 SNVLLDDDLTAHVSDFGLARLLLKFDEEsffnqLSSAGvrGTIGYAAPEYGVGGQPSING---DVYSFGILLLEMFTGKR 919
Cdd:cd14118  144 SNLLLGDDGHVKIADFGVSNEFEGDDAL-----LSSTA--GTPAFMAPEALSESRKKFSGkalDIWAMGVTLYCFVFGRC 216

                 .
gi 18408454  920 P 920
Cdd:cd14118  217 P 217
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
688-936 8.34e-10

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: 61.20  E-value: 8.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  688 EKISYGDL-RNATNGFSSSNMVGSGSFGTVYKALLLTEKKVVAVK---VLNMQRRGAMKSFMAECESLKDIRHRNLVKLL 763
Cdd:cd08229   11 QKALRPDMgYNTLANFRIEKKIGRGQFSEVYRATCLLDGVPVALKkvqIFDLMDAKARADCIKEIDLLKQLNHPNVIKYY 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  764 TACssidFQGNEFRaLIYEFMPNGSLDMWLHPEEVEEIHRPSRTLtllerLNIAIDVASVLDYLHvhcHEPIAHCDLKPS 843
Cdd:cd08229   91 ASF----IEDNELN-IVLELADAGDLSRMIKHFKKQKRLIPEKTV-----WKYFVQLCSALEHMH---SRRVMHRDIKPA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  844 NVLLDDDLTAHVSDFGLARlllkfdeesFFNQLSSAG--VRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPt 921
Cdd:cd08229  158 NVFITATGVVKLGDLGLGR---------FFSSKTTAAhsLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSP- 227
                        250
                 ....*....|....*
gi 18408454  922 neLFGGNFTLNSYTK 936
Cdd:cd08229  228 --FYGDKMNLYSLCK 240
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
708-920 9.63e-10

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: 60.73  E-value: 9.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQR-------------RGA-------------MKSFMAECESLKDIRHRNLVK 761
Cdd:cd14200    8 IGKGSYGVVKLAYNESDDKYYAMKVLSKKKllkqygfprrpppRGSkaaqgeqakplapLERVYQEIAILKKLDHVNIVK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  762 LLTAcssIDFQGNEFRALIYEFMPNGSldmwlhpeeVEEIhrPSRTLTLLERLNIAI-DVASVLDYLHvhcHEPIAHCDL 840
Cdd:cd14200   88 LIEV---LDDPAEDNLYMVFDLLRKGP---------VMEV--PSDKPFSEDQARLYFrDIVLGIEYLH---YQKIVHRDI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  841 KPSNVLLDDDLTAHVSDFGLARLLLKFDEesffnQLSSAGvrGTIGYAAPEYGVGGQPSING---DVYSFGILLLEMFTG 917
Cdd:cd14200  151 KPSNLLLGDDGHVKIADFGVSNQFEGNDA-----LLSSTA--GTPAFMAPETLSDSGQSFSGkalDVWAMGVTLYCFVYG 223

                 ...
gi 18408454  918 KRP 920
Cdd:cd14200  224 KCP 226
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
707-925 1.17e-09

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: 61.11  E-value: 1.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVLnmQRRGAMKSFMAECeSLKDIRHRNLV---KLLTACSSIdFQGNEFRALIYEF 783
Cdd:cd05620    2 VLGKGSFGKVLLAELKGKGEYFAVKAL--KKDVVLIDDDVEC-TMVEKRVLALAwenPFLTHLYCT-FQTKEHLFFVMEF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  784 MPNGSLDMWLHPEEVEEIHRPSRtltllerlnIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARl 863
Cdd:cd05620   78 LNGGDLMFHIQDKGRFDLYRATF---------YAAEIVCGLQFLH---SKGIIYRDLKLDNVMLDRDGHIKIADFGMCK- 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  864 llkfdeESFFNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP-----TNELF 925
Cdd:cd05620  145 ------ENVFGDNRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPfhgddEDELF 205
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
708-920 1.18e-09

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: 60.15  E-value: 1.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFM---AECESLKDIR------------HRNLVKLLTACSSidfq 772
Cdd:cd14077    9 IGAGSMGKVKLAKHIRTGEKCAIKIIPRASNAGLKKERekrLEKEISRDIRtireaalssllnHPHICRLRDFLRT---- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  773 gNEFRALIYEFMPNGS-LDMWLHPEEVEEIHRPSrtltllerlnIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDL 851
Cdd:cd14077   85 -PNHYYMLFEYVDGGQlLDYIISHGKLKEKQARK----------FARQIASALDYLH---RNSIVHRDLKIENILISKSG 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18408454  852 TAHVSDFGLARLllkFDEESFFNQLSsagvrGTIGYAAPEYgVGGQPSING--DVYSFGILLLEMFTGKRP 920
Cdd:cd14077  151 NIKIIDFGLSNL---YDPRRLLRTFC-----GSLYFAAPEL-LQAQPYTGPevDVWSFGVVLYVLVCGKVP 212
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
702-920 1.24e-09

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: 61.19  E-value: 1.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQ---RRGAMKSFMAECESL-KDIRHRNLVKLltacsSIDFQGNEFR 777
Cdd:cd05602    9 FHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKailKKKEEKHIMSERNVLlKNVKHPFLVGL-----HFSFQTTDKL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  778 ALIYEFMPNGSLDMWLHPEeveeihrpsRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSD 857
Cdd:cd05602   84 YFVLDYINGGELFYHLQRE---------RCFLEPRARFYAAEIASALGYLH---SLNIVYRDLKPENILLDSQGHIVLTD 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18408454  858 FGLARlllkfdeESFFNQLSSAGVRGTIGYAAPEYgVGGQP-SINGDVYSFGILLLEMFTGKRP 920
Cdd:cd05602  152 FGLCK-------ENIEPNGTTSTFCGTPEYLAPEV-LHKQPyDRTVDWWCLGAVLYEMLYGLPP 207
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
702-920 1.25e-09

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: 60.31  E-value: 1.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSfmAECESLKD--IRHRNLVKLLTACSSI-----DFQGN 774
Cdd:cd14182    5 YEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDITGGGSFSP--EEVQELREatLKEIDILRKVSGHPNIiqlkdTYETN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  775 EFRALIYEFMPNGSLDMWLhPEEVeeihrpsrTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAH 854
Cdd:cd14182   83 TFFFLVFDLMKKGELFDYL-TEKV--------TLSEKETRKIMRALLEVICALH---KLNIVHRDLKPENILLDDDMNIK 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  855 VSDFGLArllLKFDEESFFNQlssagVRGTIGYAAPEY----------GVGGQPsingDVYSFGILLLEMFTGKRP 920
Cdd:cd14182  151 LTDFGFS---CQLDPGEKLRE-----VCGTPGYLAPEIiecsmddnhpGYGKEV----DMWSTGVIMYTLLAGSPP 214
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
704-929 1.35e-09

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: 59.98  E-value: 1.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  704 SSNMVGSGSFGT-VYKALLltEKKVVAVKVLnmqrrgamksfMAECESLKDIRhrnlVKLLTA-----------CSSIDF 771
Cdd:cd13982    5 SPKVLGYGSEGTiVFRGTF--DGRPVAVKRL-----------LPEFFDFADRE----VQLLREsdehpnviryfCTEKDR 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  772 QgneFRALIYEFMPNGSLDMWLHPEEVEEIHRPSrtltlLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDD- 850
Cdd:cd13982   68 Q---FLYIALELCAASLQDLVESPRESKLFLRPG-----LEPVRLLRQIASGLAHLH---SLNIVHRDLKPQNILISTPn 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  851 ----LTAHVSDFGLARlLLKFDEESFFNqlsSAGVRGTIGYAAPEY---GVGGQPSINGDVYSFGILLLEMFT-GKRPtn 922
Cdd:cd13982  137 ahgnVRAMISDFGLCK-KLDVGRSSFSR---RSGVAGTSGWIAPEMlsgSTKRRQTRAVDIFSLGCVFYYVLSgGSHP-- 210

                 ....*..
gi 18408454  923 elFGGNF 929
Cdd:cd13982  211 --FGDKL 215
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
705-940 2.13e-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: 59.25  E-value: 2.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  705 SNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAmksfmAECESLKDIRHRNLVKLLTACSsidfqgneFRALIYEFM 784
Cdd:cd13995    9 SDFIPRGAFGKVYLAQDTKTKKRMACKLIPVEQFKP-----SDVEIQACFRHENIAELYGALL--------WEETVHLFM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLDMWLhpEEVEEIHrPSRTLtllERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDlTAHVSDFGLArll 864
Cdd:cd13995   76 EAGEGGSVL--EKLESCG-PMREF---EIIWVTKHVLKGLDFLHSK---NIIHHDIKPSNIVFMST-KAVLVDFGLS--- 142
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  865 LKFDEESFFNQlssaGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPtnelfggnfTLNSYTKSALP 940
Cdd:cd13995  143 VQMTEDVYVPK----DLRGTEIYMSPEVILCRGHNTKADIYSLGATIIHMQTGSPP---------WVRRYPRSAYP 205
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
708-947 2.30e-09

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: 60.45  E-value: 2.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLN--MQRRGAMKSFMAECESLKDIRHRNLVKLL---TACSSIDfQGNEFRaLIYE 782
Cdd:cd07878   23 VGSGAYGSVCSAYDTRLRQKVAVKKLSrpFQSLIHARRTYRELRLLKHMKHENVIGLLdvfTPATSIE-NFNEVY-LVTN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMpNGSLDMWLHPEEVEEIHRPSRTLTLLERLNiaidvasvldYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLAR 862
Cdd:cd07878  101 LM-GADLNNIVKCQKLSDEHVQFLIYQLLRGLK----------YIH---SAGIIHRDLKPSNVAVNEDCELRILDFGLAR 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  863 lllKFDEEsffnqlsSAGVRGTIGYAAPEYGVGG-QPSINGDVYSFGILLLEMFTGKrptnELFGGNFTLNSYtksalpE 941
Cdd:cd07878  167 ---QADDE-------MTGYVATRWYRAPEIMLNWmHYNQTVDIWSVGCIMAELLKGK----ALFPGNDYIDQL------K 226

                 ....*.
gi 18408454  942 RILDIV 947
Cdd:cd07878  227 RIMEVV 232
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
708-928 2.32e-09

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


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 59.64  E-value: 2.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQR-RGAMKSFMAECESLKDIRHRNLVKLLtacssiDFQGNEFR-ALIYEFMP 785
Cdd:cd07871   13 LGEGTYATVFKGRSKLTENLVALKEIRLEHeEGAPCTAIREVSLLKNLKHANIVTLH------DIIHTERClTLVFEYLD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NgSLDMWLhpeeveeihrpSRTLTLLERLNIAIDVASVLDYLHvHCHE-PIAHCDLKPSNVLLDDDLTAHVSDFGLARlL 864
Cdd:cd07871   87 S-DLKQYL-----------DNCGNLMSMHNVKIFMFQLLRGLS-YCHKrKILHRDLKPQNLLINEKGELKLADFGLAR-A 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  865 LKFDEESFFNQLSsagvrgTIGYAAPEYGVGG-QPSINGDVYSFGILLLEMFTGkRPtneLFGGN 928
Cdd:cd07871  153 KSVPTKTYSNEVV------TLWYRPPDVLLGStEYSTPIDMWGVGCILYEMATG-RP---MFPGS 207
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
703-952 2.40e-09

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: 59.16  E-value: 2.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  703 SSSNMVGSGSFGTVYKAlllTEKKV---VAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRAL 779
Cdd:cd14190    7 HSKEVLGGGKFGKVHTC---TEKRTglkLAAKVINKQNSKDKEMVLLEIQVMNQLNHRNLIQLYEA-----IETPNEIVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  780 IYEFMPNGSLdmwlhpeeVEEIHRPSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDlTAH---VS 856
Cdd:cd14190   79 FMEYVEGGEL--------FERIVDEDYHLTEVDAMVFVRQICEGIQFMH---QMRVLHLDLKPENILCVNR-TGHqvkII 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  857 DFGLARLllkfdeesfFNQLSSAGVR-GTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP---------TNELFG 926
Cdd:cd14190  147 DFGLARR---------YNPREKLKVNfGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPflgdddtetLNNVLM 217
                        250       260
                 ....*....|....*....|....*.
gi 18408454  927 GNFTLNSYTKSALPERILDIVDESIL 952
Cdd:cd14190  218 GNWYFDEETFEHVSDEAKDFVSNLII 243
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
697-920 2.47e-09

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


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 59.26  E-value: 2.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  697 NATNGFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQR-----RGAMKSFMA-ECESLKDIRHRNLVKLLTAcssid 770
Cdd:cd14194    2 NVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRtkssrRGVSREDIErEVSILKEIQHPNVITLHEV----- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  771 FQGNEFRALIYEFMPNGSLDMWLHPEEveeihrpsrTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDD 850
Cdd:cd14194   77 YENKTDVILILELVAGGELFDFLAEKE---------SLTEEEATEFLKQILNGVYYLH---SLQIAHFDLKPENIMLLDR 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  851 LTAH----VSDFGLARlllKFDeesFFNQLSSagVRGTIGYAAPEYgVGGQP-SINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14194  145 NVPKprikIIDFGLAH---KID---FGNEFKN--IFGTPEFVAPEI-VNYEPlGLEADMWSIGVITYILLSGASP 210
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
708-936 2.53e-09

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


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 59.97  E-value: 2.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLN--MQRRGAMKSFMAECESLKDIRHRNLVKLL---TACSSIDfQGNEFRaLIYE 782
Cdd:cd07880   23 VGSGAYGTVCSALDRRTGAKVAIKKLYrpFQSELFAKRAYRELRLLKHMKHENVIGLLdvfTPDLSLD-RFHDFY-LVMP 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMpNGSLDMWLHPEEVEEihrpsrtltllERLNIAI-DVASVLDYLHVhchEPIAHCDLKPSNVLLDDDLTAHVSDFGLA 861
Cdd:cd07880  101 FM-GTDLGKLMKHEKLSE-----------DRIQFLVyQMLKGLKYIHA---AGIIHRDLKPGNLAVNEDCELKILDFGLA 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  862 RlllKFDEEsffnqlsSAGVRGTIGYAAPEYGVGGQPSING-DVYSFGILLLEMFTGKrptnELFGGNFTLNSYTK 936
Cdd:cd07880  166 R---QTDSE-------MTGYVVTRWYRAPEVILNWMHYTQTvDIWSVGCIMAEMLTGK----PLFKGHDHLDQLME 227
PLN03150 PLN03150
hypothetical protein; Provisional
337-409 3.55e-09

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 60.60  E-value: 3.55e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454   337 QLETLGIGRNRLGGDLPISIANLSAkLVTLDLGGTLISGSIPYDIGNLINLQKLILDQNMLSGPLPTSLGKLL 409
Cdd:PLN03150  443 HLQSINLSGNSIRGNIPPSLGSITS-LEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSLSGRVPAALGGRL 514
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
702-920 3.79e-09

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: 59.55  E-value: 3.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVL---NMQRRGAMKSFMAECESLKDIRHRNLVKLLtaCSsidFQGNEFRA 778
Cdd:cd05599    3 FEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLrksEMLEKEQVAHVRAERDILAEADNPWVVKLY--YS---FQDEENLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGslDMwlhpeeveeihrpsrtLTLLERLNI---------------AIDvasvldylHVHCHEPIaHCDLKPS 843
Cdd:cd05599   78 LIMEFLPGG--DM----------------MTLLMKKDTlteeetrfyiaetvlAIE--------SIHKLGYI-HRDIKPD 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  844 NVLLDDDltAHV--SDFGLARLLLKfdeesffNQLSSAGVrGTIGYAAPEygVGGQPSING--DVYSFGILLLEMFTGKR 919
Cdd:cd05599  131 NLLLDAR--GHIklSDFGLCTGLKK-------SHLAYSTV-GTPDYIAPE--VFLQKGYGKecDWWSLGVIMYEMLIGYP 198

                 .
gi 18408454  920 P 920
Cdd:cd05599  199 P 199
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
705-920 4.14e-09

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: 58.89  E-value: 4.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  705 SNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIR-HRNLVKLLTAcssidFQGNEFRALIYEF 783
Cdd:cd14173    7 EEVLGEGAYARVQTCINLITNKEYAVKIIEKRPGHSRSRVFREVEMLYQCQgHRNVLELIEF-----FEEEDKFYLVFEK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  784 MPNGSLdmwlhpeeVEEIHRpSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLD--DDLT-AHVSDFGL 860
Cdd:cd14173   82 MRGGSI--------LSHIHR-RRHFNELEASVVVQDIASALDFLH---NKGIAHRDLKPENILCEhpNQVSpVKICDFDL 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  861 ARlLLKFDEESffNQLSSAGVR---GTIGYAAPEY--GVGGQPSI---NGDVYSFGILLLEMFTGKRP 920
Cdd:cd14173  150 GS-GIKLNSDC--SPISTPELLtpcGSAEYMAPEVveAFNEEASIydkRCDLWSLGVILYIMLSGYPP 214
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
702-959 4.20e-09

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: 59.24  E-value: 4.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVykalLLTEKK----VVAVKVLNMQ---RRGAMKSFMAECESLKDIRHRNLVKLLTACssidFQGN 774
Cdd:cd05616    2 FNFLMVLGKGSFGKV----MLAERKgtdeLYAVKILKKDvviQDDDVECTMVEKRVLALSGKPPFLTQLHSC----FQTM 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  775 EFRALIYEFMPNGslDMWLHPEEVEEIHRPSRTLtllerlnIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAH 854
Cdd:cd05616   74 DRLYFVMEYVNGG--DLMYHIQQVGRFKEPHAVF-------YAAEIAIGLFFLQ---SKGIIYRDLKLDNVMLDSEGHIK 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  855 VSDFGLARlllkfdeESFFNQLSSAGVRGTIGYAAPEYgVGGQP-SINGDVYSFGILLLEMFTGKRP-----TNELFGGN 928
Cdd:cd05616  142 IADFGMCK-------ENIWDGVTTKTFCGTPDYIAPEI-IAYQPyGKSVDWWAFGVLLYEMLAGQAPfegedEDELFQSI 213
                        250       260       270
                 ....*....|....*....|....*....|..
gi 18408454  929 FTLN-SYTKSALPERILDIVDESILHIGLRVG 959
Cdd:cd05616  214 MEHNvAYPKSMSKEAVAICKGLMTKHPGKRLG 245
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
694-936 4.27e-09

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: 60.02  E-value: 4.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  694 DLRNATNGFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLN---MQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssid 770
Cdd:cd05622   67 DLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSkfeMIKRSDSAFFWEERDIMAFANSPWVVQLFYA----- 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  771 FQGNEFRALIYEFMPNGSLDMWLHPEEVEEihRPSRTLTllerlniaIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDD 850
Cdd:cd05622  142 FQDDRYLYMVMEYMPGGDLVNLMSNYDVPE--KWARFYT--------AEVVLALDAIH---SMGFIHRDVKPDNMLLDKS 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  851 LTAHVSDFGLArllLKFDEESFFNQLSSAgvrGTIGYAAPEY----GVGGQPSINGDVYSFGILLLEMFTGKRPtnelFG 926
Cdd:cd05622  209 GHLKLADFGTC---MKMNKEGMVRCDTAV---GTPDYISPEVlksqGGDGYYGRECDWWSVGVFLYEMLVGDTP----FY 278
                        250
                 ....*....|
gi 18408454  927 GNFTLNSYTK 936
Cdd:cd05622  279 ADSLVGTYSK 288
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
702-891 4.39e-09

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


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 58.54  E-value: 4.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQR-RGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALI 780
Cdd:cd14083    5 YEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKAlKGKEDSLENEIAVLRKIKHPNIVQLLDI-----YESKSHLYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFMPNGSLdmwlHPEEVEEIHRPSRTLTLLERlniaiDVASVLDYLHvhcHEPIAHCDLKPSNVL---LDDDLTAHVSD 857
Cdd:cd14083   80 MELVTGGEL----FDRIVEKGSYTEKDASHLIR-----QVLEAVDYLH---SLGIVHRDLKPENLLyysPDEDSKIMISD 147
                        170       180       190
                 ....*....|....*....|....*....|....
gi 18408454  858 FGLARLllkfdEESffNQLSSAGvrGTIGYAAPE 891
Cdd:cd14083  148 FGLSKM-----EDS--GVMSTAC--GTPGYVAPE 172
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
700-920 4.47e-09

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: 58.99  E-value: 4.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  700 NGFSSSNMVGSGSFGTVYKAL-LLTEKKVVAVKVLN-----------MQRRGAMKsfmaECESLKDIRHRNLVKLltacs 767
Cdd:cd14096    1 ENYRLINKIGEGAFSNVYKAVpLRNTGKPVAIKVVRkadlssdnlkgSSRANILK----EVQIMKRLSHPNIVKL----- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  768 sIDFQGN-EFRALIYEFMPNGsldmwlhpeevEEIHRPSRTLTLLERLN--IAIDVASVLDYLHvhcHEPIAHCDLKPSN 844
Cdd:cd14096   72 -LDFQESdEYYYIVLELADGG-----------EIFHQIVRLTYFSEDLSrhVITQVASAVKYLH---EIGVVHRDIKPEN 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  845 VL---------------LDDDLT------------------AHVSDFGLARLLlkfdeesFFNQLSSAGvrGTIGYAAPE 891
Cdd:cd14096  137 LLfepipfipsivklrkADDDETkvdegefipgvggggigiVKLADFGLSKQV-------WDSNTKTPC--GTVGYTAPE 207
                        250       260
                 ....*....|....*....|....*....
gi 18408454  892 YGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14096  208 VVKDERYSKKVDMWALGCVLYTLLCGFPP 236
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
708-924 4.51e-09

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: 58.85  E-value: 4.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVY------------KALLL----TEKKVVAVKVLNMQ-RRGAMKSFMAECESLKDIRHRNLVKLLTACSSID 770
Cdd:cd05095   13 LGEGQFGEVHlceaegmekfmdKDFALevseNQPVLVAVKMLRADaNKNARNDFLKEIKIMSRLKDPNIIRLLAVCITDD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  771 FQgnefrALIYEFMPNGSLDMWLHPEEVE-EIHRPSRTLTL--LERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLL 847
Cdd:cd05095   93 PL-----CMITEYMENGDLNQFLSRQQPEgQLALPSNALTVsySDLRFMAAQIASGMKYLS---SLNFVHRDLATRNCLV 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  848 DDDLTAHVSDFGLARLLLKFDeesfFNQLSSAGVRgTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT--GKRPTNEL 924
Cdd:cd05095  165 GKNYTIKIADFGMSRNLYSGD----YYRIQGRAVL-PIRWMSWESILLGKFTTASDVWAFGVTLWETLTfcREQPYSQL 238
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
817-920 4.65e-09

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: 58.91  E-value: 4.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  817 AIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLArllLKFDEESffnqlSSAGVRGTIGYAAPEYGVGG 896
Cdd:cd05605  108 AAEITCGLEHLH---SERIVYRDLKPENILLDDHGHVRISDLGLA---VEIPEGE-----TIRGRVGTVGYMAPEVVKNE 176
                         90       100
                 ....*....|....*....|....
gi 18408454  897 QPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd05605  177 RYTFSPDWWGLGCLIYEMIEGQAP 200
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
708-914 5.92e-09

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: 58.04  E-value: 5.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSiDFQGNefraLIYEFMPNG 787
Cdd:cd14221    1 LGKGCFGQAIKVTHRETGEVMVMKELIRFDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYK-DKRLN----FITEYIKGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 SLDMWLHPEEVeeiHRPSRtltllERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARLLLkf 867
Cdd:cd14221   76 TLRGIIKSMDS---HYPWS-----QRVSFAKDIASGMAYLH---SMNIIHRDLNSHNCLVRENKSVVVADFGLARLMV-- 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  868 DEESFFNQLSSA---------GVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEM 914
Cdd:cd14221  143 DEKTQPEGLRSLkkpdrkkryTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEI 198
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
708-928 5.95e-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: 58.21  E-value: 5.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVK--VLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSidfqgNEFRALIYEFMP 785
Cdd:cd07839    8 IGEGTYGTVFKAKNRETHEIVALKrvRLDDDDEGVPSSALREICLLKELKHKNIVRLYDVLHS-----DKKLTLVFEYCD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 ----------NGSLDmwlhPEEVEeihrpSRTLTLLERLNiaidvasvldylhvHCHEP-IAHCDLKPSNVLLDDDLTAH 854
Cdd:cd07839   83 qdlkkyfdscNGDID----PEIVK-----SFMFQLLKGLA--------------FCHSHnVLHRDLKPQNLLINKNGELK 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  855 VSDFGLARlllkfdeeSF---FNQLSSAGVrgTIGYAAPEYGVGGQ---PSIngDVYSFGILLLEMFTGKRPtneLFGGN 928
Cdd:cd07839  140 LADFGLAR--------AFgipVRCYSAEVV--TLWYRPPDVLFGAKlysTSI--DMWSAGCIFAELANAGRP---LFPGN 204
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
708-917 6.23e-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: 6.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRR-GAMKSFMAECESLKDIRHRNLVKLLTACSSidfqgNEFRALIYEFM-- 784
Cdd:cd07869   13 LGEGSYATVYKGKSKVNGKLVALKVIRLQEEeGTPFTAIREASLLKGLKHANIVLLHDIIHT-----KETLTLVFEYVht 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 ---------PNGsldmwLHPEEVEeihrpsrtLTLLERLNiaidvasVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHV 855
Cdd:cd07869   88 dlcqymdkhPGG-----LHPENVK--------LFLFQLLR-------GLSYIH---QRYILHRDLKPQNLLISDTGELKL 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  856 SDFGLARlLLKFDEESFFNQLSsagvrgTIGYAAPEYGVGG-QPSINGDVYSFGILLLEMFTG 917
Cdd:cd07869  145 ADFGLAR-AKSVPSHTYSNEVV------TLWYRPPDVLLGStEYSTCLDMWGVGCIFVEMIQG 200
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
708-928 6.26e-09

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


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 58.51  E-value: 6.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNM---QRRGAMKSFMAECESLKDIRHRNlvklltacsSIDFQGNEFRA----LI 780
Cdd:cd06633   29 IGHGSFGAVYFATNSHTNEVVAIKKMSYsgkQTNEKWQDIIKEVKFLQQLKHPN---------TIEYKGCYLKDhtawLV 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFMPNGSLDMWlhpeeveEIHRpsRTLTLLERLNIAIDVASVLDYLHVHChepIAHCDLKPSNVLLDDDLTAHVSDFGL 860
Cdd:cd06633  100 MEYCLGSASDLL-------EVHK--KPLQEVEIAAITHGALQGLAYLHSHN---MIHRDIKAGNILLTEPGQVKLADFGS 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18408454  861 ARLLLKFDeeSFFnqlssagvrGTIGYAAPEYGVG---GQPSINGDVYSFGILLLEMFTGKRPtneLFGGN 928
Cdd:cd06633  168 ASIASPAN--SFV---------GTPYWMAPEVILAmdeGQYDGKVDIWSLGITCIELAERKPP---LFNMN 224
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
709-921 6.82e-09

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: 58.16  E-value: 6.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVYKALLLTEKKVVAVKVLNMQ-RRGAMKSFMAECESLKDIRHRNLV---------KLLTacssidfqgnefra 778
Cdd:cd07844    9 GEGSYATVYKGRSKLTGQLVALKEIRLEhEEGAPFTAIREASLLKDLKHANIVtlhdiihtkKTLT-------------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFM-----------PNGsldmwLHPEEVEeihrpsrtLTLLERLNiaidvasVLDYLHvhcHEPIAHCDLKPSNVLL 847
Cdd:cd07844   75 LVFEYLdtdlkqymddcGGG-----LSMHNVR--------LFLFQLLR-------GLAYCH---QRRVLHRDLKPQNLLI 131
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  848 DDDLTAHVSDFGLARlllkfdEESFFNQLSSAGVRgTIGYAAPEYGVGGQP-SINGDVYSFGILLLEMFTGkRPT 921
Cdd:cd07844  132 SERGELKLADFGLAR------AKSVPSKTYSNEVV-TLWYRPPDVLLGSTEySTSLDMWGVGCIFYEMATG-RPL 198
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
687-925 6.83e-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: 58.73  E-value: 6.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  687 HEKISYGDLrnATNGFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVL-NMQR-RGAMKSfmaECESLKDIRHR------N 758
Cdd:cd14134    1 HLIYKPGDL--LTNRYKILRLLGEGTFGKVLECWDRKRKRYVAVKIIrNVEKyREAAKI---EIDVLETLAEKdpngksH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  759 LVKLLTAcssIDFQGnefraliyefmpngsldmwlHPEEVEEIHRPSrtltLLERL--------------NIAIDVASVL 824
Cdd:cd14134   76 CVQLRDW---FDYRG--------------------HMCIVFELLGPS----LYDFLkknnygpfplehvqHIAKQLLEAV 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  825 DYLHvHCHepIAHCDLKPSNVLLDDDLTAHVS-------------------DFGLArlllKFDEESFfnqlSSagVRGTI 885
Cdd:cd14134  129 AFLH-DLK--LTHTDLKPENILLVDSDYVKVYnpkkkrqirvpkstdikliDFGSA----TFDDEYH----SS--IVSTR 195
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 18408454  886 GYAAPE--YGVG-GQPSingDVYSFGILLLEMFTGKRptneLF 925
Cdd:cd14134  196 HYRAPEviLGLGwSYPC---DVWSIGCILVELYTGEL----LF 231
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
702-920 6.98e-09

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: 58.12  E-value: 6.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQR-RGAMKSFMAECESLKDIRHRNLVKLltacSSIdFQGNEFRALI 780
Cdd:cd14167    5 YDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKAlEGKETSIENEIAVLHKIKHPNIVAL----DDI-YESGGHLYLI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFMPNGSLdmwlHPEEVEEIHRPSRTLTLLerlniaidVASVLD---YLHvhcHEPIAHCDLKPSNVL---LDDDLTAH 854
Cdd:cd14167   80 MQLVSGGEL----FDRIVEKGFYTERDASKL--------IFQILDavkYLH---DMGIVHRDLKPENLLyysLDEDSKIM 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  855 VSDFGLARLllkfdeESFFNQLSSAGvrGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14167  145 ISDFGLSKI------EGSGSVMSTAC--GTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPP 202
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
708-920 7.52e-09

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: 57.71  E-value: 7.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFMPNG 787
Cdd:cd14191   10 LGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDA-----FEEKANIVMVLEMVSGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 SLDMWLHPEEVEeihrpsrtLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVS--DFGLARlll 865
Cdd:cd14191   85 ELFERIIDEDFE--------LTERECIKYMRQISEGVEYIH---KQGIVHLDLKPENIMCVNKTGTKIKliDFGLAR--- 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  866 kfdeesffnQLSSAG----VRGTIGYAAPEYgVGGQP-SINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14191  151 ---------RLENAGslkvLFGTPEFVAPEV-INYEPiGYATDMWSIGVICYILVSGLSP 200
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
709-920 7.59e-09

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: 58.47  E-value: 7.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVYKALLLTEKKVVAVKVLNmQRRGAMKsfmaECESLKDIR-HRNLVKLltacssIDFQGNEFRA-LIYEFMPN 786
Cdd:cd14092   15 GDGSFSVCRKCVHKKTGQEFAVKIVS-RRLDTSR----EVQLLRLCQgHPNIVKL------HEVFQDELHTyLVMELLRG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  787 GSLdmwlhpeeVEEIhRPSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLL---DDDLTAHVSDFGLARl 863
Cdd:cd14092   84 GEL--------LERI-RKKKRFTESEASRIMRQLVSAVSFMH---SKGVVHRDLKPENLLFtdeDDDAEIKIVDFGFAR- 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  864 lLKFDEESF----FnqlssagvrgTIGYAAPEYgVGGQPSING-----DVYSFGILLLEMFTGKRP 920
Cdd:cd14092  151 -LKPENQPLktpcF----------TLPYAAPEV-LKQALSTQGydescDLWSLGVILYTMLSGQVP 204
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
708-928 7.84e-09

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: 58.09  E-value: 7.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQ-RRGAMKSFMAECESLKDIRHRNLVKLLTACSSidfqgNEFRALIYEFMpN 786
Cdd:cd07873   10 LGEGTYATVYKGRSKLTDNLVALKEIRLEhEEGAPCTAIREVSLLKDLKHANIVTLHDIIHT-----EKSLTLVFEYL-D 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  787 GSLDMWLhpeeveeihrpSRTLTLLERLNIAIDVASVLDYLHvHCH-EPIAHCDLKPSNVLLDDDLTAHVSDFGLARlLL 865
Cdd:cd07873   84 KDLKQYL-----------DDCGNSINMHNVKLFLFQLLRGLA-YCHrRKVLHRDLKPQNLLINERGELKLADFGLAR-AK 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18408454  866 KFDEESFFNQLSsagvrgTIGYAAPEYGVGG-QPSINGDVYSFGILLLEMFTGkRPtneLFGGN 928
Cdd:cd07873  151 SIPTKTYSNEVV------TLWYRPPDILLGStDYSTQIDMWGVGCIFYEMSTG-RP---LFPGS 204
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
708-916 8.24e-09

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


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 58.45  E-value: 8.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLT--EKKVVAVKVL---NMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSidfQGNEFRALIYE 782
Cdd:cd07842    8 IGRGTYGRVYKAKRKNgkDGKEYAIKKFkgdKEQYTGISQSACREIALLRELKHENVVSLVEVFLE---HADKSVYLLFD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FmpnGSLDMWlhpeEVEEIHRPSRTLTLLERL--NIAIDVASVLDYLHVHChepIAHCDLKPSNVLLDDDLTAH----VS 856
Cdd:cd07842   85 Y---AEHDLW----QIIKFHRQAKRVSIPPSMvkSLLWQILNGIHYLHSNW---VLHRDLKPANILVMGEGPERgvvkIG 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  857 DFGLARLllkfdeesfFNQ-----LSSAGVRGTIGYAAPEYGVGGQ---PSIngDVYSFGILLLEMFT 916
Cdd:cd07842  155 DLGLARL---------FNAplkplADLDPVVVTIWYRAPELLLGARhytKAI--DIWAIGCIFAELLT 211
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
708-924 8.34e-09

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


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 58.53  E-value: 8.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVK-------VLNMQRRGamksfMAECESLKDIRHRNLVKLLTACSSiDFQGNEFRA-- 778
Cdd:cd07855   13 IGSGAYGVVCSAIDTKSGQKVAIKkipnafdVVTTAKRT-----LRELKILRHFKHDNIIAIRDILRP-KVPYADFKDvy 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNgSLDMWLHPEEVEEIHRPSRTLTLLERlniaidvasVLDYLHVHChepIAHCDLKPSNVLLDDDLTAHVSDF 858
Cdd:cd07855   87 VVLDLMES-DLHHIIHSDQPLTLEHIRYFLYQLLR---------GLKYIHSAN---VIHRDLKPSNLLVNENCELKIGDF 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  859 GLARLLLKFDEE--SFFNQLSSagvrgTIGYAAPEYG-VGGQPSINGDVYSFGILLLEM------FTGKRPTNEL 924
Cdd:cd07855  154 GMARGLCTSPEEhkYFMTEYVA-----TRWYRAPELMlSLPEYTQAIDMWSVGCIFAEMlgrrqlFPGKNYVHQL 223
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
702-944 8.50e-09

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: 58.39  E-value: 8.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLT---EKKVVAVKVLN----MQRRGAMKSFMAECESLKDIRHRN-LVKLLTAcssidFQG 773
Cdd:cd05614    2 FELLKVLGTGAYGKVFLVRKVSghdANKLYAMKVLRkaalVQKAKTVEHTRTERNVLEHVRQSPfLVTLHYA-----FQT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  774 NEFRALIYEFMPNGslDMWLHpeeveeihrpsrtltLLERLNIAIDVASV--------LDYLHvhcHEPIAHCDLKPSNV 845
Cdd:cd05614   77 DAKLHLILDYVSGG--ELFTH---------------LYQRDHFSEDEVRFysgeiilaLEHLH---KLGIVYRDIKLENI 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  846 LLDDDLTAHVSDFGLARLLLKFDEESFFNqlssagVRGTIGYAAPEY--GVGGQPSINgDVYSFGILLLEMFTGKRPtne 923
Cdd:cd05614  137 LLDSEGHVVLTDFGLSKEFLTEEKERTYS------FCGTIEYMAPEIirGKSGHGKAV-DWWSLGILMFELLTGASP--- 206
                        250       260
                 ....*....|....*....|...
gi 18408454  924 lfggnFTLNSY--TKSALPERIL 944
Cdd:cd05614  207 -----FTLEGEknTQSEVSRRIL 224
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
709-920 8.62e-09

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: 57.84  E-value: 8.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTV--YKALLLTEKkvVAVKVLNMQRRGAMKS---FMAECESLKDIRHRNLVKLLTACSSIDFQG-NEFRALIYE 782
Cdd:cd13989    2 GSGGFGYVtlWKHQDTGEY--VAIKKCRQELSPSDKNrerWCLEVQIMKKLNHPNVVSARDVPPELEKLSpNDLPLLAME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLDMWLHpeeveeihRPSRTLTL--LERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLL---DDDLTAHVSD 857
Cdd:cd13989   80 YCSGGDLRKVLN--------QPENCCGLkeSEVRTLLSDISSAISYLH---ENRIIHRDLKPENIVLqqgGGRVIYKLID 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  858 FGLARLLlkfDEESffnqlSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd13989  149 LGYAKEL---DQGS-----LCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRP 203
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
708-944 9.82e-09

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: 57.14  E-value: 9.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQR--RGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFMP 785
Cdd:cd14072    8 IGKGNFAKVKLARHVLTGREVAIKIIDKTQlnPSSLQKLFREVRIMKILNHPNIVKLFEV-----IETEKTLYLVMEYAS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLDMWL--HPEEVEEIHRPSRTltllerlniaiDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLArl 863
Cdd:cd14072   83 GGEVFDYLvaHGRMKEKEARAKFR-----------QIVSAVQYCH---QKRIVHRDLKAENLLLDADMNIKIADFGFS-- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  864 llkfDEESFFNQLSSagVRGTIGYAAPEYGVGGQ---PSIngDVYSFGILLLEMFTGKRPtnelFGGNftlnsyTKSALP 940
Cdd:cd14072  147 ----NEFTPGNKLDT--FCGSPPYAAPELFQGKKydgPEV--DVWSLGVILYTLVSGSLP----FDGQ------NLKELR 208

                 ....
gi 18408454  941 ERIL 944
Cdd:cd14072  209 ERVL 212
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
702-920 9.92e-09

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: 58.14  E-value: 9.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKS-FMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALI 780
Cdd:cd06649    7 FERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPAIRNqIIRELQVLHECNSPYIVGFYGA-----FYSDGEISIC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFMPNGSLDMWLhpEEVEEIhrPSRTLTllerlNIAIDVASVLDYLHvHCHEpIAHCDLKPSNVLLDDDLTAHVSDFGL 860
Cdd:cd06649   82 MEHMDGGSLDQVL--KEAKRI--PEEILG-----KVSIAVLRGLAYLR-EKHQ-IMHRDVKPSNILVNSRGEIKLCDFGV 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  861 ARLLLKFDEESFFnqlssagvrGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd06649  151 SGQLIDSMANSFV---------GTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYP 201
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
708-936 1.08e-08

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: 58.19  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLN--MQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidfqgnefraliyeFMP 785
Cdd:cd07850    8 IGSGAQGIVCAAYDTVTGQNVAIKKLSrpFQNVTHAKRAYRELVLMKLVNHKNIIGLLNV-----------------FTP 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLDMWLHPEEVEEIhrpsRTLTLLERLNIAIDvASVLDYL---------HVHcHEPIAHCDLKPSNVLLDDDLTAHVS 856
Cdd:cd07850   71 QKSLEEFQDVYLVMEL----MDANLCQVIQMDLD-HERMSYLlyqmlcgikHLH-SAGIIHRDLKPSNIVVKSDCTLKIL 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  857 DFGLARLllkfDEESFFnqLSSAGVrgTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKrptnELFGGNFTLNSYTK 936
Cdd:cd07850  145 DFGLART----AGTSFM--MTPYVV--TRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRGT----VLFPGTDHIDQWNK 212
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
707-920 1.08e-08

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


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 58.09  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGtvyKALLLTEK---KVVAVKVLNMQ---RRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALI 780
Cdd:cd05595    2 LLGKGTFG---KVILVREKatgRYYAMKILRKEviiAKDEVAHTVTESRVLQNTRHPFLTALKYA-----FQTHDRLCFV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFMPNGSLDMWLHPEEVEEIHRPsrtltlleRLNIAiDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGL 860
Cdd:cd05595   74 MEYANGGELFFHLSRERVFTEDRA--------RFYGA-EIVSALEYLH---SRDVVYRDIKLENLMLDKDGHIKITDFGL 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  861 ARlllkfdeESFFNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd05595  142 CK-------EGITDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLP 194
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
706-914 1.10e-08

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


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 57.84  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTVYKALLLTEKkvVAVKVLNMQRRgamKSFMAECESLKDI--RHRNLVKLLtACSSIDFQGNEFRALIYEF 783
Cdd:cd14142   11 ECIGKGRYGEVWRGQWQGES--VAVKIFSSRDE---KSWFRETEIYNTVllRHENILGFI-ASDMTSRNSCTQLWLITHY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  784 MPNGSLDMWLHpeeveeihrpSRTLTLLERLNIAIDVASVLDYLHVH----CHEP-IAHCDLKPSNVLLDDDLTAHVSDF 858
Cdd:cd14142   85 HENGSLYDYLQ----------RTTLDHQEMLRLALSAASGLVHLHTEifgtQGKPaIAHRDLKSKNILVKSNGQCCIADL 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  859 GLArlLLKFDEESFFNQLSSAGVrGTIGYAAPEYgvgGQPSIN---------GDVYSFGILLLEM 914
Cdd:cd14142  155 GLA--VTHSQETNQLDVGNNPRV-GTKRYMAPEV---LDETINtdcfesykrVDIYAFGLVLWEV 213
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
700-920 1.12e-08

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 58.15  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  700 NGFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRrgaMKsfMAECESLKdIRHRNLVKLLTA-------CSSIDFQ 772
Cdd:cd05633    5 NDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKR---IK--MKQGETLA-LNERIMLSLVSTgdcpfivCMTYAFH 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  773 GNEFRALIYEFMPNGSLDMWLHPEEVeeihrpsrtLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLT 852
Cdd:cd05633   79 TPDKLCFILDLMNGGDLHYHLSQHGV---------FSEKEMRFYATEIILGLEHMH---NRFVVYRDLKPANILLDEHGH 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  853 AHVSDFGLArlllkfdeeSFFNQLSSAGVRGTIGYAAPEYGVGGQP-SINGDVYSFGILLLEMFTGKRP 920
Cdd:cd05633  147 VRISDLGLA---------CDFSKKKPHASVGTHGYMAPEVLQKGTAyDSSADWFSLGCMLFKLLRGHSP 206
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
708-927 1.12e-08

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: 57.21  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFMPNG 787
Cdd:cd14114   10 LGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVRKEIQIMNQLHHPKLINLHDA-----FEDDNEMVLILEFLSGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 SLdmwlhpeeVEEIHRPSRTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVS--DFGLARlll 865
Cdd:cd14114   85 EL--------FERIAAEHYKMSEAEVINYMRQVCEGLCHMHEN---NIVHLDIKPENIMCTTKRSNEVKliDFGLAT--- 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  866 KFDEESFFNQLSsagvrGTIGYAAPEYgVGGQP-SINGDVYSFGILLLEMFTGKRPtnelFGG 927
Cdd:cd14114  151 HLDPKESVKVTT-----GTAEFAAPEI-VEREPvGFYTDMWAVGVLSYVLLSGLSP----FAG 203
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
709-920 1.28e-08

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


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 57.63  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVYKALLLTEKKVVAVKVLN---MQRRGAMKSFMAECESLKDIRHRNLVKLLTacssiDFQGNEFRALIYEFMP 785
Cdd:cd05574   10 GKGDVGRVYLVRLKGTGKLFAMKVLDkeeMIKRNKVKRVLTEREILATLDHPFLPTLYA-----SFQTSTHLCFVMDYCP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGsldmwlhpeeveEIHRpsrtltLLERLN---IAIDV-----ASV---LDYLHvhcHEPIAHCDLKPSNVLLDDDltAH 854
Cdd:cd05574   85 GG------------ELFR------LLQKQPgkrLPEEVarfyaAEVllaLEYLH---LLGFVYRDLKPENILLHES--GH 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  855 V--SDFGLARLL-------------------------LKFDEESFFNqlSSAGVrGTIGYAAPEY--GVGGQPSIngDVY 905
Cdd:cd05574  142 ImlTDFDLSKQSsvtpppvrkslrkgsrrssvksiekETFVAEPSAR--SNSFV-GTEEYIAPEVikGDGHGSAV--DWW 216
                        250
                 ....*....|....*
gi 18408454  906 SFGILLLEMFTGKRP 920
Cdd:cd05574  217 TLGILLYEMLYGTTP 231
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
727-915 1.28e-08

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: 57.64  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  727 VVAVKVLNMQ-RRGAMKSFMAECESLKDIRHRNLVKLLTACSSIDFQgnefrALIYEFMPNGSLDMWLHPEEVEEIHRPS 805
Cdd:cd05096   48 LVAVKILRPDaNKNARNDFLKEVKILSRLKDPNIIRLLGVCVDEDPL-----CMITEYMENGDLNQFLSSHHLDDKEENG 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  806 R----------TLTLLERLNIAIDVASVLDYLhvhCHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARLLLKFDeesfFNQ 875
Cdd:cd05096  123 NdavppahclpAISYSSLLHVALQIASGMKYL---SSLNFVHRDLATRNCLVGENLTIKIADFGMSRNLYAGD----YYR 195
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 18408454  876 LSSAGVRgTIGYAAPEYGVGGQPSINGDVYSFGILLLEMF 915
Cdd:cd05096  196 IQGRAVL-PIRWMAWECILMGKFTTASDVWAFGVTLWEIL 234
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
708-945 1.29e-08

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: 57.02  E-value: 1.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGA--MKSFMAECESLKDIRHRNLVKLltacssidFQGNEFRALIY---E 782
Cdd:cd14071    8 IGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEenLKKIYREVQIMKMLNHPHIIKL--------YQVMETKDMLYlvtE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGsldmwlhpeEVEEIHRPSRTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLAR 862
Cdd:cd14071   80 YASNG---------EIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKR---HIVHRDLKAENLLLDANMNIKIADFGFSN 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  863 LllkFDEESFFNQLSsagvrGTIGYAAPEYGVGGQ---PSIngDVYSFGILLLEMFTGKRPtnelFGGNftlnsyTKSAL 939
Cdd:cd14071  148 F---FKPGELLKTWC-----GSPPYAAPEVFEGKEyegPQL--DIWSLGVVLYVLVCGALP----FDGS------TLQTL 207

                 ....*.
gi 18408454  940 PERILD 945
Cdd:cd14071  208 RDRVLS 213
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
702-920 1.43e-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: 57.74  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLN---MQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRA 778
Cdd:cd05597    3 FEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNkweMLKRAETACFREERDVLVNGDRRWITKLHYA-----FQDENYLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGSLDMWLH------PEEVEEIHrpsrtltlLERLNIAIDVASVLDYLHVhchepiahcDLKPSNVLLddDLT 852
Cdd:cd05597   78 LVMDYYCGGDLLTLLSkfedrlPEEMARFY--------LAEMVLAIDSIHQLGYVHR---------DIKPDNVLL--DRN 138
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  853 AHV--SDFGLArllLKFDEESFFNqlSSAGVrGTIGYAAPEY-----GVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd05597  139 GHIrlADFGSC---LKLREDGTVQ--SSVAV-GTPDYISPEIlqameDGKGRYGPECDWWSLGVCMYEMLYGETP 207
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
702-920 1.51e-08

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: 56.86  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGA---MKSFMAECESLKDIRHRNLVKLltacsSIDFQGNEFra 778
Cdd:cd14189    3 YCKGRLLGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKphqREKIVNEIELHRDLHHKHVVKF-----SHHFEDAEN-- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 lIYEFMPNGSLDMWLHpeeveeIHRPSRTLTLLERLNIAIDVASVLDYLHVhchEPIAHCDLKPSNVLLDDDLTAHVSDF 858
Cdd:cd14189   76 -IYIFLELCSRKSLAH------IWKARHTLLEPEVRYYLKQIISGLKYLHL---KGILHRDLKLGNFFINENMELKVGDF 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18408454  859 GLARLLLKFDEEsffnqlsSAGVRGTIGYAAPE--YGVGGQPSinGDVYSFGILLLEMFTGKRP 920
Cdd:cd14189  146 GLAARLEPPEQR-------KKTICGTPNYLAPEvlLRQGHGPE--SDVWSLGCVMYTLLCGNPP 200
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
729-925 1.62e-08

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: 57.02  E-value: 1.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  729 AVKVLNMQ-RRGAMKSF----MAECESLKDIRHRNLVklltacssidfqgnEFRALIYefMPNGSL------------DM 791
Cdd:cd14001   32 AVKKINSKcDKGQRSLYqerlKEEAKILKSLNHPNIV--------------GFRAFTK--SEDGSLclameyggkslnDL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  792 WLHPEEVEEIHRPSRTLtllerLNIAIDVASVLDYLHvhcHEP-IAHCDLKPSNVLLDDDL-TAHVSDFGLArllLKFDE 869
Cdd:cd14001   96 IEERYEAGLGPFPAATI-----LKVALSIARALEYLH---NEKkILHGDIKSGNVLIKGDFeSVKLCDFGVS---LPLTE 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  870 ESFFNQLSSAGVRGTIGYAAPEYGVGGQP-SINGDVYSFGILLLEMFTGKRPTNELF 925
Cdd:cd14001  165 NLEVDSDPKAQYVGTEPWKAKEALEEGGViTDKADIFAYGLVLWEMMTLSVPHLNLL 221
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
690-920 1.81e-08

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: 56.97  E-value: 1.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  690 ISYGDLRNATNGFSSsnmVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACssi 769
Cdd:cd06658   15 VSPGDPREYLDSFIK---IGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRELLFNEVVIMRDYHHENVVDMYNSY--- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  770 dFQGNEFrALIYEFMPNGSL-DMWLHPEEVEEihrpsrtltllERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLD 848
Cdd:cd06658   89 -LVGDEL-WVVMEFLEGGALtDIVTHTRMNEE-----------QIATVCLSVLRALSYLH---NQGVIHRDIKSDSILLT 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  849 DDLTAHVSDFGLARLLLKfdeesffNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd06658  153 SDGRIKLSDFGFCAQVSK-------EVPKRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPP 217
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
708-920 2.16e-08

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: 56.78  E-value: 2.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMqrrgamksfmaeceSLKDIRHRNLVK---LLTACSS---IDFQGNEF-RALI 780
Cdd:cd06622    9 LGKGNYGSVYKVLHRPTGVTMAMKEIRL--------------ELDESKFNQIIMeldILHKAVSpyiVDFYGAFFiEGAV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 Y---EFMPNGSLDMwLHPEEVEEIHRPSRTLTllerlNIAIDVASVLDYLHVHcHEpIAHCDLKPSNVLLDDDLTAHVSD 857
Cdd:cd06622   75 YmcmEYMDAGSLDK-LYAGGVATEGIPEDVLR-----RITYAVVKGLKFLKEE-HN-IIHRDVKPTNVLVNGNGQVKLCD 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  858 FGLARLLLKfdeesffnQLSSAGVrGTIGYAAPEYGVGGQPSING------DVYSFGILLLEMFTGKRP 920
Cdd:cd06622  147 FGVSGNLVA--------SLAKTNI-GCQSYMAPERIKSGGPNQNPtytvqsDVWSLGLSILEMALGRYP 206
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
706-925 2.20e-08

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: 56.18  E-value: 2.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTVYKALLLTEKKVVAVKVLNMQR-RGAMKSFMAECESLKDIRHRNLVKLLTacssiDFQGNEFRALIYEFM 784
Cdd:cd14095    6 RVIGDGNFAVVKECRDKATDKEYALKIIDKAKcKGKEHMIENEVAILRRVKHPNIVQLIE-----EYDTDTELYLVMELV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLdmwlhpeeVEEIhRPSRTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDD----LTAHVSDFGL 860
Cdd:cd14095   81 KGGDL--------FDAI-TSSTKFTERDASRMVTDLAQALKYLHSL---SIVHRDIKPENLLVVEHedgsKSLKLADFGL 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  861 ARLLlkfdEESFFNqlssagVRGTIGYAAPE------YGVGgqpsinGDVYSFGILLLEMFTG-------KRPTNELF 925
Cdd:cd14095  149 ATEV----KEPLFT------VCGTPTYVAPEilaetgYGLK------VDIWAAGVITYILLCGfppfrspDRDQEELF 210
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
707-943 2.47e-08

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: 56.93  E-value: 2.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVLNMQ---RRGAMKSFMAECESLKDIRHRNLVKLLTACssidFQGNEFRALIYEF 783
Cdd:cd05615   17 VLGKGSFGKVMLAERKGSDELYAIKILKKDvviQDDDVECTMVEKRVLALQDKPPFLTQLHSC----FQTVDRLYFVMEY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  784 MPNGslDMWLHPEEVEEIHRPSRTLtllerlnIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARl 863
Cdd:cd05615   93 VNGG--DLMYHIQQVGKFKEPQAVF-------YAAEISVGLFFLH---KKGIIYRDLKLDNVMLDSEGHIKIADFGMCK- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  864 llkfdeESFFNQLSSAGVRGTIGYAAPEYgVGGQP-SINGDVYSFGILLLEMFTGKRP-----TNELFGGNFTLN-SYTK 936
Cdd:cd05615  160 ------EHMVEGVTTRTFCGTPDYIAPEI-IAYQPyGRSVDWWAYGVLLYEMLAGQPPfdgedEDELFQSIMEHNvSYPK 232

                 ....*..
gi 18408454  937 SALPERI 943
Cdd:cd05615  233 SLSKEAV 239
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
709-914 2.57e-08

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: 56.22  E-value: 2.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVYKALLLTEKKVVAVKVLNMQ-RRGAMKSFMAECESLKDIRHRNLVKLLTACSSidfqgnefRALIY---EFM 784
Cdd:cd14046   15 GKGAFGQVVKVRNKLDGRYYAIKKIKLRsESKNNSRILREVMLLSRLNHQHVVRYYQAWIE--------RANLYiqmEYC 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSL----DMWLHpEEVEEIHRPSRTLtlLERLNiaidvasvldylHVHCHEpIAHCDLKPSNVLLDDDLTAHVSDFGL 860
Cdd:cd14046   87 EKSTLrdliDSGLF-QDTDRLWRLFRQI--LEGLA------------YIHSQG-IIHRDLKPVNIFLDSNGNVKIGDFGL 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  861 ARlLLKFDEESF---------FNQLSSAGVRGTIG---YAAPEYGVGGQPSING--DVYSFGILLLEM 914
Cdd:cd14046  151 AT-SNKLNVELAtqdinkstsAALGSSGDLTGNVGtalYVAPEVQSGTKSTYNEkvDMYSLGIIFFEM 217
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
708-914 2.66e-08

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: 56.38  E-value: 2.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKV--LNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSIDFQGNEFRALIYEFMp 785
Cdd:cd07837    9 IGEGTYGKVYKARDKNTGKLVALKKtrLEMEEEGVPSTALREVSLLQMLSQSIYIVRLLDVEHVEENGKPLLYLVFEYL- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLDMWLhpeeveEIHR--PSRTL--TLLERL--NIAIDVAsvldylhvHCHE-PIAHCDLKPSNVLLDDDLTA-HVSD 857
Cdd:cd07837   88 DTDLKKFI------DSYGrgPHNPLpaKTIQSFmyQLCKGVA--------HCHShGVMHRDLKPQNLLVDKQKGLlKIAD 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  858 FGLARlLLKFDEESFFNQLSsagvrgTIGYAAPEYGVGG-QPSINGDVYSFGILLLEM 914
Cdd:cd07837  154 LGLGR-AFTIPIKSYTHEIV------TLWYRAPEVLLGStHYSTPVDMWSVGCIFAEM 204
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
707-920 2.76e-08

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: 56.29  E-value: 2.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVLNMQRrgaMKsfMAECESLKdIRHRNLVKLLTA--------CSSIDFQGNEFRA 778
Cdd:cd05606    1 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKR---IK--MKQGETLA-LNERIMLSLVSTggdcpfivCMTYAFQTPDKLC 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGSLDMWLHPEEVeeihrpsrtLTLLERLNIAIDVASVLDYLHVHChepIAHCDLKPSNVLLDDDLTAHVSDF 858
Cdd:cd05606   75 FILDLMNGGDLHYHLSQHGV---------FSEAEMRFYAAEVILGLEHMHNRF---IVYRDLKPANILLDEHGHVRISDL 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  859 GLARlllkfdeeSFFNQLSSAGVrGTIGYAAPEYGVGGQP-SINGDVYSFGILLLEMFTGKRP 920
Cdd:cd05606  143 GLAC--------DFSKKKPHASV-GTHGYMAPEVLQKGVAyDSSADWFSLGCMLYKLLKGHSP 196
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
702-920 2.80e-08

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: 56.60  E-value: 2.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNM---QRRGAMKSFMAECESLKDIRHRNlvklltacsSIDFQGNEFRA 778
Cdd:cd06635   27 FSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYsgkQSNEKWQDIIKEVKFLQRIKHPN---------SIEYKGCYLRE 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 ----LIYEFMPNGSLDMWlhpeeveEIHRpsRTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAH 854
Cdd:cd06635   98 htawLVMEYCLGSASDLL-------EVHK--KPLQEIEIAAITHGALQGLAYLHSH---NMIHRDIKAGNILLTEPGQVK 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  855 VSDFGLARLLLKFDeeSFFnqlssagvrGTIGYAAPEYGVG---GQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd06635  166 LADFGSASIASPAN--SFV---------GTPYWMAPEVILAmdeGQYDGKVDVWSLGITCIELAERKPP 223
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
708-920 3.02e-08

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


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 55.96  E-value: 3.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQ-----RRGAMKSFMA-ECESLKDIRHRNLVKLLTAcssidFQGNEFRALIY 781
Cdd:cd14105   13 LGSGQFAVVKKCREKSTGLEYAAKFIKKRrskasRRGVSREDIErEVSILRQVLHPNIITLHDV-----FENKTDVVLIL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 EFMPNGSLDMWLhpEEVEEIHRPSRTLTLLERLNiaidvasVLDYLHVhchEPIAHCDLKPSNVLLDDDLTAH----VSD 857
Cdd:cd14105   88 ELVAGGELFDFL--AEKESLSEEEATEFLKQILD-------GVNYLHT---KNIAHFDLKPENIMLLDKNVPIprikLID 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18408454  858 FGLARlllKFDEESFFNQLSsagvrGTIGYAAPEYgVGGQP-SINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14105  156 FGLAH---KIEDGNEFKNIF-----GTPEFVAPEI-VNYEPlGLEADMWSIGVITYILLSGASP 210
pknD PRK13184
serine/threonine-protein kinase PknD;
707-920 3.18e-08

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 57.86  E-value: 3.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   707 MVGSGSFGTVYKALLLTEKKVVAVKVLN--------MQRRgamksFMAECESLKDIRHRNLVKLLTACSSIDfqgnefra 778
Cdd:PRK13184    9 LIGKGGMGEVYLAYDPVCSRRVALKKIRedlsenplLKKR-----FLREAKIAADLIHPGIVPVYSICSDGD-------- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   779 LIYEFMP--NG----SL--DMWLHPEEVEEIHRPSRTLTLLerlNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDD 850
Cdd:PRK13184   76 PVYYTMPyiEGytlkSLlkSVWQKESLSKELAEKTSVGAFL---SIFHKICATIEYVH---SKGVLHRDLKPDNILLGLF 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   851 LTAHVSDFGLA---------RLLLKFDEE-SFFNQLSSAG-VRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKR 919
Cdd:PRK13184  150 GEVVILDWGAAifkkleeedLLDIDVDERnICYSSMTIPGkIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSF 229

                  .
gi 18408454   920 P 920
Cdd:PRK13184  230 P 230
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
702-936 3.28e-08

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


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 56.83  E-value: 3.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLN--MQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSIDfQGNEFRAL 779
Cdd:cd07879   17 YTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLSrpFQSEIFAKRAYRELTLLKHMQHENVIGLLDVFTSAV-SGDEFQDF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  780 iYEFMPNGSLDMwlhpEEVEEIHRPSRTLTLLerlniAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFG 859
Cdd:cd07879   96 -YLVMPYMQTDL----QKIMGHPLSEDKVQYL-----VYQMLCGLKYIH---SAGIIHRDLKPGNLAVNEDCELKILDFG 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  860 LARlllKFDEEsffnqlsSAGVRGTIGYAAPEYGVGG-QPSINGDVYSFGILLLEMFTGKrptnELFGGNFTLNSYTK 936
Cdd:cd07879  163 LAR---HADAE-------MTGYVVTRWYRAPEVILNWmHYNQTVDIWSVGCIMAEMLTGK----TLFKGKDYLDQLTQ 226
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
700-925 3.44e-08

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: 56.16  E-value: 3.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  700 NGFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVL--NMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFR 777
Cdd:cd07848    1 NKFEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFkdSEENEEVKETTLRELKMLRTLKQENIVELKEA-----FRRRGKL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  778 ALIYEFMPNGSLDMWlhpEEVEEIHRPSRTLTLLERLNIAIDvasvldylhvHCHE-PIAHCDLKPSNVLLDDDLTAHVS 856
Cdd:cd07848   76 YLVFEYVEKNMLELL---EEMPNGVPPEKVRSYIYQLIKAIH----------WCHKnDIVHRDIKPENLLISHNDVLKLC 142
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  857 DFGLARLLLKFDEESFFNQLSsagvrgTIGYAAPEYGVGGQPSINGDVYSFGILLLE------MFTGKRPTNELF 925
Cdd:cd07848  143 DFGFARNLSEGSNANYTEYVA------TRWYRSPELLLGAPYGKAVDMWSVGCILGElsdgqpLFPGESEIDQLF 211
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
708-920 3.76e-08

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: 55.89  E-value: 3.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAE-----CESLKdirHRNLVKLLTAcssidFQGNEFRALIYE 782
Cdd:cd14086    9 LGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKLEreariCRLLK---HPNIVRLHDS-----ISEEGFHYLVFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLdmwlhpeeVEEIhrpsrtltlLERLNIAIDVAS-----VLDYLHvHCHEP-IAHCDLKPSNVLL---DDDLTA 853
Cdd:cd14086   81 LVTGGEL--------FEDI---------VAREFYSEADAShciqqILESVN-HCHQNgIVHRDLKPENLLLaskSKGAAV 142
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  854 HVSDFGLArLLLKFDEESFFnqlssaGVRGTIGYAAPE------YgvgGQPSingDVYSFGILLLEMFTGKRP 920
Cdd:cd14086  143 KLADFGLA-IEVQGDQQAWF------GFAGTPGYLSPEvlrkdpY---GKPV---DIWACGVILYILLVGYPP 202
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
708-917 3.93e-08

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: 56.05  E-value: 3.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVlnmQRRGAMKSFMAECEslkdirhrnlVKLLTACSSIDFQGNEFR---ALIYEFM 784
Cdd:cd14136   18 LGWGHFSTVWLCWDLQNKRFVALKV---VKSAQHYTEAALDE----------IKLLKCVREADPKDPGREhvvQLLDDFK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 ---PNGSldmwlHPEEVEEIHRPSrTLTLLERLN-----------IAIDVASVLDYLHVHCHepIAHCDLKPSNVLLD-D 849
Cdd:cd14136   85 htgPNGT-----HVCMVFEVLGPN-LLKLIKRYNyrgiplplvkkIARQVLQGLDYLHTKCG--IIHTDIKPENVLLCiS 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  850 DLTAHVSDFGLArlllKFDEESFFNQLSsagvrgTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTG 917
Cdd:cd14136  157 KIEVKIADLGNA----CWTDKHFTEDIQ------TRQYRSPEVILGAGYGTPADIWSTACMAFELATG 214
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
710-861 4.54e-08

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: 55.75  E-value: 4.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  710 SGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIR-HRNLVKLL---TACSSidfqGNEFRALI-YEFM 784
Cdd:cd14037   13 EGGFAHVYLVKTSNGGNRAALKRVYVNDEHDLNVCKREIEIMKRLSgHKNIVGYIdssANRSG----NGVYEVLLlMEYC 88
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  785 PNGSLDMWLHpeeveeiHRPSRTLTLLERLNIAIDVASVLDYLHvHCHEPIAHCDLKPSNVLLDDDLTAHVSDFGLA 861
Cdd:cd14037   89 KGGGVIDLMN-------QRLQTGLTESEILKIFCDVCEAVAAMH-YLKPPLIHRDLKVENVLISDSGNYKLCDFGSA 157
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
708-920 4.61e-08

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: 55.32  E-value: 4.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVL--NMQRRGAMKSFMA-ECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFM 784
Cdd:cd14187   15 LGKGGFAKCYEITDADTKEVFAGKIVpkSLLLKPHQKEKMSmEIAIHRSLAHQHVVGFHGF-----FEDNDFVYVVLELC 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLdmwlhpeevEEIHRPSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARlL 864
Cdd:cd14187   90 RRRSL---------LELHKRRKALTEPEARYYLRQIILGCQYLH---RNRVIHRDLKLGNLFLNDDMEVKIGDFGLAT-K 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  865 LKFDEEsffnqlSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14187  157 VEYDGE------RKKTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPP 206
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
707-925 4.94e-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: 4.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVL---NMQRRGAMKSFMAECESLKDIRHRNLVKLltacsSIDFQGNEFRALIYEF 783
Cdd:cd05585    1 VIGKGSFGKVMQVRKKDTSRIYALKTIrkaHIVSRSEVTHTLAERTVLAQVDCPFIVPL-----KFSFQSPEKLYLVLAF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  784 MPNGSLDMWLHPEEVEEIHRpsrtltllERLNIAiDVASVLDYLHVHchePIAHCDLKPSNVLLddDLTAHVS--DFGLA 861
Cdd:cd05585   76 INGGELFHHLQREGRFDLSR--------ARFYTA-ELLCALECLHKF---NVIYRDLKPENILL--DYTGHIAlcDFGLC 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  862 RLLLKFDEESffNQLSsagvrGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP-----TNELF 925
Cdd:cd05585  142 KLNMKDDDKT--NTFC-----GTPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPfydenTNEMY 203
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
702-920 5.18e-08

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


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 55.23  E-value: 5.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEK--KVVAVKVLNMQRRGamKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRAL 779
Cdd:cd14112    5 FSFGSEIFRGRFSVIVKAVDSTTEtdAHCAVKIFEVSDEA--SEAVREFESLRTLQHENVQRLIAA-----FKPSNFAYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  780 IYEFMPNGSLDMWLHPEEV-EEIhrpsrtltllerlnIAIDVASVLDYLHVHCHEPIAHCDLKPSNVLLDDDLTAHVS-- 856
Cdd:cd14112   78 VMEKLQEDVFTRFSSNDYYsEEQ--------------VATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSWQVKlv 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  857 DFGLARLLlkfdeesffNQLSSAGVRGTIGYAAPEYGVGGQP-SINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14112  144 DFGRAQKV---------SKLGKVPVDGDTDWASPEFHNPETPiTVQSDIWGLGVLTFCLLSGFHP 199
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
700-936 5.82e-08

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: 55.78  E-value: 5.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  700 NGFSSSNMVGSGSFGTVYkalLLTEKK---VVAVKVLnmqRRGAMKSFMAEC--ESLKDIRHRN----LVKLLTAcssid 770
Cdd:cd05601    1 KDFEVKNVIGRGHFGEVQ---VVKEKAtgdIYAMKVL---KKSETLAQEEVSffEEERDIMAKAnspwITKLQYA----- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  771 FQGNEFRALIYEFMPNGSLDMWLhpEEVEEIHRPSRTLTLLERLNIAIDVASVLDYLHVhchepiahcDLKPSNVLLDDd 850
Cdd:cd05601   70 FQDSENLYLVMEYHPGGDLLSLL--SRYDDIFEESMARFYLAELVLAIHSLHSMGYVHR---------DIKPENILIDR- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  851 lTAHV--SDFGLARlllkfdeesffnQLSSAG-VR-----GTIGYAAPE------YGVGGQPSINGDVYSFGILLLEMFT 916
Cdd:cd05601  138 -TGHIklADFGSAA------------KLSSDKtVTskmpvGTPDYIAPEvltsmnGGSKGTYGVECDWWSLGIVAYEMLY 204
                        250       260
                 ....*....|....*....|
gi 18408454  917 GKRPtnelFGGNFTLNSYTK 936
Cdd:cd05601  205 GKTP----FTEDTVIKTYSN 220
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
708-920 5.91e-08

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 54.97  E-value: 5.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLN--MQRRgamKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFMP 785
Cdd:cd14115    1 IGRGRFSIVKKCLHKATRKDVAVKFVSkkMKKK---EQAAHEAALLQHLQHPQYITLHDT-----YESPTSYILVLELMD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSL-DMWLHPEEVEEihrpsrtltllERLNIAI-DVASVLDYLHvHCHepIAHCDLKPSNVLLDddLTAHVSDFGLARL 863
Cdd:cd14115   73 DGRLlDYLMNHDELME-----------EKVAFYIrDIMEALQYLH-NCR--VAHLDIKPENLLID--LRIPVPRVKLIDL 136
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  864 LlkfDEESFFNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14115  137 E---DAVQISGHRHVHHLLGNPEFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSP 190
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
708-920 5.95e-08

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


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 55.39  E-value: 5.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKV-----LNMQRRGAMKSFMA-ECESLKDIRHRNLVKLLTAcssidFQGNEFRALIY 781
Cdd:cd14195   13 LGSGQFAIVRKCREKGTGKEYAAKFikkrrLSSSRRGVSREEIErEVNILREIQHPNIITLHDI-----FENKTDVVLIL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 EFMPNGSLDMWLhpEEVEEIHRPSRTLTLLErlniaidvasVLDYLHVHCHEPIAHCDLKPSNVLLDDDLTAH----VSD 857
Cdd:cd14195   88 ELVSGGELFDFL--AEKESLTEEEATQFLKQ----------ILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNprikLID 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18408454  858 FGLARLLLKFDEesFFNqlssagVRGTIGYAAPEYgVGGQP-SINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14195  156 FGIAHKIEAGNE--FKN------IFGTPEFVAPEI-VNYEPlGLEADMWSIGVITYILLSGASP 210
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
702-920 5.97e-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: 5.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLN---MQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRA 778
Cdd:cd05623   74 FEILKVIGRGAFGEVAVVKLKNADKVFAMKILNkweMLKRAETACFREERDVLVNGDSQWITTLHYA-----FQDDNNLY 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGSLDMWLH------PEEVEEIHrpsrtltlLERLNIAIDVASVLDYLHVhchepiahcDLKPSNVLLDDDLT 852
Cdd:cd05623  149 LVMDYYVGGDLLTLLSkfedrlPEDMARFY--------LAEMVLAIDSVHQLHYVHR---------DIKPDNILMDMNGH 211
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  853 AHVSDFGLArllLKFDEESFFNqlSSAGVrGTIGYAAPEY-----GVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd05623  212 IRLADFGSC---LKLMEDGTVQ--SSVAV-GTPDYISPEIlqameDGKGKYGPECDWWSLGVCMYEMLYGETP 278
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
702-920 6.18e-08

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: 55.36  E-value: 6.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNM--------QRRGAMKSFMAECESLKDIR-HRNLVKLLTAcssidFQ 772
Cdd:cd14181   12 YDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEVtaerlspeQLEEVRSSTLKEIHILRQVSgHPSIITLIDS-----YE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  773 GNEFRALIYEFMPNGSLDMWLhPEEVEEIHRPSRTL--TLLErlniaidvasVLDYLHVHchePIAHCDLKPSNVLLDDD 850
Cdd:cd14181   87 SSTFIFLVFDLMRRGELFDYL-TEKVTLSEKETRSImrSLLE----------AVSYLHAN---NIVHRDLKPENILLDDQ 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  851 LTAHVSDFGLArLLLKFDEEsfFNQLSsagvrGTIGYAAPEY----------GVGGQPsingDVYSFGILLLEMFTGKRP 920
Cdd:cd14181  153 LHIKLSDFGFS-CHLEPGEK--LRELC-----GTPGYLAPEIlkcsmdethpGYGKEV----DLWACGVILFTLLAGSPP 220
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
702-920 6.67e-08

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: 55.30  E-value: 6.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQR---RGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRA 778
Cdd:cd05607    4 FYEFRVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRlkkKSGEKMALLEKEILEKVNSPFIVSLAYA-----FETKTHLC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGslDMWLHPEEVEEIhrpsrtltllerlniAIDVASVLDY--------LHVHCHEpIAHCDLKPSNVLLDDD 850
Cdd:cd05607   79 LVMSLMNGG--DLKYHIYNVGER---------------GIEMERVIFYsaqitcgiLHLHSLK-IVYRDMKPENVLLDDN 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  851 LTAHVSDFGLArllLKFDEESFFNQLSsagvrGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd05607  141 GNCRLSDLGLA---VEVKEGKPITQRA-----GTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTP 202
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
708-920 6.85e-08

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: 55.78  E-value: 6.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKK-----VVAVKVLnmqRRGAM----KSFMAECESLKDI-RHRNLVKLLTACSSidfQGNEFr 777
Cdd:cd14207   15 LGRGAFGKVVQASAFGIKKsptcrVVAVKML---KEGATaseyKALMTELKILIHIgHHLNVVNLLGACTK---SGGPL- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  778 ALIYEFMPNGSL---------------DMWLHPE---------------------------------------EVEEIHR 803
Cdd:cd14207   88 MVIVEYCKYGNLsnylkskrdffvtnkDTSLQEElikekkeaeptggkkkrlesvtssesfassgfqedkslsDVEEEEE 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  804 PS-----RTLTLLERLNIAIDVASVLDYLhvhCHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARLLLKFDEesffnQLSS 878
Cdd:cd14207  168 DSgdfykRPLTMEDLISYSFQVARGMEFL---SSRKCIHRDLAARNILLSENNVVKICDFGLARDIYKNPD-----YVRK 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 18408454  879 AGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRP 920
Cdd:cd14207  240 GDARLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSlGASP 282
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
728-924 7.03e-08

Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. ILK contains N-terminal ankyrin repeats, a Pleckstrin Homology (PH) domain, and a C-terminal pseudokinase domain. It is a component of the IPP (ILK/PINCH/Parvin) complex that couples beta integrins to the actin cytoskeleton, and plays important roles in cell adhesion, spreading, invasion, and migration. ILK was initially thought to be an active kinase despite the lack of key conserved residues because of in vitro studies showing that it can phosphorylate certain protein substrates. However, in vivo experiments in Caenorhabditis elegans, Drosophila melanogaster, and mice (ILK-null and knock-in) proved that ILK is not an active kinase. In addition to actin cytoskeleton regulation, ILK also influences the microtubule network and mitotic spindle orientation. The pseudokinase domain of ILK binds several adaptor proteins including the parvins and paxillin. The ILK 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: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 54.80  E-value: 7.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  728 VAVKVLNMQRRGAMKS--FMAECESLKDIRHRNLVKLLTACSSidfqgNEFRALIYEFMPNGSLDMWLHPEEveeihrpS 805
Cdd:cd14057   21 IVAKILKVRDVTTRISrdFNEEYPRLRIFSHPNVLPVLGACNS-----PPNLVVISQYMPYGSLYNVLHEGT-------G 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  806 RTLTLLERLNIAIDVASVLDYLHVHchEP-IAHCDLKPSNVLLDDDLTAHVSdfgLARLLLKFDEES-FFNQlssagvrg 883
Cdd:cd14057   89 VVVDQSQAVKFALDIARGMAFLHTL--EPlIPRHHLNSKHVMIDEDMTARIN---MADVKFSFQEPGkMYNP-------- 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 18408454  884 tiGYAAPEYGVGGQPSIN---GDVYSFGILLLEMFTGKRPTNEL 924
Cdd:cd14057  156 --AWMAPEALQKKPEDINrrsADMWSFAILLWELVTREVPFADL 197
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
707-920 8.25e-08

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: 54.58  E-value: 8.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFMPN 786
Cdd:cd14192   11 VLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEVKNEINIMNQLNHVNLIQLYDA-----FESKTNLTLIMEYVDG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  787 GSLdmwlhpeeVEEIHRPSRTLTLLERLNIAIDVASVLDYLHVHChepIAHCDLKPSNVLLDDDlTAH---VSDFGLARl 863
Cdd:cd14192   86 GEL--------FDRITDESYQLTELDAILFTRQICEGVHYLHQHY---ILHLDLKPENILCVNS-TGNqikIIDFGLAR- 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  864 LLKFDEESFFNqlssagvRGTIGYAAPE---YGVGGQPSingDVYSFGILLLEMFTGKRP 920
Cdd:cd14192  153 RYKPREKLKVN-------FGTPEFLAPEvvnYDFVSFPT---DMWSVGVITYMLLSGLSP 202
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
707-925 8.70e-08

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: 55.08  E-value: 8.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVLN---MQRRGAMKSFMAECESLK-DIRHRNLVKLLtaCSsidFQGNEFRALIYE 782
Cdd:cd05592    2 VLGKGSFGKVMLAELKGTNQYFAIKALKkdvVLEDDDVECTMIERRVLAlASQHPFLTHLF--CT---FQTESHLFFVME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGslDMWLHpeeVEEIHRPSrtltlLERLNI-AIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLA 861
Cdd:cd05592   77 YLNGG--DLMFH---IQQSGRFD-----EDRARFyGAEIICGLQFLH---SRGIIYRDLKLDNVLLDREGHIKIADFGMC 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  862 RlllkfdeESFFNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTN-----ELF 925
Cdd:cd05592  144 K-------ENIYGENKASTFCGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHgededELF 205
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
702-920 8.70e-08

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 55.05  E-value: 8.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGamksfMAECESLKdIRHRNLVKLLTA-------CSSIDFQGN 774
Cdd:cd14223    2 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIK-----MKQGETLA-LNERIMLSLVSTgdcpfivCMSYAFHTP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  775 EFRALIYEFMPNGSLDMWLHPEEVeeihrpsrtLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAH 854
Cdd:cd14223   76 DKLSFILDLMNGGDLHYHLSQHGV---------FSEAEMRFYAAEIILGLEHMH---SRFVVYRDLKPANILLDEFGHVR 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  855 VSDFGLArlllkfdeeSFFNQLSSAGVRGTIGYAAPEY---GVGGQPSinGDVYSFGILLLEMFTGKRP 920
Cdd:cd14223  144 ISDLGLA---------CDFSKKKPHASVGTHGYMAPEVlqkGVAYDSS--ADWFSLGCMLFKLLRGHSP 201
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
708-920 8.84e-08

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


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 54.58  E-value: 8.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVL-----NMQRRGAMKSFMA-ECESLKDIRHRNLVKLLTAcssidFQGNEFRALIY 781
Cdd:cd14196   13 LGSGQFAIVKKCREKSTGLEYAAKFIkkrqsRASRRGVSREEIErEVSILRQVLHPNIITLHDV-----YENRTDVVLIL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 EFMPNGSL-DMWLHPEEVEEIHRPSRTLTLLERLNiaidvasvldYLHVhchEPIAHCDLKPSNV-LLDDDL-TAHVS-- 856
Cdd:cd14196   88 ELVSGGELfDFLAQKESLSEEEATSFIKQILDGVN----------YLHT---KKIAHFDLKPENImLLDKNIpIPHIKli 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  857 DFGLARlllKFDEESFFNQlssagVRGTIGYAAPEYgVGGQP-SINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14196  155 DFGLAH---EIEDGVEFKN-----IFGTPEFVAPEI-VNYEPlGLEADMWSIGVITYILLSGASP 210
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
702-920 8.86e-08

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: 55.03  E-value: 8.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNM---QRRGAMKSFMAECESLKDIRHRNlvklltacsSIDFQGNEFRA 778
Cdd:cd06634   17 FSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYsgkQSNEKWQDIIKEVKFLQKLRHPN---------TIEYRGCYLRE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 ----LIYEFMPNGSLDMWlhpeeveEIHRpsRTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAH 854
Cdd:cd06634   88 htawLVMEYCLGSASDLL-------EVHK--KPLQEVEIAAITHGALQGLAYLHSH---NMIHRDVKAGNILLTEPGLVK 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  855 VSDFGLARLLLKFDeeSFFnqlssagvrGTIGYAAPEYGVG---GQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd06634  156 LGDFGSASIMAPAN--SFV---------GTPYWMAPEVILAmdeGQYDGKVDVWSLGITCIELAERKPP 213
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
708-920 9.19e-08

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: 54.54  E-value: 9.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEK-------KVVAVKVLNM----QRrgamksFMAECESLKDIR-HRNLVKLLTAcssidFQGNE 775
Cdd:cd14019    9 IGEGTFSSVYKAEDKLHDlydrnkgRLVALKHIYPtsspSR------ILNELECLERLGgSNNVSGLITA-----FRNED 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  776 FRALIYEFMPNgsldmwlhpeevEEIHRPSRTLTLLErlnIAIDVASVLDYL-HVHCHEpIAHCDLKPSNVLLDDDLTAH 854
Cdd:cd14019   78 QVVAVLPYIEH------------DDFRDFYRKMSLTD---IRIYLRNLFKALkHVHSFG-IIHRDVKPGNFLYNRETGKG 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18408454  855 V-SDFGLARlllkfDEESFFNQLSS-AGVRgtiGYAAPE--YGVGGQ-PSIngDVYSFGILLLEMFTGKRP 920
Cdd:cd14019  142 VlVDFGLAQ-----REEDRPEQRAPrAGTR---GFRAPEvlFKCPHQtTAI--DIWSAGVILLSILSGRFP 202
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
702-923 9.43e-08

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


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 54.61  E-value: 9.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIY 781
Cdd:cd14166    5 FIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSSLENEIAVLKRIKHENIVTLEDI-----YESTTHYYLVM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 EFMPNGSLDMWLHPEEVEEIHRPSRTLTllerlniaiDVASVLDYLHvhcHEPIAHCDLKPSNVLL---DDDLTAHVSDF 858
Cdd:cd14166   80 QLVSGGELFDRILERGVYTEKDASRVIN---------QVLSAVKYLH---ENGIVHRDLKPENLLYltpDENSKIMITDF 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  859 GLARLllkfdEEsffNQLSSAGVrGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTNE 923
Cdd:cd14166  148 GLSKM-----EQ---NGIMSTAC-GTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYE 203
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
677-920 1.07e-07

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: 55.04  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  677 NPTPSTLEVLHEKISYgdlRNATNGFSSSNMVGSGSFGtvyKALLLTEK---KVVAVKVLNMQ---RRGAMKSFMAECES 750
Cdd:cd05594    5 NSGAEEMEVSLTKPKH---KVTMNDFEYLKLLGKGTFG---KVILVKEKatgRYYAMKILKKEvivAKDEVAHTLTENRV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  751 LKDIRHRNLVKLltacsSIDFQGNEFRALIYEFMPNGSLDMWLHPEEVEEIHRPsrtltlleRLNIAiDVASVLDYLHvh 830
Cdd:cd05594   79 LQNSRHPFLTAL-----KYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRA--------RFYGA-EIVSALDYLH-- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  831 CHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARlllkfdeESFFNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGIL 910
Cdd:cd05594  143 SEKNVVYRDLKLENLMLDKDGHIKITDFGLCK-------EGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVV 215
                        250
                 ....*....|
gi 18408454  911 LLEMFTGKRP 920
Cdd:cd05594  216 MYEMMCGRLP 225
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
288-462 1.08e-07

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 53.64  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  288 LGMNENNLTgSIPTFGNVPNLKLLFLHTNSLGSdssrdlefLTSLTNCTQLETLGIGRNRLGgdlpiSIANLSA--KLVT 365
Cdd:cd21340    7 LYLNDKNIT-KIDNLSLCKNLKVLYLYDNKITK--------IENLEFLTNLTHLYLQNNQIE-----KIENLENlvNLKK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  366 LDLGGTLIS---GsipydIGNLINLQKL-ILDQNMLSG-PL---PTSLGKLLN-LRYLSLFSNRLSggIPAFIGNMTMLE 436
Cdd:cd21340   73 LYLGGNRISvveG-----LENLTNLEELhIENQRLPPGeKLtfdPRSLAALSNsLRVLNISGNNID--SLEPLAPLRNLE 145
                        170       180
                 ....*....|....*....|....*...
gi 18408454  437 TLDLSNNGFEGIVPTS--LGNCSHLLEL 462
Cdd:cd21340  146 QLDASNNQISDLEELLdlLSSWPSLREL 173
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
708-918 1.08e-07

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: 55.05  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLN--MQRRGAMKSFMAECESLKDIRHRNLVKLL---TACSSIDfqgnEFRA--LI 780
Cdd:cd07877   25 VGSGAYGSVCAAFDTKTGLRVAVKKLSrpFQSIIHAKRTYRELRLLKHMKHENVIGLLdvfTPARSLE----EFNDvyLV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFMpNGSLDMWLHPEEVEEIHRPSRTLTLLERLNiaidvasvldYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGL 860
Cdd:cd07877  101 THLM-GADLNNIVKCQKLTDDHVQFLIYQILRGLK----------YIH---SADIIHRDLKPSNLAVNEDCELKILDFGL 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  861 ARlllKFDEEsffnqlsSAGVRGTIGYAAPEYGVGG-QPSINGDVYSFGILLLEMFTGK 918
Cdd:cd07877  167 AR---HTDDE-------MTGYVATRWYRAPEIMLNWmHYNQTVDIWSVGCIMAELLTGR 215
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
708-928 1.14e-07

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: 54.61  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQ-RRGAMKSFMAECESLKDIRHRNLVKLLTACSSidfqgNEFRALIYEFMPN 786
Cdd:cd07872   14 LGEGTYATVFKGRSKLTENLVALKEIRLEhEEGAPCTAIREVSLLKDLKHANIVTLHDIVHT-----DKSLTLVFEYLDK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  787 gslDMWLHPEEVEEIhrpsrtltlLERLNIAIDVASVLDYLhVHCHE-PIAHCDLKPSNVLLDDDLTAHVSDFGLARlLL 865
Cdd:cd07872   89 ---DLKQYMDDCGNI---------MSMHNVKIFLYQILRGL-AYCHRrKVLHRDLKPQNLLINERGELKLADFGLAR-AK 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18408454  866 KFDEESFFNQLSsagvrgTIGYAAPEYGVG-GQPSINGDVYSFGILLLEMFTGkRPtneLFGGN 928
Cdd:cd07872  155 SVPTKTYSNEVV------TLWYRPPDVLLGsSEYSTQIDMWGVGCIFFEMASG-RP---LFPGS 208
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
681-917 1.24e-07

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


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 54.71  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  681 STLEVLHEKISYGdlrnatngFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRgAMKSFMAECESLKDIRHRNLV 760
Cdd:cd14225   32 SYLKVLHDHIAYR--------YEILEVIGKGSFGQVVKALDHKTNEHVAIKIIRNKKR-FHHQALVEVKILDALRRKDRD 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  761 KLLTACSSIDFqgNEFR---ALIYEFMpngSLDMWlhpEEVEEIHRPSRTLTLLERLNIaidvaSVLDYLHVHCHEPIAH 837
Cdd:cd14225  103 NSHNVIHMKEY--FYFRnhlCITFELL---GMNLY---ELIKKNNFQGFSLSLIRRFAI-----SLLQCLRLLYRERIIH 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  838 CDLKPSNVLLDD--DLTAHVSDFGLArlllKFDEESFFNQLSSAgvrgtiGYAAPEYGVGGQPSINGDVYSFGILLLEMF 915
Cdd:cd14225  170 CDLKPENILLRQrgQSSIKVIDFGSS----CYEHQRVYTYIQSR------FYRSPEVILGLPYSMAIDMWSLGCILAELY 239

                 ..
gi 18408454  916 TG 917
Cdd:cd14225  240 TG 241
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
670-936 1.27e-07

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: 55.01  E-value: 1.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  670 KKNKETNNPTPSTLEVLHEkisYGDLRNATNGFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLN---MQRRGAMKSFMA 746
Cdd:cd05621   25 RKNKNIDNFLNRYEKIVNK---IRELQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSkfeMIKRSDSAFFWE 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  747 ECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFMPNGSLDMWLHPEEVEEihRPSRTLTllerlniaIDVASVLDY 826
Cdd:cd05621  102 ERDIMAFANSPWVVQLFCA-----FQDDKYLYMVMEYMPGGDLVNLMSNYDVPE--KWAKFYT--------AEVVLALDA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  827 LHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLArllLKFDEESFFNQLSSAgvrGTIGYAAPEY----GVGGQPSING 902
Cdd:cd05621  167 IH---SMGLIHRDVKPDNMLLDKYGHLKLADFGTC---MKMDETGMVHCDTAV---GTPDYISPEVlksqGGDGYYGREC 237
                        250       260       270
                 ....*....|....*....|....*....|....
gi 18408454  903 DVYSFGILLLEMFTGKRPtnelFGGNFTLNSYTK 936
Cdd:cd05621  238 DWWSVGVFLFEMLVGDTP----FYADSLVGTYSK 267
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
696-924 1.35e-07

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: 54.26  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  696 RNATNGFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNE 775
Cdd:cd06646    5 RNPQHDYELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEPGDDFSLIQQEIFMVKECKHCNIVAYFGS-----YLSRE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  776 FRALIYEFMPNGSLdmwlhpeevEEIHRPSRTLTLLERLNIAIDVASVLDYLHVHCHepiAHCDLKPSNVLLDDDLTAHV 855
Cdd:cd06646   80 KLWICMEYCGGGSL---------QDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGK---MHRDIKGANILLTDNGDVKL 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  856 SDFGLARLLLKF--DEESFFnqlssagvrGTIGYAAPEYGV----GGQPSInGDVYSFGILLLEMFTGKRPTNEL 924
Cdd:cd06646  148 ADFGVAAKITATiaKRKSFI---------GTPYWMAPEVAAveknGGYNQL-CDIWAVGITAIELAELQPPMFDL 212
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
708-927 1.35e-07

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


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 54.79  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSIDFQGN-------EFRAL- 779
Cdd:cd07854   13 LGCGSNGLVFSAVDSDCDKRVAVKKIVLTDPQSVKHALREIKIIRRLDHDNIVKVYEVLGPSGSDLTedvgsltELNSVy 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  780 -IYEFMpNGSLDMWLHPEEVEEIHRPSRTLTLLERLNiaidvasvldYLHvhcHEPIAHCDLKPSNVLLD-DDLTAHVSD 857
Cdd:cd07854   93 iVQEYM-ETDLANVLEQGPLSEEHARLFMYQLLRGLK----------YIH---SANVLHRDLKPANVFINtEDLVLKIGD 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18408454  858 FGLARLLlkfDEE-SFFNQLSSAGVrgTIGYAAPEYGVggQP---SINGDVYSFGILLLEMFTGKrptnELFGG 927
Cdd:cd07854  159 FGLARIV---DPHySHKGYLSEGLV--TKWYRSPRLLL--SPnnyTKAIDMWAAGCIFAEMLTGK----PLFAG 221
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
702-950 1.40e-07

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: 55.01  E-value: 1.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLN---MQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRA 778
Cdd:cd05624   74 FEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNkweMLKRAETACFREERNVLVNGDCQWITTLHYA-----FQDENYLY 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGSLDMWLH------PEEVEEIHrpsrtltlLERLNIAIDVASVLDYLHVhchepiahcDLKPSNVLLDDDLT 852
Cdd:cd05624  149 LVMDYYVGGDLLTLLSkfedklPEDMARFY--------IGEMVLAIHSIHQLHYVHR---------DIKPDNVLLDMNGH 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  853 AHVSDFGLArllLKFDEESFFNqlSSAGVrGTIGYAAPEY------GVgGQPSINGDVYSFGILLLEMFTGKRP-----T 921
Cdd:cd05624  212 IRLADFGSC---LKMNDDGTVQ--SSVAV-GTPDYISPEIlqamedGM-GKYGPECDWWSLGVCMYEMLYGETPfyaesL 284
                        250       260
                 ....*....|....*....|....*....
gi 18408454  922 NELFGGnfTLNSYTKSALPERILDIVDES 950
Cdd:cd05624  285 VETYGK--IMNHEERFQFPSHVTDVSEEA 311
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
705-920 1.46e-07

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 55.26  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   705 SNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQ--RRGAMKSFMAECESLKDIRHRNLVKLLTACSSIDFQGNE---FRAL 779
Cdd:PTZ00283   37 SRVLGSGATGTVLCAKRVSDGEPFAVKVVDMEgmSEADKNRAQAEVCCLLNCDFFSIVKCHEDFAKKDPRNPEnvlMIAL 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   780 IYEFMPNGSLDmwlhpEEVEEIHRPSRTLTLLERLNIAIDVasVLDYLHVHCHEPIaHCDLKPSNVLLDDDLTAHVSDFG 859
Cdd:PTZ00283  117 VLDYANAGDLR-----QEIKSRAKTNRTFREHEAGLLFIQV--LLAVHHVHSKHMI-HRDIKSANILLCSNGLVKLGDFG 188
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454   860 larlllkfdeesfFNQLSSAGVRGTIG--------YAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:PTZ00283  189 -------------FSKMYAATVSDDVGrtfcgtpyYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRP 244
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
799-920 1.50e-07

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: 54.85  E-value: 1.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  799 EEIHRPSRTLTLLERLNIAIDVASVLDYLHV-HChepiAHCDLKPSNVLLDDDLTAHVSDFGLARlllkfDEESFFNQLS 877
Cdd:cd05106  200 EEDTEDSWPLDLDDLLRFSSQVAQGMDFLASkNC----IHRDVAARNVLLTDGRVAKICDFGLAR-----DIMNDSNYVV 270
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 18408454  878 SAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRP 920
Cdd:cd05106  271 KGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSlGKSP 314
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
702-920 1.58e-07

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: 54.23  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQR---RGAMKSFMAECESLKDIRHRNLVKLLTACSSID-------- 770
Cdd:cd05631    2 FRHYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRikkRKGEAMALNEKRILEKVNSRFVVSLAYAYETKDalclvlti 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  771 FQGNEFRALIYEfMPNGSLDmwlhpeEVEEIHRPSRTLTLLERLNiaidvasvldylhvhcHEPIAHCDLKPSNVLLDDD 850
Cdd:cd05631   82 MNGGDLKFHIYN-MGNPGFD------EQRAIFYAAELCCGLEDLQ----------------RERIVYRDLKPENILLDDR 138
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  851 LTAHVSDFGLArllLKFDEESffnqlSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd05631  139 GHIRISDLGLA---VQIPEGE-----TVRGRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSP 200
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
708-917 1.63e-07

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 54.17  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKAL--LLTEKKVVAVKVLNMQRRGAMKS----FMAECESLKDIR-HRNLVKLLTACSSIDFQGNEFRALI 780
Cdd:cd14020    8 LGQGSSASVYRVSsgRGADQPTSALKEFQLDHQGSQESgdygFAKERAALEQLQgHRNIVTLYGVFTNHYSANVPSRCLL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFMPNGSLDMWLHPEEveeihrPSRTLTLLErlNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLD-DDLTAHVSDFG 859
Cdd:cd14020   88 LELLDVSVSELLLRSSN------QGCSMWMIQ--HCARDVLEALAFLH---HEGYVHADLKPRNILWSaEDECFKLIDFG 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  860 LarlllkfdeeSFFNQLSSAGVRGTIGYAAPEYGV------GGQPSING-----DVYSFGILLLEMFTG 917
Cdd:cd14020  157 L----------SFKEGNQDVKYIQTDGYRAPEAELqnclaqAGLQSETEctsavDLWSLGIVLLEMFSG 215
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
708-920 1.64e-07

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


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 54.22  E-value: 1.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACssidFQGNEFRALIyEFMPNG 787
Cdd:cd06659   29 IGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQRRELLFNEVVIMRDYQHPNVVEMYKSY----LVGEELWVLM-EYLQGG 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 SLDmwlhpEEVEEIHrpsrtLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGlarlllkf 867
Cdd:cd06659  104 ALT-----DIVSQTR-----LNEEQIATVCEAVLQALAYLH---SQGVIHRDIKSDSILLTLDGRVKLSDFG-------- 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  868 deesFFNQLSS-----AGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd06659  163 ----FCAQISKdvpkrKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPP 216
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
816-920 1.64e-07

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: 53.97  E-value: 1.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  816 IAIDVASVLDYLHVHCHepIAHCDLKPSNVLLDDDLTAHVSDFGLARLLLkfdeesffNQLSSAGVRGTIGYAAPEY--- 892
Cdd:cd06617  108 IAVSIVKALEYLHSKLS--VIHRDVKPSNVLINRNGQVKLCDFGISGYLV--------DSVAKTIDAGCKPYMAPERinp 177
                         90       100
                 ....*....|....*....|....*....
gi 18408454  893 -GVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd06617  178 eLNQKGYDVKSDVWSLGITMIELATGRFP 206
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
702-920 1.78e-07

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: 53.85  E-value: 1.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLT---EKKVVAVKVLN----MQRRGAMKSFMAECESLKDIRHRN-LVKLLTAcssidFQG 773
Cdd:cd05613    2 FELLKVLGTGAYGKVFLVRKVSghdAGKLYAMKVLKkatiVQKAKTAEHTRTERQVLEHIRQSPfLVTLHYA-----FQT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  774 NEFRALIYEFMPNGSLdmWLHPEEVEEIHRPSRTLTLLErlniaidVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTA 853
Cdd:cd05613   77 DTKLHLILDYINGGEL--FTHLSQRERFTENEVQIYIGE-------IVLALEHLH---KLGIIYRDIKLENILLDSSGHV 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  854 HVSDFGLARLLLKFDEESFFNqlssagVRGTIGYAAPEYGVGGQPSING--DVYSFGILLLEMFTGKRP 920
Cdd:cd05613  145 VLTDFGLSKEFLLDENERAYS------FCGTIEYMAPEIVRGGDSGHDKavDWWSLGVLMYELLTGASP 207
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
401-588 1.79e-07

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 54.28  E-value: 1.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  401 LPTSLGKLLNLRYLSLFSNRLSGGIPAFIGNMT---MLETLDLSNNGFEG----IVPTSLGNCSHLLE-LWIGDNKLNGT 472
Cdd:cd00116   73 LLQGLTKGCGLQELDLSDNALGPDGCGVLESLLrssSLQELKLNNNGLGDrglrLLAKGLKDLPPALEkLVLGRNRLEGA 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  473 ----IPLEIMKIQQLLRLDMSGNSL----IGSLPQDIGALQNLGTLSLGDNKL----SGKLPQTLGNCLTMESLFLEGNL 540
Cdd:cd00116  153 sceaLAKALRANRDLKELNLANNGIgdagIRALAEGLKANCNLEVLDLNNNGLtdegASALAETLASLKSLEVLNLGDNN 232
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  541 FyGDIP-------DLKGLVGVKEVDLSNNDL----SGSIPEYFASFSKLEYLNLSFNNL 588
Cdd:cd00116  233 L-TDAGaaalasaLLSPNISLLTLSLSCNDItddgAKDLAEVLAEKESLLELDLRGNKF 290
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
700-876 1.84e-07

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: 54.47  E-value: 1.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  700 NGFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVL---NMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEF 776
Cdd:cd05629    1 EDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLlksEMFKKDQLAHVKAERDVLAESDSPWVVSLYYS-----FQDAQY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  777 RALIYEFMPNGSLDMWLHPEEV--EEIHRpsrtlTLLERLNIAIDVASVLDYLHVhchepiahcDLKPSNVLLDDDLTAH 854
Cdd:cd05629   76 LYLIMEFLPGGDLMTMLIKYDTfsEDVTR-----FYMAECVLAIEAVHKLGFIHR---------DIKPDNILIDRGGHIK 141
                        170       180
                 ....*....|....*....|..
gi 18408454  855 VSDFGLARLLLKFDEESFFNQL 876
Cdd:cd05629  142 LSDFGLSTGFHKQHDSAYYQKL 163
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
695-920 2.20e-07

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: 53.46  E-value: 2.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  695 LRNATNGFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNM--QRRGAMKsfmAECESLKDI-RHRNLVklltacssiDF 771
Cdd:cd06608    1 LPDPAGIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIieDEEEEIK---LEINILRKFsNHPNIA---------TF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  772 QGNEFRA----------LIYEFMPNGSL-DMwlhpeeVEEIHRPSRTLTllERLnIAI---DVASVLDYLHVHchePIAH 837
Cdd:cd06608   69 YGAFIKKdppggddqlwLVMEYCGGGSVtDL------VKGLRKKGKRLK--EEW-IAYilrETLRGLAYLHEN---KVIH 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  838 CDLKPSNVLLDDDltAHVS--DFGLARlllkfdeesffnQLSSA-GVRGT-IG---YAAPEYGVGGQ---PSIN--GDVY 905
Cdd:cd06608  137 RDIKGQNILLTEE--AEVKlvDFGVSA------------QLDSTlGRRNTfIGtpyWMAPEVIACDQqpdASYDarCDVW 202
                        250
                 ....*....|....*
gi 18408454  906 SFGILLLEMFTGKRP 920
Cdd:cd06608  203 SLGITAIELADGKPP 217
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
708-931 2.46e-07

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: 53.28  E-value: 2.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKsfMAECESLKDIRhrnLVKLLTACSSidfqgNEFRALIYEFMPNG 787
Cdd:cd13991   14 IGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFRAEE--LMACAGLTSPR---VVPLYGAVRE-----GPWVNIFMDLKEGG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 SLDMWLH-----PEEVEeIHRPSRTLTLLErlniaidvasvldYLHvhcHEPIAHCDLKPSNVLLDDDLT-AHVSDFGLA 861
Cdd:cd13991   84 SLGQLIKeqgclPEDRA-LHYLGQALEGLE-------------YLH---SRKILHGDVKADNVLLSSDGSdAFLCDFGHA 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18408454  862 RLLlkfDEESFFNQLSSAG-VRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTNELFGGNFTL 931
Cdd:cd13991  147 ECL---DPDGLGKSLFTGDyIPGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPWTQYYSGPLCL 214
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
702-920 2.61e-07

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


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 53.09  E-value: 2.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALllTEKKV---VAVKVLNMQRRGAMKSFMA-ECESLKDIRHRNLVKLLtacssiDFQGNEFR 777
Cdd:cd14201    8 YSRKDLVGHGAFAVVFKGR--HRKKTdweVAIKSINKKNLSKSQILLGkEIKILKELQHENIVALY------DVQEMPNS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  778 A-LIYEFMPNGSLDMWLhpeEVEEIHRPSRTLTLLERlniaidVASVLDYLHvhcHEPIAHCDLKPSNVLLD-------- 848
Cdd:cd14201   80 VfLVMEYCNGGDLADYL---QAKGTLSEDTIRVFLQQ------IAAAMRILH---SKGIIHRDLKPQNILLSyasrkkss 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  849 -DDLTAHVSDFGLARLLLkfdeesffNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14201  148 vSGIRIKIADFGFARYLQ--------SNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPP 212
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
706-924 2.69e-07

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: 53.38  E-value: 2.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTVYKALLLTEKKVVAVKVLNM--QRRGAMKSFMAECESLKDIRHRNLVKL--LTACSSIDFqgnefralIY 781
Cdd:cd07843   11 NRIEEGTYGVVYRARDKKTGEIVALKKLKMekEKEGFPITSLREINILLKLQHPNIVTVkeVVVGSNLDK--------IY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 ---EFMPNgSLDMWLhpEEVEEIHRPSRTLTLLERLNIAIDvasvldYLHVHChepIAHCDLKPSNVLLDDDLTAHVSDF 858
Cdd:cd07843   83 mvmEYVEH-DLKSLM--ETMKQPFLQSEVKCLMLQLLSGVA------HLHDNW---ILHRDLKTSNLLLNNRGILKICDF 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  859 GLARlllKFdeESFFNQLSSAGVrgTIGYAAPEYGVGGQ---PSIngDVYS----FGILLLE--MFTGKRPTNEL 924
Cdd:cd07843  151 GLAR---EY--GSPLKPYTQLVV--TLWYRAPELLLGAKeysTAI--DMWSvgciFAELLTKkpLFPGKSEIDQL 216
LRRNT_2 pfam08263
Leucine rich repeat N-terminal domain; Leucine Rich Repeats pfam00560 are short sequence ...
22-61 2.71e-07

Leucine rich repeat N-terminal domain; Leucine Rich Repeats pfam00560 are short sequence motifs present in a number of proteins with diverse functions and cellular locations. Leucine Rich Repeats are often flanked by cysteine rich domains. This domain is often found at the N-terminus of tandem leucine rich repeats.


Pssm-ID: 462411 [Multi-domain]  Cd Length: 41  Bit Score: 47.67  E-value: 2.71e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 18408454     22 DETDRQALLQFKSQVSeDKRVVLSSWNHSFP-LCNWKGVTC 61
Cdd:pfam08263    1 LNDDGQALLAFKSSLN-DPPGALSSWNSSSSdPCSWTGVTC 40
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
690-920 3.03e-07

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: 53.09  E-value: 3.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  690 ISYGDLRNATNGFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRgAMKSFMAECESLKDI-RHRNLVKLLTACSS 768
Cdd:cd06636    6 IDLSALRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTED-EEEEIKLEINMLKKYsHHRNIATYYGAFIK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  769 IDFQGNEFRA-LIYEFMPNGSldmwlhpeeVEEIHRPSRTLTLLERLnIAIDVASVLDYL-HVHCHEPIaHCDLKPSNVL 846
Cdd:cd06636   85 KSPPGHDDQLwLVMEFCGAGS---------VTDLVKNTKGNALKEDW-IAYICREILRGLaHLHAHKVI-HRDIKGQNVL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  847 LDDDLTAHVSDFGLARLLLKfdeesffnqlsSAGVR----GTIGYAAPEY-GVGGQP----SINGDVYSFGILLLEMFTG 917
Cdd:cd06636  154 LTENAEVKLVDFGVSAQLDR-----------TVGRRntfiGTPYWMAPEViACDENPdatyDYRSDIWSLGITAIEMAEG 222

                 ...
gi 18408454  918 KRP 920
Cdd:cd06636  223 APP 225
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
708-920 3.12e-07

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


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 52.94  E-value: 3.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMqrRGAMKSFM-AECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFMpn 786
Cdd:cd14104    8 LGRGQFGIVHRCVETSSKKTYMAKFVKV--KGADQVLVkKEISILNIARHRNILRLHES-----FESHEELVMIFEFI-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  787 GSLDMWlhpeevEEIHRPSRTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVS--DFGLARLL 864
Cdd:cd14104   79 SGVDIF------ERITTARFELNEREIVSYVRQVCEALEFLHSK---NIGHFDIRPENIIYCTRRGSYIKiiEFGQSRQL 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  865 LKFDeeSFFNQLSSAgvrgtiGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14104  150 KPGD--KFRLQYTSA------EFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINP 197
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
707-920 3.26e-07

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: 53.26  E-value: 3.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVykalLLTEKK----VVAVKVLnmQRRGAMKSFMAECeSLKDIRHRNLVK---LLTACSSIdFQGNEFRAL 779
Cdd:cd05591    2 VLGKGSFGKV----MLAERKgtdeVYAIKVL--KKDVILQDDDVDC-TMTEKRILALAAkhpFLTALHSC-FQTKDRLFF 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  780 IYEFMPNGSLdMWlhpeeveEIHRpSRTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFG 859
Cdd:cd05591   74 VMEYVNGGDL-MF-------QIQR-ARKFDEPRARFYAAEVTLALMFLHRH---GVIYRDLKLDNILLDAEGHCKLADFG 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  860 LARlllkfdeESFFNQLSSAGVRGTIGYAAPE------YGvggqPSIngDVYSFGILLLEMFTGKRP 920
Cdd:cd05591  142 MCK-------EGILNGKTTTTFCGTPDYIAPEilqeleYG----PSV--DWWALGVLMYEMMAGQPP 195
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
708-917 3.40e-07

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


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 53.49  E-value: 3.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLN--MQRRGAMKSFMAECESLKDIRHRNLVKLL---TACSSIDfqgnEFRA--LI 780
Cdd:cd07876   29 IGSGAQGIVCAAFDTVLGINVAVKKLSrpFQNQTHAKRAYRELVLLKCVNHKNIISLLnvfTPQKSLE----EFQDvyLV 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFMpNGSLDMWLHPEEVEEihrpsRTLTLLERLNIAIDvasvldylHVHChEPIAHCDLKPSNVLLDDDLTAHVSDFGL 860
Cdd:cd07876  105 MELM-DANLCQVIHMELDHE-----RMSYLLYQMLCGIK--------HLHS-AGIIHRDLKPSNIVVKSDCTLKILDFGL 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  861 ARlllkfdeESFFNQLSSAGVRgTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTG 917
Cdd:cd07876  170 AR-------TACTNFMMTPYVV-TRYYRAPEVILGMGYKENVDIWSVGCIMGELVKG 218
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
708-891 3.69e-07

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


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 52.61  E-value: 3.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKallLTEK---KVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQ-GNEFrALIYEF 783
Cdd:cd14103    1 LGRGKFGTVYR---CVEKatgKELAAKFIKCRKAKDREDVRNEIEIMNQLRHPRLLQLYDA-----FEtPREM-VLVMEY 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  784 MPNGSLdmwlhpeeVEEIHRPSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVS--DFGLA 861
Cdd:cd14103   72 VAGGEL--------FERVVDDDFELTERDCILFMRQICEGVQYMH---KQGILHLDLKPENILCVSRTGNQIKiiDFGLA 140
                        170       180       190
                 ....*....|....*....|....*....|.
gi 18408454  862 RlllKFDEEsffnqlSSAGVR-GTIGYAAPE 891
Cdd:cd14103  141 R---KYDPD------KKLKVLfGTPEFVAPE 162
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
709-859 4.02e-07

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: 50.13  E-value: 4.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  709 GSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIR--HRNLVKLLTACSSidfqgNEFRALIYEFMPN 786
Cdd:cd13968    2 GEGASAKVFWAEGECTTIGVAVKIGDDVNNEEGEDLESEMDILRRLKglELNIPKVLVTEDV-----DGPNILLMELVKG 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  787 GSLDMWLHPEEVEEIhrpsrtltLLERlnIAIDVASVLDYLHVhchEPIAHCDLKPSNVLLDDDLTAHVSDFG 859
Cdd:cd13968   77 GTLIAYTQEEELDEK--------DVES--IMYQLAECMRLLHS---FHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
708-920 4.16e-07

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: 52.26  E-value: 4.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLlTEKKVVAVKVLNMQR---RGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFM 784
Cdd:cd14161   11 LGKGTYGRVKKARD-SSGRLVAIKSIRKDRikdEQDLLHIRREIEIMSSLNHPHIISVYEV-----FENSSKIVIVMEYA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGslDMWLHPEEveeihrpSRTLTLLERLNIAIDVASVLDYlhvhCHEP-IAHCDLKPSNVLLDDDLTAHVSDFGLARL 863
Cdd:cd14161   85 SRG--DLYDYISE-------RQRLSELEARHFFRQIVSAVHY----CHANgIVHRDLKLENILLDANGNIKIADFGLSNL 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  864 llkFDEESFFNQLSsagvrGTIGYAAPEYgVGGQPSINGDV--YSFGILLLEMFTGKRP 920
Cdd:cd14161  152 ---YNQDKFLQTYC-----GSPLYASPEI-VNGRPYIGPEVdsWSLGVLLYILVHGTMP 201
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
692-935 4.45e-07

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: 52.96  E-value: 4.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  692 YGDLRNATNGFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLnmqrrgaMKSFMA---------ECESLKDIRHRNLVKL 762
Cdd:cd07856    2 FGTVFEITTRYSDLQPVGMGAFGLVCSARDQLTGQNVAVKKI-------MKPFSTpvlakrtyrELKLLKHLRHENIISL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  763 ltacSSIDFQGNEFRALIYEFMPNgsldmwlhpeeveEIHR--PSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDL 840
Cdd:cd07856   75 ----SDIFISPLEDIYFVTELLGT-------------DLHRllTSRPLEKQFIQYFLYQILRGLKYVH---SAGVIHRDL 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  841 KPSNVLLDDDLTAHVSDFGLARLllkfdEESffnQLSsaGVRGTIGYAAPEYGVGGQP-SINGDVYSFGILLLEMFTGKr 919
Cdd:cd07856  135 KPSNILVNENCDLKICDFGLARI-----QDP---QMT--GYVSTRYYRAPEIMLTWQKyDVEVDIWSAGCIFAEMLEGK- 203
                        250
                 ....*....|....*.
gi 18408454  920 ptnELFGGNFTLNSYT 935
Cdd:cd07856  204 ---PLFPGKDHVNQFS 216
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
736-925 4.67e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 53.46  E-value: 4.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   736 QRRGAMksfmAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIyefMPNGSLDMWLHPEEveeihrpSRTLTLLERLN 815
Cdd:PHA03212  126 QRGGTA----TEAHILRAINHPSIIQLKGT-----FTYNKFTCLI---LPRYKTDLYCYLAA-------KRNIAICDILA 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   816 IAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARLLLKFDEESFFnqlssaGVRGTIGYAAPE---- 891
Cdd:PHA03212  187 IERSVLRAIQYLH---ENRIIHRDIKAENIFINHPGDVCLGDFGAACFPVDINANKYY------GWAGTIATNAPEllar 257
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 18408454   892 --YGvggqPSIngDVYSFGILLLEMFTGKrptNELF 925
Cdd:PHA03212  258 dpYG----PAV--DIWSAGIVLFEMATCH---DSLF 284
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
707-923 5.11e-07

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: 52.39  E-value: 5.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVLNM-----QRRGAMKSFMAECESLKDIRHRNLVKLLTACSSidfQGNEFRALIY 781
Cdd:cd06651   14 LLGQGAFGRVYLCYDVDTGRELAAKQVQFdpespETSKEVSALECEIQLLKNLQHERIVQYYGCLRD---RAEKTLTIFM 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 EFMPNGSLDMWL--HPEEVEEIHRpSRTLTLLERLNiaidvasvldYLHVHChepIAHCDLKPSNVLLDDDLTAHVSDFG 859
Cdd:cd06651   91 EYMPGGSVKDQLkaYGALTESVTR-KYTRQILEGMS----------YLHSNM---IVHRDIKGANILRDSAGNVKLGDFG 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  860 LARLLLKFdeesffnQLSSAGVRGTIG---YAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTNE 923
Cdd:cd06651  157 ASKRLQTI-------CMSGTGIRSVTGtpyWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAE 216
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
703-920 5.48e-07

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


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 52.22  E-value: 5.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  703 SSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYE 782
Cdd:cd14193    7 NKEEILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEEVKNEIEVMNQLNHANLIQLYDA-----FESRNDIVLVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLdmwlhpeeVEEIHRPSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVS--DFGL 860
Cdd:cd14193   82 YVDGGEL--------FDRIIDENYNLTELDTILFIKQICEGIQYMH---QMYILHLDLKPENILCVSREANQVKiiDFGL 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  861 ARlLLKFDEESFFNqlssagvRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14193  151 AR-RYKPREKLRVN-------FGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSP 202
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
708-920 6.52e-07

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: 52.57  E-value: 6.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLnmqrrgAMKSFMAECESLKDIRHRNLVKLLTACSS-------IDFQGNEFRALI 780
Cdd:cd05586    1 IGKGTFGQVYQVRKKDTRRIYAMKVL------SKKVIVAKKEVAHTIGERNILVRTALDESpfivglkFSFQTPTDLYLV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFMPNGSLDMWLHPEEVEEIHRPsrtltlleRLNIAidvASVLDYLHVHCHEpIAHCDLKPSNVLLDDDLTAHVSDFGL 860
Cdd:cd05586   75 TDYMSGGELFWHLQKEGRFSEDRA--------KFYIA---ELVLALEHLHKND-IVYRDLKPENILLDANGHIALCDFGL 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  861 ARLLLKFDEESffNQLSsagvrGTIGYAAPEY-----GVGGQPsingDVYSFGILLLEMFTGKRP 920
Cdd:cd05586  143 SKADLTDNKTT--NTFC-----GTTEYLAPEVlldekGYTKMV----DFWSLGVLVFEMCCGWSP 196
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
706-920 6.61e-07

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: 52.10  E-value: 6.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTV----YKALLLTEKKV-VAVKVL---NMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSIDFQGnefr 777
Cdd:cd14076    7 RTLGEGEFGKVklgwPLPKANHRSGVqVAIKLIrrdTQQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYIG---- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  778 aLIYEFMPNGSL-DMWLHPEEVEEihrpSRTLTLLERLniaidvASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVS 856
Cdd:cd14076   83 -IVLEFVSGGELfDYILARRRLKD----SVACRLFAQL------ISGVAYLH---KKGVVHRDLKLENLLLDKNRNLVIT 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  857 DFGLARlllKFDEesFFNQLSSAGVrGTIGYAAPEYGVGGQP--SINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14076  149 DFGFAN---TFDH--FNGDLMSTSC-GSPCYAAPELVVSDSMyaGRKADIWSCGVILYAMLAGYLP 208
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
708-920 6.85e-07

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: 52.68  E-value: 6.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLL-----TEKKVVAVKVLnmqRRGAMKS----FMAECESLKDI-RHRNLVKLLTACSSidfQGNEFr 777
Cdd:cd05103   15 LGRGAFGQVIEADAFgidktATCRTVAVKML---KEGATHSehraLMSELKILIHIgHHLNVVNLLGACTK---PGGPL- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  778 ALIYEFMPNGSLDMWLHPE-----------------------------------------------------EVEEIHRP 804
Cdd:cd05103   88 MVIVEFCKFGNLSAYLRSKrsefvpyktkgarfrqgkdyvgdisvdlkrrldsitssqssassgfveekslsDVEEEEAG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  805 S-----RTLTLLERLNIAIDVASVLDYLhvhCHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARLLLKfDEEsffnQLSSA 879
Cdd:cd05103  168 QedlykDFLTLEDLICYSFQVAKGMEFL---ASRKCIHRDLAARNILLSENNVVKICDFGLARDIYK-DPD----YVRKG 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 18408454  880 GVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRP 920
Cdd:cd05103  240 DARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSlGASP 281
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
824-924 7.60e-07

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: 51.75  E-value: 7.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  824 LDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLARLllkfdeesfFNQLS--SAGVR-GTIGYAAPEYGVGGQPSI 900
Cdd:cd14111  112 LEYLHGR---RVLHLDIKPDNIMVTNLNAIKIVDFGSAQS---------FNPLSlrQLGRRtGTLEYMAPEMVKGEPVGP 179
                         90       100
                 ....*....|....*....|....
gi 18408454  901 NGDVYSFGILLLEMFTGKRPTNEL 924
Cdd:cd14111  180 PADIWSIGVLTYIMLSGRSPFEDQ 203
PLN03210 PLN03210
Resistant to P. syringae 6; Provisional
242-514 8.09e-07

Resistant to P. syringae 6; Provisional


Pssm-ID: 215633 [Multi-domain]  Cd Length: 1153  Bit Score: 53.34  E-value: 8.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   242 GYNHFSGRLRpdlgillpnLLSFN------MGGNYFTGSIPTTLSNISTLERL--------GMNENNLTGS-----IPTF 302
Cdd:PLN03210  583 GFDYLPPKLR---------LLRWDkyplrcMPSNFRPENLVKLQMQGSKLEKLwdgvhsltGLRNIDLRGSknlkeIPDL 653
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   303 GNVPNLKLLFLHTNSLGSDSSRDLEFLTSLTN-----CTQLETLGIGRN-------RLGGDLPI-SIANLSAKLVTLDLG 369
Cdd:PLN03210  654 SMATNLETLKLSDCSSLVELPSSIQYLNKLEDldmsrCENLEILPTGINlkslyrlNLSGCSRLkSFPDISTNISWLDLD 733
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   370 GTLISgSIPYDIgNLINLQKLIL---------DQNMLSGPLPTSLGKLLNLRYLSLFSNRLSggIPAFIGNMTMLETLDL 440
Cdd:PLN03210  734 ETAIE-EFPSNL-RLENLDELILcemkseklwERVQPLTPLMTMLSPSLTRLFLSDIPSLVE--LPSSIQNLHKLEHLEI 809
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   441 SNN----------GFEGIVPTSLGNCSHL-----LELWIGDNKLNGT----IPLEIMKIQQLLRLDMSGNSLIGSLPQDI 501
Cdd:PLN03210  810 ENCinletlptgiNLESLESLDLSGCSRLrtfpdISTNISDLNLSRTgieeVPWWIEKFSNLSFLDMNGCNNLQRVSLNI 889
                         330
                  ....*....|...
gi 18408454   502 GALQNLGTLSLGD 514
Cdd:PLN03210  890 SKLKHLETVDFSD 902
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
702-920 8.54e-07

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: 51.97  E-value: 8.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQR-RGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALI 780
Cdd:cd14168   12 FEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKAlKGKESSIENEIAVLRKIKHENIVALEDI-----YESPNHLYLV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFMPNGSLdmwlHPEEVEEIHRPSRTLTLLERlniaiDVASVLDYLHVHchePIAHCDLKPSNVLL---DDDLTAHVSD 857
Cdd:cd14168   87 MQLVSGGEL----FDRIVEKGFYTEKDASTLIR-----QVLDAVYYLHRM---GIVHRDLKPENLLYfsqDEESKIMISD 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  858 FGLARLllkfdeESFFNQLSSAGvrGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14168  155 FGLSKM------EGKGDVMSTAC--GTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPP 209
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
707-914 9.85e-07

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: 51.51  E-value: 9.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEkkvVAVKVLNM--QRRGAMKSFMAECESLKDIRHRNLVKLLTACSSidfqgNEFRALIYEFM 784
Cdd:cd14152    7 LIGQGRWGKVHRGRWHGE---VAIRLLEIdgNNQDHLKLFKKEVMNYRQTRHENVVLFMGACMH-----PPHLAIITSFC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLDMWlhpeeveeIHRPSRTLTLLERLNIAIDVASVLDYLHVhchEPIAHCDLKPSNVLLDDDLTAhVSDFGLARLL 864
Cdd:cd14152   79 KGRTLYSF--------VRDPKTSLDINKTRQIAQEIIKGMGYLHA---KGIVHKDLKSKNVFYDNGKVV-ITDFGLFGIS 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  865 LKFDEESFFNQLSSAgvRGTIGYAAPE----YGVGGQP-----SINGDVYSFGILLLEM 914
Cdd:cd14152  147 GVVQEGRRENELKLP--HDWLCYLAPEivreMTPGKDEdclpfSKAADVYAFGTIWYEL 203
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
708-928 1.01e-06

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: 51.11  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECES--LKDIRHRNLVKLLTAcssidFQGNEFRALIYEFMP 785
Cdd:cd08225    8 IGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASKKEVilLAKMKHPNIVTFFAS-----FQENGRLFIVMEYCD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLdmwlhpeeVEEIHRpSRTLTLLERLNIAIDVASVLDYLHVHcHEPIAHCDLKPSNVLLDDD-LTAHVSDFGLARLL 864
Cdd:cd08225   83 GGDL--------MKRINR-QRGVLFSEDQILSWFVQISLGLKHIH-DRKILHRDIKSQNIFLSKNgMVAKLGDFGIARQL 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  865 lkfDEESFFNQLSSagvrGTIGYAAPEYgVGGQPSING-DVYSFGILLLEMFTGKRPtnelFGGN 928
Cdd:cd08225  153 ---NDSMELAYTCV----GTPYYLSPEI-CQNRPYNNKtDIWSLGCVLYELCTLKHP----FEGN 205
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
702-920 1.02e-06

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: 51.98  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYkallLTEKK----VVAVKVL---NMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGN 774
Cdd:cd05627    4 FESLKVIGRGAFGEVR----LVQKKdtghIYAMKILrkaDMLEKEQVAHIRAERDILVEADGAWVVKMFYS-----FQDK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  775 EFRALIYEFMPNGSLDMWLHPEEV--EEihrpsRTLTLLERLNIAIDVASVLDYLHVhchepiahcDLKPSNVLLDDDLT 852
Cdd:cd05627   75 RNLYLIMEFLPGGDMMTLLMKKDTlsEE-----ATQFYIAETVLAIDAIHQLGFIHR---------DIKPDNLLLDAKGH 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  853 AHVSDFGLARLLLKFDEESFFNQLS----------------------------SAGVRGTIGYAAPEygVGGQPSING-- 902
Cdd:cd05627  141 VKLSDFGLCTGLKKAHRTEFYRNLThnppsdfsfqnmnskrkaetwkknrrqlAYSTVGTPDYIAPE--VFMQTGYNKlc 218
                        250
                 ....*....|....*...
gi 18408454  903 DVYSFGILLLEMFTGKRP 920
Cdd:cd05627  219 DWWSLGVIMYEMLIGYPP 236
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
708-868 1.19e-06

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


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 51.80  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVL---NMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFM 784
Cdd:cd05610   12 ISRGAFGKVYLGRKKNNSKLYAVKVVkkaDMINKNMVHQVQAERDALALSKSPFIVHLYYS-----LQSANNVYLVMEYL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLDMWLH-----PEEveeihrpsrtltlLERLNIAiDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFG 859
Cdd:cd05610   87 IGGDVKSLLHiygyfDEE-------------MAVKYIS-EVALALDYLHRH---GIIHRDLKPDNMLISNEGHIKLTDFG 149

                 ....*....
gi 18408454  860 LARLLLKFD 868
Cdd:cd05610  150 LSKVTLNRE 158
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
708-936 1.27e-06

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


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 51.97  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLN--MQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidfqgnefraliyeFMP 785
Cdd:cd07875   32 IGSGAQGIVCAAYDAILERNVAIKKLSrpFQNQTHAKRAYRELVLMKCVNHKNIIGLLNV-----------------FTP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLdmwlhpEEVEEIHRPSRTL--TLLERLNIAIDvASVLDYL---------HVHChEPIAHCDLKPSNVLLDDDLTAH 854
Cdd:cd07875   95 QKSL------EEFQDVYIVMELMdaNLCQVIQMELD-HERMSYLlyqmlcgikHLHS-AGIIHRDLKPSNIVVKSDCTLK 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  855 VSDFGLARLLlkfdEESFFNQLSSAgvrgTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRptneLFGGNFTLNSY 934
Cdd:cd07875  167 ILDFGLARTA----GTSFMMTPYVV----TRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGV----LFPGTDHIDQW 234

                 ..
gi 18408454  935 TK 936
Cdd:cd07875  235 NK 236
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
708-999 1.40e-06

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: 51.20  E-value: 1.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKkvVAVKVLNMQRRGamkSFMAECESLKDI--RHRNLVKLLTAcssiDFQGNEFRA---LIYE 782
Cdd:cd14219   13 IGKGRYGEVWMGKWRGEK--VAVKVFFTTEEA---SWFRETEIYQTVlmRHENILGFIAA----DIKGTGSWTqlyLITD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLDMWLHpeeveeihrpSRTLTLLERLNIAIDVASVLDYLHVHC-----HEPIAHCDLKPSNVLLDDDLTAHVSD 857
Cdd:cd14219   84 YHENGSLYDYLK----------STTLDTKAMLKLAYSSVSGLCHLHTEIfstqgKPAIAHRDLKSKNILVKKNGTCCIAD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  858 FGLArllLKFDEESFFNQLSSAGVRGTIGYAAPEYGVGG------QPSINGDVYSFGILLLEMftGKRPTNELFGGNFTL 931
Cdd:cd14219  154 LGLA---VKFISDTNEVDIPPNTRVGTKRYMPPEVLDESlnrnhfQSYIMADMYSFGLILWEV--ARRCVSGGIVEEYQL 228
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  932 nSYTKSALPERILDIVDESILHIGLRVGFP----VVECLTMVFEVGLRCCEESPMNRLATSIVVKELISIRE 999
Cdd:cd14219  229 -PYHDLVPSDPSYEDMREIVCIKRLRPSFPnrwsSDECLRQMGKLMTECWAHNPASRLTALRVKKTLAKMSE 299
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
696-924 1.46e-06

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


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 50.81  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  696 RNATNGFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKlltacssidFQGNE 775
Cdd:cd06645    7 RNPQEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAVVQQEIIMMKDCKHSNIVA---------YFGSY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  776 FRA----LIYEFMPNGSLdmwlhpeevEEIHRPSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDL 851
Cdd:cd06645   78 LRRdklwICMEFCGGGSL---------QDIYHVTGPLSESQIAYVSRETLQGLYYLH---SKGKMHRDIKGANILLTDNG 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  852 TAHVSDFGLARLLLKF--DEESFFnqlssagvrGTIGYAAPEYGV----GGQPSInGDVYSFGILLLEMFTGKRPTNEL 924
Cdd:cd06645  146 HVKLADFGVSAQITATiaKRKSFI---------GTPYWMAPEVAAverkGGYNQL-CDIWAVGITAIELAELQPPMFDL 214
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
708-937 1.55e-06

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: 51.24  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVykalLLTEKK----VVAVKVLnmQRRGAMKSFMAECESLKdirhRNLVKL------LTACSSIdFQGNEFR 777
Cdd:cd05587    4 LGKGSFGKV----MLAERKgtdeLYAIKIL--KKDVIIQDDDVECTMVE----KRVLALsgkppfLTQLHSC-FQTMDRL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  778 ALIYEFMPNGslDMWLHPEEVEEIHRPSRTLtllerlnIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSD 857
Cdd:cd05587   73 YFVMEYVNGG--DLMYHIQQVGKFKEPVAVF-------YAAEIAVGLFFLHSK---GIIYRDLKLDNVMLDAEGHIKIAD 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  858 FGLARlllkfdeESFFNQLSSAGVRGTIGYAAPEYgVGGQP---SIngDVYSFGILLLEMFTGKRP-----TNELFGGNF 929
Cdd:cd05587  141 FGMCK-------EGIFGGKTTRTFCGTPDYIAPEI-IAYQPygkSV--DWWAYGVLLYEMLAGQPPfdgedEDELFQSIM 210

                 ....*....
gi 18408454  930 TLN-SYTKS 937
Cdd:cd05587  211 EHNvSYPKS 219
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
707-923 1.61e-06

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: 50.70  E-value: 1.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKS------------FMAECESLKdirHRNLVKLLTACSSID-Fqg 773
Cdd:cd14005    7 LLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTEWAMingpvpvpleiaLLLKASKPG---VPGVIRLLDWYERPDgF-- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  774 nefrALIYEFmPNGSLDMWlhpEEVEEIHRPSRTLT--LLERLNIAIDvasvldylhvHCHEP-IAHCDLKPSNVLLD-D 849
Cdd:cd14005   82 ----LLIMER-PEPCQDLF---DFITERGALSENLAriIFRQVVEAVR----------HCHQRgVLHRDIKDENLLINlR 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  850 DLTAHVSDFGLARLLLKFDEESFfnqlssagvRGTIGYAAPEY---GV-GGQPSIngdVYSFGILLLEMFTGKRPTNE 923
Cdd:cd14005  144 TGEVKLIDFGCGALLKDSVYTDF---------DGTRVYSPPEWirhGRyHGRPAT---VWSLGILLYDMLCGDIPFEN 209
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
824-918 1.65e-06

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: 51.25  E-value: 1.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  824 LDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARlllKFDEESFFNQLSSAGVRGTIGYAAPEYGVGGQPSING- 902
Cdd:cd07857  118 LKYIH---SANVLHRDLKPGNLLVNADCELKICDFGLAR---GFSENPGENAGFMTEYVATRWYRAPEIMLSFQSYTKAi 191
                         90
                 ....*....|....*.
gi 18408454  903 DVYSFGILLLEMFTGK 918
Cdd:cd07857  192 DVWSVGCILAELLGRK 207
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
279-439 1.80e-06

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 50.17  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  279 LSNISTLERLGMNENNLTgSIPTFGNVPNLKLLFLHTNSLgsdssrdlEFLTSLTNCTQLETLGIGRNRLGGDLPI---- 354
Cdd:cd21340   42 LEFLTNLTHLYLQNNQIE-KIENLENLVNLKKLYLGGNRI--------SVVEGLENLTNLEELHIENQRLPPGEKLtfdp 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  355 -SIANLSAKLVTLDLGGTLIsgSIPYDIGNLINLQKLILDQNMLS--GPLPTSLGKLLNLRYLSLFSNRLSGGI---PAF 428
Cdd:cd21340  113 rSLAALSNSLRVLNISGNNI--DSLEPLAPLRNLEQLDASNNQISdlEELLDLLSSWPSLRELDLTGNPVCKKPkyrDKI 190
                        170
                 ....*....|.
gi 18408454  429 IGNMTMLETLD 439
Cdd:cd21340  191 ILASKSLEVLD 201
PLN03150 PLN03150
hypothetical protein; Provisional
258-318 1.81e-06

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 51.74  E-value: 1.81e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454   258 LPNLLSFNMGGNYFTGSIPTTLSNISTLERLGMNENNLTGSIP-TFGNVPNLKLLFLHTNSL 318
Cdd:PLN03150  441 LRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPeSLGQLTSLRILNLNGNSL 502
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
708-920 2.03e-06

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


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 50.81  E-value: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVL------NMQRR-GAMKSfmaeCESlkdirHRNLVKLltaCSSIDFQGNEFraLI 780
Cdd:cd14179   15 LGEGSFSICRKCLHKKTNQEYAVKIVskrmeaNTQREiAALKL----CEG-----HPNIVKL---HEVYHDQLHTF--LV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFMPNGSLdmwlhpeeVEEIHRpSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLL---DDDLTAHVSD 857
Cdd:cd14179   81 MELLKGGEL--------LERIKK-KQHFSETEASHIMRKLVSAVSHMH---DVGVVHRDLKPENLLFtdeSDNSEIKIID 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  858 FGLARLllkfdeESFFNQLSSAGVRgTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14179  149 FGFARL------KPPDNQPLKTPCF-TLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVP 204
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
708-927 2.04e-06

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: 51.02  E-value: 2.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDI--RHRNLVKL----------------------- 762
Cdd:cd13977    8 VGRGSYGVVYEAVVRRTGARVAVKKIRCNAPENVELALREFWALSSIqrQHPNVIQLeecvlqrdglaqrmshgssksdl 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  763 --------LTACSSIDFQGNEFRALIYEFMPNGSLDMWLHPEeveeihRPSRTLTLlerlNIAIDVASVLDYLHvhcHEP 834
Cdd:cd13977   88 ylllvetsLKGERCFDPRSACYLWFVMEFCDGGDMNEYLLSR------RPDRQTNT----SFMLQLSSALAFLH---RNQ 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  835 IAHCDLKPSNVLLD---DDLTAHVSDFGLARLL----LKFDEESFFNQ--LSSAGvrGTIGYAAPEYGvGGQPSINGDVY 905
Cdd:cd13977  155 IVHRDLKPDNILIShkrGEPILKVADFGLSKVCsgsgLNPEEPANVNKhfLSSAC--GSDFYMAPEVW-EGHYTAKADIF 231
                        250       260
                 ....*....|....*....|....*..
gi 18408454  906 SFGILLLEM-----FTGKRPTNELFGG 927
Cdd:cd13977  232 ALGIIIWAMveritFRDGETKKELLGT 258
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
708-915 2.07e-06

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: 50.64  E-value: 2.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMK---SFMAECESLKDIRHRNLVKLLTAC-SSIDFqgnefrALIYEF 783
Cdd:cd05086    5 IGNGWFGKVLLGEIYTGTSVARVVVKELKASANPKeqdDFLQQGEPYYILQHPNILQCVGQCvEAIPY------LLVFEF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  784 MPNGSLDMWLHPEEvEEIHRPSRTLtLLERLniAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLARL 863
Cdd:cd05086   79 CDLGDLKTYLANQQ-EKLRGDSQIM-LLQRM--ACEIAAGLAHMHKH---NFLHSDLALRNCYLTSDLTVKVGDYGIGFS 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18408454  864 LLKFD-----EESFFnqlssagvrgTIGYAAPEYGVGGQPSI-------NGDVYSFGILLLEMF 915
Cdd:cd05086  152 RYKEDyietdDKKYA----------PLRWTAPELVTSFQDGLlaaeqtkYSNIWSLGVTLWELF 205
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
706-918 2.20e-06

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 50.91  E-value: 2.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   706 NMVGSGSFGTVYKALLLTEKKVVAVK-VLNMQRRGAMKSF-------------MAECESLKDIRHRNLVKLLTAcssidF 771
Cdd:PTZ00024   15 AHLGEGTYGKVEKAYDTLTGKIVAIKkVKIIEISNDVTKDrqlvgmcgihfttLRELKIMNEIKHENIMGLVDV-----Y 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   772 QGNEFRALIYEFMPNgsldmwlhpeeveEIHRPSRTLTLLERLNIAIDVASVLDYLHVHCHEPIAHCDLKPSNVLLDDDL 851
Cdd:PTZ00024   90 VEGDFINLVMDIMAS-------------DLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKG 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454   852 TAHVSDFGLARlllKFDEESFFNQLSSAGVRG----------TIGYAAPEYGVGGQP-SINGDVYSFGILLLEMFTGK 918
Cdd:PTZ00024  157 ICKIADFGLAR---RYGYPPYSDTLSKDETMQrreemtskvvTLWYRAPELLMGAEKyHFAVDMWSVGCIFAELLTGK 231
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
815-913 2.24e-06

putative serine/threonine kinase; Provisional


Pssm-ID: 165211 [Multi-domain]  Cd Length: 294  Bit Score: 50.72  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   815 NIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLARLLLKFDEESFFNQLSSAGVRGTIGYAAPEYGV 894
Cdd:PHA02882  130 NIMKDMLTTLEYIHEH---GISHGDIKPENIMVDGNNRGYIIDYGIASHFIIHGKHIEYSKEQKDLHRGTLYYAGLDAHN 206
                          90
                  ....*....|....*....
gi 18408454   895 GGQPSINGDVYSFGILLLE 913
Cdd:PHA02882  207 GACVTRRGDLESLGYCMLK 225
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
702-920 2.28e-06

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: 51.19  E-value: 2.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYkallLTEKK----VVAVKVL---NMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGN 774
Cdd:cd05628    3 FESLKVIGRGAFGEVR----LVQKKdtghVYAMKILrkaDMLEKEQVGHIRAERDILVEADSLWVVKMFYS-----FQDK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  775 EFRALIYEFMPNGSLDMWLHPEEV--EEihrpsRTLTLLERLNIAIDVASVLDYLHVhchepiahcDLKPSNVLLDDDLT 852
Cdd:cd05628   74 LNLYLIMEFLPGGDMMTLLMKKDTltEE-----ETQFYIAETVLAIDSIHQLGFIHR---------DIKPDNLLLDSKGH 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  853 AHVSDFGLARLLLKFDEESFFNQLSSA----------------------------GVRGTIGYAAPEYGVGGQPSINGDV 904
Cdd:cd05628  140 VKLSDFGLCTGLKKAHRTEFYRNLNHSlpsdftfqnmnskrkaetwkrnrrqlafSTVGTPDYIAPEVFMQTGYNKLCDW 219
                        250
                 ....*....|....*.
gi 18408454  905 YSFGILLLEMFTGKRP 920
Cdd:cd05628  220 WSLGVIMYEMLIGYPP 235
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
694-920 2.28e-06

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


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 50.84  E-value: 2.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  694 DLRNATNGFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLN---MQRRGAMKSFMAEceslKDIR-HRN---LVKLLTAc 766
Cdd:cd05596   20 KLRMNAEDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSkfeMIKRSDSAFFWEE----RDIMaHANsewIVQLHYA- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  767 ssidFQGNEFRALIYEFMPNGSLdmwlhpeeveeihrpsrtLTLLERLNIAIDVAS--------VLDYLHvhcHEPIAHC 838
Cdd:cd05596   95 ----FQDDKYLYMVMDYMPGGDL------------------VNLMSNYDVPEKWARfytaevvlALDAIH---SMGFVHR 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  839 DLKPSNVLLDDDLTAHVSDFGLArllLKFDEESffnQLSSAGVRGTIGYAAPEY----GVGGQPSINGDVYSFGILLLEM 914
Cdd:cd05596  150 DVKPDNMLLDASGHLKLADFGTC---MKMDKDG---LVRSDTAVGTPDYISPEVlksqGGDGVYGRECDWWSVGVFLYEM 223

                 ....*.
gi 18408454  915 FTGKRP 920
Cdd:cd05596  224 LVGDTP 229
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
708-920 2.35e-06

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: 50.32  E-value: 2.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRgamksfmaECESLKDI-----RHRNLVKLLTAcssidFQGNEFRALIYE 782
Cdd:cd14091    8 IGKGSYSVCKRCIHKATGKEYAVKIIDKSKR--------DPSEEIEIllrygQHPNIITLRDV-----YDDGNSVYLVTE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLdmwlhpeeVEEIHRpSRTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDL----TAHVSDF 858
Cdd:cd14091   75 LLRGGEL--------LDRILR-QKFFSEREASAVMKTLTKTVEYLHSQ---GVVHRDLKPSNILYADESgdpeSLRICDF 142
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  859 GLARlllkfdeesffnQLssagvRG----------TIGYAAPE------YGVGgqpsinGDVYSFGILLLEMFTGKRP 920
Cdd:cd14091  143 GFAK------------QL-----RAengllmtpcyTANFVAPEvlkkqgYDAA------CDIWSLGVLLYTMLAGYTP 197
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
702-928 3.28e-06

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: 50.38  E-value: 3.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLN-------MQRRgamksfMAECESLKDIRHRNLVKLLTACSSIDFQgn 774
Cdd:cd07849    7 YQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISpfehqtyCLRT------LREIKILLRFKHENIIGILDIQRPPTFE-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  775 EFRA--LIYEFMPNgslDMwlhpeeveeiHRPSRTLTL------------LERLNiAIDVASVLdylhvhchepiaHCDL 840
Cdd:cd07849   79 SFKDvyIVQELMET---DL----------YKLIKTQHLsndhiqyflyqiLRGLK-YIHSANVL------------HRDL 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  841 KPSNVLLDDDLTAHVSDFGLARLLLKFDEESFFNQLSSAgvrgTIGYAAPEYGV---GGQPSIngDVYSFGILLLEMFTG 917
Cdd:cd07849  133 KPSNLLLNTNCDLKICDFGLARIADPEHDHTGFLTEYVA----TRWYRAPEIMLnskGYTKAI--DIWSVGCILAEMLSN 206
                        250
                 ....*....|.
gi 18408454  918 kRPtneLFGGN 928
Cdd:cd07849  207 -RP---LFPGK 213
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
708-920 3.31e-06

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: 50.01  E-value: 3.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKsfmaECESLKDI-RHRNLVKLLTAcssidFQGNEFRALIYEFMPN 786
Cdd:cd14177   12 IGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPSE----EIEILMRYgQHPNIITLKDV-----YDDGRYVYLVTELMKG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  787 GSLdmwlhpeeVEEIHRpSRTLTLLERLNIAIDVASVLDYLHVhchEPIAHCDLKPSNVLLDDDL----TAHVSDFGLAR 862
Cdd:cd14177   83 GEL--------LDRILR-QKFFSEREASAVLYTITKTVDYLHC---QGVVHRDLKPSNILYMDDSanadSIRICDFGFAK 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  863 lLLKFDEESFFNQLSSAgvrgtiGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14177  151 -QLRGENGLLLTPCYTA------NFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTP 201
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
695-920 3.42e-06

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: 50.10  E-value: 3.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  695 LRNATNGFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQrRGAMKSFMAECESLKDI-RHRNLVKLLTACSSIDFQG 773
Cdd:cd06637    1 LRDPAGIFELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVT-GDEEEEIKQEINMLKKYsHHRNIATYYGAFIKKNPPG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  774 NEFRA-LIYEFMPNGSldmwlhpeeVEEIHRPSRTLTLLERLnIAIDVASVLDYL-HVHCHEPIaHCDLKPSNVLLDDDL 851
Cdd:cd06637   80 MDDQLwLVMEFCGAGS---------VTDLIKNTKGNTLKEEW-IAYICREILRGLsHLHQHKVI-HRDIKGQNVLLTENA 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  852 TAHVSDFGLARLLLKfdeesffnqlsSAGVR----GTIGYAAPEY-GVGGQP----SINGDVYSFGILLLEMFTGKRP 920
Cdd:cd06637  149 EVKLVDFGVSAQLDR-----------TVGRRntfiGTPYWMAPEViACDENPdatyDFKSDLWSLGITAIEMAEGAPP 215
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
702-920 4.19e-06

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: 49.24  E-value: 4.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGA---MKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRA 778
Cdd:cd14188    3 YCRGKVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKphqREKIDKEIELHRILHHKHVVQFYHY-----FEDKENIY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGSLdmwlhpeevEEIHRPSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDF 858
Cdd:cd14188   78 ILLEYCSRRSM---------AHILKARKVLTEPEVRYYLRQIVSGLKYLH---EQEILHRDLKLGNFFINENMELKVGDF 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  859 GLARLLlkfdeESFFNQLSSagVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14188  146 GLAARL-----EPLEHRRRT--ICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPP 200
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
708-920 4.35e-06

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: 49.87  E-value: 4.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVL------NMQRRGAMksfMAECESlkdirHRNLVKLLtacssiDFQGNEFRA-LI 780
Cdd:cd14180   14 LGEGSFSVCRKCRHRQSGQEYAVKIIsrrmeaNTQREVAA---LRLCQS-----HPNIVALH------EVLHDQYHTyLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFMPNGSLdmwlhpeeVEEIhRPSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDD---LTAHVSD 857
Cdd:cd14180   80 MELLRGGEL--------LDRI-KKKARFSESEASQLMRSLVSAVSFMH---EAGVVHRDLKPENILYADEsdgAVLKVID 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  858 FGLARLllkFDEESFFNQLSSAgvrgTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14180  148 FGFARL---RPQGSRPLQTPCF----TLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVP 203
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
699-920 4.40e-06

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: 50.02  E-value: 4.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  699 TNGFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKsfmaECESL-KDIRHRNLVKLLTAcssidFQGNEFR 777
Cdd:cd14176   18 TDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE----EIEILlRYGQHPNIITLKDV-----YDDGKYV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  778 ALIYEFMPNGSLdmwlhpeeVEEIHRpSRTLTLLERLNIAIDVASVLDYLHVhchEPIAHCDLKPSNVLLDDDL----TA 853
Cdd:cd14176   89 YVVTELMKGGEL--------LDKILR-QKFFSEREASAVLFTITKTVEYLHA---QGVVHRDLKPSNILYVDESgnpeSI 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  854 HVSDFGLARlLLKFDEESFFNQLSSAgvrgtiGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14176  157 RICDFGFAK-QLRAENGLLMTPCYTA------NFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTP 216
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
708-920 4.42e-06

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: 49.26  E-value: 4.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKAL-LLTEKKVvAVKVLNMQR--RGAMKSFMAECESLKDIRHRNLVKLLTACSSIdfqgnEFRALIYEFM 784
Cdd:cd14075   10 LGSGNFSQVKLGIhQLTKEKV-AIKILDKTKldQKTQRLLSREISSMEKLHHPNIIRLYEVVETL-----SKLHLVMEYA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLDMWLHPE-EVEEIHrpSRtltllerlNIAIDVASVLDYLHVHChepIAHCDLKPSNVLLDDDLTAHVSDFGLARL 863
Cdd:cd14075   84 SGGELYTKISTEgKLSESE--AK--------PLFAQIVSAVKHMHENN---IIHRDLKAENVFYASNNCVKVGDFGFSTH 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  864 LlkfDEESFFNQLSsagvrGTIGYAAPE-----YGVGgqpsINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14075  151 A---KRGETLNTFC-----GSPPYAAPElfkdeHYIG----IYVDIWALGVLLYFMVTGVMP 200
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
708-918 4.56e-06

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


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 50.06  E-value: 4.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKAL-LLTEKKVVAVKVLN-MQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSIDFQGNEFRALIYEFMp 785
Cdd:cd07858   13 IGRGAYGIVCSAKnSETNEKVAIKKIANaFDNRIDAKRTLREIKLLRHLDHENVIAIKDIMPPPHREAFNDVYIVYELM- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 ngslDMWLHpeeveEIHRPSRTLT----------LLERLNiaidvasvldYLHvhcHEPIAHCDLKPSNVLLDDDLTAHV 855
Cdd:cd07858   92 ----DTDLH-----QIIRSSQTLSddhcqyflyqLLRGLK----------YIH---SANVLHRDLKPSNLLLNANCDLKI 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  856 SDFGLARllLKFDEESFFNQLSSagvrgTIGYAAPE-------YGVggqpSIngDVYSFGILLLEMFTGK 918
Cdd:cd07858  150 CDFGLAR--TTSEKGDFMTEYVV-----TRWYRAPElllncseYTT----AI--DVWSVGCIFAELLGRK 206
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
700-954 5.83e-06

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: 49.26  E-value: 5.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  700 NGFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKsfmaECESLKDI-RHRNLVKLLTAcssidFQGNEFRA 778
Cdd:cd14175    1 DGYVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPSE----EIEILLRYgQHPNIITLKDV-----YDDGKHVY 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGSLdmwlhpeeVEEIHRpSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDL----TAH 854
Cdd:cd14175   72 LVTELMRGGEL--------LDKILR-QKFFSEREASSVLHTICKTVEYLH---SQGVVHRDLKPSNILYVDESgnpeSLR 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  855 VSDFGLARlLLKFDEESFFNQLSSAgvrgtiGYAAPEYgVGGQPSING-DVYSFGILLLEMFTGKRP-------TNE--- 923
Cdd:cd14175  140 ICDFGFAK-QLRAENGLLMTPCYTA------NFVAPEV-LKRQGYDEGcDIWSLGILLYTMLAGYTPfangpsdTPEeil 211
                        250       260       270
                 ....*....|....*....|....*....|...
gi 18408454  924 --LFGGNFTLNSYTKSALPERILDIVDEsILHI 954
Cdd:cd14175  212 trIGSGKFTLSGGNWNTVSDAAKDLVSK-MLHV 243
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
805-925 6.41e-06

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: 49.62  E-value: 6.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  805 SRTLTLLERLNIAIDVASVLDYLhvhCHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARLLLKfDEesffNQLSSAGVRGT 884
Cdd:cd05107  233 SPALSYMDLVGFSYQVANGMEFL---ASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMR-DS----NYISKGSTFLP 304
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 18408454  885 IGYAAPEYGVGGQPSINGDVYSFGILLLEMFT------GKRPTNELF 925
Cdd:cd05107  305 LKWMAPESIFNNLYTTLSDVWSFGILLWEIFTlggtpyPELPMNEQF 351
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
410-590 6.45e-06

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 49.93  E-value: 6.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  410 NLRYLSLFSNRLSGGIPAFIGNMTMLETLDLSNNGFEGIVPTSLGNCSHLLELWIGDNKLNGTIPLEIMKIQQLLRLDMS 489
Cdd:COG4886    1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  490 GNSLIGSLPQDIGALQNLGTLSLGDNKLSGKLPQtlgncltMESLFLEGNLFYGDIPDLKGLVGVKEVDLSNNDLSgSIP 569
Cdd:COG4886   81 LLSLLLLGLTDLGDLTNLTELDLSGNEELSNLTN-------LESLDLSGNQLTDLPEELANLTNLKELDLSNNQLT-DLP 152
                        170       180
                 ....*....|....*....|.
gi 18408454  570 EYFASFSKLEYLNLSFNNLEG 590
Cdd:COG4886  153 EPLGNLTNLKSLDLSNNQLTD 173
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
707-920 6.61e-06

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: 49.28  E-value: 6.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGtvyKALLLTEKK---VVAVKVLNMQ---RRGAMKSFMAECESLKDIRHRNLVKLltacsSIDFQGNEFRALI 780
Cdd:cd05571    2 VLGKGTFG---KVILCREKAtgeLYAIKILKKEviiAKDEVAHTLTENRVLQNTRHPFLTSL-----KYSFQTNDRLCFV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  781 YEFMPNGSLDMWLHPEEV--EEihrpsRTltlleRLNIAiDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDF 858
Cdd:cd05571   74 MEYVNGGELFFHLSRERVfsED-----RT-----RFYGA-EIVLALGYLHSQ---GIVYRDLKLENLLLDKDGHIKITDF 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  859 GLARlllkfDEESFFNQLSSagVRGTIGYAAPE------YG--VggqpsingDVYSFGILLLEMFTGKRP 920
Cdd:cd05571  140 GLCK-----EEISYGATTKT--FCGTPEYLAPEvledndYGraV--------DWWGLGVVMYEMMCGRLP 194
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
707-924 7.50e-06

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


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 48.89  E-value: 7.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVLNM-----QRRGAMKSFMAECESLKDIRHRNLVKLLTACSsiDFQGNEFrALIY 781
Cdd:cd06652    9 LLGQGAFGRVYLCYDADTGRELAVKQVQFdpespETSKEVNALECEIQLLKNLLHERIVQYYGCLR--DPQERTL-SIFM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 EFMPNGSLDMWL--HPEEVEEIHRpSRTLTLLERLNiaidvasvldYLHVHChepIAHCDLKPSNVLLDDDLTAHVSDFG 859
Cdd:cd06652   86 EYMPGGSIKDQLksYGALTENVTR-KYTRQILEGVH----------YLHSNM---IVHRDIKGANILRDSVGNVKLGDFG 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  860 LARLLLKFdeesffnQLSSAG---VRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTNEL 924
Cdd:cd06652  152 ASKRLQTI-------CLSGTGmksVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWAEF 212
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
707-920 7.80e-06

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 49.21  E-value: 7.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKK-----VVAVKVLnmqRRGAM----KSFMAECESLKDI-RHRNLVKLLTACSsidfQGNEF 776
Cdd:cd05102   14 VLGHGAFGKVVEASAFGIDKsssceTVAVKML---KEGATasehKALMSELKILIHIgNHLNVVNLLGACT----KPNGP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  777 RALIYEFMPNGSLDMWLH---------------------------------PEEVEEIHRPSRT---------------- 807
Cdd:cd05102   87 LMVIVEFCKYGNLSNFLRakregfspyrersprtrsqvrsmveavradrrsRQGSDRVASFTEStsstnqprqevddlwq 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  808 --LTLLERLNIAIDVASVLDYLhvhCHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARLLLKfDEEsffnQLSSAGVRGTI 885
Cdd:cd05102  167 spLTMEDLICYSFQVARGMEFL---ASRKCIHRDLAARNILLSENNVVKICDFGLARDIYK-DPD----YVRKGSARLPL 238
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 18408454  886 GYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRP 920
Cdd:cd05102  239 KWMAPESIFDKVYTTQSDVWSFGVLLWEIFSlGASP 274
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
704-920 8.29e-06

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: 48.77  E-value: 8.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  704 SSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAmksfmaECESlkDIRHRNLV-KLLTACSSID-----FQGNEFR 777
Cdd:cd14198   12 TSKELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQ------DCRA--EILHEIAVlELAKSNPRVVnlhevYETTSEI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  778 ALIYEFMPNGSLDMWLHPEEVEEIhrPSRTLTLLERlniaidvaSVLDYLHVHCHEPIAHCDLKPSNVLLDD-----DLT 852
Cdd:cd14198   84 ILILEYAAGGEIFNLCVPDLAEMV--SENDIIRLIR--------QILEGVYYLHQNNIVHLDLKPQNILLSSiyplgDIK 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18408454  853 ahVSDFGLARlllkfdeesffnQLSSAG----VRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14198  154 --IVDFGMSR------------KIGHACelreIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESP 211
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
751-920 8.57e-06

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: 48.56  E-value: 8.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  751 LKDIRHRNlVKLLTACssidFQGNEFRALIYEFMPNGSLDMWLHPEEVEeihrpsrtLTLLERLNIAIDVASVLDYLHvh 830
Cdd:cd14043   50 LRELRHEN-VNLFLGL----FVDCGILAIVSEHCSRGSLEDLLRNDDMK--------LDWMFKSSLLLDLIKGMRYLH-- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  831 cHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARLL----LKFDEESFFNQLssagvrgtigYAAPEY----GVGGQPSING 902
Cdd:cd14043  115 -HRGIVHGRLKSRNCVVDGRFVLKITDYGYNEILeaqnLPLPEPAPEELL----------WTAPELlrdpRLERRGTFPG 183
                        170
                 ....*....|....*...
gi 18408454  903 DVYSFGILLLEMFTGKRP 920
Cdd:cd14043  184 DVFSFAIIMQEVIVRGAP 201
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
826-920 1.03e-05

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


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 48.39  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  826 YLHVHchePIAHCDLKPSNVLLDDDL---TAHVSDFGLARlLLKFDEEsffnqlsSAGVRGTIGYAAPEYGVGGQPSING 902
Cdd:cd14197  126 FLHNN---NVVHLDLKPQNILLTSESplgDIKIVDFGLSR-ILKNSEE-------LREIMGTPEYVAPEILSYEPISTAT 194
                         90
                 ....*....|....*...
gi 18408454  903 DVYSFGILLLEMFTGKRP 920
Cdd:cd14197  195 DMWSIGVLAYVMLTGISP 212
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
708-920 1.05e-05

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: 48.27  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGtvyKALLLTEK---KVVAVKVLNM------QRRGAMKsfmaECESLKDIRHRNLVkllTACSSIDFQGNEFra 778
Cdd:cd08218    8 IGEGSFG---KALLVKSKedgKQYVIKEINIskmspkEREESRK----EVAVLSKMKHPNIV---QYQESFEENGNLY-- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  779 LIYEFMPNGSLDMWLHPEeveeihrpsRTLTLLERLNIAIDVASVLDYLHVHcHEPIAHCDLKPSNVLLDDDLTAHVSDF 858
Cdd:cd08218   76 IVMDYCDGGDLYKRINAQ---------RGVLFPEDQILDWFVQLCLALKHVH-DRKILHRDIKSQNIFLTKDGIIKLGDF 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  859 GLARLLLKFDEesffnqLSSAGVrGTIGYAAPEYgVGGQPSIN-GDVYSFGILLLEMFTGKRP 920
Cdd:cd08218  146 GIARVLNSTVE------LARTCI-GTPYYLSPEI-CENKPYNNkSDIWALGCVLYEMCTLKHA 200
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
699-920 1.13e-05

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: 48.47  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  699 TNGFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKsfmaECESL-KDIRHRNLVKLLTAcssidFQGNEFR 777
Cdd:cd14178    2 TDGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPSE----EIEILlRYGQHPNIITLKDV-----YDDGKFV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  778 ALIYEFMPNGSLdmwlhpeeVEEIHRpSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDL----TA 853
Cdd:cd14178   73 YLVMELMRGGEL--------LDRILR-QKCFSEREASAVLCTITKTVEYLH---SQGVVHRDLKPSNILYMDESgnpeSI 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  854 HVSDFGLARlLLKFDEESFFNQLSSAgvrgtiGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14178  141 RICDFGFAK-QLRAENGLLMTPCYTA------NFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTP 200
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
770-916 1.22e-05

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: 48.87  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  770 DFQGNEF-RALIYEFMPNGSLDMWLHPEEVEeihrpsrTLTLLERLNIAIDVASVLDYLhvhCHEPIAHCDLKPSNVLLD 848
Cdd:cd05105  202 DIQRSNYdRPASYKGSNDSEVKNLLSDDGSE-------GLTTLDLLSFTYQVARGMEFL---ASKNCVHRDLAARNVLLA 271
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454  849 DDLTAHVSDFGLARLLLKFDeesffNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT 916
Cdd:cd05105  272 QGKIVKICDFGLARDIMHDS-----NYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFS 334
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
85-220 1.28e-05

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 47.47  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   85 SIGNLSFLVSLD-LY---------ENFFGgtipqevgqLSRLEYLDMGINYLRgpIPLGLYNCSRLLNLRLDSNRLGGSV 154
Cdd:cd21340   38 KIENLEFLTNLThLYlqnnqiekiENLEN---------LVNLKKLYLGGNRIS--VVEGLENLTNLEELHIENQRLPPGE 106
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18408454  155 P------SELGSLTNLVQLNLYGNNMRGklPTSLGNLTLLEQLALSHNNLE--GEIPSDVAQLTQIWSLQLVAN 220
Cdd:cd21340  107 KltfdprSLAALSNSLRVLNISGNNIDS--LEPLAPLRNLEQLDASNNQISdlEELLDLLSSWPSLRELDLTGN 178
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
708-936 1.43e-05

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


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 48.55  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLN--MQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidfqgnefraliyeFMP 785
Cdd:cd07874   25 IGSGAQGIVCAAYDAVLDRNVAIKKLSrpFQNQTHAKRAYRELVLMKCVNHKNIISLLNV-----------------FTP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLdmwlhpEEVEEIHRPSRTL--TLLERLNIAIDvASVLDYL---------HVHChEPIAHCDLKPSNVLLDDDLTAH 854
Cdd:cd07874   88 QKSL------EEFQDVYLVMELMdaNLCQVIQMELD-HERMSYLlyqmlcgikHLHS-AGIIHRDLKPSNIVVKSDCTLK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  855 VSDFGLARLLlkfdEESFFnqLSSAGVrgTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRptneLFGGNFTLNSY 934
Cdd:cd07874  160 ILDFGLARTA----GTSFM--MTPYVV--TRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKI----LFPGRDYIDQW 227

                 ..
gi 18408454  935 TK 936
Cdd:cd07874  228 NK 229
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
707-945 1.61e-05

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: 47.71  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVL-----NMQRRGAMKSFMAECESLKDIRHRNLVKLLtACssidFQGNEFRAL-- 779
Cdd:cd06653    9 LLGRGAFGEVYLCYDADTGRELAVKQVpfdpdSQETSKEVNALECEIQLLKNLRHDRIVQYY-GC----LRDPEEKKLsi 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  780 IYEFMPNGSLDMWL--HPEEVEEIHRpSRTLTLLERLNiaidvasvldYLHVHChepIAHCDLKPSNVLLDDDLTAHVSD 857
Cdd:cd06653   84 FVEYMPGGSVKDQLkaYGALTENVTR-RYTRQILQGVS----------YLHSNM---IVHRDIKGANILRDSAGNVKLGD 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  858 FGLARLLlkfdEESFFNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPTNEL--FGGNFTLNSY- 934
Cdd:cd06653  150 FGASKRI----QTICMSGTGIKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWAEYeaMAAIFKIATQp 225
                        250
                 ....*....|.
gi 18408454  935 TKSALPERILD 945
Cdd:cd06653  226 TKPQLPDGVSD 236
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
708-917 1.73e-05

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: 47.59  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKK------VVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSIDfqgnefRALIY 781
Cdd:cd14208    7 LGKGSFTKIYRGLRTDEEDdercetEVLLKVMDPTHGNCQESFLEAASIMSQISHKHLVLLHGVCVGKD------SIMVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  782 EFMPNGSLDMWLHPEEVEEIhrpsrtLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTA------HV 855
Cdd:cd14208   81 EFVCHGALDLYLKKQQQKGP------VAISWKLQVVKQLAYALNYLE---DKQLVHGNVSAKKVLLSREGDKgsppfiKL 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  856 SDFGLARLLLkfDEESFFNQlssagvrgtIGYAAPEYGVGGQP-SINGDVYSFGILLLEMFTG 917
Cdd:cd14208  152 SDPGVSIKVL--DEELLAER---------IPWVAPECLSDPQNlALEADKWGFGATLWEIFSG 203
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
708-920 2.08e-05

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: 47.51  E-value: 2.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVlnMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFMPNG 787
Cdd:cd14085   11 LGRGATSVVYRCRQKGTQKPYAVKK--LKKTVDKKIVRTEIGVLLRLSHPNIIKLKEI-----FETPTEISLVLELVTGG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 SLdmwlHPEEVEEIHRPSRtltllerlNIAIDVASVLD---YLHVHchePIAHCDLKPSNVL---LDDDLTAHVSDFGLA 861
Cdd:cd14085   84 EL----FDRIVEKGYYSER--------DAADAVKQILEavaYLHEN---GIVHRDLKPENLLyatPAPDAPLKIADFGLS 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  862 RLLLkfdeesffNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14085  149 KIVD--------QQVTMKTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEP 199
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
707-920 2.38e-05

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: 46.95  E-value: 2.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVLNMQR-RGAMKSFMAECESLKDIRHRNLVKLLtacSSIDFQGNEFraLIYEFMP 785
Cdd:cd14184    8 VIGDGNFAVVKECVERSTGKEFALKIIDKAKcCGKEHLIENEVSILRRVKHPNIIMLI---EEMDTPAELY--LVMELVK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGSLdmwlhpeeVEEIhRPSRTLTLLERLNIAIDVASVLDYLHVHChepIAHCDLKPSNVLL----DDDLTAHVSDFGLA 861
Cdd:cd14184   83 GGDL--------FDAI-TSSTKYTERDASAMVYNLASALKYLHGLC---IVHRDIKPENLLVceypDGTKSLKLGDFGLA 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  862 RLLlkfdEESFFNqlssagVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14184  151 TVV----EGPLYT------VCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPP 199
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
704-846 2.51e-05

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: 47.33  E-value: 2.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  704 SSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIR-HRNLVKLltacssIDFQGNEFR-ALIY 781
Cdd:cd14174    6 TDELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSRVFREVETLYQCQgNKNILEL------IEFFEDDTRfYLVF 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  782 EFMPNGSLDMWLHPEEveeiHRPSRtltllERLNIAIDVASVLDYLHVhchEPIAHCDLKPSNVL 846
Cdd:cd14174   80 EKLRGGSILAHIQKRK----HFNER-----EASRVVRDIASALDFLHT---KGIAHRDLKPENIL 132
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
708-923 2.51e-05

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


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 47.02  E-value: 2.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQR--RGAMKSFMAECESLKDIRHRNLVKLLTAcssIDFQGNEFraLIYEFMP 785
Cdd:cd14074   11 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKldDVSKAHLFQEVRCMKLVQHPNVVRLYEV---IDTQTKLY--LILELGD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  786 NGslDMW----LHPEEVEEihrpSRTLTLLERLNIAIDvasvldylhvHCHE-PIAHCDLKPSNVLLDDDL-TAHVSDFG 859
Cdd:cd14074   86 GG--DMYdyimKHENGLNE----DLARKYFRQIVSAIS----------YCHKlHVVHRDLKPENVVFFEKQgLVKLTDFG 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  860 LARLLLKFDeesffnQLSSAGvrGTIGYAAPEYGVGGQ---PSIngDVYSFGILLLEMFTGKRPTNE 923
Cdd:cd14074  150 FSNKFQPGE------KLETSC--GSLAYSAPEILLGDEydaPAV--DIWSLGVILYMLVCGQPPFQE 206
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
708-920 2.95e-05

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Genetic variations in TTBK1 are linked to Alzheimer's disease (AD). Hyperphosphorylated tau is a major component of paired helical filaments that accumulate in the brain of AD patients. Studies in transgenic mice show that TTBK1 is involved in the phosphorylation-dependent pathogenic aggregation of tau. The TTBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271032 [Multi-domain]  Cd Length: 262  Bit Score: 46.94  E-value: 2.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRrgAMKSFMAECESLKDIRHRNLVKLLTACSsidfQGNEFRALIyefmpng 787
Cdd:cd14130    8 IGGGGFGEIYEAMDLLTRENVALKVESAQQ--PKQVLKMEVAVLKKLQGKDHVCRFIGCG----RNEKFNYVV------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 sldMWLHPEEVEEIHR--PSRTLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNV----LLDDDLTAHVSDFGLA 861
Cdd:cd14130   75 ---MQLQGRNLADLRRsqPRGTFTLSTTLRLGKQILESIEAIH---SVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLA 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  862 RLLLKFDEESFFNQlSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14130  149 RQYTNTTGEVRPPR-NVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLP 206
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
699-920 4.49e-05

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


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 46.53  E-value: 4.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  699 TNGFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQR-RGAMKSFMAECESLKDIRHRNLVKLLTACSSIdfqgNEFR 777
Cdd:cd14183    5 SERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKcRGKEHMIQNEVSILRRVKHPNIVLLIEEMDMP----TELY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  778 aLIYEFMPNGSLdmwlhpeeVEEIHRPSRtLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLL----DDDLTA 853
Cdd:cd14183   81 -LVMELVKGGDL--------FDAITSTNK-YTERDASGMLYNLASAIKYLH---SLNIVHRDIKPENLLVyehqDGSKSL 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  854 HVSDFGLARLLlkfdEESFFNqlssagVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14183  148 KLGDFGLATVV----DGPLYT------VCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPP 204
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
816-920 4.82e-05

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: 46.95  E-value: 4.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  816 IAIDVASVLDYLHVHchePIAHCDLKPSNVLLDDDLTAHVSDFGLARLLLK-FDEESFFNqlssagvrGTIGYAAPEYGV 894
Cdd:cd05618  126 YSAEISLALNYLHER---GIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRpGDTTSTFC--------GTPNYIAPEILR 194
                         90       100
                 ....*....|....*....|....*.
gi 18408454  895 GGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd05618  195 GEDYGFSVDWWALGVLMFEMMAGRSP 220
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
706-891 4.87e-05

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: 46.42  E-value: 4.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  706 NMVGSGSFGTVYKALLLTEKKVVAVKVLNMQR-RGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFM 784
Cdd:cd14169    9 EKLGEGAFSEVVLAQERGSQRLVALKCIPKKAlRGKEAMVENEIAVLRRINHENIVSLEDI-----YESPTHLYLAMELV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  785 PNGSLDMWLhpeeveeIHRPSRTLTLLERLniaidVASVLD---YLHvhcHEPIAHCDLKPSNVLLD---DDLTAHVSDF 858
Cdd:cd14169   84 TGGELFDRI-------IERGSYTEKDASQL-----IGQVLQavkYLH---QLGIVHRDLKPENLLYAtpfEDSKIMISDF 148
                        170       180       190
                 ....*....|....*....|....*....|...
gi 18408454  859 GLArlllKFDEEsffNQLSSAGvrGTIGYAAPE 891
Cdd:cd14169  149 GLS----KIEAQ---GMLSTAC--GTPGYVAPE 172
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
691-928 5.04e-05

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


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 46.38  E-value: 5.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  691 SYGDLRNATNGFSSSN------MVGSGSFGTVYKALLLTEKKVVAVKVLNMQRrgaMKSFMAECESLKDIR-HRNLVKLL 763
Cdd:cd14132    3 EYWDYENLNVEWGSQDdyeiirKIGRGKYSEVFEGINIGNNEKVVIKVLKPVK---KKKIKREIKILQNLRgGPNIVKLL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  764 TACssIDFQGNEFrALIYEFMPNGSLDMwLHPeeveeihrpsrTLTLLERLNIAIDVASVLDYLHVHchePIAHCDLKPS 843
Cdd:cd14132   80 DVV--KDPQSKTP-SLIFEYVNNTDFKT-LYP-----------TLTDYDIRYYMYELLKALDYCHSK---GIMHRDVKPH 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  844 NVLLDDDL-TAHVSDFGLArlllkfdeeSFFNQLSSAGVR-GTIGYAAPEYGVGGQ---PSIngDVYSFGILLLEMFTGK 918
Cdd:cd14132  142 NIMIDHEKrKLRLIDWGLA---------EFYHPGQEYNVRvASRYYKGPELLVDYQyydYSL--DMWSLGCMLASMIFRK 210
                        250
                 ....*....|
gi 18408454  919 RPtneLFGGN 928
Cdd:cd14132  211 EP---FFHGH 217
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
817-920 5.34e-05

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: 46.55  E-value: 5.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  817 AIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARlllkfdeESFFNQLSSAGVRGTIGYAAPEYGVGG 896
Cdd:cd05617  122 AAEICIALNFLH---ERGIIYRDLKLDNVLLDADGHIKLTDYGMCK-------EGLGPGDTTSTFCGTPNYIAPEILRGE 191
                         90       100
                 ....*....|....*....|....
gi 18408454  897 QPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd05617  192 EYGFSVDWWALGVLMFEMMAGRSP 215
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
702-944 5.96e-05

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: 46.38  E-value: 5.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  702 FSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAE--------CESLKdirHRNLVKLLTACSSidfqg 773
Cdd:cd14094    5 YELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSPGLSTEdlkreasiCHMLK---HPHIVELLETYSS----- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  774 NEFRALIYEFMPNGSLDMwlhpeevEEIHRPSRTLTLLERlniaidVAS-----VLDYLHvHCHE-PIAHCDLKPSNVLL 847
Cdd:cd14094   77 DGMLYMVFEFMDGADLCF-------EIVKRADAGFVYSEA------VAShymrqILEALR-YCHDnNIIHRDVKPHCVLL 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  848 ---DDDLTAHVSDFGLARLLLKfdeesffNQLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRPtnel 924
Cdd:cd14094  143 askENSAPVKLGGFGVAIQLGE-------SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLP---- 211
                        250       260
                 ....*....|....*....|
gi 18408454  925 FGGnftlnsyTKSALPERIL 944
Cdd:cd14094  212 FYG-------TKERLFEGII 224
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
824-918 8.59e-05

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


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 45.89  E-value: 8.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  824 LDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARlLLKFDEESFFNQLSSagvrgTIGYAAPEYGVGGQPSING- 902
Cdd:cd07853  116 LKYLH---SAGILHRDIKPGNLLVNSNCVLKICDFGLAR-VEEPDESKHMTQEVV-----TQYYRAPEILMGSRHYTSAv 186
                         90
                 ....*....|....*.
gi 18408454  903 DVYSFGILLLEMFTGK 918
Cdd:cd07853  187 DIWSVGCIFAELLGRR 202
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
708-918 1.02e-04

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


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 45.44  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSidfQGNEFRALIYEFMPNg 787
Cdd:cd07867   10 VGRGTYGHVYKAKRKDGKDEKEYALKQIEGTGISMSACREIALLRELKHPNVIALQKVFLS---HSDRKVWLLFDYAEH- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 slDMWlHPEEVEEIHRPSRTLTLLERLNIAIDVASVLDYLHVHCHEPIAHCDLKPSNVLL----DDDLTAHVSDFGLARL 863
Cdd:cd07867   86 --DLW-HIIKFHRASKANKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARL 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  864 LlkfdeESFFNQLSSAG-VRGTIGYAAPEYGVGGQPSING-DVYSFGILLLEMFTGK 918
Cdd:cd07867  163 F-----NSPLKPLADLDpVVVTFWYRAPELLLGARHYTKAiDIWAIGCIFAELLTSE 214
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
708-928 1.13e-04

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: 45.32  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQ----RRGAMksfmaECESLK------DIR-HRNLVKLL------------T 764
Cdd:cd14212    7 LGQGTFGQVVKCQDLKTNKLVAVKVLKNKpayfRQAML-----EIAILTllntkyDPEdKHHIVRLLdhfmhhghlcivF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  765 ACSSIDF----QGNEFRALiyefmpngsldmwlhpeeveeihrpsrTLTLLERLNIAIdvasvLDYLHVHCHEPIAHCDL 840
Cdd:cd14212   82 ELLGVNLyellKQNQFRGL---------------------------SLQLIRKFLQQL-----LDALSVLKDARIIHCDL 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  841 KPSNVLLDDDLTAHVS--DFGLA----RLLLKFDEESFfnqlssagvrgtigYAAPEYGVGGQPSINGDVYSFGILLLEM 914
Cdd:cd14212  130 KPENILLVNLDSPEIKliDFGSAcfenYTLYTYIQSRF--------------YRSPEVLLGLPYSTAIDMWSLGCIAAEL 195
                        250
                 ....*....|....
gi 18408454  915 FTGkRPtneLFGGN 928
Cdd:cd14212  196 FLG-LP---LFPGN 205
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
824-917 1.13e-04

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


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 45.51  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  824 LDYLHVHchePIAHCDLKPSNVLLDDDLTA--HVSDFGLArlllKFDEESFFNQLSSAgvrgtiGYAAPEYGVGGQPSIN 901
Cdd:cd14224  181 LDALHRN---KIIHCDLKPENILLKQQGRSgiKVIDFGSS----CYEHQRIYTYIQSR------FYRAPEVILGARYGMP 247
                         90
                 ....*....|....*.
gi 18408454  902 GDVYSFGILLLEMFTG 917
Cdd:cd14224  248 IDMWSFGCILAELLTG 263
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
687-924 1.28e-04

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: 44.98  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  687 HEKISYGDLRNATNGFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVLNmqrrgAMKSFMAECESLKDI-----RHRNLVK 761
Cdd:cd06639    9 SSMLGLESLADPSDTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILD-----PISDVDEEIEAEYNIlrslpNHPNVVK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  762 LLTACSSID-FQGNEFrALIYEFMPNGSLDmwlhpEEVEEIHRPSRTLTllERLNIAIDVASVLDYLHVHCHEpIAHCDL 840
Cdd:cd06639   84 FYGMFYKADqYVGGQL-WLVLELCNGGSVT-----ELVKGLLKCGQRLD--EAMISYILYGALLGLQHLHNNR-IIHRDV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  841 KPSNVLLDDDLTAHVSDFGLARlllkfdeesffnQLSSAGVR-----GTIGYAAPEYGVGGQP-----SINGDVYSFGIL 910
Cdd:cd06639  155 KGNNILLTTEGGVKLVDFGVSA------------QLTSARLRrntsvGTPFWMAPEVIACEQQydysyDARCDVWSLGIT 222
                        250
                 ....*....|....
gi 18408454  911 LLEMFTGKRPTNEL 924
Cdd:cd06639  223 AIELADGDPPLFDM 236
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
708-920 1.51e-04

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Mutations in TTBK2 is associated with the development of spinocerebellar ataxia type 11, belonging to a group of neurodegenerative disorders characterized by progressive incoordination, dysarthria and impairment of eye movements. Brain tissues of SCA11 patients show the presence of neurofibrillary tangles and tau deposition in the brain, similar to Alzheimer's disease (AD) patients. The TTBK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271031 [Multi-domain]  Cd Length: 262  Bit Score: 44.66  E-value: 1.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRrgAMKSFMAECESLKDIRHRNLVKLLTACSsidfQGNEFRALIyefmpng 787
Cdd:cd14129    8 IGGGGFGEIYDALDLLTRENVALKVESAQQ--PKQVLKMEVAVLKKLQGKDHVCRFIGCG----RNDRFNYVV------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 sldMWLHPEEVEEIHRP-SR-TLTLLERLNIAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTA----HVSDFGLA 861
Cdd:cd14129   75 ---MQLQGRNLADLRRSqSRgTFTISTTLRLGRQILESIESIH---SVGFLHRDIKPSNFAMGRFPSTcrkcYMLDFGLA 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18408454  862 RlllkfdeeSFFNQL-------SSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd14129  149 R--------QFTNSCgdvrpprAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLP 206
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
723-920 1.66e-04

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 45.39  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   723 TEKKVVAVKVLNMQRRGAMKSfmAECESLKDIRHRNLVKLLTacssiDFQGNEFRALIYEFMPNGSLDMWLHPEEVEEIH 802
Cdd:PTZ00267   93 KEKVVAKFVMLNDERQAAYAR--SELHCLAACDHFGIVKHFD-----DFKSDDKLLLIMEYGSGGDLNKQIKQRLKEHLP 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   803 RPSRTLTLLerlniAIDVASVLDYLHVHChepIAHCDLKPSNVLLDDDLTAHVSDFGLARlllKFDEESFFNQLSSagVR 882
Cdd:PTZ00267  166 FQEYEVGLL-----FYQIVLALDEVHSRK---MMHRDLKSANIFLMPTGIIKLGDFGFSK---QYSDSVSLDVASS--FC 232
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 18408454   883 GTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:PTZ00267  233 GTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRP 270
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
708-918 2.09e-04

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


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 44.66  E-value: 2.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  708 VGSGSFGTVYKALLLTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACSSidfQGNEFRALIYEFMPNg 787
Cdd:cd07868   25 VGRGTYGHVYKAKRKDGKDDKDYALKQIEGTGISMSACREIALLRELKHPNVISLQKVFLS---HADRKVWLLFDYAEH- 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  788 slDMWlHPEEVEEIHRPSRTLTLLERLNIAIDVASVLDYLHVHCHEPIAHCDLKPSNVLL----DDDLTAHVSDFGLARL 863
Cdd:cd07868  101 --DLW-HIIKFHRASKANKKPVQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARL 177
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18408454  864 LlkfdeESFFNQLSSAG-VRGTIGYAAPEYGVGGQPSING-DVYSFGILLLEMFTGK 918
Cdd:cd07868  178 F-----NSPLKPLADLDpVVVTFWYRAPELLLGARHYTKAiDIWAIGCIFAELLTSE 229
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
700-920 2.30e-04

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: 44.51  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  700 NGFSSSNMVGSGSFGTVYKAL---LLTEKKV--VAVKVLNMQRRGAMK-SFMAECESLKDI-RHRNLVKLLTACS----- 767
Cdd:cd05104   35 DRLRFGKTLGAGAFGKVVEATaygLAKADSAmtVAVKMLKPSAHSTEReALMSELKVLSYLgNHINIVNLLGACTvggpt 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  768 -------------------------SIDFQGNE---FRALIYEFMP-----NGSLDMWLHPEEVEEIHRPSR-------- 806
Cdd:cd05104  115 lviteyccygdllnflrrkrdsficPKFEDLAEaalYRNLLHQREMacdslNEYMDMKPSVSYVVPTKADKRrgvrsgsy 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  807 -----TLTLLERLNIAIDVASVLDY-------LHVHCHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARlllkfDEESFFN 874
Cdd:cd05104  195 vdqdvTSEILEEDELALDTEDLLSFsyqvakgMEFLASKNCIHRDLAARNILLTHGRITKICDFGLAR-----DIRNDSN 269
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 18408454  875 QLSSAGVRGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFT-GKRP 920
Cdd:cd05104  270 YVVKGNARLPVKWMAPESIFECVYTFESDVWSYGILLWEIFSlGSSP 316
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
724-918 2.38e-04

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: 44.11  E-value: 2.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  724 EKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKlltacssidFQGN-EFRALIY---EFMPNGSLDMWLHpeevE 799
Cdd:cd14044   30 DKKVVILKDLKNNEGNFTEKQKIELNKLLQIDYYNLTK---------FYGTvKLDTMIFgviEYCERGSLRDVLN----D 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  800 EIHRPSRTLTLLE-RLNIAIDVASVLDYLHVHCHEpiAHCDLKPSNVLLDDDLTAHVSDFGLARLLLKFDEEsffnqlss 878
Cdd:cd14044   97 KISYPDGTFMDWEfKISVMYDIAKGMSYLHSSKTE--VHGRLKSTNCVVDSRMVVKITDFGCNSILPPSKDL-------- 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 18408454  879 agvrgtigYAAPEYGVGGQPSINGDVYSFGILLLEMFTGK 918
Cdd:cd14044  167 --------WTAPEHLRQAGTSQKGDVYSYGIIAQEIILRK 198
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
327-500 2.89e-04

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 44.40  E-value: 2.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  327 EFLTSLTNCTQLETLGIGRNRLGGDLPISIANLsaklvtldlggtlisgsipydIGNLINLQKLILDQNMLSGPLPTSLG 406
Cdd:COG5238  255 ALAEALKNNTTVETLYLSGNQIGAEGAIALAKA---------------------LQGNTTLTSLDLSVNRIGDEGAIALA 313
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  407 KLL----NLRYLSLFSNRLSG----GIPAFIGNMTMLETLDLSNN-----GFEGIVpTSLGNCSHLLELWIGDNKLN--G 471
Cdd:COG5238  314 EGLqgnkTLHTLNLAYNGIGAqgaiALAKALQENTTLHSLDLSDNqigdeGAIALA-KYLEGNTTLRELNLGKNNIGkqG 392
                        170       180       190
                 ....*....|....*....|....*....|
gi 18408454  472 TIPL-EIMKIQQLLRLDMSGNsLIGSLPQD 500
Cdd:COG5238  393 AEALiDALQTNRLHTLILDGN-LIGAEAQQ 421
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
143-373 3.97e-04

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 43.88  E-value: 3.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  143 LRLDSNRLGGS----VPSELGSLTNLVQLNLYGNNMRGK------LPTSLGNLTLLEQLALSHNNLEGEIPSDVAQLTQI 212
Cdd:cd00116   28 LRLEGNTLGEEaakaLASALRPQPSLKELCLSLNETGRIprglqsLLQGLTKGCGLQELDLSDNALGPDGCGVLESLLRS 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  213 WSLQLVANNFSGVFPPAlynlssLKLLGIGynhfsgrlrpdLGILLPNLLSFNMGGNYFTG----SIPTTLSNISTLERL 288
Cdd:cd00116  108 SSLQELKLNNNGLGDRG------LRLLAKG-----------LKDLPPALEKLVLGRNRLEGasceALAKALRANRDLKEL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  289 GMNENNLTGS-IPT----FGNVPNLKLLFLHTNSLGSDSSRDLEfLTSLTNCtQLETLGIGRNRLgGDLPIS-----IAN 358
Cdd:cd00116  171 NLANNGIGDAgIRAlaegLKANCNLEVLDLNNNGLTDEGASALA-ETLASLK-SLEVLNLGDNNL-TDAGAAalasaLLS 247
                        250
                 ....*....|....*
gi 18408454  359 LSAKLVTLDLGGTLI 373
Cdd:cd00116  248 PNISLLTLSLSCNDI 262
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
707-920 4.58e-04

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: 43.56  E-value: 4.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGTVYKALLLTEKKVVAVKVLNmqrrgamKSFMAECESLKDIR-----------HRNLVKLlTACssidFQGNE 775
Cdd:cd05588    2 VIGRGSYAKVLMVELKKTKRIYAMKVIK-------KELVNDDEDIDWVQtekhvfetasnHPFLVGL-HSC----FQTES 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  776 FRALIYEFMPNGslDMWLH-------PEEVEEIHrpsrtltllerlniAIDVASVLDYLHvhcHEPIAHCDLKPSNVLLD 848
Cdd:cd05588   70 RLFFVIEFVNGG--DLMFHmqrqrrlPEEHARFY--------------SAEISLALNFLH---EKGIIYRDLKLDNVLLD 130
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18408454  849 DDLTAHVSDFGLARLLLK-FDEESFFNqlssagvrGTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd05588  131 SEGHIKLTDYGMCKEGLRpGDTTSTFC--------GTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSP 195
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
756-920 5.60e-04

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 42.92  E-value: 5.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   756 HRNLVKLLTACSSIDFQgnefrALIYEFMPNGslDMWlhpeeveEIHRPSRTLTLLERLNIAIDVASVLDYLHVHchePI 835
Cdd:PHA03390   68 NPNFIKLYYSVTTLKGH-----VLIMDYIKDG--DLF-------DLLKKEGKLSEAEVKKIIRQLVEALNDLHKH---NI 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   836 AHCDLKPSNVLLDDDLT-AHVSDFGLARLLlkfDEESFFnqlssagvRGTIGYAAPEygvggqpSINGDVY--SF----- 907
Cdd:PHA03390  131 IHNDIKLENVLYDRAKDrIYLCDYGLCKII---GTPSCY--------DGTLDYFSPE-------KIKGHNYdvSFdwwav 192
                         170
                  ....*....|...
gi 18408454   908 GILLLEMFTGKRP 920
Cdd:PHA03390  193 GVLTYELLTGKHP 205
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
707-920 5.99e-04

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: 42.65  E-value: 5.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  707 MVGSGSFGtvyKALL----LTEKKVVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYE 782
Cdd:cd08219    7 VVGEGSFG---RALLvqhvNSDQKYAMKEIRLPKSSSAVEDSRKEAVLLAKMKHPNIVAFKES-----FEADGHLYIVME 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  783 FMPNGSLdmwlhpeeVEEIhRPSRTLTLLERLNIAIDVASVLDYLHVHcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLAR 862
Cdd:cd08219   79 YCDGGDL--------MQKI-KLQRGKLFPEDTILQWFVQMCLGVQHIH-EKRVLHRDIKSKNIFLTQNGKVKLGDFGSAR 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454  863 LLLkfdeesffNQLSSAGVR-GTIGYAAPEYGVGGQPSINGDVYSFGILLLEMFTGKRP 920
Cdd:cd08219  149 LLT--------SPGAYACTYvGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHP 199
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
695-917 6.25e-04

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


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 43.15  E-value: 6.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  695 LRNATNGFSSSNMVGSGSFGTVYKALLLTEKKVVAVKVL----NMQRRGAMKSFMAECESLKDIRHRNLVKlltacSSID 770
Cdd:cd14228   10 LCSMTNSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILknhpSYARQGQIEVSILSRLSSENADEYNFVR-----SYEC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  771 FQGNEFRALIYEFMPNGSLDMW----LHPEEVEEIhRPsrtltLLERLNIAIDVASVLDYLHVhchepiahcDLKPSNVL 846
Cdd:cd14228   85 FQHKNHTCLVFEMLEQNLYDFLkqnkFSPLPLKYI-RP-----ILQQVATALMKLKSLGLIHA---------DLKPENIM 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18408454  847 LDDDL----TAHVSDFGLARLLLKFDEESFFNQLSsagvrgtigYAAPEYGVGGQPSINGDVYSFGILLLEMFTG 917
Cdd:cd14228  150 LVDPVrqpyRVKVIDFGSASHVSKAVCSTYLQSRY---------YRAPEIILGLPFCEAIDMWSLGCVIAELFLG 215
LRR_8 pfam13855
Leucine rich repeat;
138-198 7.08e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 38.66  E-value: 7.08e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18408454    138 SRLLNLRLDSNRLGGSVPSELGSLTNLVQLNLYGNNMRGKLPTSLGNLTLLEQLALSHNNL 198
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
666-920 7.67e-04

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 43.05  E-value: 7.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   666 LRKRKKNKETNNPTPSTlevlheKISYGDlrnatngFSSSNMVGSGSFGTVYKALLLTEK-KVVAVKVL---NMQRRGAM 741
Cdd:PTZ00426    9 LHKKKDSDSTKEPKRKN------KMKYED-------FNFIRTLGTGSFGRVILATYKNEDfPPVAIKRFeksKIIKQKQV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   742 KSFMAECESLKDIRHRNLVKLLTAcssidFQGNEFRALIYEFMPNGSLDMWLH-----PEEVEEIHrpsrtltllerlni 816
Cdd:PTZ00426   76 DHVFSERKILNYINHPFCVNLYGS-----FKDESYLYLVLEFVIGGEFFTFLRrnkrfPNDVGCFY-------------- 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454   817 AIDVASVLDYLHvhcHEPIAHCDLKPSNVLLDDDLTAHVSDFGLARLLlkfdeesffnQLSSAGVRGTIGYAAPEYGVGG 896
Cdd:PTZ00426  137 AAQIVLIFEYLQ---SLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVV----------DTRTYTLCGTPEYIAPEILLNV 203
                         250       260
                  ....*....|....*....|....
gi 18408454   897 QPSINGDVYSFGILLLEMFTGKRP 920
Cdd:PTZ00426  204 GHGKAADWWTLGIFIYEILVGCPP 227
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
824-926 8.40e-04

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


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 42.39  E-value: 8.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  824 LDYLHVHchePIAHCDLKPSNVLLDDdlTAHV--SDFGLARLLL----------KFDEESffNQLSSAGVRGTIGYAAPE 891
Cdd:cd05609  113 LEYLHSY---GIVHRDLKPDNLLITS--MGHIklTDFGLSKIGLmslttnlyegHIEKDT--REFLDKQVCGTPEYIAPE 185
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 18408454  892 ------YgvgGQPSingDVYSFGILLLEMFTGKRP-----TNELFG 926
Cdd:cd05609  186 vilrqgY---GKPV---DWWAMGIILYEFLVGCVPffgdtPEELFG 225
LRR_8 pfam13855
Leucine rich repeat;
532-588 2.75e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.12  E-value: 2.75e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 18408454    532 ESLFLEGNLFYGDIPD-LKGLVGVKEVDLSNNDLSGSIPEYFASFSKLEYLNLSFNNL 588
Cdd:pfam13855    4 RSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
435-493 5.38e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 36.35  E-value: 5.38e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 18408454    435 LETLDLSNNGFEGIVPTSLGNCSHLLELWIGDNKLNGTIPLEIMKIQQLLRLDMSGNSL 493
Cdd:pfam13855    3 LRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
249-493 7.62e-03

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 39.65  E-value: 7.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  249 RLRPDLGILLPNLLSFNMGGN-YFTGSIPTTLSNISTLERLGMNENNLT----GSIPTFGNVPNLKLLFLHTNSLGSDSS 323
Cdd:cd00116   46 ALRPQPSLKELCLSLNETGRIpRGLQSLLQGLTKGCGLQELDLSDNALGpdgcGVLESLLRSSSLQELKLNNNGLGDRGL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  324 RDLEflTSLTNCT-QLETLGIGRNRLGGDLpisianlsaklvTLDLGGTLISGSipydignliNLQKLILDQNMLSGPLP 402
Cdd:cd00116  126 RLLA--KGLKDLPpALEKLVLGRNRLEGAS------------CEALAKALRANR---------DLKELNLANNGIGDAGI 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18408454  403 TSLGKLL----NLRYLSLFSN--------RLSGGIPAFIGnmtmLETLDLSNN-----GFEGIVPTSLGNCSHLLELWIG 465
Cdd:cd00116  183 RALAEGLkancNLEVLDLNNNgltdegasALAETLASLKS----LEVLNLGDNnltdaGAAALASALLSPNISLLTLSLS 258
                        250       260       270
                 ....*....|....*....|....*....|..
gi 18408454  466 DNKL--NGTIPL-EIMK-IQQLLRLDMSGNSL 493
Cdd:cd00116  259 CNDItdDGAKDLaEVLAeKESLLELDLRGNKF 290
 
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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