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Conserved domains on  [gi|161076872|ref|NP_001097148|]
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guanylyl cyclase at 32E, isoform B [Drosophila melanogaster]

Protein Classification

receptor-type guanylate cyclase( domain architecture ID 11570892)

receptor-type guanylate cyclase catalyzes the conversion of guanosine triphosphate (GTP) to 3',5'-cyclic guanosine monophosphate (cGMP) and pyrophosphate

Gene Ontology:  GO:0004383|GO:0005525
PubMed:  16815030

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PBP1_SAP_GC-like cd06370
Ligand-binding domain of membrane bound guanylyl cyclases; Ligand-binding domain of membrane ...
44-448 3.43e-163

Ligand-binding domain of membrane bound guanylyl cyclases; Ligand-binding domain of membrane bound guanylyl cyclases (GCs), which are known to be activated by sperm-activating peptides (SAPs), such as speract or resact. These ligand peptides are released by a range of invertebrates to stimulate the metabolism and motility of spermatozoa and are also potent chemoattractants. These GCs contain a single transmembrane segment, an extracellular ligand binding domain, and intracellular protein kinase-like and cyclase catalytic domains. GCs of insect and nematodes, which exhibit high sequence similarity to the speract receptor are also included in this model.


:

Pssm-ID: 380593 [Multi-domain]  Cd Length: 400  Bit Score: 490.22  E-value: 3.43e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   44 INIGFLAEYS-------QMRVTLGGLPLAIEDVNKNPNLLPGKKLAFKPVDIGHKmsayRVKPLRAMTQMREAGVTAFIG 116
Cdd:cd06370     1 ITIGYLTPYSgagsydrQGRVISGAITLAVDDVNNDPNLLPGHTLSFVWNDTRCD----ELLSIRAMTELWKRGVSAFIG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  117 PDESCTTEALLASAWNTPMLSFKCSDPIVSNKSTFHTFARTLAPASKVSKSVISLLNAFHWNKFSIVVSSKPIWgSDVAR 196
Cdd:cd06370    77 PGCTCATEARLAAAFNLPMISYKCADPEVSDKSLYPTFARTIPPDSQISKSVIALLKHFNWNKVSIVYENETKW-SKIAD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  197 AIQELAEARNFTISHFKYISD-YIPTTKTLSQIDKIIEETYATTRIYVFIGEHIAMVDFVRGLQNRRLLESGDYIVVSVD 275
Cdd:cd06370   156 TIKELLELNNIEINHEEYFPDpYPYTTSHGNPFDKIVEETKEKTRIYVFLGDYSLLREFMYYAEDLGLLDNGDYVVIGVE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  276 DEIYDSNRRvNIMERNYLDPYIRKEKSKSLDkiSFRSVIKISMTYPQNPHIRDICSKIKDYARKTPFLVPYHQRVFDNIS 355
Cdd:cd06370   236 LDQYDVDDP-AKYPNFLSGDYTKNDTKEALE--AFRSVLIVTPSPPTNPEYEKFTKKVKEYNKLPPFNFPNPEGIEKTKE 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  356 VPIYGLHLYDSVMIYVRAITEVLRLGGDIYDGNLVMSHIFNRSYHSIQGFDVYIDSNGDAEGNYTVITLQNDvgSGASIG 435
Cdd:cd06370   313 VPIYAAYLYDAVMLYARALNETLAEGGDPRDGTAIISKIRNRTYESIQGFDVYIDENGDAEGNYTLLALKPN--KGTNDG 390
                         410
                  ....*....|...
gi 161076872  436 SlakMSMQPVGFF 448
Cdd:cd06370   391 S---YGLHPVGTF 400
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
550-832 1.39e-143

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: 434.33  E-value: 1.39e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  550 TNKNIFQICRQSILVVGEPNKrsFTNIALFRGNIVAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVI 629
Cdd:cd14042     1 SLSSSSYGSLMTAASFDQSQI--FTKTGYYKGNLVAIKKVNKKRIDLTREVLKELKHMRDLQHDNLTRFIGACVDPPNIC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  630 IFTTYCARGSLEDVLANEDLHLDHMFISSLVSDILKGMIYLHDSEIISHGNLRSSNCLIDSRWVCQISDFGLHELKAGQE 709
Cdd:cd14042    79 ILTEYCPKGSLQDILENEDIKLDWMFRYSLIHDIVKGMHYLHDSEIKSHGNLKSSNCVVDSRFVLKITDFGLHSFRSGQE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  710 EPNKSELELKRALCMAPELLRDAYRPGRGSQKGDVYSFGILLYEMIGRKGPWG--DTAYSKEEIIqfVKCPEMLQHGVFR 787
Cdd:cd14042   159 PPDDSHAYYAKLLWTAPELLRDPNPPPPGTQKGDVYSFGIILQEIATRQGPFYeeGPDLSPKEII--KKKVRNGEKPPFR 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 161076872  788 PALTHTHldIPDYIRKCLCQCWDEDPEVRPDIRLVRMHLKELQAG 832
Cdd:cd14042   237 PSLDELE--CPDEVLSLMQRCWAEDPEERPDFSTLRNKLKKLNKG 279
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
865-1057 7.92e-93

Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl cyclases. Eubacterial homologues are known. Two residues (Asn, Arg) are thought to be involved in catalysis. These cyclases have important roles in a diverse range of cellular processes.


:

Pssm-ID: 214485  Cd Length: 194  Bit Score: 295.71  E-value: 7.92e-93
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872    865 EEKKKTDMLLYQMLPRPVAELLKRG-DPVEAECFDCVTILFSDIVGFTELCTTSTPFEVVEMLNDWYTCCDSIISNYDVY 943
Cdd:smart00044    1 EEKKKTDRLLDQLLPASVAEQLKRGgSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQIIDRHGGY 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872    944 KVETIGDAYMVVSGLPLQNGSRHAGEIASLALHLLETVGNLKIRHKPTEtVQLRIGVHSGPCAAGVVGQKMPRYCLFGDT 1023
Cdd:smart00044   81 KVKTIGDAYMVASGLPEEALVDHAELIADEALDMVEELKTVLVQHREEG-LRVRIGIHTGPVVAGVVGIRMPRYCLFGDT 159
                           170       180       190
                    ....*....|....*....|....*....|....*
gi 161076872   1024 VNTASRMESTGDSMRIHISEATYQLLQ-VIGSYVC 1057
Cdd:smart00044  160 VNLASRMESAGDPGQIQVSEETYSLLArRGGQFVF 194
 
Name Accession Description Interval E-value
PBP1_SAP_GC-like cd06370
Ligand-binding domain of membrane bound guanylyl cyclases; Ligand-binding domain of membrane ...
44-448 3.43e-163

Ligand-binding domain of membrane bound guanylyl cyclases; Ligand-binding domain of membrane bound guanylyl cyclases (GCs), which are known to be activated by sperm-activating peptides (SAPs), such as speract or resact. These ligand peptides are released by a range of invertebrates to stimulate the metabolism and motility of spermatozoa and are also potent chemoattractants. These GCs contain a single transmembrane segment, an extracellular ligand binding domain, and intracellular protein kinase-like and cyclase catalytic domains. GCs of insect and nematodes, which exhibit high sequence similarity to the speract receptor are also included in this model.


Pssm-ID: 380593 [Multi-domain]  Cd Length: 400  Bit Score: 490.22  E-value: 3.43e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   44 INIGFLAEYS-------QMRVTLGGLPLAIEDVNKNPNLLPGKKLAFKPVDIGHKmsayRVKPLRAMTQMREAGVTAFIG 116
Cdd:cd06370     1 ITIGYLTPYSgagsydrQGRVISGAITLAVDDVNNDPNLLPGHTLSFVWNDTRCD----ELLSIRAMTELWKRGVSAFIG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  117 PDESCTTEALLASAWNTPMLSFKCSDPIVSNKSTFHTFARTLAPASKVSKSVISLLNAFHWNKFSIVVSSKPIWgSDVAR 196
Cdd:cd06370    77 PGCTCATEARLAAAFNLPMISYKCADPEVSDKSLYPTFARTIPPDSQISKSVIALLKHFNWNKVSIVYENETKW-SKIAD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  197 AIQELAEARNFTISHFKYISD-YIPTTKTLSQIDKIIEETYATTRIYVFIGEHIAMVDFVRGLQNRRLLESGDYIVVSVD 275
Cdd:cd06370   156 TIKELLELNNIEINHEEYFPDpYPYTTSHGNPFDKIVEETKEKTRIYVFLGDYSLLREFMYYAEDLGLLDNGDYVVIGVE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  276 DEIYDSNRRvNIMERNYLDPYIRKEKSKSLDkiSFRSVIKISMTYPQNPHIRDICSKIKDYARKTPFLVPYHQRVFDNIS 355
Cdd:cd06370   236 LDQYDVDDP-AKYPNFLSGDYTKNDTKEALE--AFRSVLIVTPSPPTNPEYEKFTKKVKEYNKLPPFNFPNPEGIEKTKE 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  356 VPIYGLHLYDSVMIYVRAITEVLRLGGDIYDGNLVMSHIFNRSYHSIQGFDVYIDSNGDAEGNYTVITLQNDvgSGASIG 435
Cdd:cd06370   313 VPIYAAYLYDAVMLYARALNETLAEGGDPRDGTAIISKIRNRTYESIQGFDVYIDENGDAEGNYTLLALKPN--KGTNDG 390
                         410
                  ....*....|...
gi 161076872  436 SlakMSMQPVGFF 448
Cdd:cd06370   391 S---YGLHPVGTF 400
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
550-832 1.39e-143

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: 434.33  E-value: 1.39e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  550 TNKNIFQICRQSILVVGEPNKrsFTNIALFRGNIVAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVI 629
Cdd:cd14042     1 SLSSSSYGSLMTAASFDQSQI--FTKTGYYKGNLVAIKKVNKKRIDLTREVLKELKHMRDLQHDNLTRFIGACVDPPNIC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  630 IFTTYCARGSLEDVLANEDLHLDHMFISSLVSDILKGMIYLHDSEIISHGNLRSSNCLIDSRWVCQISDFGLHELKAGQE 709
Cdd:cd14042    79 ILTEYCPKGSLQDILENEDIKLDWMFRYSLIHDIVKGMHYLHDSEIKSHGNLKSSNCVVDSRFVLKITDFGLHSFRSGQE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  710 EPNKSELELKRALCMAPELLRDAYRPGRGSQKGDVYSFGILLYEMIGRKGPWG--DTAYSKEEIIqfVKCPEMLQHGVFR 787
Cdd:cd14042   159 PPDDSHAYYAKLLWTAPELLRDPNPPPPGTQKGDVYSFGIILQEIATRQGPFYeeGPDLSPKEII--KKKVRNGEKPPFR 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 161076872  788 PALTHTHldIPDYIRKCLCQCWDEDPEVRPDIRLVRMHLKELQAG 832
Cdd:cd14042   237 PSLDELE--CPDEVLSLMQRCWAEDPEERPDFSTLRNKLKKLNKG 279
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
865-1057 7.92e-93

Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl cyclases. Eubacterial homologues are known. Two residues (Asn, Arg) are thought to be involved in catalysis. These cyclases have important roles in a diverse range of cellular processes.


Pssm-ID: 214485  Cd Length: 194  Bit Score: 295.71  E-value: 7.92e-93
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872    865 EEKKKTDMLLYQMLPRPVAELLKRG-DPVEAECFDCVTILFSDIVGFTELCTTSTPFEVVEMLNDWYTCCDSIISNYDVY 943
Cdd:smart00044    1 EEKKKTDRLLDQLLPASVAEQLKRGgSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQIIDRHGGY 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872    944 KVETIGDAYMVVSGLPLQNGSRHAGEIASLALHLLETVGNLKIRHKPTEtVQLRIGVHSGPCAAGVVGQKMPRYCLFGDT 1023
Cdd:smart00044   81 KVKTIGDAYMVASGLPEEALVDHAELIADEALDMVEELKTVLVQHREEG-LRVRIGIHTGPVVAGVVGIRMPRYCLFGDT 159
                           170       180       190
                    ....*....|....*....|....*....|....*
gi 161076872   1024 VNTASRMESTGDSMRIHISEATYQLLQ-VIGSYVC 1057
Cdd:smart00044  160 VNLASRMESAGDPGQIQVSEETYSLLArRGGQFVF 194
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
892-1076 1.36e-77

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 253.32  E-value: 1.36e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   892 VEAECFDCVTILFSDIVGFTELCTTSTPFEVVEMLNDWYTCCDSIISNYDVYKVETIGDAYMVVSGLPlQNGSRHAGEIA 971
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLP-EPSPAHARKIA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   972 SLALHLLETVGNLKIRHKptETVQLRIGVHSGPCAAGVVGQKMPRYCLFGDTVNTASRMESTGDSMRIHISEATYQLLQV 1051
Cdd:pfam00211   80 EMALDMLEAIGEVNVESS--EGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKT 157
                          170       180
                   ....*....|....*....|....*
gi 161076872  1052 iGSYVCIERGLTSIKGKGDMRTYWL 1076
Cdd:pfam00211  158 -EGFEFTERGEIEVKGKGKMKTYFL 181
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
900-1076 1.54e-66

cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.


Pssm-ID: 143636 [Multi-domain]  Cd Length: 177  Bit Score: 222.07  E-value: 1.54e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  900 VTILFSDIVGFTELCTTSTPFEVVEMLNDWYTCCDSIISNYDVYKVETIGDAYMVVSGLPLQNGsRHAGEIASLALHLLE 979
Cdd:cd07302     2 VTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHE-DHAERAVRAALEMQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  980 TVGNLKIRHKPTETVQLRIGVHSGPCAAGVVGQKMPRYCLFGDTVNTASRMESTGDSMRIHISEATYQLLQVIGsYVCIE 1059
Cdd:cd07302    81 ALAELNAEREGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGDAG-FEFEE 159
                         170
                  ....*....|....*...
gi 161076872 1060 RGLTSIKGK-GDMRTYWL 1076
Cdd:cd07302   160 LGEVELKGKsGPVRVYRL 177
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
852-1083 8.41e-48

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 176.53  E-value: 8.41e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  852 LEGLVQERTNLLYEEKKKTDMLLYQMLPRPVAELLK------RGDPVEAEcfdcVTILFSDIVGFTELCTTSTPFEVVEM 925
Cdd:COG2114   173 LLLALLLLLLLALRERERLRDLLGRYLPPEVAERLLaggeelRLGGERRE----VTVLFADIVGFTALSERLGPEELVEL 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  926 LNDWYTCCDSIISNYDVYKVETIGDAYMVVSGLPLQNGSrHAGEIASLALHLLETVG--NLKIRHKPTETVQLRIGVHSG 1003
Cdd:COG2114   249 LNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVARED-HAERAVRAALAMQEALAelNAELPAEGGPPLRVRIGIHTG 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872 1004 PCAAGVVG-QKMPRYCLFGDTVNTASRMESTGDSMRIHISEATYQLLQviGSYVCIERGLTSIKGKGD-MRTYWLTKRQQ 1081
Cdd:COG2114   328 EVVVGNIGsEDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLR--DRFEFRELGEVRLKGKAEpVEVYELLGAKE 405

                  ..
gi 161076872 1082 PE 1083
Cdd:COG2114   406 AA 407
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
584-817 7.01e-38

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


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 143.07  E-value: 7.01e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872    584 VAMKKIHKKSVDITRS-IRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVL---ANEDLHLDHMFisSL 659
Cdd:smart00221   31 VAVKTLKEDASEQQIEeFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVMEYMPGGDLLDYLrknRPKELSLSDLL--SF 108
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872    660 VSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHElkagqeepNKSELELKRALC-------MAPELLRDa 732
Cdd:smart00221  109 ALQIARGMEYLESKNFI-HRDLAARNCLVGENLVVKISDFGLSR--------DLYDDDYYKVKGgklpirwMAPESLKE- 178
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872    733 yrpGRGSQKGDVYSFGILLYEMI--GRKGPWGDTAyskEEIIQFVKCPEMLQhgvfRPAlththlDIPDYIRKCLCQCWD 810
Cdd:smart00221  179 ---GKFTSKSDVWSFGVLLWEIFtlGEEPYPGMSN---AEVLEYLKKGYRLP----KPP------NCPPELYKLMLQCWA 242

                    ....*..
gi 161076872    811 EDPEVRP 817
Cdd:smart00221  243 EDPEDRP 249
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
584-826 9.33e-38

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: 142.64  E-value: 9.33e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   584 VAMKKIHKKSVDITR-SIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSD 662
Cdd:pfam07714   31 VAVKTLKEGADEEEReDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTEYMPGGDLLDFLRKHKRKLTLKDLLSMALQ 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   663 ILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSElELKRALC-MAPELLRDayrpGRGSQK 741
Cdd:pfam07714  111 IAKGMEYLESKNFV-HRDLAARNCLVSENLVVKISDFGLSRDIYDDDYYRKRG-GGKLPIKwMAPESLKD----GKFTSK 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   742 GDVYSFGILLYEMI--GRKgPWGDtaYSKEEIIQFVK------CPEmlqhgvfrpalththlDIPDYIRKCLCQCWDEDP 813
Cdd:pfam07714  185 SDVWSFGVLLWEIFtlGEQ-PYPG--MSNEEVLEFLEdgyrlpQPE----------------NCPDELYDLMKQCWAYDP 245
                          250
                   ....*....|...
gi 161076872   814 EVRPDIRLVRMHL 826
Cdd:pfam07714  246 EDRPTFSELVEDL 258
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
59-427 1.51e-32

Receptor family ligand binding region; This family includes extracellular ligand binding domains of a wide range of receptors. This family also includes the bacterial amino acid binding proteins of known structure.


Pssm-ID: 460062 [Multi-domain]  Cd Length: 347  Bit Score: 130.20  E-value: 1.51e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872    59 LGGLPLAIEDVNKNPNLLPGKKLAFKPVDighkmSAYR-VKPLRAMTQMREAGVTAFIGPDES--CTTEALLASAWNTPM 135
Cdd:pfam01094    3 LLAVRLAVEDINADPGLLPGTKLEYIILD-----TCCDpSLALAAALDLLKGEVVAIIGPSCSsvASAVASLANEWKVPL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   136 LSFKCSDPIVSNKSTFHTFARTLAPASKVSKSVISLLNAFHWNKFSiVVSSKPIWGSDVARAIQELAEARNFTISHfkyi 215
Cdd:pfam01094   78 ISYGSTSPALSDLNRYPTFLRTTPSDTSQADAIVDILKHFGWKRVA-LIYSDDDYGESGLQALEDALRERGIRVAY---- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   216 SDYIPTTKTLSQI-DKIIEETYATTRIYVFIGEHIAMvdfvrglqnRRLLESGdyivvsvddeiydsnRRVNIMERNYLd 294
Cdd:pfam01094  153 KAVIPPAQDDDEIaRKLLKEVKSRARVIVVCCSSETA---------RRLLKAA---------------RELGMMGEGYV- 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   295 pYIRKE-KSKSLDKIS------FRSVIKISMTYPQNPhirdicsKIKDYARKTPFLVPYHQRvFDNISVPIYGLHLYDSV 367
Cdd:pfam01094  208 -WIATDgLTTSLVILNpstleaAGGVLGFRLHPPDSP-------EFSEFFWEKLSDEKELYE-NLGGLPVSYGALAYDAV 278
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   368 MIYVRAITEVLRLG---------GDIYDGNLVMSHIFNRSYHSIQGfDVYIDSNGD-AEGNYTVITLQND 427
Cdd:pfam01094  279 YLLAHALHNLLRDDkpgracgalGPWNGGQKLLRYLKNVNFTGLTG-NVQFDENGDrINPDYDILNLNGS 347
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
584-833 1.31e-15

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 81.21  E-value: 1.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHK---KSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDlHLDHMFISSLV 660
Cdd:COG0515    35 VALKVLRPelaADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEGESLADLLRRRG-PLPPAEALRIL 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRAlCMAPELLRDAyRPGRGSq 740
Cdd:COG0515   114 AQLAEALAAAHAAGIV-HRDIKPANILLTPDGRVKLIDFGIARALGGATLTQTGTVVGTPG-YMAPEQARGE-PVDPRS- 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  741 kgDVYSFGILLYEMI-GRKGPWGDTAYskeeiiqfvkcpEMLQHGVFR--PALTHTHLDIPDY----IRKCLcqcwDEDP 813
Cdd:COG0515   190 --DVYSLGVTLYELLtGRPPFDGDSPA------------ELLRAHLREppPPPSELRPDLPPAldaiVLRAL----AKDP 251
                         250       260
                  ....*....|....*....|.
gi 161076872  814 EVRP-DIRLVRMHLKELQAGL 833
Cdd:COG0515   252 EERYqSAAELAAALRAVLRSL 272
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
581-761 3.37e-13

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 72.55  E-value: 3.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKI---HKKSVdiTRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANedlhlDHMFIS 657
Cdd:PLN00034   99 GRLYALKVIygnHEDTV--RRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLEGTHIA-----DEQFLA 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  658 SLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSelELKRALCMAPELLRDAYRPGR 737
Cdd:PLN00034  172 DVARQILSGIAYLHRRHIV-HRDIKPSNLLINSAKNVKIADFGVSRILAQTMDPCNS--SVGTIAYMSPERINTDLNHGA 248
                         170       180       190
                  ....*....|....*....|....*....|...
gi 161076872  738 -GSQKGDVYSFGILLYEM--------IGRKGPW 761
Cdd:PLN00034  249 yDGYAGDIWSLGVSILEFylgrfpfgVGRQGDW 281
 
Name Accession Description Interval E-value
PBP1_SAP_GC-like cd06370
Ligand-binding domain of membrane bound guanylyl cyclases; Ligand-binding domain of membrane ...
44-448 3.43e-163

Ligand-binding domain of membrane bound guanylyl cyclases; Ligand-binding domain of membrane bound guanylyl cyclases (GCs), which are known to be activated by sperm-activating peptides (SAPs), such as speract or resact. These ligand peptides are released by a range of invertebrates to stimulate the metabolism and motility of spermatozoa and are also potent chemoattractants. These GCs contain a single transmembrane segment, an extracellular ligand binding domain, and intracellular protein kinase-like and cyclase catalytic domains. GCs of insect and nematodes, which exhibit high sequence similarity to the speract receptor are also included in this model.


Pssm-ID: 380593 [Multi-domain]  Cd Length: 400  Bit Score: 490.22  E-value: 3.43e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   44 INIGFLAEYS-------QMRVTLGGLPLAIEDVNKNPNLLPGKKLAFKPVDIGHKmsayRVKPLRAMTQMREAGVTAFIG 116
Cdd:cd06370     1 ITIGYLTPYSgagsydrQGRVISGAITLAVDDVNNDPNLLPGHTLSFVWNDTRCD----ELLSIRAMTELWKRGVSAFIG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  117 PDESCTTEALLASAWNTPMLSFKCSDPIVSNKSTFHTFARTLAPASKVSKSVISLLNAFHWNKFSIVVSSKPIWgSDVAR 196
Cdd:cd06370    77 PGCTCATEARLAAAFNLPMISYKCADPEVSDKSLYPTFARTIPPDSQISKSVIALLKHFNWNKVSIVYENETKW-SKIAD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  197 AIQELAEARNFTISHFKYISD-YIPTTKTLSQIDKIIEETYATTRIYVFIGEHIAMVDFVRGLQNRRLLESGDYIVVSVD 275
Cdd:cd06370   156 TIKELLELNNIEINHEEYFPDpYPYTTSHGNPFDKIVEETKEKTRIYVFLGDYSLLREFMYYAEDLGLLDNGDYVVIGVE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  276 DEIYDSNRRvNIMERNYLDPYIRKEKSKSLDkiSFRSVIKISMTYPQNPHIRDICSKIKDYARKTPFLVPYHQRVFDNIS 355
Cdd:cd06370   236 LDQYDVDDP-AKYPNFLSGDYTKNDTKEALE--AFRSVLIVTPSPPTNPEYEKFTKKVKEYNKLPPFNFPNPEGIEKTKE 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  356 VPIYGLHLYDSVMIYVRAITEVLRLGGDIYDGNLVMSHIFNRSYHSIQGFDVYIDSNGDAEGNYTVITLQNDvgSGASIG 435
Cdd:cd06370   313 VPIYAAYLYDAVMLYARALNETLAEGGDPRDGTAIISKIRNRTYESIQGFDVYIDENGDAEGNYTLLALKPN--KGTNDG 390
                         410
                  ....*....|...
gi 161076872  436 SlakMSMQPVGFF 448
Cdd:cd06370   391 S---YGLHPVGTF 400
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
550-832 1.39e-143

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: 434.33  E-value: 1.39e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  550 TNKNIFQICRQSILVVGEPNKrsFTNIALFRGNIVAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVI 629
Cdd:cd14042     1 SLSSSSYGSLMTAASFDQSQI--FTKTGYYKGNLVAIKKVNKKRIDLTREVLKELKHMRDLQHDNLTRFIGACVDPPNIC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  630 IFTTYCARGSLEDVLANEDLHLDHMFISSLVSDILKGMIYLHDSEIISHGNLRSSNCLIDSRWVCQISDFGLHELKAGQE 709
Cdd:cd14042    79 ILTEYCPKGSLQDILENEDIKLDWMFRYSLIHDIVKGMHYLHDSEIKSHGNLKSSNCVVDSRFVLKITDFGLHSFRSGQE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  710 EPNKSELELKRALCMAPELLRDAYRPGRGSQKGDVYSFGILLYEMIGRKGPWG--DTAYSKEEIIqfVKCPEMLQHGVFR 787
Cdd:cd14042   159 PPDDSHAYYAKLLWTAPELLRDPNPPPPGTQKGDVYSFGIILQEIATRQGPFYeeGPDLSPKEII--KKKVRNGEKPPFR 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 161076872  788 PALTHTHldIPDYIRKCLCQCWDEDPEVRPDIRLVRMHLKELQAG 832
Cdd:cd14042   237 PSLDELE--CPDEVLSLMQRCWAEDPEERPDFSTLRNKLKKLNKG 279
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
865-1057 7.92e-93

Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl cyclases. Eubacterial homologues are known. Two residues (Asn, Arg) are thought to be involved in catalysis. These cyclases have important roles in a diverse range of cellular processes.


Pssm-ID: 214485  Cd Length: 194  Bit Score: 295.71  E-value: 7.92e-93
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872    865 EEKKKTDMLLYQMLPRPVAELLKRG-DPVEAECFDCVTILFSDIVGFTELCTTSTPFEVVEMLNDWYTCCDSIISNYDVY 943
Cdd:smart00044    1 EEKKKTDRLLDQLLPASVAEQLKRGgSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQIIDRHGGY 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872    944 KVETIGDAYMVVSGLPLQNGSRHAGEIASLALHLLETVGNLKIRHKPTEtVQLRIGVHSGPCAAGVVGQKMPRYCLFGDT 1023
Cdd:smart00044   81 KVKTIGDAYMVASGLPEEALVDHAELIADEALDMVEELKTVLVQHREEG-LRVRIGIHTGPVVAGVVGIRMPRYCLFGDT 159
                           170       180       190
                    ....*....|....*....|....*....|....*
gi 161076872   1024 VNTASRMESTGDSMRIHISEATYQLLQ-VIGSYVC 1057
Cdd:smart00044  160 VNLASRMESAGDPGQIQVSEETYSLLArRGGQFVF 194
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
565-829 2.47e-78

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: 258.86  E-value: 2.47e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  565 VGEPNKRSFTNIalFRGNIVAMKKIHKKSVDiTRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVL 644
Cdd:cd13992    11 TGEPKYVKKVGV--YGGRTVAIKHITFSRTE-KRTILQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  645 ANEDLHLDHMFISSLVSDILKGMIYLHDSEIISHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELEL-KRALC 723
Cdd:cd13992    88 LNREIKMDWMFKSSFIKDIVKGMNYLHSSSIGYHGRLKSSNCLVDSRWVVKLTDFGLRNLLEEQTNHQLDEDAQhKKLLW 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  724 MAPELLRDAYRPGRGSQKGDVYSFGILLYEMIGRKGPWGDTAYSKEEIIQFV--KCPemlqhgvFRPALTHTHLDIPDYI 801
Cdd:cd13992   168 TAPELLRGSLLEVRGTQKGDVYSFAIILYEILFRSDPFALEREVAIVEKVISggNKP-------FRPELAVLLDEFPPRL 240
                         250       260
                  ....*....|....*....|....*...
gi 161076872  802 RKCLCQCWDEDPEVRPDIRLVRMHLKEL 829
Cdd:cd13992   241 VLLVKQCWAENPEKRPSFKQIKKTLTEN 268
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
892-1076 1.36e-77

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 253.32  E-value: 1.36e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   892 VEAECFDCVTILFSDIVGFTELCTTSTPFEVVEMLNDWYTCCDSIISNYDVYKVETIGDAYMVVSGLPlQNGSRHAGEIA 971
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLP-EPSPAHARKIA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   972 SLALHLLETVGNLKIRHKptETVQLRIGVHSGPCAAGVVGQKMPRYCLFGDTVNTASRMESTGDSMRIHISEATYQLLQV 1051
Cdd:pfam00211   80 EMALDMLEAIGEVNVESS--EGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKT 157
                          170       180
                   ....*....|....*....|....*
gi 161076872  1052 iGSYVCIERGLTSIKGKGDMRTYWL 1076
Cdd:pfam00211  158 -EGFEFTERGEIEVKGKGKMKTYFL 181
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
900-1076 1.54e-66

cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.


Pssm-ID: 143636 [Multi-domain]  Cd Length: 177  Bit Score: 222.07  E-value: 1.54e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  900 VTILFSDIVGFTELCTTSTPFEVVEMLNDWYTCCDSIISNYDVYKVETIGDAYMVVSGLPLQNGsRHAGEIASLALHLLE 979
Cdd:cd07302     2 VTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHE-DHAERAVRAALEMQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  980 TVGNLKIRHKPTETVQLRIGVHSGPCAAGVVGQKMPRYCLFGDTVNTASRMESTGDSMRIHISEATYQLLQVIGsYVCIE 1059
Cdd:cd07302    81 ALAELNAEREGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGDAG-FEFEE 159
                         170
                  ....*....|....*...
gi 161076872 1060 RGLTSIKGK-GDMRTYWL 1076
Cdd:cd07302   160 LGEVELKGKsGPVRVYRL 177
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
574-819 3.03e-59

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: 204.56  E-value: 3.03e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  574 TNIAlFRGNIVAMKKIH-KKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLD 652
Cdd:cd14043    17 TGVA-YEGDWVWLKKFPgGSHTELRPSTKNVFSKLRELRHENVNLFLGLFVDCGILAIVSEHCSRGSLEDLLRNDDMKLD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  653 HMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHEL----KAGQEEPNKSELelkraLCMAPEL 728
Cdd:cd14043    96 WMFKSSLLLDLIKGMRYLHHRGIV-HGRLKSRNCVVDGRFVLKITDYGYNEIleaqNLPLPEPAPEEL-----LWTAPEL 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  729 LRDAYRPGRGSQKGDVYSFGILLYEMIGRKGPWGDTAYSKEEIIQFVKCPEMLqhgvFRPALThthLDI--PDYIrKCLC 806
Cdd:cd14043   170 LRDPRLERRGTFPGDVFSFAIIMQEVIVRGAPYCMLGLSPEEIIEKVRSPPPL----CRPSVS---MDQapLECI-QLMK 241
                         250
                  ....*....|...
gi 161076872  807 QCWDEDPEVRPDI 819
Cdd:cd14043   242 QCWSEAPERRPTF 254
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
577-818 3.21e-52

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: 183.89  E-value: 3.21e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  577 ALFRGNIVAMKKIHKKSVD--ITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHM 654
Cdd:cd13999    12 GKWRGTDVAIKKLKVEDDNdeLLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLYDLLHKKKIPLSWS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  655 FISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELElkrALC-MAPELLR-DA 732
Cdd:cd13999    92 LRLKIALDIARGMNYLHSPPII-HRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTGVVG---TPRwMAPEVLRgEP 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  733 YrpgrgSQKGDVYSFGILLYEMIGRKGPWGDtaYSKEEIIQFVkcpemlqhgVFRPALTHTHLDIPDYIRKCLCQCWDED 812
Cdd:cd13999   168 Y-----TEKADVYSFGIVLWELLTGEVPFKE--LSPIQIAAAV---------VQKGLRPPIPPDCPPELSKLIKRCWNED 231

                  ....*.
gi 161076872  813 PEVRPD 818
Cdd:cd13999   232 PEKRPS 237
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
852-1083 8.41e-48

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 176.53  E-value: 8.41e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  852 LEGLVQERTNLLYEEKKKTDMLLYQMLPRPVAELLK------RGDPVEAEcfdcVTILFSDIVGFTELCTTSTPFEVVEM 925
Cdd:COG2114   173 LLLALLLLLLLALRERERLRDLLGRYLPPEVAERLLaggeelRLGGERRE----VTVLFADIVGFTALSERLGPEELVEL 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  926 LNDWYTCCDSIISNYDVYKVETIGDAYMVVSGLPLQNGSrHAGEIASLALHLLETVG--NLKIRHKPTETVQLRIGVHSG 1003
Cdd:COG2114   249 LNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVARED-HAERAVRAALAMQEALAelNAELPAEGGPPLRVRIGIHTG 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872 1004 PCAAGVVG-QKMPRYCLFGDTVNTASRMESTGDSMRIHISEATYQLLQviGSYVCIERGLTSIKGKGD-MRTYWLTKRQQ 1081
Cdd:COG2114   328 EVVVGNIGsEDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLR--DRFEFRELGEVRLKGKAEpVEVYELLGAKE 405

                  ..
gi 161076872 1082 PE 1083
Cdd:COG2114   406 AA 407
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
570-826 3.56e-45

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: 164.26  E-value: 3.56e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  570 KRSFTNIALFRGNIVAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDL 649
Cdd:cd14045    19 KKPFTQTGIYDGRTVAIKKIAKKSFTLSKRIRKEVKQVRELDHPNLCKFIGGCIEVPNVAIITEYCPKGSLNDVLLNEDI 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  650 HLDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAgQEEPNKSELELKRAL--CMAPE 727
Cdd:cd14045    99 PLNWGFRFSFATDIARGMAYLHQHKIY-HGRLKSSNCVIDDRWVCKIADYGLTTYRK-EDGSENASGYQQRLMqvYLPPE 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  728 LLRDAYRpgRGSQKGDVYSFGILLYEMIGRKGPWGDTAYSKEEiiqfvkcpemlqhgVFRPALthTHLDIPDYIRKCLC- 806
Cdd:cd14045   177 NHSNTDT--EPTQATDVYSYAIILLEIATRNDPVPEDDYSLDE--------------AWCPPL--PELISGKTENSCPCp 238
                         250       260
                  ....*....|....*....|....*...
gi 161076872  807 --------QCWDEDPEVRPDIRLVRMHL 826
Cdd:cd14045   239 adyvelirRCRKNNPAQRPTFEQIKKTL 266
PBP1_NPR_GC-like cd06352
ligand-binding domain of membrane guanylyl-cyclase receptors; Ligand-binding domain of ...
45-430 7.78e-44

ligand-binding domain of membrane guanylyl-cyclase receptors; Ligand-binding domain of membrane guanylyl-cyclase receptors. Membrane guanylyl cyclases (GC) have a single membrane-spanning region and are activated by endogenous and exogenous peptides. This family can be divided into three major subfamilies: the natriuretic peptide receptors (NPRs), sensory organ-specific membrane GCs, and the enterotoxin/guanylin receptors. The binding of peptide ligands to the receptor results in the activation of the cytosolic catalytic domain. Three types of NPRs have been cloned from mammalian tissues: NPR-A/GC-A, NPR-B/ GC-B, and NPR-C. In addition, two of the GCs, GC-D and GC-G, appear to be pseudogenes in humans. Atrial natriuretic peptide (ANP) and brain natriuretic peptide (BNP) are produced in the heart, and both bind to the NPR-A. NPR-C, also termed the clearance receptor, binds each of the natriuretic peptides and can alter circulating levels of these peptides. The ligand binding domain of the NPRs exhibits strong structural similarity to the type 1 periplasmic binding fold protein family.


Pssm-ID: 380575 [Multi-domain]  Cd Length: 391  Bit Score: 164.45  E-value: 7.78e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   45 NIGFLAEYSQ------MRVTLGGLPLAIEDVNKNPNLLPGKKLAFKPVDIGHKMSAyrvKPLRAMTQMREAGVTAFIGP- 117
Cdd:cd06352     1 KVGVLAPSNSqslpvgYARSAPAIDIAIERINSEGLLLPGFNFEFTYRDSCCDESE---AVGAAADLIYKRNVDVFIGPa 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  118 -DESCTTEALLASAWNTPMLSFKCSDPIVSNKSTFHTFARTLAPASKVSKSVISLLNAFHWNKFSIVVSSK-PIWGSDVA 195
Cdd:cd06352    78 cSAAADAVGRLATYWNIPIITWGAVSASFLDKSRYPTLTRTSPNSLSLAEALLALLKQFNWKRAAIIYSDDdSKCFSIAN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  196 RAIQELAEARNFTISHFKYISdyiptTKTLSQIDKIIEETYATTRIYVFIGEhiamvdfvrGLQNRRLLE--------SG 267
Cdd:cd06352   158 DLEDALNQEDNLTISYYEFVE-----VNSDSDYSSILQEAKKRARIIVLCFD---------SETVRQFMLaahdlgmtNG 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  268 DYIVVSVDDEIYDSnrrvnimERNYLDPYIRKEKSKSLDKISFRSVIKISMTYPQNPHIRDICSKIKDYARKTPFLVPYH 347
Cdd:cd06352   224 EYVFIFIELFKDGF-------GGNSTDGWERNDGRDEDAKQAYESLLVISLSRPSNPEYDNFSKEVKARAKEPPFYCYDA 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  348 qrvfDNISVPIYGLHLYDSVMIYVRAITEVLRLGGDIYDGNLVMSHIFNRSYHSIQGfDVYIDSNGDAEGNYTVITLQND 427
Cdd:cd06352   297 ----SEEEVSPYAAALYDAVYLYALALNETLAEGGNYRNGTAIAQRMWNRTFQGITG-PVTIDSNGDRDPDYALLDLDPS 371

                  ...
gi 161076872  428 VGS 430
Cdd:cd06352   372 TGK 374
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
584-827 1.48e-38

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: 144.99  E-value: 1.48e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDITRS-IRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSL--- 659
Cdd:cd00192    26 VAVKTLKEDASESERKdFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYMEGGDLLDFLRKSRPVFPSPEPSTLslk 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  660 -----VSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL---HELKAGQEEPNKSELELKralCMAPELLRD 731
Cdd:cd00192   106 dllsfAIQIAKGMEYLASKKFV-HRDLAARNCLVGEDLVVKISDFGLsrdIYDDDYYRKKTGGKLPIR---WMAPESLKD 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  732 ayrpGRGSQKGDVYSFGILLYEMI--GRKgPWGDtaYSKEEIIQFVKCPEMLQhgvfRPAlththlDIPDYIRKCLCQCW 809
Cdd:cd00192   182 ----GIFTSKSDVWSFGVLLWEIFtlGAT-PYPG--LSNEEVLEYLRKGYRLP----KPE------NCPDELYELMLSCW 244
                         250
                  ....*....|....*...
gi 161076872  810 DEDPEVRPDIRLVRMHLK 827
Cdd:cd00192   245 QLDPEDRPTFSELVERLE 262
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
584-817 7.01e-38

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


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 143.07  E-value: 7.01e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872    584 VAMKKIHKKSVDITRS-IRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVL---ANEDLHLDHMFisSL 659
Cdd:smart00221   31 VAVKTLKEDASEQQIEeFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVMEYMPGGDLLDYLrknRPKELSLSDLL--SF 108
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872    660 VSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHElkagqeepNKSELELKRALC-------MAPELLRDa 732
Cdd:smart00221  109 ALQIARGMEYLESKNFI-HRDLAARNCLVGENLVVKISDFGLSR--------DLYDDDYYKVKGgklpirwMAPESLKE- 178
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872    733 yrpGRGSQKGDVYSFGILLYEMI--GRKGPWGDTAyskEEIIQFVKCPEMLQhgvfRPAlththlDIPDYIRKCLCQCWD 810
Cdd:smart00221  179 ---GKFTSKSDVWSFGVLLWEIFtlGEEPYPGMSN---AEVLEYLKKGYRLP----KPP------NCPPELYKLMLQCWA 242

                    ....*..
gi 161076872    811 EDPEVRP 817
Cdd:smart00221  243 EDPEDRP 249
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
584-826 9.33e-38

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: 142.64  E-value: 9.33e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   584 VAMKKIHKKSVDITR-SIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSD 662
Cdd:pfam07714   31 VAVKTLKEGADEEEReDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTEYMPGGDLLDFLRKHKRKLTLKDLLSMALQ 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   663 ILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSElELKRALC-MAPELLRDayrpGRGSQK 741
Cdd:pfam07714  111 IAKGMEYLESKNFV-HRDLAARNCLVSENLVVKISDFGLSRDIYDDDYYRKRG-GGKLPIKwMAPESLKD----GKFTSK 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   742 GDVYSFGILLYEMI--GRKgPWGDtaYSKEEIIQFVK------CPEmlqhgvfrpalththlDIPDYIRKCLCQCWDEDP 813
Cdd:pfam07714  185 SDVWSFGVLLWEIFtlGEQ-PYPG--MSNEEVLEFLEdgyrlpQPE----------------NCPDELYDLMKQCWAYDP 245
                          250
                   ....*....|...
gi 161076872   814 EVRPDIRLVRMHL 826
Cdd:pfam07714  246 EDRPTFSELVEDL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
584-817 2.70e-37

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 141.13  E-value: 2.70e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872    584 VAMKKIHKKSVDITRS-IRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSD 662
Cdd:smart00219   31 VAVKTLKEDASEQQIEeFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVMEYMEGGDLLSYLRKNRPKLSLSDLLSFALQ 110
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872    663 ILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHelKAGQEEPNKSELELKRAL-CMAPELLRDayrpGRGSQK 741
Cdd:smart00219  111 IARGMEYLESKNFI-HRDLAARNCLVGENLVVKISDFGLS--RDLYDDDYYRKRGGKLPIrWMAPESLKE----GKFTSK 183
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161076872    742 GDVYSFGILLYEMI--GRKGPWGDTAyskEEIIQFVKCPEMLQhgvfRPAlththlDIPDYIRKCLCQCWDEDPEVRP 817
Cdd:smart00219  184 SDVWSFGVLLWEIFtlGEQPYPGMSN---EEVLEYLKNGYRLP----QPP------NCPPELYDLMLQCWAEDPEDRP 248
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
581-825 4.40e-36

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 137.66  E-value: 4.40e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872    581 GNIVAMKKIHKKSVDITR-SIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDlHLDHMFISSL 659
Cdd:smart00220   24 GKLVAIKVIKKKKIKKDReRILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCEGGDLFDLLKKRG-RLSEDEARFY 102
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872    660 VSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkAGQEEPNkselELKRALC-----MAPELLRdayr 734
Cdd:smart00220  103 LRQILSALEYLHSKGIV-HRDLKPENILLDEDGHVKLADFGL----ARQLDPG----EKLTTFVgtpeyMAPEVLL---- 169
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872    735 pGRG-SQKGDVYSFGILLYEMIGRKGPWgDTAYSKEEIIQFVKCPemlqhgvfRPALTHTHLDIPDYIRKCLCQCWDEDP 813
Cdd:smart00220  170 -GKGyGKAVDIWSLGVILYELLTGKPPF-PGDDQLLELFKKIGKP--------KPPFPPPEWDISPEAKDLIRKLLVKDP 239
                           250
                    ....*....|..
gi 161076872    814 EVRPDIRLVRMH 825
Cdd:smart00220  240 EKRLTAEEALQH 251
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
581-783 2.93e-35

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: 133.94  E-value: 2.93e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVD-ITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSL 659
Cdd:cd00180    18 GKKVAVKVIPKEKLKkLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLKDLLKENKGPLSEEEALSI 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  660 VSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRALCMAPELLRDAYRpgrgS 739
Cdd:cd00180    98 LRQLLSALEYLHSNGII-HRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGGTTPPYYAPPELLGGRYY----G 172
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 161076872  740 QKGDVYSFGILLYEMigrkgpwgdtayskEEIIQFVKCpeMLQH 783
Cdd:cd00180   173 PKVDIWSLGVILYEL--------------EELKDLIRR--MLQY 200
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
899-1040 7.06e-34

Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.


Pssm-ID: 143637 [Multi-domain]  Cd Length: 133  Bit Score: 126.70  E-value: 7.06e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  899 CVTILFSDIVGFTELCTTSTPFEVVEMLNDWYTCCDSIISNYDVYKVETIGDAYMVVSGLPlqngsrHAGEIASLALHLL 978
Cdd:cd07556     1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSGLD------HPAAAVAFAEDMR 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161076872  979 ETVgnLKIRHKPTETVQLRIGVHSGPCAAGVVGQKmPRYCLFGDTVNTASRMESTGDSMRIH 1040
Cdd:cd07556    75 EAV--SALNQSEGNPVRVRIGIHTGPVVVGVIGSR-PQYDVWGALVNLASRMESQAKAGQVL 133
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
59-427 1.51e-32

Receptor family ligand binding region; This family includes extracellular ligand binding domains of a wide range of receptors. This family also includes the bacterial amino acid binding proteins of known structure.


Pssm-ID: 460062 [Multi-domain]  Cd Length: 347  Bit Score: 130.20  E-value: 1.51e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872    59 LGGLPLAIEDVNKNPNLLPGKKLAFKPVDighkmSAYR-VKPLRAMTQMREAGVTAFIGPDES--CTTEALLASAWNTPM 135
Cdd:pfam01094    3 LLAVRLAVEDINADPGLLPGTKLEYIILD-----TCCDpSLALAAALDLLKGEVVAIIGPSCSsvASAVASLANEWKVPL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   136 LSFKCSDPIVSNKSTFHTFARTLAPASKVSKSVISLLNAFHWNKFSiVVSSKPIWGSDVARAIQELAEARNFTISHfkyi 215
Cdd:pfam01094   78 ISYGSTSPALSDLNRYPTFLRTTPSDTSQADAIVDILKHFGWKRVA-LIYSDDDYGESGLQALEDALRERGIRVAY---- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   216 SDYIPTTKTLSQI-DKIIEETYATTRIYVFIGEHIAMvdfvrglqnRRLLESGdyivvsvddeiydsnRRVNIMERNYLd 294
Cdd:pfam01094  153 KAVIPPAQDDDEIaRKLLKEVKSRARVIVVCCSSETA---------RRLLKAA---------------RELGMMGEGYV- 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   295 pYIRKE-KSKSLDKIS------FRSVIKISMTYPQNPhirdicsKIKDYARKTPFLVPYHQRvFDNISVPIYGLHLYDSV 367
Cdd:pfam01094  208 -WIATDgLTTSLVILNpstleaAGGVLGFRLHPPDSP-------EFSEFFWEKLSDEKELYE-NLGGLPVSYGALAYDAV 278
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   368 MIYVRAITEVLRLG---------GDIYDGNLVMSHIFNRSYHSIQGfDVYIDSNGD-AEGNYTVITLQND 427
Cdd:pfam01094  279 YLLAHALHNLLRDDkpgracgalGPWNGGQKLLRYLKNVNFTGLTG-NVQFDENGDrINPDYDILNLNGS 347
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
583-820 8.10e-32

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: 125.77  E-value: 8.10e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  583 IVAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLAN-----EDLHLDHMFIS 657
Cdd:cd14044    33 VVILKDLKNNEGNFTEKQKIELNKLLQIDYYNLTKFYGTVKLDTMIFGVIEYCERGSLRDVLNDkisypDGTFMDWEFKI 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  658 SLVSDILKGMIYLHDSEIISHGNLRSSNCLIDSRWVCQISDFGLhelkagqeepnKSELELKRALCMAPELLRDAyrpgR 737
Cdd:cd14044   113 SVMYDIAKGMSYLHSSKTEVHGRLKSTNCVVDSRMVVKITDFGC-----------NSILPPSKDLWTAPEHLRQA----G 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  738 GSQKGDVYSFGILLYEMIGRKgpwgDTAYS------KEEI--IQFVK--CPemlqhgvFRPALThthLDIPDYIRKCLC- 806
Cdd:cd14044   178 TSQKGDVYSYGIIAQEIILRK----ETFYTaacsdrKEKIyrVQNPKgmKP-------FRPDLN---LESAGEREREVYg 243
                         250
                  ....*....|....*..
gi 161076872  807 ---QCWDEDPEVRPDIR 820
Cdd:cd14044   244 lvkNCWEEDPEKRPDFK 260
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
581-817 5.57e-30

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: 119.93  E-value: 5.57e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKI--HKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLA-----NEDLhldh 653
Cdd:cd06606    25 GELMAVKEVelSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVPGGSLASLLKkfgklPEPV---- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  654 mfISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLheLKAGQEEPNKSELELKR--ALCMAPELLRD 731
Cdd:cd06606   101 --VRKYTRQILEGLEYLHSNGIV-HRDIKGANILVDSDGVVKLADFGC--AKRLAEIATGEGTKSLRgtPYWMAPEVIRG 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  732 AyRPGRGSqkgDVYSFGILLYEMIGRKGPWGDTAYSKE---EIIQFVKCPEMlqhgvfrPAltHTHLDIPDYIRKCLCQc 808
Cdd:cd06606   176 E-GYGRAA---DIWSLGCTVIEMATGKPPWSELGNPVAalfKIGSSGEPPPI-------PE--HLSEEAKDFLRKCLQR- 241

                  ....*....
gi 161076872  809 wdeDPEVRP 817
Cdd:cd06606   242 ---DPKKRP 247
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
581-819 7.08e-29

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: 116.53  E-value: 7.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLV 660
Cdd:cd05122    25 GQIVAIKKINLESKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFCSGGSLKDLLKNTNKTLTEQQIAYVC 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkAGQEEPNKSELELKRALC-MAPELLRD-AYrpgrg 738
Cdd:cd05122   105 KEVLKGLEYLHSHGII-HRDIKAANILLTSDGEVKLIDFGL----SAQLSDGKTRNTFVGTPYwMAPEVIQGkPY----- 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  739 SQKGDVYSFGILLYEMIGRKGPWGDTAYSKE-EIIQFVKCPEmLQHGVFRPAlththlDIPDYIRKCLcqcwDEDPEVRP 817
Cdd:cd05122   175 GFKADIWSLGITAIEMAEGKPPYSELPPMKAlFLIATNGPPG-LRNPKKWSK------EFKDFLKKCL----QKDPEKRP 243

                  ..
gi 161076872  818 DI 819
Cdd:cd05122   244 TA 245
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
584-830 3.26e-28

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: 115.14  E-value: 3.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSV--DITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVS 661
Cdd:cd14063    25 VAIKLLNIDYLneEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTSLCKGRTLYSLIHERKEKFDFNKTVQIAQ 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  662 DILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCqISDFGLHELKaGQEEPNKSELELKRA---LC-MAPELLRdAYRPGR 737
Cdd:cd14063   105 QICQGMGYLHAKGII-HKDLKSKNIFLENGRVV-ITDFGLFSLS-GLLQPGRREDTLVIPngwLCyLAPEIIR-ALSPDL 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  738 G-------SQKGDVYSFGILLYEMIGRKGPWGDTaySKEEIIQFVKCPemlqhgvFRPALthTHLDIPDYIRKCLCQCWD 810
Cdd:cd14063   181 DfeeslpfTKASDVYAFGTVWYELLAGRWPFKEQ--PAESIIWQVGCG-------KKQSL--SQLDIGREVKDILMQCWA 249
                         250       260
                  ....*....|....*....|
gi 161076872  811 EDPEVRPDIRLVRMHLKELQ 830
Cdd:cd14063   250 YDPEKRPTFSDLLRMLERLP 269
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
581-829 6.36e-28

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: 114.68  E-value: 6.36e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSV-DITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFIS-- 657
Cdd:cd14066    17 GTVVAVKRLNEMNCaASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLEDRLHCHKGSPPLPWPQrl 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  658 SLVSDILKGMIYLHDSE---IIsHGNLRSSNCLIDSRWVCQISDFGLHELkAGQEEPNKSELELKRALC-MAPELLRDay 733
Cdd:cd14066    97 KIAKGIARGLEYLHEECpppII-HGDIKSSNILLDEDFEPKLTDFGLARL-IPPSESVSKTSAVKGTIGyLAPEYIRT-- 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  734 rpGRGSQKGDVYSFGILLYEMIGRKGPW--GDTAYSKEEIIQFVK------CPEMLQHGVfRPALTHTHLDIPDYIRKCL 805
Cdd:cd14066   173 --GRVSTKSDVYSFGVVLLELLTGKPAVdeNRENASRKDLVEWVEskgkeeLEDILDKRL-VDDDGVEEEEVEALLRLAL 249
                         250       260
                  ....*....|....*....|....
gi 161076872  806 CqCWDEDPEVRPDIRLVRMHLKEL 829
Cdd:cd14066   250 L-CTRSDPSLRPSMKEVVQMLEKL 272
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
577-826 3.28e-27

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: 112.06  E-value: 3.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  577 ALFRGNIVAMKKIhKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHL----- 651
Cdd:cd05039    25 GDYRGQKVAVKCL-KDDSTAAQAFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIVTEYMAKGSLVDYLRSRGRAVitrkd 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  652 DHMFisslVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLheLKAGQEEPNKSELELKRAlcmAPELLRD 731
Cdd:cd05039   104 QLGF----ALDVCEGMEYLESKKFV-HRDLAARNVLVSEDNVAKVSDFGL--AKEASSNQDGGKLPIKWT---APEALRE 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  732 ayrpGRGSQKGDVYSFGILLYEMIGrkgpWGDTAYSK---EEIIQFVK------CPEmlqhgvfrpalththlDIPDYIR 802
Cdd:cd05039   174 ----KKFSTKSDVWSFGILLWEIYS----FGRVPYPRiplKDVVPHVEkgyrmeAPE----------------GCPPEVY 229
                         250       260
                  ....*....|....*....|....
gi 161076872  803 KCLCQCWDEDPEVRPDIRLVRMHL 826
Cdd:cd05039   230 KVMKNCWELDPAKRPTFKQLREKL 253
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
579-826 1.31e-26

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: 109.51  E-value: 1.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  579 FRGNIVAMKKI-HKKSVDItrsirkelKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLaNEDLHLDHMFIS 657
Cdd:cd14059    14 FRGEEVAVKKVrDEKETDI--------KHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLYEVL-RAGREITPSLLV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  658 SLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHelKAGQEEPNKSELELKRALcMAPELLRDayRPgr 737
Cdd:cd14059    85 DWSKQIASGMNYLHLHKII-HRDLKSPNVLVTYNDVLKISDFGTS--KELSEKSTKMSFAGTVAW-MAPEVIRN--EP-- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  738 GSQKGDVYSFGILLYEMIGRKGPWGDTAYSKeeIIqfvkcpemlqHGVFRPALthtHLDI----PDYIRKCLCQCWDEDP 813
Cdd:cd14059   157 CSEKVDIWSFGVVLWELLTGEIPYKDVDSSA--II----------WGVGSNSL---QLPVpstcPDGFKLLMKQCWNSKP 221
                         250
                  ....*....|...
gi 161076872  814 EVRPDIRLVRMHL 826
Cdd:cd14059   222 RNRPSFRQILMHL 234
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
581-817 2.28e-26

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: 110.16  E-value: 2.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVDITRS-IRKELKLMREVRHENIINFIGASTDHG--SVIIFTTYCARGSLEDVLANEDLHLDHMFIS 657
Cdd:cd05038    33 GEQVAVKSLQPSGEEQHMSdFKREIEILRTLDHEYIVKYKGVCESPGrrSLRLIMEYLPSGSLRDYLQRHRDQIDLKRLL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  658 SLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHE-LKAGQEEPNKSELELKRALCMAPELLRDAyrpg 736
Cdd:cd05038   113 LFASQICKGMEYLGSQRYI-HRDLAARNILVESEDLVKISDFGLAKvLPEDKEYYYVKEPGESPIFWYAPECLRES---- 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  737 RGSQKGDVYSFGILLYEMIGRKGPwgdtaySKEEIIQFvkcpeMLQHGVFRPALTHTHL--------------DIPDYIR 802
Cdd:cd05038   188 RFSSASDVWSFGVTLYELFTYGDP------SQSPPALF-----LRMIGIAQGQMIVTRLlellksgerlprppSCPDEVY 256
                         250
                  ....*....|....*
gi 161076872  803 KCLCQCWDEDPEVRP 817
Cdd:cd05038   257 DLMKECWEYEPQDRP 271
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
579-822 5.40e-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: 108.25  E-value: 5.40e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  579 FRGN---IVAMKKIhkKSVDITRS----IRKELKLMREVRHENIINFIGASTDHGSVIIfTTYCARGSLEDVLANEDLHL 651
Cdd:cd14062    10 YKGRwhgDVAVKKL--NVTDPTPSqlqaFKNEVAVLRKTRHVNILLFMGYMTKPQLAIV-TQWCEGSSLYKHLHVLETKF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  652 DHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKA------GQEEPNKSelelkrALCMA 725
Cdd:cd14062    87 EMLQLIDIARQTAQGMDYLHAKNII-HRDLKSNNIFLHEDLTVKIGDFGLATVKTrwsgsqQFEQPTGS------ILWMA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  726 PELLR----DAYrpgrgSQKGDVYSFGILLYEMIGRKGPWGDTAySKEEIIQFVKCpemlqhGVFRPALTHTHLDIPDYI 801
Cdd:cd14062   160 PEVIRmqdeNPY-----SFQSDVYAFGIVLYELLTGQLPYSHIN-NRDQILFMVGR------GYLRPDLSKVRSDTPKAL 227
                         250       260
                  ....*....|....*....|.
gi 161076872  802 RKCLCQCWDEDPEVRPDIRLV 822
Cdd:cd14062   228 RRLMEDCIKFQRDERPLFPQI 248
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
584-817 6.66e-26

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: 108.31  E-value: 6.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDI--TRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANE--DLHLDHMFisSL 659
Cdd:cd13978    21 VAIKCLHSSPNCIeeRKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLKSLLEREiqDVPWSLRF--RI 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  660 VSDILKGMIYLH--DSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKA---GQEEPNKSELELKRALCMAPELLRDAYR 734
Cdd:cd13978    99 IHEIALGMNFLHnmDPPLL-HHDLKPENILLDNHFHVKISDFGLSKLGMksiSANRRRGTENLGGTPIYMAPEAFDDFNK 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  735 pgRGSQKGDVYSFGILLYEMIGRKGPWGDtAYSKEEIIQFVkcpemlQHGvFRPALTHTHLDIPDYIRKCLCQ----CWD 810
Cdd:cd13978   178 --KPTSKSDVYSFAIVIWAVLTRKEPFEN-AINPLLIMQIV------SKG-DRPSLDDIGRLKQIENVQELISlmirCWD 247

                  ....*..
gi 161076872  811 EDPEVRP 817
Cdd:cd13978   248 GNPDARP 254
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
577-829 2.02e-24

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: 103.67  E-value: 2.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  577 ALFRGNIVAMKKIhkKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLdHMFI 656
Cdd:cd14058    12 ARWRNQIVAVKII--ESESEKKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLYNVLHGKEPKP-IYTA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  657 SSLVSDIL---KGMIYLH---DSEIIsHGNLRSSNCLIDSRW-VCQISDFGLHELKAGQEEPNKSElelkrALCMAPEll 729
Cdd:cd14058    89 AHAMSWALqcaKGVAYLHsmkPKALI-HRDLKPPNLLLTNGGtVLKICDFGTACDISTHMTNNKGS-----AAWMAPE-- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  730 rdAYRPGRGSQKGDVYSFGILLYEMIGRKGPWGDTAYSKEEIIQFVkcpemlqHGVFRPALTHThldIPDYIRKCLCQCW 809
Cdd:cd14058   161 --VFEGSKYSEKCDVFSWGIILWEVITRRKPFDHIGGPAFRIMWAV-------HNGERPPLIKN---CPKPIESLMTRCW 228
                         250       260
                  ....*....|....*....|
gi 161076872  810 DEDPEVRPDIRLVRMHLKEL 829
Cdd:cd14058   229 SKDPEKRPSMKEIVKIMSHL 248
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
577-817 3.29e-24

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: 103.62  E-value: 3.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  577 ALFRGNIVAMKKI--HKKSVDITRSIRKELKLMReVRHENIINFIGAST----DHGSVIIFTtYCARGSLEDVL--ANED 648
Cdd:cd13979    22 ATYKGETVAVKIVrrRRKNRASRQSFWAELNAAR-LRHENIVRVLAAETgtdfASLGLIIME-YCGNGTLQQLIyeGSEP 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  649 LHLDHMFISSLvsDILKGMIYLHdSEIISHGNLRSSNCLIDSRWVCQISDFGLHELkagQEEPNKSELELK--RALC--M 724
Cdd:cd13979   100 LPLAHRILISL--DIARALRFCH-SHGIVHLDVKPANILISEQGVCKLCDFGCSVK---LGEGNEVGTPRShiGGTYtyR 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  725 APELLRDAyrpgRGSQKGDVYSFGILLYEMIGRKGPW-GDTAYSkeeIIQFVKcpemlqHGVfRPALTHTHLDIP-DYIR 802
Cdd:cd13979   174 APELLKGE----RVTPKADIYSFGITLWQMLTRELPYaGLRQHV---LYAVVA------KDL-RPDLSGLEDSEFgQRLR 239
                         250
                  ....*....|....*
gi 161076872  803 KCLCQCWDEDPEVRP 817
Cdd:cd13979   240 SLISRCWSAQPAERP 254
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
584-757 5.24e-23

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: 99.49  E-value: 5.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDiTRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSDI 663
Cdd:cd14065    20 VMVMKELKRFDE-QRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLEELLKSMDEQLPWSQRVSLAKDI 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  664 LKGMIYLHDSEIIsHGNLRSSNCLI---DSRWVCQISDFGLHElKAGQEEPNKSELELKRALC-----MAPELLR-DAYr 734
Cdd:cd14065    99 ASGMAYLHSKNII-HRDLNSKNCLVreaNRGRNAVVADFGLAR-EMPDEKTKKPDRKKRLTVVgspywMAPEMLRgESY- 175
                         170       180
                  ....*....|....*....|...
gi 161076872  735 pgrgSQKGDVYSFGILLYEMIGR 757
Cdd:cd14065   176 ----DEKVDVFSFGIVLCEIIGR 194
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
581-826 5.75e-23

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


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 100.03  E-value: 5.75e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLV 660
Cdd:cd14221    18 GEVMVMKELIRFDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRGIIKSMDSHYPWSQRVSFA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRA------------LCMAPEL 728
Cdd:cd14221    98 KDIASGMAYLHSMNII-HRDLNSHNCLVRENKSVVVADFGLARLMVDEKTQPEGLRSLKKPdrkkrytvvgnpYWMAPEM 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  729 LRdayrpGRG-SQKGDVYSFGILLYEMIGRKGpwGDTAYskeeiiqfvkCPEMLQHGVFRPALTHTHL--DIPDYIRKCL 805
Cdd:cd14221   177 IN-----GRSyDEKVDVFSFGIVLCEIIGRVN--ADPDY----------LPRTMDFGLNVRGFLDRYCppNCPPSFFPIA 239
                         250       260
                  ....*....|....*....|....*...
gi 161076872  806 CQCWDEDPEVRPD-------IRLVRMHL 826
Cdd:cd14221   240 VLCCDLDPEKRPSfsklehwLETLRMHL 267
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
578-830 8.90e-23

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: 99.32  E-value: 8.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  578 LFRGNI---VAMK--KIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIfTTYCARGSLEDVLANEDLHLD 652
Cdd:cd14150    16 VFRGKWhgdVAVKilKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGFMTRPNFAII-TQWCEGSSLYRHLHVTETRFD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  653 HMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRALCMAPELLRdA 732
Cdd:cd14150    95 TMQLIDVARQTAQGMDYLHAKNII-HRDLKSNNIFLHEGLTVKIGDFGLATVKTRWSGSQQVEQPSGSILWMAPEVIR-M 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  733 YRPGRGSQKGDVYSFGILLYEMIGRKGPWGDTAySKEEIIQfvkcpeMLQHGVFRPALTHTHLDIPDYIRKCLCQCWDED 812
Cdd:cd14150   173 QDTNPYSFQSDVYAYGVVLYELMSGTLPYSNIN-NRDQIIF------MVGRGYLSPDLSKLSSNCPKAMKRLLIDCLKFK 245
                         250
                  ....*....|....*...
gi 161076872  813 PEVRPDIRLVRMHLKELQ 830
Cdd:cd14150   246 REERPLFPQILVSIELLQ 263
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
581-817 9.41e-23

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: 99.01  E-value: 9.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIH-----KKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDlHLDHMF 655
Cdd:cd06632    25 GDFFAVKEVSlvdddKKSRESVKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVPGGSIHKLLQRYG-AFEEPV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  656 ISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkAGQEEPNKSELELKRALC-MAPELLRdAYR 734
Cdd:cd06632   104 IRLYTRQILSGLAYLHSRNTV-HRDIKGANILVDTNGVVKLADFGM----AKHVEAFSFAKSFKGSPYwMAPEVIM-QKN 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  735 PGRGSQkGDVYSFGILLYEMIGRKGPWGDtaYSKEEII-QFVKCPEMlqhgvfrPAL-THTHLDIPDYIRKCLCQcwdeD 812
Cdd:cd06632   178 SGYGLA-VDIWSLGCTVLEMATGKPPWSQ--YEGVAAIfKIGNSGEL-------PPIpDHLSPDAKDFIRLCLQR----D 243

                  ....*
gi 161076872  813 PEVRP 817
Cdd:cd06632   244 PEDRP 248
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
602-817 1.98e-22

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: 97.74  E-value: 1.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  602 KELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANED---LHLDHMFisSLVSDILKGMIYLHDSEIIsH 678
Cdd:cd05034    39 QEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSKGSLLDYLRTGEgraLRLPQLI--DMAAQIASGMAYLESRNYI-H 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  679 GNLRSSNCLIDSRWVCQISDFGLHEL-KAGQEEPNKSE-LELKRAlcmAPEllrdAYRPGRGSQKGDVYSFGILLYEMI- 755
Cdd:cd05034   116 RDLAARNILVGENNVCKVADFGLARLiEDDEYTAREGAkFPIKWT---APE----AALYGRFTIKSDVWSFGILLYEIVt 188
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161076872  756 -GRKgPWgdTAYSKEEIIQFVK------CPEmlqhgvfrpalththlDIPDYIRKCLCQCWDEDPEVRP 817
Cdd:cd05034   189 yGRV-PY--PGMTNREVLEQVErgyrmpKPP----------------GCPDELYDIMLQCWKKEPEERP 238
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
583-825 1.99e-22

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: 98.17  E-value: 1.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  583 IVAMKKIHKK--SVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANE---DLHLDHMFIS 657
Cdd:cd14069    28 AVAVKFVDMKraPGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEYASGGELFDKIEPDvgmPEDVAQFYFQ 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  658 SLVSdilkGMIYLHdSEIISHGNLRSSNCLIDSRWVCQISDFGLhelkAGQEEPNKSELELKRAlC-----MAPELL-RD 731
Cdd:cd14069   108 QLMA----GLKYLH-SCGITHRDIKPENLLLDENDNLKISDFGL----ATVFRYKGKERLLNKM-CgtlpyVAPELLaKK 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  732 AYRpgrgSQKGDVYSFGILLYEMIGRKGPWGDTAYSKEEIIQFVKCPEMLQHGvfRPALTHTHLDIpdyIRKCLcqcwDE 811
Cdd:cd14069   178 KYR----AEPVDVWSCGIVLFAMLAGELPWDQPSDSCQEYSDWKENKKTYLTP--WKKIDTAALSL---LRKIL----TE 244
                         250
                  ....*....|....
gi 161076872  812 DPEVRPDIRLVRMH 825
Cdd:cd14069   245 NPNKRITIEDIKKH 258
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
601-829 3.10e-22

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: 98.12  E-value: 3.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  601 RKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSDILKGMIYLHDSEIIsHGN 680
Cdd:cd14152    44 KKEVMNYRQTRHENVVLFMGACMHPPHLAIITSFCKGRTLYSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIV-HKD 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  681 LRSSNCLIDSRWVCqISDFGLHELKA-GQEEPNKSELELKRA-LC-MAPELLRDAyRPGRG------SQKGDVYSFGILL 751
Cdd:cd14152   123 LKSKNVFYDNGKVV-ITDFGLFGISGvVQEGRRENELKLPHDwLCyLAPEIVREM-TPGKDedclpfSKAADVYAFGTIW 200
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161076872  752 YEMIGRKGPWGDTAysKEEIIQFVKCPEMLqhgvfRPALTHTHLDipDYIRKCLCQCWDEDPEVRPDIRLVRMHLKEL 829
Cdd:cd14152   201 YELQARDWPLKNQP--AEALIWQIGSGEGM-----KQVLTTISLG--KEVTEILSACWAFDLEERPSFTLLMDMLEKL 269
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
602-817 3.55e-22

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: 97.13  E-value: 3.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  602 KELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSDILKGMIYLHDSEIIsHGNL 681
Cdd:cd05041    42 QEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGSLLTFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCI-HRDL 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  682 RSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRALCMAPEllrdAYRPGRGSQKGDVYSFGILLYEMIGrkgpW 761
Cdd:cd05041   121 AARNCLVGENNVLKISDFGMSREEEDGEYTVSDGLKQIPIKWTAPE----ALNYGRYTSESDVWSFGILLWEIFS----L 192
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 161076872  762 GDTAYSKEEIIQfvkCPEMLQHGVFRPALTHThldiPDYIRKCLCQCWDEDPEVRP 817
Cdd:cd05041   193 GATPYPGMSNQQ---TREQIESGYRMPAPELC----PEAVYRLMLQCWAYDPENRP 241
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
581-818 4.02e-22

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: 97.28  E-value: 4.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVDItRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLV 660
Cdd:cd06614    25 GKEVAIKKMRLRKQNK-ELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMDGGSLTDIITQNPVRMNESQIAYVC 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkAGQEEPNKSelelKR------ALCMAPEL-LRDAY 733
Cdd:cd06614   104 REVLQGLEYLHSQNVI-HRDIKSDNILLSKDGSVKLADFGF----AAQLTKEKS----KRnsvvgtPYWMAPEViKRKDY 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  734 rpgrgSQKGDVYSFGILLYEMIGrkgpwGDTAYSKEEiiqfvkcPEML-----QHGVfrPALTHTHL---DIPDYIRKCL 805
Cdd:cd06614   175 -----GPKVDIWSLGIMCIEMAE-----GEPPYLEEP-------PLRAlflitTKGI--PPLKNPEKwspEFKDFLNKCL 235
                         250
                  ....*....|...
gi 161076872  806 CQcwdeDPEVRPD 818
Cdd:cd06614   236 VK----DPEKRPS 244
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
602-833 5.06e-22

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: 96.78  E-value: 5.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  602 KELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANeDLHLDHMFISSLVSDILKGMIYLHDSEIIsHGNL 681
Cdd:cd14155    37 REVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNLEQLLDS-NEPLSWTVRVKLALDIARGLSYLHSKGIF-HRDL 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  682 RSSNCLI---DSRWVCQISDFGLHElKAGQEEPNKSELE-LKRALCMAPELLRDAYRpgrgSQKGDVYSFGILLYEMIGR 757
Cdd:cd14155   115 TSKNCLIkrdENGYTAVVGDFGLAE-KIPDYSDGKEKLAvVGSPYWMAPEVLRGEPY----NEKADVFSYGIILCEIIAR 189
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161076872  758 KGpwGDTAYskeeiiqfvkCPEMLQHGVFRPALTHTHLDIP-DYIRKCLcQCWDEDPEVRPDIRLVRMHLKELQAGL 833
Cdd:cd14155   190 IQ--ADPDY----------LPRTEDFGLDYDAFQHMVGDCPpDFLQLAF-NCCNMDPKSRPSFHDIVKTLEEILEKL 253
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
531-829 6.69e-22

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: 96.59  E-value: 6.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  531 WKVDMKDVT---VINLGEYNNptnknifqicrqsiLVVGEpnkrsftnialFRGNIVAMKKIhkKSVDITRSIRKELKLM 607
Cdd:cd05082     1 WALNMKELKllqTIGKGEFGD--------------VMLGD-----------YRGNKVAVKCI--KNDATAQAFLAEASVM 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  608 REVRHENIINFIGAST-DHGSVIIFTTYCARGSLEDVLANED---LHLDHMFISSLvsDILKGMIYLHDSEIIsHGNLRS 683
Cdd:cd05082    54 TQLRHSNLVQLLGVIVeEKGGLYIVTEYMAKGSLVDYLRSRGrsvLGGDCLLKFSL--DVCEAMEYLEGNNFV-HRDLAA 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  684 SNCLIDSRWVCQISDFGLheLKAGQEEPNKSELELKRAlcmAPELLRDAyrpgRGSQKGDVYSFGILLYEMIGrkgpWGD 763
Cdd:cd05082   131 RNVLVSEDNVAKVSDFGL--TKEASSTQDTGKLPVKWT---APEALREK----KFSTKSDVWSFGILLWEIYS----FGR 197
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161076872  764 TAYSKEEIIQFVkcpemlqhgvfrPALTHTH-LDIPD----YIRKCLCQCWDEDPEVRPDIRLVRMHLKEL 829
Cdd:cd05082   198 VPYPRIPLKDVV------------PRVEKGYkMDAPDgcppAVYDVMKNCWHLDAAMRPSFLQLREQLEHI 256
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
577-826 1.11e-21

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: 95.96  E-value: 1.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  577 ALFRGNI-VAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANED---LHLD 652
Cdd:cd05148    25 GLWKNRVrVAIKILKSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITELMEKGSLLAFLRSPEgqvLPVA 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  653 HMF-ISSLVSDilkGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHEL-KAGQEEPNKSELELKRAlcmAPEllr 730
Cdd:cd05148   105 SLIdMACQVAE---GMAYLEEQNSI-HRDLAARNILVGEDLVCKVADFGLARLiKEDVYLSSDKKIPYKWT---APE--- 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  731 dAYRPGRGSQKGDVYSFGILLYEMIGRkgpwGDTAYskeeiiqfvkcPEMLQHGVFRPALTHTHL----DIPDYIRKCLC 806
Cdd:cd05148   175 -AASHGTFSTKSDVWSFGILLYEMFTY----GQVPY-----------PGMNNHEVYDQITAGYRMpcpaKCPQEIYKIML 238
                         250       260
                  ....*....|....*....|
gi 161076872  807 QCWDEDPEVRPDIRLVRMHL 826
Cdd:cd05148   239 ECWAAEPEDRPSFKALREEL 258
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
579-817 1.20e-21

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: 95.98  E-value: 1.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  579 FRGNI-VAMKKIHKKSVDITRSIrKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFIS 657
Cdd:cd05059    25 WRGKIdVAIKMIKEGSMSEDDFI-EEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMANGCLLNYLRERRGKFQTEQLL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  658 SLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNK--SELELKRAlcmAPELLRDayrp 735
Cdd:cd05059   104 EMCKDVCEAMEYLESNGFI-HRDLAARNCLVGEQNVVKVSDFGLARYVLDDEYTSSvgTKFPVKWS---PPEVFMY---- 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  736 GRGSQKGDVYSFGILLYEMI-GRKGPWGDtaYSKEEIIqfvkcpEMLQHG--VFRPALTHTHldipdyIRKCLCQCWDED 812
Cdd:cd05059   176 SKFSSKSDVWSFGVLMWEVFsEGKMPYER--FSNSEVV------EHISQGyrLYRPHLAPTE------VYTIMYSCWHEK 241

                  ....*
gi 161076872  813 PEVRP 817
Cdd:cd05059   242 PEERP 246
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
572-763 1.56e-21

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: 95.68  E-value: 1.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  572 SFTNIAL----FRGNIVAMKKIHKKSVDITRSIRK---------ELKLMREVRHENIINFIGASTDHGSVIIFTTYCARG 638
Cdd:cd06628    12 SFGSVYLgmnaSSGELMAVKQVELPSVSAENKDRKksmldalqrEIALLRELQHENIVQYLGSSSDANHLNIFLEYVPGG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  639 SLEDVLANEDlHLDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLH---ELKAGQEEPNKSE 715
Cdd:cd06628    92 SVATLLNNYG-AFEESLVRNFVRQILKGLNYLHNRGII-HRDIKGANILVDNKGGIKISDFGISkklEANSLSTKNNGAR 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 161076872  716 LELK-RALCMAPELLRDAYRpgrgSQKGDVYSFGILLYEMIGRKGPWGD 763
Cdd:cd06628   170 PSLQgSVFWMAPEVVKQTSY----TRKADIWSLGCLVVEMLTGTHPFPD 214
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
581-829 1.83e-21

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: 95.65  E-value: 1.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLV 660
Cdd:cd14154    18 GEVMVMKELIRFDEEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTLKDVLKDMARPLPWAQRVRFA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEP--NKSELELKRAL---------------- 722
Cdd:cd14154    98 KDIASGMAYLHSMNII-HRDLNSHNCLVREDKTVVVADFGLARLIVEERLPsgNMSPSETLRHLkspdrkkrytvvgnpy 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  723 CMAPELLRdayrpGRG-SQKGDVYSFGILLYEMIGRKgpWGDTAYskeeiiqfvkCPEMLQHGV----FRPALTHthlDI 797
Cdd:cd14154   177 WMAPEMLN-----GRSyDEKVDIFSFGIVLCEIIGRV--EADPDY----------LPRTKDFGLnvdsFREKFCA---GC 236
                         250       260       270
                  ....*....|....*....|....*....|..
gi 161076872  798 PDYIRKCLCQCWDEDPEVRPDIRLVRMHLKEL 829
Cdd:cd14154   237 PPPFFKLAFLCCDLDPEKRPPFETLEEWLEAL 268
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
573-825 2.11e-21

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: 95.45  E-value: 2.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  573 FTNIALFRGNIVAMKKI--HKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLh 650
Cdd:cd06626    17 YTAVNLDTGELMAMKEIrfQDNDPKTIKEIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQEGTLEELLRHGRI- 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  651 LDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLH-ELKAGQEEPNKSELELKR--ALCMAPE 727
Cdd:cd06626    96 LDEAVIRVYTLQLLEGLAYLHENGIV-HRDIKPANIFLDSNGLIKLGDFGSAvKLKNNTTTMAPGEVNSLVgtPAYMAPE 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  728 LLRDAYRPGRGsQKGDVYSFGILLYEMIGRKGPWGDtaYSKEEIIqfvkcpeMLQHGVFRPALTHTHLDIPDYIRKCLCQ 807
Cdd:cd06626   175 VITGNKGEGHG-RAADIWSLGCVVLEMATGKRPWSE--LDNEWAI-------MYHVGMGHKPPIPDSLQLSPEGKDFLSR 244
                         250
                  ....*....|....*...
gi 161076872  808 CWDEDPEVRPDIRLVRMH 825
Cdd:cd06626   245 CLESDPKKRPTASELLDH 262
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
562-829 2.24e-21

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: 95.74  E-value: 2.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  562 ILVVGEPNkrsFTNIALFR--------GNIVAMKKIHKK-SVDITRSIRKELKLMREVRHENIINFIGASTDHG--SVII 630
Cdd:cd05080     9 IRDLGEGH---FGKVSLYCydptndgtGEMVAVKALKADcGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQGgkSLQL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  631 FTTYCARGSLEDVLANEDLHLDHMFIssLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHE-LKAGQE 709
Cdd:cd05080    86 IMEYVPLGSLRDYLPKHSIGLAQLLL--FAQQICEGMAYLHSQHYI-HRDLAARNVLLDNDRLVKIGDFGLAKaVPEGHE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  710 EPNKSELELKRALCMAPELLRDAyrpgRGSQKGDVYSFGILLYEMIGRKGPWGDTAYSKEEIIQF-------VKCPEMLQ 782
Cdd:cd05080   163 YYRVREDGDSPVFWYAPECLKEY----KFYYASDVWSFGVTLYELLTHCDSSQSPPTKFLEMIGIaqgqmtvVRLIELLE 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 161076872  783 HGVFRPALThthlDIPDYIRKCLCQCWDEDPEVRPDIRLVRMHLKEL 829
Cdd:cd05080   239 RGERLPCPD----KCPQEVYHLMKNCWETEASFRPTFENLIPILKTV 281
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
584-757 2.44e-21

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: 94.89  E-value: 2.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDiTRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSDI 663
Cdd:cd14156    20 VMVVKIYKNDVD-QHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLEELLAREELPLSWREKVELACDI 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  664 LKGMIYLHdSEIISHGNLRSSNCLI--DSRWV-CQISDFGLHElKAGQEEPNKSELELK---RALCMAPELLR-DAYrpg 736
Cdd:cd14156    99 SRGMVYLH-SKNIYHRDLNSKNCLIrvTPRGReAVVTDFGLAR-EVGEMPANDPERKLSlvgSAFWMAPEMLRgEPY--- 173
                         170       180
                  ....*....|....*....|.
gi 161076872  737 rgSQKGDVYSFGILLYEMIGR 757
Cdd:cd14156   174 --DRKVDVFSFGIVLCEILAR 192
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
581-818 3.28e-21

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: 94.60  E-value: 3.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKI--HKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLA-----NEDLhldh 653
Cdd:cd06627    25 GEFVAIKQIslEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYVENGSLASIIKkfgkfPESL---- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  654 mfISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhELKAGQEEPNKSElelkrALC----MAPELL 729
Cdd:cd06627   101 --VAVYIYQVLEGLAYLHEQGVI-HRDIKGANILTTKDGLVKLADFGV-ATKLNEVEKDENS-----VVGtpywMAPEVI 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  730 RdayrpGRG-SQKGDVYSFGILLYEMIGRKGPWGD-TAYSKeeIIQFVKCPEmlqhgvfrPALThthLDIPDYIRKCLCQ 807
Cdd:cd06627   172 E-----MSGvTTASDIWSVGCTVIELLTGNPPYYDlQPMAA--LFRIVQDDH--------PPLP---ENISPELRDFLLQ 233
                         250
                  ....*....|.
gi 161076872  808 CWDEDPEVRPD 818
Cdd:cd06627   234 CFQKDPTLRPS 244
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
584-817 8.38e-21

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: 93.72  E-value: 8.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDITR--SIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDhmFISSLVS 661
Cdd:cd14027    20 VVLKTVYTGPNCIEHneALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMHVLKKVSVPLS--VKGRIIL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  662 DILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKR----------ALC-MAPELLR 730
Cdd:cd14027    98 EIIEGMAYLHGKGVI-HKDLKPENILVDNDFHIKIADLGLASFKMWSKLTKEEHNEQREvdgtakknagTLYyMAPEHLN 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  731 DAYrpGRGSQKGDVYSFGILLYEMIGRKGPWGDtAYSKEEIIQFVKCPEmlqhgvfRPALTHTHLDIPDYIRKCLCQCWD 810
Cdd:cd14027   177 DVN--AKPTEKSDVYSFAIVLWAIFANKEPYEN-AINEDQIIMCIKSGN-------RPDVDDITEYCPREIIDLMKLCWE 246

                  ....*..
gi 161076872  811 EDPEVRP 817
Cdd:cd14027   247 ANPEARP 253
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
592-825 3.46e-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: 92.06  E-value: 3.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  592 KSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLAN-----EDLhldhmfISSLVSDILKG 666
Cdd:cd06629    47 RQKTVVDALKSEIDTLKDLDHPNIVQYLGFEETEDYFSIFLEYVPGGSIGSCLRKygkfeEDL------VRFFTRQILDG 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  667 MIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHElKAGQEEPNKSELELKRAL-CMAPELLrDAYRPGRgSQKGDVY 745
Cdd:cd06629   121 LAYLHSKGIL-HRDLKADNILVDLEGICKISDFGISK-KSDDIYGNNGATSMQGSVfWMAPEVI-HSQGQGY-SAKVDIW 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  746 SFGILLYEMIGRKGPWgdtaySKEEIIQFvkcpeMLQHGVFR-----PALTHTHLDIPDYIRKClCQCwdeDPEVRPDIR 820
Cdd:cd06629   197 SLGCVVLEMLAGRRPW-----SDDEAIAA-----MFKLGNKRsappvPEDVNLSPEALDFLNAC-FAI---DPRDRPTAA 262

                  ....*
gi 161076872  821 LVRMH 825
Cdd:cd06629   263 ELLSH 267
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
581-830 4.64e-20

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: 92.00  E-value: 4.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHG--SVIIFTTYCARGSLEDVLANEDLHLDHMFISS 658
Cdd:cd14205    33 GEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGrrNLRLIMEYLPYGSLRDYLQKHKERIDHIKLLQ 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  659 LVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHE-LKAGQE-----EPNKSELelkraLCMAPELLRDA 732
Cdd:cd14205   113 YTSQICKGMEYLGTKRYI-HRDLATRNILVENENRVKIGDFGLTKvLPQDKEyykvkEPGESPI-----FWYAPESLTES 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  733 yrpgRGSQKGDVYSFGILLYEMI----GRKGP-------WGDTAYSKEEIIQFVkcpEMLQHGVFRPALThthlDIPDYI 801
Cdd:cd14205   187 ----KFSVASDVWSFGVVLYELFtyieKSKSPpaefmrmIGNDKQGQMIVFHLI---ELLKNNGRLPRPD----GCPDEI 255
                         250       260
                  ....*....|....*....|....*....
gi 161076872  802 RKCLCQCWDEDPEVRPDIRLVRMHLKELQ 830
Cdd:cd14205   256 YMIMTECWNNNVNQRPSFRDLALRVDQIR 284
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
581-826 5.48e-20

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: 91.73  E-value: 5.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHkksVDITRSIRK----ELKLMREVRHENIINFIGA-STDHGSVIIFTTYCARGSLEDVLA-----NEDLh 650
Cdd:cd06620    30 GTIMAKKVIH---IDAKSSVRKqilrELQILHECHSPYIVSFYGAfLNENNNIIICMEYMDCGSLDKILKkkgpfPEEV- 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  651 ldhmfISSLVSDILKGMIYLHDSEIISHGNLRSSNCLIDSRWVCQISDFGLhelkAGQEEPNKSELELKRALCMAPELLR 730
Cdd:cd06620   106 -----LGKIAVAVLEGLTYLYNVHRIIHRDIKPSNILVNSKGQIKLCDFGV----SGELINSIADTFVGTSTYMSPERIQ 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  731 -DAYrpgrgSQKGDVYSFGILLYEMIGRKGPWG-----DTAYSKEEIIQfvkcpEMLQHGVFRPALTHTHLDI-PDYIRK 803
Cdd:cd06620   177 gGKY-----SVKSDVWSLGLSIIELALGEFPFAgsnddDDGYNGPMGIL-----DLLQRIVNEPPPRLPKDRIfPKDLRD 246
                         250       260
                  ....*....|....*....|....
gi 161076872  804 CLCQCWDEDPEVRPDIR-LVRMHL 826
Cdd:cd06620   247 FVDRCLLKDPRERPSPQlLLDHDP 270
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
577-816 5.74e-20

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: 91.62  E-value: 5.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  577 ALFRGNIVAMKKI---HKKSVDITRSIRKELKLmrevRHENIINFIGASTdHGSVI-----IFTTYCARGSLEDVLANED 648
Cdd:cd14053    14 AQYLNRLVAVKIFplqEKQSWLTEREIYSLPGM----KHENILQFIGAEK-HGESLeaeywLITEFHERGSLCDYLKGNV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  649 LHLDHM--FISSLVsdilKGMIYLHDsEI----------ISHGNLRSSNCLIDSRWVCQISDFGLH-ELKAGQeEPNKSE 715
Cdd:cd14053    89 ISWNELckIAESMA----RGLAYLHE-DIpatngghkpsIAHRDFKSKNVLLKSDLTACIADFGLAlKFEPGK-SCGDTH 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  716 LELKRALCMAPELL-------RDAYRpgrgsqKGDVYSFGILLYEMIGR----KGPWGDTAYSKEEIIQFVKCPEMLQHG 784
Cdd:cd14053   163 GQVGTRRYMAPEVLegainftRDAFL------RIDMYAMGLVLWELLSRcsvhDGPVDEYQLPFEEEVGQHPTLEDMQEC 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 161076872  785 V----FRPAlththldIPDYIRK-----CLCQ----CWDEDPEVR 816
Cdd:cd14053   237 VvhkkLRPQ-------IRDEWRKhpglaQLCEtieeCWDHDAEAR 274
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
602-828 6.03e-20

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: 90.75  E-value: 6.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  602 KELKLMREVRHENIINFIGASTDHgSVIIFTTYCARGSLEDVLANEDLHldHMFISSLV---SDILKGMIYLHDSEIIsH 678
Cdd:cd14203    39 EEAQIMKKLRHDKLVQLYAVVSEE-PIYIVTEFMSKGSLLDFLKDGEGK--YLKLPQLVdmaAQIASGMAYIERMNYI-H 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  679 GNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNK--SELELKRAlcmAPEllrdAYRPGRGSQKGDVYSFGILLYEMIg 756
Cdd:cd14203   115 RDLRAANILVGDNLVCKIADFGLARLIEDNEYTARqgAKFPIKWT---APE----AALYGRFTIKSDVWSFGILLTELV- 186
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161076872  757 RKGPWGDTAYSKEEIIqfvkcpEMLQHGVFRPALThthlDIPDYIRKCLCQCWDEDPEVRPDIRLVRMHLKE 828
Cdd:cd14203   187 TKGRVPYPGMNNREVL------EQVERGYRMPCPP----GCPESLHELMCQCWRKDPEERPTFEYLQSFLED 248
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
581-825 6.94e-20

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: 90.61  E-value: 6.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKK---SVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLaNEDLHLDHMFIS 657
Cdd:cd14007    25 GFIVALKVISKSqlqKSGLEHQLRREIEIQSHLRHPNILRLYGYFEDKKRIYLILEYAPNGELYKEL-KKQKRFDEKEAA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  658 SLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkAGQEEPNKselelKRALC-----MAPELLRda 732
Cdd:cd14007   104 KYIYQLALALDYLHSKNII-HRDIKPENILLGSNGELKLADFGW----SVHAPSNR-----RKTFCgtldyLPPEMVE-- 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  733 yrpGRG-SQKGDVYSFGILLYEMIGRKGPWGDTaySKEEIIQfvkcpeMLQHGvfrpalthtHLDIPDYI----RKCLCQ 807
Cdd:cd14007   172 ---GKEyDYKVDIWSLGVLCYELLVGKPPFESK--SHQETYK------RIQNV---------DIKFPSSVspeaKDLISK 231
                         250
                  ....*....|....*...
gi 161076872  808 CWDEDPEVRPDIRLVRMH 825
Cdd:cd14007   232 LLQKDPSKRLSLEQVLNH 249
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
580-817 1.26e-19

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: 89.63  E-value: 1.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  580 RGNIVAMKKIHKksvditrsIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLA---NEDLHLDHmfI 656
Cdd:cd14060    17 QDKEVAVKKLLK--------IEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFDYLNsneSEEMDMDQ--I 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  657 SSLVSDILKGMIYLHDSEIIS--HGNLRSSNCLIDSRWVCQISDFGlhelkAGQEEPNKSELELKRAL-CMAPELLRDAy 733
Cdd:cd14060    87 MTWATDIAKGMHYLHMEAPVKviHRDLKSRNVVIAADGVLKICDFG-----ASRFHSHTTHMSLVGTFpWMAPEVIQSL- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  734 rPgrGSQKGDVYSFGILLYEMIGRKGPWGDtayskeeiIQFVKCPEMLQHGVFRPALTHThldIPDYIRKCLCQCWDEDP 813
Cdd:cd14060   161 -P--VSETCDTYSYGVVLWEMLTREVPFKG--------LEGLQVAWLVVEKNERPTIPSS---CPRSFAELMRRCWEADV 226

                  ....
gi 161076872  814 EVRP 817
Cdd:cd14060   227 KERP 230
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
581-820 1.90e-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: 89.44  E-value: 1.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKI--HKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLAN---------EDL 649
Cdd:cd08215    25 GKLYVLKEIdlSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEYADGGDLAQKIKKqkkkgqpfpEEQ 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  650 HLDhMFIsslvsDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL-HELkagqeepnKSELELKRALC----- 723
Cdd:cd08215   105 ILD-WFV-----QICLALKYLHSRKIL-HRDLKTQNIFLTKDGVVKLGDFGIsKVL--------ESTTDLAKTVVgtpyy 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  724 MAPELLRD-AYrpgrgSQKGDVYSFGILLYEMIGRKGPWgdTAYSKEEIIQfvkcpeMLQHGVFRPALTHTHLDIPDYIR 802
Cdd:cd08215   170 LSPELCENkPY-----NYKSDIWALGCVLYELCTLKHPF--EANNLPALVY------KIVKGQYPPIPSQYSSELRDLVN 236
                         250
                  ....*....|....*...
gi 161076872  803 KCLcqcwDEDPEVRPDIR 820
Cdd:cd08215   237 SML----QKDPEKRPSAN 250
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
598-833 1.94e-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: 89.74  E-value: 1.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  598 RSIRKELKLMREVRHENIINFIGASTDhGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSDILKGMIYLHDSEIIs 677
Cdd:cd14151    49 QAFKNEVGVLRKTRHVNILLFMGYSTK-PQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSII- 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  678 HGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRALCMAPELLR----DAYrpgrgSQKGDVYSFGILLYE 753
Cdd:cd14151   127 HRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRmqdkNPY-----SFQSDVYAFGIVLYE 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  754 MIGRKGPWGDTAySKEEIIqfvkcpEMLQHGVFRPALTHTHLDIPDYIRKCLCQCWDEDPEVRPDIRLVRMHLKELQAGL 833
Cdd:cd14151   202 LMTGQLPYSNIN-NRDQII------FMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSL 274
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
584-829 2.47e-19

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: 89.39  E-value: 2.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDITRSIRkELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANE--DLHLDHMFisSLVS 661
Cdd:cd05068    35 VAVKTLKPGTMDPEDFLR-EAQIMKKLRHPKLIQLYAVCTLEEPIYIITELMKHGSLLEYLQGKgrSLQLPQLI--DMAA 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  662 DILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSE---LELKRAlcmAPEllrdAYRPGRG 738
Cdd:cd05068   112 QVASGMAYLESQNYI-HRDLAARNVLVGENNICKVADFGLARVIKVEDEYEAREgakFPIKWT---APE----AANYNRF 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  739 SQKGDVYSFGILLYEMIGrkgpWGDTAY---SKEEIIQfvkcpeMLQHGVFRPALTHThldiPDYIRKCLCQCWDEDPEV 815
Cdd:cd05068   184 SIKSDVWSFGILLTEIVT----YGRIPYpgmTNAEVLQ------QVERGYRMPCPPNC----PPQLYDIMLECWKADPME 249
                         250
                  ....*....|....
gi 161076872  816 RPDIRLVRMHLKEL 829
Cdd:cd05068   250 RPTFETLQWKLEDF 263
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
580-829 2.87e-19

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: 88.74  E-value: 2.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  580 RGNIVAMKKIH------KKSVDItrsIRKELKLMREVRHENIINFIGASTDHGS-VIIFTTYCARGSLEDVLANEDLHLD 652
Cdd:cd14064    15 RNKIVAIKRYRantycsKSDVDM---FCREVSILCRLNHPCVIQFVGACLDDPSqFAIVTQYVSGGSLFSLLHEQKRVID 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  653 HMFISSLVSDILKGMIYLHDS-EIISHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSElELKRALCMAPELLRD 731
Cdd:cd14064    92 LQSKLIIAVDVAKGMEYLHNLtQPIIHRDLNSHNILLYEDGHAVVADFGESRFLQSLDEDNMTK-QPGNLRWMAPEVFTQ 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  732 AyrpGRGSQKGDVYSFGILLYEMIGRKGPWgdtAYSKEEiiqfVKCPEMLQHGVfRPALTHThldIPDYIRKCLCQCWDE 811
Cdd:cd14064   171 C---TRYSIKADVFSYALCLWELLTGEIPF---AHLKPA----AAAADMAYHHI-RPPIGYS---IPKPISSLLMRGWNA 236
                         250
                  ....*....|....*...
gi 161076872  812 DPEVRPDIRLVRMHLKEL 829
Cdd:cd14064   237 EPESRPSFVEIVALLEPC 254
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
581-818 3.36e-19

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: 88.80  E-value: 3.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKS-VDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLAnEDLHLDHMFISSL 659
Cdd:cd06623    26 GKIYALKKIHVDGdEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMDGGSLADLLK-KVGKIPEPVLAYI 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  660 VSDILKGMIYLH-DSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkagqeepnKSELELKRALC---------MAPELL 729
Cdd:cd06623   105 ARQILKGLDYLHtKRHII-HRDIKPSNLLINSKGEVKIADFGI-----------SKVLENTLDQCntfvgtvtyMSPERI 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  730 R-DAYrpgrgSQKGDVYSFGILLYEMIGRKGPwgdtaYSKEEIIQFvkcPEMLQHGVFRPAL----THTHLDIPDYIRKC 804
Cdd:cd06623   173 QgESY-----SYAADIWSLGLTLLECALGKFP-----FLPPGQPSF---FELMQAICDGPPPslpaEEFSPEFRDFISAC 239
                         250
                  ....*....|....
gi 161076872  805 LCQcwdeDPEVRPD 818
Cdd:cd06623   240 LQK----DPKKRPS 249
PBP1_NPR-like cd06373
Ligand binding domain of natriuretic peptide receptor (NPR) family; Ligand binding domain of ...
64-429 3.89e-19

Ligand binding domain of natriuretic peptide receptor (NPR) family; Ligand binding domain of natriuretic peptide receptor (NPR) family which consists of three different subtypes: type A natriuretic peptide receptor (NPR-A, or GC-A), type B natriuretic peptide receptors (NPR-B, or GC-B), and type C natriuretic peptide receptor (NPR-C). There are three types of natriuretic peptide (NP) ligands specific to the receptors: atrial NP (ANP), brain or B-type NP (BNP), and C-type NP (CNP). The NP family is thought to have arisen through gene duplication during evolution and plays an essential role in cardiovascular and body fluid homeostasis. ANP and BNP bind mainly to NPR-A, while CNP binds specifically to NPR-B. Both NPR-A and NPR-B have guanylyl cyclase catalytic activity and produces intracellular secondary messenger cGMP in response to peptide-ligand binding. Consequently, the NPR-A activation results in vasodilation and inhibition of vascular smooth muscle cell proliferation. NPR-C acts as the receptor for all the three members of NP family, and functions as a clearance receptor. Unlike NPR-A and -B, NPR-C lacks an intracellular guanylyl cyclase domain and is thought to exert biological actions by sequestration of released natriuretic peptides and/or inhibition of adenylyl cyclase.


Pssm-ID: 380596 [Multi-domain]  Cd Length: 394  Bit Score: 91.18  E-value: 3.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   64 LAIEDVNKNPnLLPGKKLAFKPVDIghKMSAYrVKPLRAMTQMREAGVTAFIGP--DESCTTEALLASAWNTPMLSFKCS 141
Cdd:cd06373    25 LALRRVERRG-FLPGWRFQVHYRDT--KCSDT-LAPLAAVDLYCAKKVDVFLGPvcEYALAPVARYAGHWNVPVLTAGGL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  142 DPIVSNKSTFHTFARTLAPASKVSKSVISLLNAFHWNKFSIVVSS---KPIWGSD---VARAIQELaearnFTISHFKYI 215
Cdd:cd06373   101 AAGFDDKTEYPLLTRMGGSYVKLGEFVLTLLRHFGWRRVALLYHDnlrRKAGNSNcyfTLEGIFNA-----LTGERDSIH 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  216 SDYIPTTKTLSQIDKIIEETYATTRIyVFIgehIAMVDFVRG--LQNRRL-LESGDYIVVSVDdeIYDSNRRVNIMERNY 292
Cdd:cd06373   176 KSFDEFDETKDDFEILLKRVSNSARI-VIL---CASPDTVREimLAAHELgMINGEYVFFNID--LFSSSSKGARPWYRE 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  293 LDPYIRKEKSKsldkISFRSVIKISMTYPQNPHIRDICSKIKDYARKTpflvpyhqrvFDNISVPIYGLHL-----YDSV 367
Cdd:cd06373   250 NDTDERNEKAR----KAYRALLTVTLRRPDSPEYRNFSEEVKERAKEK----------YNYFTYGDEEVNSfvgafHDAV 315
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161076872  368 MIYVRAITEVLRLGGDIYDGNLVMSHIFNRSYHSIQGfDVYIDSNGDAEGNYTVITLQNDVG 429
Cdd:cd06373   316 LLYALALNETLAEGGSPRNGTEITERMWNRTFEGITG-NVSIDANGDRNADYSLLDMNPVTG 376
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
584-817 3.99e-19

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: 88.62  E-value: 3.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANE--DLHLDHMFISSLVS 661
Cdd:cd06624    36 IAIKEIPERDSREVQPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGGSLSALLRSKwgPLKDNENTIGYYTK 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  662 DILKGMIYLHDSEIIsHGNLRSSNCLIDS-RWVCQISDFGLHELKAG---QEEPNKSELELkralcMAPELLRDAYRpGR 737
Cdd:cd06624   116 QILEGLKYLHDNKIV-HRDIKGDNVLVNTySGVVKISDFGTSKRLAGinpCTETFTGTLQY-----MAPEVIDKGQR-GY 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  738 GSQkGDVYSFGILLYEMIGRKGPwgdtayskeeiiqFVkcpEML--QHGVFRPALTHTHLDIPDYI----RKCLCQCWDE 811
Cdd:cd06624   189 GPP-ADIWSLGCTIIEMATGKPP-------------FI---ELGepQAAMFKVGMFKIHPEIPESLseeaKSFILRCFEP 251

                  ....*.
gi 161076872  812 DPEVRP 817
Cdd:cd06624   252 DPDKRA 257
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
581-825 4.45e-19

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: 88.38  E-value: 4.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSV--------------DITRSIRKELKLMREVRHENIINFIGA--STDHGSVIIFTTYCARGSLEDVL 644
Cdd:cd14008    18 GQLYAIKIFNKSRLrkrregkndrgkikNALDDVRREIAIMKKLDHPNIVRLYEVidDPESDKLYLVLEYCEGGPVMELD 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  645 ANEDL------HLDHMFIsslvsDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKagqeepNKSELEL 718
Cdd:cd14008    98 SGDRVpplpeeTARKYFR-----DLVLGLEYLHENGIV-HRDIKPENLLLTADGTVKISDFGVSEMF------EDGNDTL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  719 KRALC----MAPELLRDAYRPGRGSqKGDVYSFGILLYEMIGRKGPW-GDTAYSKEEIIQFVKCPEMlqhgvFRPALTHt 793
Cdd:cd14008   166 QKTAGtpafLAPELCDGDSKTYSGK-AADIWALGVTLYCLVFGRLPFnGDNILELYEAIQNQNDEFP-----IPPELSP- 238
                         250       260       270
                  ....*....|....*....|....*....|..
gi 161076872  794 hlDIPDYIRKCLCQcwdeDPEVRPDIRLVRMH 825
Cdd:cd14008   239 --ELKDLLRRMLEK----DPEKRITLKEIKEH 264
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
552-835 4.64e-19

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: 88.59  E-value: 4.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  552 KNIFQICRQSILVVGEPNKRSFTNI--ALFRGNIVAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHgSVI 629
Cdd:cd05070     1 KDVWEIPRESLQLIKRLGNGQFGEVwmGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEE-PIY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  630 IFTTYCARGSLEDVLAN-EDLHLDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQ 708
Cdd:cd05070    80 IVTEYMSKGSLLDFLKDgEGRALKLPNLVDMAAQVAAGMAYIERMNYI-HRDLRSANILVGNGLICKIADFGLARLIEDN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  709 EEPNK--SELELKRAlcmAPEllrdAYRPGRGSQKGDVYSFGILLYEMIgRKGPWGDTAYSKEEIIqfvkcpEMLQHGVF 786
Cdd:cd05070   159 EYTARqgAKFPIKWT---APE----AALYGRFTIKSDVWSFGILLTELV-TKGRVPYPGMNNREVL------EQVERGYR 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 161076872  787 RPALThthlDIPDYIRKCLCQCWDEDPEVRPDIRLVRMHLKELQAGLKP 835
Cdd:cd05070   225 MPCPQ----DCPISLHELMIHCWKKDPEERPTFEYLQGFLEDYFTATEP 269
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
555-858 4.77e-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: 88.56  E-value: 4.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  555 FQICRQSILVVGEPNKRSFTNIAL-FRGNI--VAMKKIHKKSVDItRSIRKELKLMREVRHENIINFIGASTDHGSVIIF 631
Cdd:cd05072     2 WEIPRESIKLVKKLGAGQFGEVWMgYYNNStkVAVKTLKPGTMSV-QAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  632 TTYCARGSLEDVLANED---LHLDHMFISSlvSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQ 708
Cdd:cd05072    81 TEYMAKGSLLDFLKSDEggkVLLPKLIDFS--AQIAEGMAYIERKNYI-HRDLRAANVLVSESLMCKIADFGLARVIEDN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  709 EEPNK--SELELKRAlcmAPEllrdAYRPGRGSQKGDVYSFGILLYEMIgrkgPWGDTAY---SKEEIIQfvkcpeMLQH 783
Cdd:cd05072   158 EYTARegAKFPIKWT---APE----AINFGSFTIKSDVWSFGILLYEIV----TYGKIPYpgmSNSDVMS------ALQR 220
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161076872  784 GVFRPALThthlDIPDYIRKCLCQCWDEDPEVRPdirlvrmhlkelqaglkpnIFDNMLSIMEKYAYNLEGLVQE 858
Cdd:cd05072   221 GYRMPRME----NCPDELYDIMKTCWKEKAEERP-------------------TFDYLQSVLDDFYTATEGQYQQ 272
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
603-826 8.94e-19

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: 87.29  E-value: 8.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  603 ELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSDILKGMIYLHDSEIIsHGNLR 682
Cdd:cd05084    44 EARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDFLTFLRTEGPRLKVKELIRMVENAAAGMEYLESKHCI-HRDLA 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  683 SSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRALCMAPEllrdAYRPGRGSQKGDVYSFGILLYEMIGRkgpwG 762
Cdd:cd05084   123 ARNCLVTEKNVLKISDFGMSREEEDGVYAATGGMKQIPVKWTAPE----ALNYGRYSSESDVWSFGILLWETFSL----G 194
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161076872  763 DTAY-------SKEEIIQFVK--CPEmlqhgvfrpalththlDIPDYIRKCLCQCWDEDPEVRPDIRLVRMHL 826
Cdd:cd05084   195 AVPYanlsnqqTREAVEQGVRlpCPE----------------NCPDEVYRLMEQCWEYDPRKRPSFSTVHQDL 251
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
581-830 1.02e-18

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


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 88.03  E-value: 1.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHG--SVIIFTTYCARGSLEDVLANEDLHLDHMFISS 658
Cdd:cd05081    33 GALVAVKQLQHSGPDQQRDFQREIQILKALHSDFIVKYRGVSYGPGrrSLRLVMEYLPSGCLRDFLQRHRARLDASRLLL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  659 LVSDILKGMIYLhDSEIISHGNLRSSNCLIDSRWVCQISDFGLHELKAGQE------EPNKSELelkraLCMAPELLRDA 732
Cdd:cd05081   113 YSSQICKGMEYL-GSRRCVHRDLAARNILVESEAHVKIADFGLAKLLPLDKdyyvvrEPGQSPI-----FWYAPESLSDN 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  733 YRpgrgSQKGDVYSFGILLYEMIgrkgPWGDTAYS-KEEIIQFVKCP----------EMLQHGVFRPALThthlDIPDYI 801
Cdd:cd05081   187 IF----SRQSDVWSFGVVLYELF----TYCDKSCSpSAEFLRMMGCErdvpalcrllELLEEGQRLPAPP----ACPAEV 254
                         250       260
                  ....*....|....*....|....*....
gi 161076872  802 RKCLCQCWDEDPEVRPDIRLVRMHLKELQ 830
Cdd:cd05081   255 HELMKLCWAPSPQDRPSFSALGPQLDMLW 283
PBP1_NPR_A cd06385
Ligand-binding domain of type A natriuretic peptide receptor; Ligand-binding domain of type A ...
64-420 1.27e-18

Ligand-binding domain of type A natriuretic peptide receptor; Ligand-binding domain of type A natriuretic peptide receptor (NPR-A). NPR-A is one of three known single membrane-spanning natriuretic peptide receptors that regulate blood volume, blood pressure, ventricular hypertrophy, pulmonary hypertension, fat metabolism, and long bone growth. In mammals there are three natriuretic peptides: ANP, BNP, and CNP. NPR-A is highly expressed in kidney, adrenal, terminal ileum, adipose, aortic, and lung tissues. The rank order of NPR-A activation by natriuretic peptides is ANP>BNP>>CNP. Single allele-inactivating mutations in the promoter of human NPR-A are associated with hypertension and heart failure.


Pssm-ID: 380608 [Multi-domain]  Cd Length: 408  Bit Score: 89.87  E-value: 1.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   64 LAIEDVNKNPNLLPGK--KLAFKPVDIGHKMSAYRVKPLRAMTQMREAGVTAFIGP--DESCTTEALLASAWNTPMLSFK 139
Cdd:cd06385    26 LALERVNARPDLLPGWhvRTVLGSSENKEGVCSDSTAPLVAVDLKFEHHPAVFLGPgcVYTAAPVARFTAHWRVPLLTAG 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  140 CSDPIVSNKSTFHTFARTLAPASKVSKSVISLLNAFHWNKFSIVV------SSKPIWGSdVARAIQELAEARNFTISHFK 213
Cdd:cd06385   106 APALGFGVKDEYALTTRTGPSHKKLGEFVARLHRRYGWERRALLVyadrkgDDRPCFFA-VEGLYMQLRRRLNITVDDLV 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  214 YISDyipttkTLSQIDKIIEETYATTR-IYVfigehIAMVDFVRGLQN---RRLLESGDYIVVSVD-------DEIYDSN 282
Cdd:cd06385   185 FNED------EPLNYTELLRDIRQKGRvIYV-----CCSPDTFRKLMLqawREGLCGEDYAFFYIDifgaslqSGQFPDP 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  283 RRvnimernyldPYIRKEKSKSLDKISFRSVIKISMTYPQNPHIRDICSKIKDYARKtpflvPYHQRVFDNISVPIYGlH 362
Cdd:cd06385   254 QR----------PWERGDADDNSAREAFQAVKIITYKEPDNPEYKEFLKQLKTEAME-----MFNFTVEDGLMNLIAA-S 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 161076872  363 LYDSVMIYVRAITEVLRLGGDIYDGNLVMSHIFNRSYHSIQGFdVYIDSNGDAEGNYT 420
Cdd:cd06385   318 FHDGVLLYAHAVNETLAHGGTVTNGSAITQRMWNRSFYGVTGY-VKIDENGDRETDFS 374
Pkinase pfam00069
Protein kinase domain;
580-817 1.53e-18

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 85.76  E-value: 1.53e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   580 RGNIVAMKKIHKKSVD--ITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLaNEDLHLDHMFIS 657
Cdd:pfam00069   23 TGKIVAIKKIKKEKIKkkKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYVEGGSLFDLL-SEKGAFSEREAK 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   658 SLVSDILKGMiylhdseiiSHGNLRSSNClIDSRWvcqisdfglhelkagqeepnkselelkralcMAPELLRD-AYrpg 736
Cdd:pfam00069  102 FIMKQILEGL---------ESGSSLTTFV-GTPWY-------------------------------MAPEVLGGnPY--- 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   737 rgSQKGDVYSFGILLYEMIGRKGPWGDtAYSKEEIIQFVKCPEMLQHGVFRpalththldIPDYIRKCLCQCWDEDPEVR 816
Cdd:pfam00069  138 --GPKVDVWSLGCILYELLTGKPPFPG-INGNEIYELIIDQPYAFPELPSN---------LSEEAKDLLKKLLKKDPSKR 205

                   .
gi 161076872   817 P 817
Cdd:pfam00069  206 L 206
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
578-755 2.81e-18

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: 86.78  E-value: 2.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  578 LFRGNI----VAMKKIHKKSV----DITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLA--NE 647
Cdd:cd14158    31 VFKGYIndknVAVKKLAAMVDisteDLTKQFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMPNGSLLDRLAclND 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  648 DLHLDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRALCMAPE 727
Cdd:cd14158   111 TPPLSWHMRCKIAQGTANGINYLHENNHI-HRDIKSANILLDETFVPKISDFGLARASEKFSQTIMTERIVGTTAYMAPE 189
                         170       180
                  ....*....|....*....|....*...
gi 161076872  728 LLRdayrpGRGSQKGDVYSFGILLYEMI 755
Cdd:cd14158   190 ALR-----GEITPKSDIFSFGVVLLEII 212
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
603-820 3.11e-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: 86.70  E-value: 3.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  603 ELKLMREV-RHENIINFIGASTDHGSVIIFTTYCARGSLEDVL---------ANEDL---HLDHMFISSLVS---DILKG 666
Cdd:cd05053    66 EMEMMKMIgKHKNIINLLGACTQDGPLYVVVEYASKGNLREFLrarrppgeeASPDDprvPEEQLTQKDLVSfayQVARG 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  667 MIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL----HELKAGQEEPNkSELELKralCMAPELLRD-AYrpgrgSQK 741
Cdd:cd05053   146 MEYLASKKCI-HRDLAARNVLVTEDNVMKIADFGLardiHHIDYYRKTTN-GRLPVK---WMAPEALFDrVY-----THQ 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  742 GDVYSFGILLYEMIgrkgPWGDTAY---SKEEIIQFVKCPEMLQhgvfRPALThthldiPDYIRKCLCQCWDEDPEVRPD 818
Cdd:cd05053   216 SDVWSFGVLLWEIF----TLGGSPYpgiPVEELFKLLKEGHRME----KPQNC------TQELYMLMRDCWHEVPSQRPT 281

                  ..
gi 161076872  819 IR 820
Cdd:cd05053   282 FK 283
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
581-818 3.20e-18

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: 85.86  E-value: 3.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHkksVDITRSIRK----ELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLAN-----EDLhL 651
Cdd:cd06605    26 GQIMAVKVIR---LEIDEALQKqilrELDVLHKCNSPYIVGFYGAFYSEGDISICMEYMDGGSLDKILKEvgripERI-L 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  652 DHMFISslvsdILKGMIYLHDSEIISHGNLRSSNCLIDSRWVCQISDFGLhelkAGQEEPNKSELELKRALCMAPELLrd 731
Cdd:cd06605   102 GKIAVA-----VVKGLIYLHEKHKIIHRDVKPSNILVNSRGQVKLCDFGV----SGQLVDSLAKTFVGTRSYMAPERI-- 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  732 ayRPGRGSQKGDVYSFGILLYEMIGRKGPWGD-TAYSKEEIIQFVKC-----PEMLQHGVFRPALTHThldipdyirkcL 805
Cdd:cd06605   171 --SGGKYTVKSDIWSLGLSLVELATGRFPYPPpNAKPSMMIFELLSYivdepPPLLPSGKFSPDFQDF-----------V 237
                         250
                  ....*....|...
gi 161076872  806 CQCWDEDPEVRPD 818
Cdd:cd06605   238 SQCLQKDPTERPS 250
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
577-829 3.53e-18

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: 85.52  E-value: 3.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  577 ALFRGNIVAMKKI---HKKSVDITR-SIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLD 652
Cdd:cd14061    13 GIWRGEEVAVKAArqdPDEDISVTLeNVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGGALNRVLAGRKIPPH 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  653 HMFISSLvsDILKGMIYLHDSEIIS--HGNLRSSNCLIDSRW--------VCQISDFGLhelkaGQEEPNKSELELKRAL 722
Cdd:cd14061    93 VLVDWAI--QIARGMNYLHNEAPVPiiHRDLKSSNILILEAIenedlenkTLKITDFGL-----AREWHKTTRMSAAGTY 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  723 C-MAPELLRDAyrpgRGSQKGDVYSFGILLYEMIGrkgpwGDTAYSKEEIIQFVkcpemlqHGVFRPALThthLDIPDY- 800
Cdd:cd14061   166 AwMAPEVIKSS----TFSKASDVWSYGVLLWELLT-----GEVPYKGIDGLAVA-------YGVAVNKLT---LPIPSTc 226
                         250       260       270
                  ....*....|....*....|....*....|..
gi 161076872  801 ---IRKCLCQCWDEDPEVRPDIRLVRMHLKEL 829
Cdd:cd14061   227 pepFAQLMKDCWQPDPHDRPSFADILKQLENI 258
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
576-757 4.83e-18

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: 85.79  E-value: 4.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  576 IALFRGNIVAMKKIHKKSvdiTRSIRKELKLMREV--RHENIINFIGAS-TDHGSV---IIFTTYCARGSLEDVLANEDL 649
Cdd:cd14056    13 LGKYRGEKVAVKIFSSRD---EDSWFRETEIYQTVmlRHENILGFIAADiKSTGSWtqlWLITEYHEHGSLYDYLQRNTL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  650 HLDHMFisSLVSDILKGMIYLHdSEI--------ISHGNLRSSNCLIDSRWVCQISDFGL---HELKAGQ-EEPNKSELE 717
Cdd:cd14056    90 DTEEAL--RLAYSAASGLAHLH-TEIvgtqgkpaIAHRDLKSKNILVKRDGTCCIADLGLavrYDSDTNTiDIPPNPRVG 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 161076872  718 LKRAlcMAPELLRDAYRPGRGSQ--KGDVYSFGILLYEMIGR 757
Cdd:cd14056   167 TKRY--MAPEVLDDSINPKSFESfkMADIYSFGLVLWEIARR 206
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
581-817 5.16e-18

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: 85.01  E-value: 5.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSvDITrSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLV 660
Cdd:cd06612    28 GQVVAIKVVPVEE-DLQ-EIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYCGAGSVSDIMKITNKTLTEEEIAAIL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkAGQ--EEPNKSELELKRALCMAPE-LLRDAYrpgr 737
Cdd:cd06612   106 YQTLKGLEYLHSNKKI-HRDIKAGNILLNEEGQAKLADFGV----SGQltDTMAKRNTVIGTPFWMAPEvIQEIGY---- 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  738 gSQKGDVYSFGILLYEMIGRKGPWGDtayskeeiIQFVKCPEMLQHgvfRPALThthLDIP--------DYIRKCLCQcw 809
Cdd:cd06612   177 -NNKADIWSLGITAIEMAEGKPPYSD--------IHPMRAIFMIPN---KPPPT---LSDPekwspefnDFVKKCLVK-- 239

                  ....*...
gi 161076872  810 deDPEVRP 817
Cdd:cd06612   240 --DPEERP 245
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
584-827 6.71e-18

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


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 85.50  E-value: 6.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKK-SVDITRSIRKELKLMREVRHENIINFIGAST-DHGSVIIFTtYCARGSL----------EDVLANEDLH- 650
Cdd:cd05048    38 VAIKTLKENaSPKTQQDFRREAELMSDLQHPNIVCLLGVCTkEQPQCMLFE-YMAHGDLheflvrhsphSDVGVSSDDDg 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  651 ----LDHMFISSLVSDILKGMIYLhDSEIISHGNLRSSNCLIDSRWVCQISDFGLHELKAGQE---EPNKSELELKralC 723
Cdd:cd05048   117 tassLDQSDFLHIAIQIAAGMEYL-SSHHYVHRDLAARNCLVGDGLTVKISDFGLSRDIYSSDyyrVQSKSLLPVR---W 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  724 MAPEllrdAYRPGRGSQKGDVYSFGILLYEMI--GRKGPWGdtaYSKEEIIQFVK------CPEmlqhgvfrpalththl 795
Cdd:cd05048   193 MPPE----AILYGKFTTESDVWSFGVVLWEIFsyGLQPYYG---YSNQEVIEMIRsrqllpCPE---------------- 249
                         250       260       270
                  ....*....|....*....|....*....|..
gi 161076872  796 DIPDYIRKCLCQCWDEDPEVRPDIRLVRMHLK 827
Cdd:cd05048   250 DCPARVYSLMVECWHEIPSRRPRFKEIHTRLR 281
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
579-761 7.27e-18

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: 84.74  E-value: 7.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  579 FRGNIVAMKKIHKKsvdiTRSIRKELKLMREVR-------HENIINFIGASTDHGSVIIFTTYCARGSLEDVLAN--EDL 649
Cdd:cd13997    23 VDGCLYAVKKSKKP----FRGPKERARALREVEahaalgqHPNIVRYYSSWEEGGHLYIQMELCENGSLQDALEElsPIS 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  650 HLDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL-HEL-KAGQEEPNKSELelkralcMAPE 727
Cdd:cd13997    99 KLSEAEVWDLLLQVALGLAFIHSKGIV-HLDIKPDNIFISNKGTCKIGDFGLaTRLeTSGDVEEGDSRY-------LAPE 170
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 161076872  728 LLRDAYRPgrgSQKGDVYSFGILLYEMIG-----RKGPW 761
Cdd:cd13997   171 LLNENYTH---LPKADIFSLGVTVYEAATgeplpRNGQQ 206
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
573-818 7.82e-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: 84.72  E-value: 7.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  573 FTNIALFRGNIVAMKKIH--KKSVDItRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVL--ANED 648
Cdd:cd06610    18 YAAYCLPKKEKVAIKRIDleKCQTSM-DELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPLLSGGSLLDIMksSYPR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  649 LHLDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGlheLKAGQEEPNKSELELKRAL----C- 723
Cdd:cd06610    97 GGLDEAIIATVLKEVLKGLEYLHSNGQI-HRDVKAGNILLGEDGSVKIADFG---VSASLATGGDRTRKVRKTFvgtpCw 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  724 MAPELLrdayRPGRG-SQKGDVYSFGILLYEMIGRKGPWGDTAYSKEEIIQFVKCPEMLQHGVFRPALTHThldIPDYIR 802
Cdd:cd06610   173 MAPEVM----EQVRGyDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNDPPSLETGADYKKYSKS---FRKMIS 245
                         250
                  ....*....|....*.
gi 161076872  803 KCLCQcwdeDPEVRPD 818
Cdd:cd06610   246 LCLQK----DPSKRPT 257
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
581-825 8.33e-18

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: 84.79  E-value: 8.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIH------KKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHM 654
Cdd:cd06630    25 GTLMAVKQVSfcrnssSEQEEVVEAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMAGGSVASLLSKYGAFSENV 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  655 FISSLVSdILKGMIYLHDSEIIsHGNLRSSNCLIDSR-WVCQISDFGLHELKAGQeepNKSELELKRALC-----MAPEL 728
Cdd:cd06630   105 IINYTLQ-ILRGLAYLHDNQII-HRDLKGANLLVDSTgQRLRIADFGAAARLASK---GTGAGEFQGQLLgtiafMAPEV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  729 LR-DAYrpGRGSqkgDVYSFGILLYEMIGRKGPWGDTAYSKEEIIqfvkcpemlqhgVFRPALTHTHLDIPDY----IRK 803
Cdd:cd06630   180 LRgEQY--GRSC---DVWSVGCVIIEMATAKPPWNAEKISNHLAL------------IFKIASATTPPPIPEHlspgLRD 242
                         250       260
                  ....*....|....*....|..
gi 161076872  804 CLCQCWDEDPEVRPDIRLVRMH 825
Cdd:cd06630   243 VTLRCLELQPEDRPPARELLKH 264
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
577-816 1.43e-17

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: 84.41  E-value: 1.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  577 ALFRGNIVAMKKIhkkSVDITRSIRKELKLMREV--RHENIINFIGA---STDHGSVIIFTT-YCARGSLEDVLANEDLH 650
Cdd:cd13998    14 ASLKNEPVAVKIF---SSRDKQSWFREKEIYRTPmlKHENILQFIAAderDTALRTELWLVTaFHPNGSL*DYLSLHTID 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  651 LDHMFisSLVSDILKGMIYLHdSEI---------ISHGNLRSSNCLIDSRWVCQISDFGL---HELKAGQEE-PNKSELE 717
Cdd:cd13998    91 WVSLC--RLALSVARGLAHLH-SEIpgctqgkpaIAHRDLKSKNILVKNDGTCCIADFGLavrLSPSTGEEDnANNGQVG 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  718 LKRAlcMAPELLRDAYRPGRGS--QKGDVYSFGILLYEMIGR----KGPWGDTAYSKEEIIQFVKCPEMLQHGV----FR 787
Cdd:cd13998   168 TKRY--MAPEVLEGAINLRDFEsfKRVDIYAMGLVLWEMASRctdlFGIVEEYKPPFYSEVPNHPSFEDMQEVVvrdkQR 245
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 161076872  788 PalththlDIPDYIRKC-----LC----QCWDEDPEVR 816
Cdd:cd13998   246 P-------NIPNRWLSHpglqsLAetieECWDHDAEAR 276
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
581-818 1.48e-17

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: 84.23  E-value: 1.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFIsSLV 660
Cdd:cd14222    18 GKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKDFLRADDPFPWQQKV-SFA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHEL------KAGQEEPNKSELELKR------------AL 722
Cdd:cd14222    97 KGIASGMAYLHSMSII-HRDLNSHNCLIKLDKTVVVADFGLSRLiveekkKPPPDKPTTKKRTLRKndrkkrytvvgnPY 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  723 CMAPELLRDAyrpgRGSQKGDVYSFGILLYEMIGRkgpwgdtAYSKEEIIqfvkcPEMLQHGV--------FRPAlthth 794
Cdd:cd14222   176 WMAPEMLNGK----SYDEKVDIFSFGIVLCEIIGQ-------VYADPDCL-----PRTLDFGLnvrlfwekFVPK----- 234
                         250       260
                  ....*....|....*....|....
gi 161076872  795 lDIPDYIRKCLCQCWDEDPEVRPD 818
Cdd:cd14222   235 -DCPPAFFPLAAICCRLEPDSRPA 257
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
577-831 1.57e-17

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: 83.88  E-value: 1.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  577 ALFRGNIVAMKKI-HKKSVDIT---RSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHlD 652
Cdd:cd14148    13 GLWRGEEVAVKAArQDPDEDIAvtaENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGALNRALAGKKVP-P 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  653 HMFISSLVSdILKGMIYLHDSEI--ISHGNLRSSNCLIDSRW--------VCQISDFGLhelkaGQEEPNKSELELKRAL 722
Cdd:cd14148    92 HVLVNWAVQ-IARGMNYLHNEAIvpIIHRDLKSSNILILEPIenddlsgkTLKITDFGL-----AREWHKTTKMSAAGTY 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  723 C-MAPELLRDAYRpgrgSQKGDVYSFGILLYEMIGRKGPWgdtayskEEIIQFVkcpemLQHGVFRPALThthLDI---- 797
Cdd:cd14148   166 AwMAPEVIRLSLF----SKSSDVWSFGVLLWELLTGEVPY-------REIDALA-----VAYGVAMNKLT---LPIpstc 226
                         250       260       270
                  ....*....|....*....|....*....|....
gi 161076872  798 PDYIRKCLCQCWDEDPEVRPDIRLVrmhLKELQA 831
Cdd:cd14148   227 PEPFARLLEECWDPDPHGRPDFGSI---LKRLED 257
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
598-817 2.49e-17

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: 83.31  E-value: 2.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  598 RSIRKELKLMREVRHENIINFIGASTDHGSVIIftTYCARGSLEDVLANEDLHLDHMFisSLVSDILKGMIYLHD-SEII 676
Cdd:cd14025    40 MELLEEAKKMEMAKFRHILPVYGICSEPVGLVM--EYMETGSLEKLLASEPLPWELRF--RIIHETAVGMNFLHCmKPPL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  677 SHGNLRSSNCLIDSRWVCQISDFGLHELkagQEEPNKSELELKrALC-----MAPELLRDAYRPgrGSQKGDVYSFGILL 751
Cdd:cd14025   116 LHLDLKPANILLDAHYHVKISDFGLAKW---NGLSHSHDLSRD-GLRgtiayLPPERFKEKNRC--PDTKHDVYSFAIVI 189
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161076872  752 YEMIGRKGPWGDTAYSKEEIIQFVKcpemlqhGVfRPALTHTHLDIPDYIRKCLC---QCWDEDPEVRP 817
Cdd:cd14025   190 WGILTQKKPFAGENNILHIMVKVVK-------GH-RPSLSPIPRQRPSECQQMIClmkRCWDQDPRKRP 250
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
584-817 2.71e-17

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: 82.99  E-value: 2.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDITRSIrKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSDI 663
Cdd:cd05114    31 VAIKAIREGAMSEEDFI-EEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENGCLLNYLRQRRGKLSRDMLLSMCQDV 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  664 LKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRALCmAPELlrdaYRPGRGSQKGD 743
Cdd:cd05114   110 CEGMEYLERNNFI-HRDLAARNCLVNDTGVVKVSDFGMTRYVLDDQYTSSSGAKFPVKWS-PPEV----FNYSKFSSKSD 183
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161076872  744 VYSFGILLYEMIGR-KGPWgdTAYSKEEIIQFVKcpemLQHGVFRPALThthldiPDYIRKCLCQCWDEDPEVRP 817
Cdd:cd05114   184 VWSFGVLMWEVFTEgKMPF--ESKSNYEVVEMVS----RGHRLYRPKLA------SKSVYEVMYSCWHEKPEGRP 246
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
603-817 3.09e-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: 83.10  E-value: 3.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  603 ELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSDILKGMIYLHDSEIIsHGNLR 682
Cdd:cd05063    56 EASIMGQFSHHNIIRLEGVVTKFKPAMIITEYMENGALDKYLRDHDGEFSSYQLVGMLRGIAAGMKYLSDMNYV-HRDLA 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  683 SSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRAL-CMAPELLrdAYRpgRGSQKGDVYSFGILLYEMIGrkgpW 761
Cdd:cd05063   135 ARNILVNSNLECKVSDFGLSRVLEDDPEGTYTTSGGKIPIrWTAPEAI--AYR--KFTSASDVWSFGIVMWEVMS----F 206
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 161076872  762 GDTAY---SKEEIIQfvkcpeMLQHGVFRPAlthtHLDIPDYIRKCLCQCWDEDPEVRP 817
Cdd:cd05063   207 GERPYwdmSNHEVMK------AINDGFRLPA----PMDCPSAVYQLMLQCWQQDRARRP 255
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
584-837 3.95e-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: 83.16  E-value: 3.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDhGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSDI 663
Cdd:cd14149    39 VKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTK-DNLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQT 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  664 LKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRALCMAPELLRdAYRPGRGSQKGD 743
Cdd:cd14149   118 AQGMDYLHAKNII-HRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSILWMAPEVIR-MQDNNPFSFQSD 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  744 VYSFGILLYEMIGRKGPWGDTAySKEEIIQfvkcpeMLQHGVFRPALTHTHLDIPDYIRKCLCQCWDEDPEVRPDIRLVR 823
Cdd:cd14149   196 VYSYGIVLYELMTGELPYSHIN-NRDQIIF------MVGRGYASPDLSKLYKNCPKAMKRLVADCIKKVKEERPLFPQIL 268
                         250
                  ....*....|....
gi 161076872  824 MHLKELQAGLkPNI 837
Cdd:cd14149   269 SSIELLQHSL-PKI 281
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
584-835 6.01e-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: 6.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIhKKSVDITRSIRKELKLMREVRHENIINFIGASTDHgSVIIFTTYCARGSLEDVLANED-LHLDHMFISSLVSD 662
Cdd:cd05069    39 VAIKTL-KPGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEE-PIYIVTEFMGKGSLLDFLKEGDgKYLKLPQLVDMAAQ 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  663 ILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNK--SELELKRAlcmAPEllrdAYRPGRGSQ 740
Cdd:cd05069   117 IADGMAYIERMNYI-HRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARqgAKFPIKWT---APE----AALYGRFTI 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  741 KGDVYSFGILLYEMIgRKGPWGDTAYSKEEIIQFVK------CPEmlqhgvfrpalththlDIPDYIRKCLCQCWDEDPE 814
Cdd:cd05069   189 KSDVWSFGILLTELV-TKGRVPYPGMVNREVLEQVErgyrmpCPQ----------------GCPESLHELMKLCWKKDPD 251
                         250       260
                  ....*....|....*....|.
gi 161076872  815 VRPDIRLVRMHLKELQAGLKP 835
Cdd:cd05069   252 ERPTFEYIQSFLEDYFTATEP 272
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
602-830 6.09e-17

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: 82.81  E-value: 6.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  602 KELKLMREVRHENIINFIGAStDHGSVI-----IFTTYCARGSLEDVLANEDLHLDHMfiSSLVSDILKGMIYLHdSEI- 675
Cdd:cd14055    44 KDIFTDASLKHENILQFLTAE-ERGVGLdrqywLITAYHENGSLQDYLTRHILSWEDL--CKMAGSLARGLAHLH-SDRt 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  676 --------ISHGNLRSSNCLIDSRWVCQISDFGLhelkAGQEEPNKSELELKR------ALCMAPELL--RDAYRPGRGS 739
Cdd:cd14055   120 pcgrpkipIAHRDLKSSNILVKNDGTCVLADFGL----ALRLDPSLSVDELANsgqvgtARYMAPEALesRVNLEDLESF 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  740 QKGDVYSFGILLYEMIGR----------KGPWGDTAYSKeeiiqfvKCPEMLQ----HGVFRPalththlDIPDYIRK-- 803
Cdd:cd14055   196 KQIDVYSMALVLWEMASRceasgevkpyELPFGSKVRER-------PCVESMKdlvlRDRGRP-------EIPDSWLThq 261
                         250       260       270
                  ....*....|....*....|....*....|....
gi 161076872  804 ---CLC----QCWDEDPEVRPDIRLVRMHLKELQ 830
Cdd:cd14055   262 gmcVLCdtitECWDHDPEARLTASCVAERFNELK 295
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
584-818 8.78e-17

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: 82.53  E-value: 8.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKS-VDITRSIRKELKLMREV-RHENIINFIGASTDHGSVIIFTTYCARGSLEDVL-ANEDLHLDHMFISSLV 660
Cdd:cd05055    68 VAVKMLKPTAhSSEREALMSELKIMSHLgNHENIVNLLGACTIGGPILVITEYCCYGDLLNFLrRKRESFLTLEDLLSFS 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL-HELKAGQEEPNK--SELELKralCMAPE-LLRDAYrpg 736
Cdd:cd05055   148 YQVAKGMAFLASKNCI-HRDLAARNVLLTHGKIVKICDFGLaRDIMNDSNYVVKgnARLPVK---WMAPEsIFNCVY--- 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  737 rgSQKGDVYSFGILLYEMIGrkgpWGDTAYSkeEIIQFVKCPEMLQHG--VFRPALThthldiPDYIRKCLCQCWDEDPE 814
Cdd:cd05055   221 --TFESDVWSYGILLWEIFS----LGSNPYP--GMPVDSKFYKLIKEGyrMAQPEHA------PAEIYDIMKTCWDADPL 286

                  ....
gi 161076872  815 VRPD 818
Cdd:cd05055   287 KRPT 290
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
577-831 1.90e-16

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: 80.85  E-value: 1.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  577 ALFRGNIVAMKKIHKK-SVDIT---RSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLD 652
Cdd:cd14146    13 ATWKGQEVAVKAARQDpDEDIKataESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGTLNRALAAANAAPG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  653 ---------HMFISSLVSdILKGMIYLHDSEI--ISHGNLRSSNCL----IDSRWVC----QISDFGLhelkaGQEEPNK 713
Cdd:cd14146    93 prrarrippHILVNWAVQ-IARGMLYLHEEAVvpILHRDLKSSNILllekIEHDDICnktlKITDFGL-----AREWHRT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  714 SELELKRALC-MAPELLRDAYRpgrgSQKGDVYSFGILLYEMIGrkgpwGDTAYSKEEIIQfvkcpemLQHGVFRPALTh 792
Cdd:cd14146   167 TKMSAAGTYAwMAPEVIKSSLF----SKGSDIWSYGVLLWELLT-----GEVPYRGIDGLA-------VAYGVAVNKLT- 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 161076872  793 thLDI----PDYIRKCLCQCWDEDPEVRPDIRLVrmhLKELQA 831
Cdd:cd14146   230 --LPIpstcPEPFAKLMKECWEQDPHIRPSFALI---LEQLTA 267
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
579-754 1.92e-16

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: 80.37  E-value: 1.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  579 FRGNIVAMKKIHK--KSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYcARGSLEDVLanEDlhlDHMFI 656
Cdd:cd14002    24 YTGQVVALKFIPKrgKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEY-AQGELFQIL--ED---DGTLP 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  657 SSLVSDILKGMI----YLHDSEIIsHGNLRSSNCLIDSRWVCQISDFG-----------LHELKAgqeEPnkselelkra 721
Cdd:cd14002    98 EEEVRSIAKQLVsalhYLHSNRII-HRDMKPQNILIGKGGVVKLCDFGfaramscntlvLTSIKG---TP---------- 163
                         170       180       190
                  ....*....|....*....|....*....|...
gi 161076872  722 LCMAPELLRDayRPgrGSQKGDVYSFGILLYEM 754
Cdd:cd14002   164 LYMAPELVQE--QP--YDHTADLWSLGCILYEL 192
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
598-817 2.12e-16

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: 80.68  E-value: 2.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  598 RSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSDILKGMIYLHDSEIIs 677
Cdd:cd05066    50 RDFLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEYMENGSLDAFLRKHDGQFTVIQLVGMLRGIASGMKYLSDMGYV- 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  678 HGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRAL-CMAPELLrdAYRpgRGSQKGDVYSFGILLYEMIG 756
Cdd:cd05066   129 HRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEAAYTTRGGKIPIrWTAPEAI--AYR--KFTSASDVWSYGIVMWEVMS 204
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161076872  757 rkgpWGDTAY---SKEEIIQFVkcpemlQHGVFRPAlthtHLDIPDYIRKCLCQCWDEDPEVRP 817
Cdd:cd05066   205 ----YGERPYwemSNQDVIKAI------EEGYRLPA----PMDCPAALHQLMLDCWQKDRNERP 254
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
602-835 2.14e-16

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: 80.89  E-value: 2.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  602 KELKLMREVRHENIINFIGASTDHgSVIIFTTYCARGSLEDVLANED---LHLDHMFisSLVSDILKGMIYLHDSEIIsH 678
Cdd:cd05071    53 QEAQVMKKLRHEKLVQLYAVVSEE-PIYIVTEYMSKGSLLDFLKGEMgkyLRLPQLV--DMAAQIASGMAYVERMNYV-H 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  679 GNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNK--SELELKRAlcmAPEllrdAYRPGRGSQKGDVYSFGILLYEMiG 756
Cdd:cd05071   129 RDLRAANILVGENLVCKVADFGLARLIEDNEYTARqgAKFPIKWT---APE----AALYGRFTIKSDVWSFGILLTEL-T 200
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161076872  757 RKGPWGDTAYSKEEIIqfvkcpEMLQHGVFRPALThthlDIPDYIRKCLCQCWDEDPEVRPDIRLVRMHLKELQAGLKP 835
Cdd:cd05071   201 TKGRVPYPGMVNREVL------DQVERGYRMPCPP----ECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEP 269
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
582-754 2.36e-16

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: 80.42  E-value: 2.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  582 NIVAMKKIHK-KSVDITRSIRkelkLMREVRHENIINFIG--ASTDHGSVIifTTYCARGSLEDVLAnEDLHLDHMFISS 658
Cdd:cd14010    26 EFVAIKCVDKsKRPEVLNEVR----LTHELKHPNVLKFYEwyETSNHLWLV--VEYCTGGDLETLLR-QDGNLPESSVRK 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  659 LVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL---------HELKAGQEEPNKSELELKRALC-----M 724
Cdd:cd14010    99 FGRDLVRGLHYIHSKGII-YCDLKPSNILLDGNGTLKLSDFGLarregeilkELFGQFSDEGNVNKVSKKQAKRgtpyyM 177
                         170       180       190
                  ....*....|....*....|....*....|
gi 161076872  725 APELLRDayrpGRGSQKGDVYSFGILLYEM 754
Cdd:cd14010   178 APELFQG----GVHSFASDLWALGCVLYEM 203
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
581-817 2.48e-16

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: 80.32  E-value: 2.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVDITRSI---RKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLA-NEDLHLDHmfI 656
Cdd:cd14014    25 GRPVAIKVLRPELAEDEEFRerfLREARALARLSHPNIVRVYDVGEDDGRPYIVMEYVEGGSLADLLReRGPLPPRE--A 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  657 SSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhELKAGQEEPNKSELELKRALCMAPELLRDayrpG 736
Cdd:cd14014   103 LRILAQIADALAAAHRAGIV-HRDIKPANILLTEDGRVKLTDFGI-ARALGDSGLTQTGSVLGTPAYMAPEQARG----G 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  737 RGSQKGDVYSFGILLYEMIGRKGPWgdTAYSKEEIIQFVKCPEMLQHGVFRPalththlDIPDYIRKCLCQCWDEDPEVR 816
Cdd:cd14014   177 PVDPRSDIYSLGVVLYELLTGRPPF--DGDSPAAVLAKHLQEAPPPPSPLNP-------DVPPALDAIILRALAKDPEER 247

                  .
gi 161076872  817 P 817
Cdd:cd14014   248 P 248
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
582-828 3.35e-16

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: 80.84  E-value: 3.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  582 NIVAMKKIHKKSVDITRS-IRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVL---ANEDLHLDHMFIS 657
Cdd:cd05051    47 VLVAVKMLRPDASKNAREdFLKEVKIMSQLKDPNIVRLLGVCTRDEPLCMIVEYMENGDLNQFLqkhEAETQGASATNSK 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  658 SL--------VSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL-HELKAGqeepNKSELELKRAL---CMA 725
Cdd:cd05051   127 TLsygtllymATQIASGMKYLESLNFV-HRDLATRNCLVGPNYTIKIADFGMsRNLYSG----DYYRIEGRAVLpirWMA 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  726 PE--LLrdayrpGRGSQKGDVYSFGILLYE--MIGRKGPWGDtaYSKEEIIQFVkcpemlqHGVFRPALTHTHLD----I 797
Cdd:cd05051   202 WEsiLL------GKFTTKSDVWAFGVTLWEilTLCKEQPYEH--LTDEQVIENA-------GEFFRDDGMEVYLSrppnC 266
                         250       260       270
                  ....*....|....*....|....*....|.
gi 161076872  798 PDYIRKCLCQCWDEDPEVRPDIRLVRMHLKE 828
Cdd:cd05051   267 PKEIYELMLECWRRDEEDRPTFREIHLFLQR 297
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
584-817 4.66e-16

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: 79.54  E-value: 4.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDITRSIrKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSDI 663
Cdd:cd05113    31 VAIKMIKEGSMSEDEFI-EEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNYLREMRKRFQTQQLLEMCKDV 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  664 LKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNK--SELELKRAlcmAPELLRDAyrpgRGSQK 741
Cdd:cd05113   110 CEAMEYLESKQFL-HRDLAARNCLVNDQGVVKVSDFGLSRYVLDDEYTSSvgSKFPVRWS---PPEVLMYS----KFSSK 181
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161076872  742 GDVYSFGILLYEMIGR-KGPWgdTAYSKEEIIQFVkcpeMLQHGVFRPALThthldiPDYIRKCLCQCWDEDPEVRP 817
Cdd:cd05113   182 SDVWAFGVLMWEVYSLgKMPY--ERFTNSETVEHV----SQGLRLYRPHLA------SEKVYTIMYSCWHEKADERP 246
PBP1_GC_G-like cd06372
Ligand-binding domain of membrane guanylyl cyclase G; This group includes the ligand-binding ...
61-425 4.89e-16

Ligand-binding domain of membrane guanylyl cyclase G; This group includes the ligand-binding domain of membrane guanylyl cyclase G (GC-G) which is a sperm surface receptor and might function, similar to its sea urchin counterpart, in the early signaling event that regulates the Ca2+ influx/efflux and subsequent motility response in sperm. GC-G appears to be a pseudogene in human. Furthermore, in contrast to the other orphan receptor GCs, GC-G has a broad tissue distribution in rat, including lung, intestine, kidney, and skeletal muscle.


Pssm-ID: 380595 [Multi-domain]  Cd Length: 390  Bit Score: 81.77  E-value: 4.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   61 GLPLAIEDVNKNPNLLPGKKLAFKPVDIG--HKMSayrvkpLRA-MTQMREAGVTAFIGPdeSCTTEA----LLASAWNT 133
Cdd:cd06372    22 AIQLAVDKVNSEPSLLGNYSLDFVYTDCGcnAKES------LGAfIDQVQKENISALFGP--ACPEAAevtgLLASEWNI 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  134 PMLSFKCSDPIVSNKSTFHTFARTLAPASKVSKSVISLLNAFHWNKFSIV--VSSKPIWG--SDVARAIQELAEArNFTI 209
Cdd:cd06372    94 PMFGFVGQSPKLDDRDVYDTYVKLVPPLQRIGEVLVKTLQFFGWTHVAMFggSSATSTWDkvDELWKSVENQLKF-NFNV 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  210 -SHFKYisdyipTTKTLSQIDKIIEETYATTRIYVFIGEHIAMVDFVRGLQNRRLLeSGDYIVVSVDDeiydsnrrvniM 288
Cdd:cd06372   173 tAKVKY------DTSNPDLLQENLRYISSVARVIVLICSSEDARSILLEAEKLGLM-DGEYVFFLLQQ-----------F 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  289 ERNYLDPYIRKEKSKSLDKiSFRSVIKISMTYPQNPHIRDICSKIKDYARKTPFlvpyHQRVFDNISVPIYGLHLYDSVM 368
Cdd:cd06372   235 EDSFWKEVLNDEKNQVFLK-AYEMVFLIAQSSYGTYGYSDFRKQVHQKLRRAPF----YSSISSEDQVSPYSAYLHDAVL 309
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 161076872  369 IYVRAITEVLRLGGDIYDGNLVMSHIFNRSYHSIQGFD--VYIDSNGDAEGNYTVITLQ 425
Cdd:cd06372   310 LYAMGLKEMLKDGKDPRDGRALLQTLRGYNQTTFYGITglVYLDVQGERHMDYSVYDLQ 368
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
589-817 5.57e-16

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. The KSR2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 79.67  E-value: 5.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  589 IHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSDILKGMI 668
Cdd:cd14153    32 IERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYSVVRDAKVVLDVNKTRQIAQEIVKGMG 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  669 YLHDSEIIsHGNLRSSNCLIDSRWVCqISDFGLHE----LKAGQEEpnkSELELKRA-LC-MAPELLRDaYRPGRG---- 738
Cdd:cd14153   112 YLHAKGIL-HKDLKSKNVFYDNGKVV-ITDFGLFTisgvLQAGRRE---DKLRIQSGwLChLAPEIIRQ-LSPETEedkl 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  739 --SQKGDVYSFGILLYEMIGRKGPWGDTaySKEEIIqfvkcpemLQHGV-FRPALthTHLDIPDYIRKCLCQCWDEDPEV 815
Cdd:cd14153   186 pfSKHSDVFAFGTIWYELHAREWPFKTQ--PAEAII--------WQVGSgMKPNL--SQIGMGKEISDILLFCWAYEQEE 253

                  ..
gi 161076872  816 RP 817
Cdd:cd14153   254 RP 255
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
584-817 5.61e-16

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: 79.96  E-value: 5.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMK--KIHKKSVDITRS-IRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSL- 659
Cdd:cd14026    25 VAIKclKLDSPVGDSERNcLLKEAEILHKARFSYILPILGICNEPEFLGIVTEYMTNGSLNELLHEKDIYPDVAWPLRLr 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  660 -VSDILKGMIYLHD-SEIISHGNLRSSNCLIDSRWVCQISDFGLHE---LKAGQEEPNKSELELKRALCMAPEllrdAYR 734
Cdd:cd14026   105 iLYEIALGVNYLHNmSPPLLHHDLKTQNILLDGEFHVKIADFGLSKwrqLSISQSRSSKSAPEGGTIIYMPPE----EYE 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  735 PG---RGSQKGDVYSFGILLYEMIGRKGPWgdtayskEEIIQfvkcPEMLQHGVF---RPALTHTHL--DIPDYIR--KC 804
Cdd:cd14026   181 PSqkrRASVKHDIYSYAIIMWEVLSRKIPF-------EEVTN----PLQIMYSVSqghRPDTGEDSLpvDIPHRATliNL 249
                         250
                  ....*....|...
gi 161076872  805 LCQCWDEDPEVRP 817
Cdd:cd14026   250 IESGWAQNPDERP 262
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
584-829 6.96e-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: 6.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDITrSIRKELKLMREVRHENIINfIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHM-FISSLVSD 662
Cdd:cd05073    38 VAVKTMKPGSMSVE-AFLAEANVMKTLQHDKLVK-LHAVVTKEPIYIITEFMAKGSLLDFLKSDEGSKQPLpKLIDFSAQ 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  663 ILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNK--SELELKRAlcmAPEllrdAYRPGRGSQ 740
Cdd:cd05073   116 IAEGMAFIEQRNYI-HRDLRAANILVSASLVCKIADFGLARVIEDNEYTARegAKFPIKWT---APE----AINFGSFTI 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  741 KGDVYSFGILLYEMIGrkgpWGDTAY---SKEEIIQfvkcpeMLQHGvFRPALTHThldIPDYIRKCLCQCWDEDPEVRP 817
Cdd:cd05073   188 KSDVWSFGILLMEIVT----YGRIPYpgmSNPEVIR------ALERG-YRMPRPEN---CPEELYNIMMRCWKNRPEERP 253
                         250
                  ....*....|..
gi 161076872  818 DIRLVRMHLKEL 829
Cdd:cd05073   254 TFEYIQSVLDDF 265
PBP1_GPCR_family_C-like cd06350
ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory ...
65-251 8.07e-16

ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory transmission on the cellular surface through initial binding of glutamate; categorized into ionotropic glutamate receptors (iGluRs) and metabotropic glutamate receptors (m; Ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory transmission on the cellular surface through initial binding of glutamate and are categorized into ionotropic glutamate receptors (iGluRs) and metabotropic glutamate receptors (mGluRs). The metabotropic glutamate receptors (mGluR) are key receptors in the modulation of excitatory synaptic transmission in the central nervous system. The mGluRs are coupled to G proteins and are thus distinct from the iGluRs which internally contain ligand-gated ion channels. The mGluR structure is divided into three regions: the extracellular region, the seven-spanning transmembrane region and the cytoplasmic region. The extracellular region is further divided into the ligand-binding domain (LBD) and the cysteine-rich domain. The LBD has sequence similarity to the LIVBP, which is a bacterial periplasmic protein (PBP), as well as to the extracellular region of both iGluR and the gamma-aminobutyric acid (GABA)b receptor. iGluRs are divided into three main subtypes based on pharmacological profile: NMDA, AMPA, and kainate receptors. All family C GPCRs have a large extracellular N terminus that contain a domain with homology to bacterial periplasmic amino acid-binding proteins.


Pssm-ID: 380573  Cd Length: 350  Bit Score: 80.42  E-value: 8.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   65 AIEDVNKNPNLLPGKKLAF--------KPVDIGH-----KMSAYRVKPLRAMTQMREAGVTAFIGPDESCTTEAL--LAS 129
Cdd:cd06350    36 AIEEINNDSSLLPNVTLGYdirdtcssSSVALESsleflLDNGIKLLANSNGQNIGPPNIVAVIGAASSSVSIAVanLLG 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  130 AWNTPMLSFKCSDPIVSNKSTFHTFARTLAPASKVSKSVISLLNAFHWNKFSIVVSSKpIWGSDVARAIQELAEARNFTI 209
Cdd:cd06350   116 LFKIPQISYASTSPELSDKIRYPYFLRTVPSDTLQAKAIADLLKHFNWNYVSTVYSDD-DYGRSGIEAFEREAKERGICI 194
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 161076872  210 SHFKYISDYIPTTKTLSQIDKIIEETYATTrIYVFIGEHIAM 251
Cdd:cd06350   195 AQTIVIPENSTEDEIKRIIDKLKSSPNAKV-VVLFLTESDAR 235
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
580-763 8.29e-16

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


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 79.02  E-value: 8.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  580 RGNIVAMKKIHKKSVDITRSIRKELKLMREV------RHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLhLDH 653
Cdd:cd06631    24 TGQLIAVKQVELDTSDKEKAEKEYEKLQEEVdllktlKHVNIVGYLGTCLEDNVVSIFMEFVPGGSIASILARFGA-LEE 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  654 MFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL-HELKAGQEEPNKSELeLKRA----LCMAPEL 728
Cdd:cd06631   103 PVFCRYTKQILEGVAYLHNNNVI-HRDIKGNNIMLMPNGVIKLIDFGCaKRLCINLSSGSQSQL-LKSMrgtpYWMAPEV 180
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 161076872  729 LRDAyrpGRGsQKGDVYSFGILLYEMIGRKGPWGD 763
Cdd:cd06631   181 INET---GHG-RKSDIWSIGCTVFEMATGKPPWAD 211
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
581-824 1.21e-15

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 78.31  E-value: 1.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKS-VDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDL---HLDHMFI 656
Cdd:cd14664    17 GTLVAVKRLKGEGtQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGSLGELLHSRPEsqpPLDWETR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  657 SSLVSDILKGMIYLHD--SEIISHGNLRSSNCLIDSRWVCQISDFGLHELKagqeEPNKSELELKRALC---MAPELLRD 731
Cdd:cd14664    97 QRIALGSARGLAYLHHdcSPLIIHRDVKSNNILLDEEFEAHVADFGLAKLM----DDKDSHVMSSVAGSygyIAPEYAYT 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  732 ayrpGRGSQKGDVYSFGILLYEMIGRKGPWGDTAYSKE-EIIQFVK--CPEMLQHGVFRPALTHTHLD--IPDYIRKCLc 806
Cdd:cd14664   173 ----GKVSEKSDVYSYGVVLLELITGKRPFDEAFLDDGvDIVDWVRglLEEKKVEALVDPDLQGVYKLeeVEQVFQVAL- 247
                         250
                  ....*....|....*....
gi 161076872  807 QCWDEDPEVRPDIR-LVRM 824
Cdd:cd14664   248 LCTQSSPMERPTMReVVRM 266
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
585-830 1.29e-15

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: 78.54  E-value: 1.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  585 AMKKIHK-KSVDITRSIRKELKLMREV-RHENIINFIGASTDHGSVIIFTTYCARGSLEDVL-------ANEDLHLDHMF 655
Cdd:cd05047    26 AIKRMKEyASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLrksrvleTDPAFAIANST 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  656 ISSLVS--------DILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHElkaGQEEPNKSELELKRALCMAPE 727
Cdd:cd05047   106 ASTLSSqqllhfaaDVARGMDYLSQKQFI-HRDLAARNILVGENYVAKIADFGLSR---GQEVYVKKTMGRLPVRWMAIE 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  728 LLRDAYRpgrgSQKGDVYSFGILLYEMIGrkgpWGDTAYSKeeiiqfVKCPEM---LQHGvFRpalTHTHLDIPDYIRKC 804
Cdd:cd05047   182 SLNYSVY----TTNSDVWSYGVLLWEIVS----LGGTPYCG------MTCAELyekLPQG-YR---LEKPLNCDDEVYDL 243
                         250       260
                  ....*....|....*....|....*.
gi 161076872  805 LCQCWDEDPEVRPDIRLVRMHLKELQ 830
Cdd:cd05047   244 MRQCWREKPYERPSFAQILVSLNRML 269
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
584-833 1.31e-15

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 81.21  E-value: 1.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHK---KSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDlHLDHMFISSLV 660
Cdd:COG0515    35 VALKVLRPelaADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEGESLADLLRRRG-PLPPAEALRIL 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRAlCMAPELLRDAyRPGRGSq 740
Cdd:COG0515   114 AQLAEALAAAHAAGIV-HRDIKPANILLTPDGRVKLIDFGIARALGGATLTQTGTVVGTPG-YMAPEQARGE-PVDPRS- 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  741 kgDVYSFGILLYEMI-GRKGPWGDTAYskeeiiqfvkcpEMLQHGVFR--PALTHTHLDIPDY----IRKCLcqcwDEDP 813
Cdd:COG0515   190 --DVYSLGVTLYELLtGRPPFDGDSPA------------ELLRAHLREppPPPSELRPDLPPAldaiVLRAL----AKDP 251
                         250       260
                  ....*....|....*....|.
gi 161076872  814 EVRP-DIRLVRMHLKELQAGL 833
Cdd:COG0515   252 EERYqSAAELAAALRAVLRSL 272
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
584-826 1.41e-15

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: 78.07  E-value: 1.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDiTRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSDI 663
Cdd:cd05112    31 VAIKTIREGAMS-EEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGCLSDYLRTQRGLFSAETLLGMCLDV 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  664 LKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHE--LKAGQEEPNKSELELKRAlcmAPELlrdaYRPGRGSQK 741
Cdd:cd05112   110 CEGMAYLEEASVI-HRDLAARNCLVGENQVVKVSDFGMTRfvLDDQYTSSTGTKFPVKWS---SPEV----FSFSRYSSK 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  742 GDVYSFGILLYEMIGRkgpwGDTAY---SKEEIIQFVKCpemlQHGVFRPALTHTHldipdyIRKCLCQCWDEDPEVRPD 818
Cdd:cd05112   182 SDVWSFGVLMWEVFSE----GKIPYenrSNSEVVEDINA----GFRLYKPRLASTH------VYEIMNHCWKERPEDRPS 247

                  ....*...
gi 161076872  819 IRLVRMHL 826
Cdd:cd05112   248 FSLLLRQL 255
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
577-817 1.61e-15

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: 78.16  E-value: 1.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  577 ALFRGNIVAMKKI-HKKSVDITRSI---RKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLD 652
Cdd:cd14145    25 AIWIGDEVAVKAArHDPDEDISQTIenvRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFARGGPLNRVLSGKRIPPD 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  653 hmFISSLVSDILKGMIYLHDSEIIS--HGNLRSSNCLI--------DSRWVCQISDFGLhelkaGQEEPNKSELELKRAL 722
Cdd:cd14145   105 --ILVNWAVQIARGMNYLHCEAIVPviHRDLKSSNILIlekvengdLSNKILKITDFGL-----AREWHRTTKMSAAGTY 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  723 C-MAPELLRDAYRpgrgSQKGDVYSFGILLYEMIGRKGPW-GDTAYSkeeiiqfvkcpemLQHGVfrpALTHTHLDI--- 797
Cdd:cd14145   178 AwMAPEVIRSSMF----SKGSDVWSYGVLLWELLTGEVPFrGIDGLA-------------VAYGV---AMNKLSLPIpst 237
                         250       260
                  ....*....|....*....|.
gi 161076872  798 -PDYIRKCLCQCWDEDPEVRP 817
Cdd:cd14145   238 cPEPFARLMEDCWNPDPHSRP 258
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
572-817 1.76e-15

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


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 78.04  E-value: 1.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  572 SFTNI--ALFRGNIVAMKKIHKK---------------------SVDITRSIRKELKLMREVRHENIINFIGASTDHGSV 628
Cdd:cd14000     6 GFGSVyrASYKGEPVAVKIFNKHtssnfanvpadtmlrhlratdAMKNFRLLRQELTVLSHLHHPSIVYLLGIGIHPLML 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  629 IIftTYCARGSLEDVL---ANEDLHLDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLI-----DSRWVCQISDFG 700
Cdd:cd14000    86 VL--ELAPLGSLDHLLqqdSRSFASLGRTLQQRIALQVADGLRYLHSAMII-YRDLKSHNVLVwtlypNSAIIIKIADYG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  701 LhelkAGQEEPNKSELELKRALCMAPELLRdayRPGRGSQKGDVYSFGILLYEMIGRKGPWgdtayskEEIIQFVKCPEM 780
Cdd:cd14000   163 I----SRQCCRMGAKGSEGTPGFRAPEIAR---GNVIYNEKVDVFSFGMLLYEILSGGAPM-------VGHLKFPNEFDI 228
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 161076872  781 lqHGVFRPALTHTHLDIPDYIRKCLCQCWDEDPEVRP 817
Cdd:cd14000   229 --HGGLRPPLKQYECAPWPEVEVLMKKCWKENPQQRP 263
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
584-828 1.81e-15

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: 77.84  E-value: 1.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDITRS-IRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVL------ANEDLHLDHMFI 656
Cdd:cd05044    29 VAVKTLRKGATDQEKAeFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILELMEGGDLLSYLraarptAFTPPLLTLKDL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  657 SSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSR----WVCQISDFGLhelkagQEEPNKSELELKRA------LCMAP 726
Cdd:cd05044   109 LSICVDVAKGCVYLEDMHFV-HRDLAARNCLVSSKdyreRVVKIGDFGL------ARDIYKNDYYRKEGegllpvRWMAP 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  727 ELLRDayrpGRGSQKGDVYSFGILLYEMIGR-KGPWgdTAYSKEEIIQFVKCPEMLQhgvfRPAlththlDIPDYIRKCL 805
Cdd:cd05044   182 ESLVD----GVFTTQSDVWAFGVLMWEILTLgQQPY--PARNNLEVLHFVRAGGRLD----QPD------NCPDDLYELM 245
                         250       260
                  ....*....|....*....|...
gi 161076872  806 CQCWDEDPEVRPDIRLVRMHLKE 828
Cdd:cd05044   246 LRCWSTDPEERPSFARILEQLQN 268
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
584-829 2.06e-15

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: 77.62  E-value: 2.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDITrSIRKELKLMREVRHENIINFIGASTDHgSVIIFTTYCARGSLEDVLANEDLHldHMFISSLV--- 660
Cdd:cd05067    34 VAIKSLKQGSMSPD-AFLAEANLMKQLQHQRLVRLYAVVTQE-PIYIITEYMENGSLVDFLKTPSGI--KLTINKLLdma 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNK--SELELKRAlcmAPEllrdAYRPGRG 738
Cdd:cd05067   110 AQIAEGMAFIEERNYI-HRDLRAANILVSDTLSCKIADFGLARLIEDNEYTARegAKFPIKWT---APE----AINYGTF 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  739 SQKGDVYSFGILLYEMIgrkgPWGDTAY---SKEEIIQFVK------CPEmlqhgvfrpalththlDIPDYIRKCLCQCW 809
Cdd:cd05067   182 TIKSDVWSFGILLTEIV----THGRIPYpgmTNPEVIQNLErgyrmpRPD----------------NCPEELYQLMRLCW 241
                         250       260
                  ....*....|....*....|
gi 161076872  810 DEDPEVRPDIRLVRMHLKEL 829
Cdd:cd05067   242 KERPEDRPTFEYLRSVLEDF 261
PBP1_glutamate_receptors-like cd06269
ligand-binding domain of family C G-protein couples receptors (GPCRs), membrane bound guanylyl ...
64-292 2.06e-15

ligand-binding domain of family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases such as natriuretic peptide receptors (NPRs), and N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of ionotropic glutamate rece; This CD represents the ligand-binding domain of the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases such as the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the ionotropic glutamate receptors, all of which are structurally similar and related to the periplasmic-binding fold type 1 family. The family C GPCRs consists of metabotropic glutamate receptor (mGluR), a calcium-sensing receptor (CaSR), gamma-aminobutyric acid receptor (GABAbR), the promiscuous L-alpha-amino acid receptor GPR6A, families of taste and pheromone receptors, and orphan receptors. Truncated splicing variants of the orphan receptors are not included in this CD. The family C GPCRs are activated by endogenous agonists such as amino acids, ions, and sugar based molecules. Their amino terminal ligand-binding region is homologous to the bacterial leucine-isoleucine-valine binding protein (LIVBP) and a leucine binding protein (LBP). The ionotropic glutamate receptors (iGluRs) have an integral ion channel and are subdivided into three major groups based on their pharmacology and structural similarities: NMDA receptors, AMPA receptors, and kainate receptors. The family of membrane bound guanylyl cyclases is further divided into three subfamilies: the ANP receptor (GC-A)/C-type natriuretic peptide receptor (GC-B), the heat-stable enterotoxin receptor (GC-C)/sensory organ specific membrane GCs such as retinal receptors (GC-E, GC-F), and olfactory receptors (GC-D and GC-G).


Pssm-ID: 380493 [Multi-domain]  Cd Length: 332  Bit Score: 79.00  E-value: 2.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   64 LAIEDVNKNPNLLPGKKLAFKPVDigHKMSAYRVkPLRAMTQMREAGVTAFIGPDESCTTEAL--LASAWNTPMLSFKCS 141
Cdd:cd06269    24 LALSDVNSRPDLLPKTTLGLAIRD--SECNPTQA-LLSACDLLAAAKVVAILGPGCSASAAPVanLARHWDIPVLSYGAT 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  142 DPIVSNKSTFHTFARTLAPASKVSKSVISLLNAFHWNKFSIVVSSKpIWGSDVARAIQELAEARNFTISHfkyiSDYIPT 221
Cdd:cd06269   101 APGLSDKSRYAYFLRTVPPDSKQADAMLALVRRLGWNKVVLIYSDD-EYGEFGLEGLEELFQEKGGLITS----RQSFDE 175
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161076872  222 TKTLsQIDKIIEEtYATTRIYVFIGehIAMVDFVRGLQN--RRL-LESGDYIVVSVDDEIYDSNRRVNIMERNY 292
Cdd:cd06269   176 NKDD-DLTKLLRN-LRDTEARVIIL--LASPDTARSLMLeaKRLdMTSKDYVWFVIDGEASSSDEHGDEARQAA 245
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
588-820 2.40e-15

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: 77.27  E-value: 2.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  588 KIHKKSVDITRSIRKELKLMREVRHENIINFIGA--STDHGSVIIFTTYCARGSLEDVLANEDlHLDHMFISSLVSDILK 665
Cdd:cd13983    35 KLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDSweSKSKKEVIFITELMTSGTLKQYLKRFK-RLKLKVIKSWCRQILE 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  666 GMIYLH--DSEIIsHGNLRSSNCLID-SRWVCQISDFGLHELKAGQeepnkselelKRALC------MAPELLRDAYRPg 736
Cdd:cd13983   114 GLNYLHtrDPPII-HRDLKCDNIFINgNTGEVKIGDLGLATLLRQS----------FAKSVigtpefMAPEMYEEHYDE- 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  737 rgsqKGDVYSFGILLYEMIGRKGPWGDTA-----YSKeeIIQFVKcPEMLQHgVFRPalththlDIPDYIRKCLCQcwde 811
Cdd:cd13983   182 ----KVDIYAFGMCLLEMATGEYPYSECTnaaqiYKK--VTSGIK-PESLSK-VKDP-------ELKDFIEKCLKP---- 242

                  ....*....
gi 161076872  812 dPEVRPDIR 820
Cdd:cd13983   243 -PDERPSAR 250
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
579-827 3.14e-15

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: 76.84  E-value: 3.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  579 FRGNIVAMKKIhkkSVDIT-RSIRKELKLMREVRHENIINFIGASTdHGSVIIFTTYCARGSLEDVLANED---LHLDHM 654
Cdd:cd05083    27 YMGQKVAVKNI---KCDVTaQAFLEETAVMTKLQHKNLVRLLGVIL-HNGLYIVMELMSKGNLVNFLRSRGralVPVIQL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  655 FISSLvsDILKGMIYLhDSEIISHGNLRSSNCLIDSRWVCQISDFGLHelKAGQEEPNKSELELKRAlcmAPELLRDayr 734
Cdd:cd05083   103 LQFSL--DVAEGMEYL-ESKKLVHRDLAARNILVSEDGVAKISDFGLA--KVGSMGVDNSRLPVKWT---APEALKN--- 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  735 pGRGSQKGDVYSFGILLYEMIGrkgpWGDTAYSKEEIIQFVKCpemLQHGvFRpalththLDIPD----YIRKCLCQCWD 810
Cdd:cd05083   172 -KKFSSKSDVWSYGVLLWEVFS----YGRAPYPKMSVKEVKEA---VEKG-YR-------MEPPEgcppDVYSIMTSCWE 235
                         250
                  ....*....|....*..
gi 161076872  811 EDPEVRPDIRLVRMHLK 827
Cdd:cd05083   236 AEPGKRPSFKKLREKLE 252
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
584-818 3.21e-15

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: 77.00  E-value: 3.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHK-KSVDITRSIRKELKLMREVRHENIINFIGASTdhGSVIIFTTYCAR-GSLEDVLANeDLHLDHMFISSLVS 661
Cdd:cd05060    26 VAVKTLKQeHEKAGKKEFLREASVMAQLDHPCIVRLIGVCK--GEPLMLVMELAPlGPLLKYLKK-RREIPVSDLKELAH 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  662 DILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHE-LKAGQEEpNKSELELKRAL-CMAPELLRdaYrpGRGS 739
Cdd:cd05060   103 QVAMGMAYLESKHFV-HRDLAARNVLLVNRHQAKISDFGMSRaLGAGSDY-YRATTAGRWPLkWYAPECIN--Y--GKFS 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  740 QKGDVYSFGILLYEMIGRKG-PWGDTaySKEEIIQFVKCPEMLQhgvfRPALThthldiPDYIRKCLCQCWDEDPEVRPD 818
Cdd:cd05060   177 SKSDVWSYGVTLWEAFSYGAkPYGEM--KGPEVIAMLESGERLP----RPEEC------PQEIYSIMLSCWKYRPEDRPT 244
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
560-761 3.47e-15

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: 77.84  E-value: 3.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  560 QSILVVGEPNKR----------------SFTNIALfrGNIVAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGAST 623
Cdd:cd06655     9 RTIVSIGDPKKKytryekigqgasgtvfTAIDVAT--GQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSFL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  624 DHGSVIIFTTYCARGSLEDVLAneDLHLDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhe 703
Cdd:cd06655    87 VGDELFVVMEYLAGGSLTDVVT--ETCMDEAQIAAVCRECLQALEFLHANQVI-HRDIKSDNVLLGMDGSVKLTDFGF-- 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161076872  704 lkAGQEEPNKSELE--LKRALCMAPELL-RDAYRPgrgsqKGDVYSFGILLYEMIGRKGPW 761
Cdd:cd06655   162 --CAQITPEQSKRStmVGTPYWMAPEVVtRKAYGP-----KVDIWSLGIMAIEMVEGEPPY 215
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
585-755 3.95e-15

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: 76.95  E-value: 3.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  585 AMKKIHkksvdITRSIRKELKLMREVR------HENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLH--LDHMFI 656
Cdd:cd13996    35 AIKKIR-----LTEKSSASEKVLREVKalaklnHPNIVRYYTAWVEEPPLYIQMELCEGGTLRDWIDRRNSSskNDRKLA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  657 SSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSR-WVCQISDFGL-HELKAGQEEPNKSELELKRA-----------LC 723
Cdd:cd13996   110 LELFKQILKGVSYIHSKGIV-HRDLKPSNIFLDNDdLQVKIGDFGLaTSIGNQKRELNNLNNNNNGNtsnnsvgigtpLY 188
                         170       180       190
                  ....*....|....*....|....*....|...
gi 161076872  724 MAPELLR-DAYrpgrgSQKGDVYSFGILLYEMI 755
Cdd:cd13996   189 ASPEQLDgENY-----NEKADIYSLGIILFEML 216
PBP1_GABAb_receptor cd06366
ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for ...
64-472 4.29e-15

ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for gamma-aminobutyric acid (GABA); Ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for gamma-aminobutyric acid (GABA). GABA is the major inhibitory neurotransmitter in the mammalian CNS and, like glutamate and other transmitters, acts via both ligand gated ion channels (GABAa receptors) and G-protein coupled receptors (GABAb receptor or GABAbR). GABAa receptors are members of the ionotropic receptor superfamily which includes alpha-adrenergic and glycine receptors. The GABAb receptor is a member of a receptor superfamily which includes the mGlu receptors. The GABAb receptor is coupled to G alpha-i proteins, and activation causes a decrease in calcium, an increase in potassium membrane conductance, and inhibition of cAMP formation. The response is thus inhibitory and leads to hyperpolarization and decreased neurotransmitter release, for example.


Pssm-ID: 380589 [Multi-domain]  Cd Length: 404  Bit Score: 78.83  E-value: 4.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   64 LAIEDVNKNPNLLPGKKLAFKPVDIghkmsayRVKPLRAMTQMREA-----GVTAFIGP--DESCTTEALLASAWNTPML 136
Cdd:cd06366    26 MALEHINNRSDILPGYNLELIWNDT-------QCDPGLGLKALYDLlytppPKVMLLGPgcSSVTEPVAEASKYWNLVQL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  137 SFKCSDPIVSNKSTFHTFARTLAPASKVSKSVISLLNAFHWNKFSIVVSSKPIwGSDVARAIQELAEARNFTIshfkyIS 216
Cdd:cd06366    99 SYAATSPALSDRKRYPYFFRTVPSDTAFNPARIALLKHFGWKRVATIYQNDEV-FSSTAEDLEELLEEANITI-----VA 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  217 DYIPTTKTLSQIDKIIEETYAttRI-YVFIGEHIAmvdfvrglqnRRLLEsgdyivvsvddEIYDSN----RRVNIMeRN 291
Cdd:cd06366   173 TESFSSEDPTDQLENLKEKDA--RIiIGLFYEDAA----------RKVFC-----------EAYKLGmygpKYVWIL-PG 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  292 YLDPYIRKEKSKSLD--KISFRSVIKISMTYPQNPHIRDicsKIKDYARKTP--FLVPYHQRVFD-NISVPIYGLHLYDS 366
Cdd:cd06366   229 WYDDNWWDVPDNDVNctPEQMLEALEGHFSTELLPLNPD---NTKTISGLTAqeFLKEYLERLSNsNYTGSPYAPFAYDA 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  367 VmiYVRAIT---------EVLRLGGDIYDGNLVMSHIFNRSYHSIQgFD-----VYIDSNGDAEGNYTVITLQNDvgsga 432
Cdd:cd06366   306 V--WAIALAlnktieklaEYNKTLEDFTYNDKEMADLFLEAMNSTS-FEgvsgpVSFDSKGDRLGTVDIEQLQGG----- 377
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 161076872  433 sigslakmSMQPVGFFaydkNSVIPEFRYIKNDrPIQWLN 472
Cdd:cd06366   378 --------SYVKVGLY----DPNADSLLLLNES-SIVWPG 404
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
584-817 4.60e-15

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


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 76.64  E-value: 4.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDITRS-IRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSD 662
Cdd:cd05033    35 VAIKTLKSGYSDKQRLdFLTEASIMGQFDHPNVIRLEGVVTKSRPVMIVTEYMENGSLDKFLRENDGKFTVTQLVGMLRG 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  663 ILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKagqeEPNKSELELK----RALCMAPELLrdAYRpgRG 738
Cdd:cd05033   115 IASGMKYLSEMNYV-HRDLAARNILVNSDLVCKVSDFGLSRRL----EDSEATYTTKggkiPIRWTAPEAI--AYR--KF 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  739 SQKGDVYSFGILLYEMI--GRKGPWGdtaYSKEEIIQFVkcpemlQHGVFRPAlthtHLDIPDYIRKCLCQCWDEDPEVR 816
Cdd:cd05033   186 TSASDVWSFGIVMWEVMsyGERPYWD---MSNQDVIKAV------EDGYRLPP----PMDCPSALYQLMLDCWQKDRNER 252

                  .
gi 161076872  817 P 817
Cdd:cd05033   253 P 253
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
565-761 4.90e-15

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: 76.50  E-value: 4.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  565 VGEPNKR--------------SFTNIALFRGNIVAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVII 630
Cdd:cd06647     2 VGDPKKKytrfekigqgasgtVYTAIDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  631 FTTYCARGSLEDVLAneDLHLDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkAGQEE 710
Cdd:cd06647    82 VMEYLAGGSLTDVVT--ETCMDEGQIAAVCRECLQALEFLHSNQVI-HRDIKSDNILLGMDGSVKLTDFGF----CAQIT 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 161076872  711 PNKSelelKRALC------MAPELL-RDAYRPgrgsqKGDVYSFGILLYEMIGRKGPW 761
Cdd:cd06647   155 PEQS----KRSTMvgtpywMAPEVVtRKAYGP-----KVDIWSLGIMAIEMVEGEPPY 203
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
579-829 5.69e-15

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: 76.61  E-value: 5.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  579 FRGNIVAMKKIHK---KSVDIT-RSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHlDHM 654
Cdd:cd14147    24 WRGELVAVKAARQdpdEDISVTaESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAGGPLSRALAGRRVP-PHV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  655 FISSLVSdILKGMIYLHDSEIIS--HGNLRSSNCLIDSRWV--------CQISDFGLhelkaGQEEPNKSELELKRALC- 723
Cdd:cd14147   103 LVNWAVQ-IARGMHYLHCEALVPviHRDLKSNNILLLQPIEnddmehktLKITDFGL-----AREWHKTTQMSAAGTYAw 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  724 MAPELLRdAYRPGRGSqkgDVYSFGILLYEMIGRKGPWgdtayskeeiiQFVKCPEmLQHGVFRPALThthLDIP----D 799
Cdd:cd14147   177 MAPEVIK-ASTFSKGS---DVWSFGVLLWELLTGEVPY-----------RGIDCLA-VAYGVAVNKLT---LPIPstcpE 237
                         250       260       270
                  ....*....|....*....|....*....|
gi 161076872  800 YIRKCLCQCWDEDPEVRPDIRLVRMHLKEL 829
Cdd:cd14147   238 PFAQLMADCWAQDPHRRPDFASILQQLEAL 267
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
584-817 5.74e-15

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


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 76.61  E-value: 5.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKK-SVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVL----ANED-------LHL 651
Cdd:cd05032    39 VAIKTVNENaSMRERIEFLNEASVMKEFNCHHVVRLLGVVSTGQPTLVVMELMAKGDLKSYLrsrrPEAEnnpglgpPTL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  652 DHMFisSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSElelKRAL---CMAPEL 728
Cdd:cd05032   119 QKFI--QMAAEIADGMAYLAAKKFV-HRDLAARNCMVAEDLTVKIGDFGMTRDIYETDYYRKGG---KGLLpvrWMAPES 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  729 LRDAYRpgrgSQKGDVYSFGILLYEMIgrkgPWGDTAY---SKEEIIQFVKcpemlQHGVFRPALThthldIPDYIRKCL 805
Cdd:cd05032   193 LKDGVF----TTKSDVWSFGVVLWEMA----TLAEQPYqglSNEEVLKFVI-----DGGHLDLPEN-----CPDKLLELM 254
                         250
                  ....*....|..
gi 161076872  806 CQCWDEDPEVRP 817
Cdd:cd05032   255 RMCWQYNPKMRP 266
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
577-758 6.84e-15

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


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 76.79  E-value: 6.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  577 ALFRGNIVAMKKIHKKS----VDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDvlaneDLHLD 652
Cdd:cd14159    12 AVMRNTEYAVKRLKEDSeldwSVVKNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVYLPNGSLED-----RLHCQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  653 HMFISSLVS---DIL----KGMIYLH-DSEIISHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSEL-----ELK 719
Cdd:cd14159    87 VSCPCLSWSqrlHVLlgtaRAIQYLHsDSPSLIHGDVKSSNILLDAALNPKLGDFGLARFSRRPKQPGMSSTlartqTVR 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 161076872  720 RALCMAPEllrDAYRPGRGSQKGDVYSFGILLYEMI-GRK 758
Cdd:cd14159   167 GTLAYLPE---EYVKTGTLSVEIDVYSFGVVLLELLtGRR 203
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
598-817 9.45e-15

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: 75.68  E-value: 9.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  598 RSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSDILKGMIYLHDSEIIs 677
Cdd:cd05065    50 RDFLSEASIMGQFDHPNIIHLEGVVTKSRPVMIITEFMENGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYV- 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  678 HGNLRSSNCLIDSRWVCQISDFGLHE-LKAGQEEPN-KSELELKRAL-CMAPELLrdAYRpgRGSQKGDVYSFGILLYEM 754
Cdd:cd05065   129 HRDLAARNILVNSNLVCKVSDFGLSRfLEDDTSDPTyTSSLGGKIPIrWTAPEAI--AYR--KFTSASDVWSYGIVMWEV 204
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161076872  755 IGrkgpWGDTAY---SKEEIIQFVKcpemlQHGVFRPAlththLDIPDYIRKCLCQCWDEDPEVRP 817
Cdd:cd05065   205 MS----YGERPYwdmSNQDVINAIE-----QDYRLPPP-----MDCPTALHQLMLDCWQKDRNLRP 256
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
585-755 9.92e-15

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: 75.87  E-value: 9.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  585 AMKKI-HKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEdLHLDHMFISSLVSDI 663
Cdd:cd14046    35 AIKKIkLRSESKNNSRILREVMLLSRLNHQHVVRYYQAWIERANLYIQMEYCEKSTLRDLIDSG-LFQDTDRLWRLFRQI 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  664 LKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL-HELKAGQEEP----NKSELELKR-----------ALCMAPE 727
Cdd:cd14046   114 LEGLAYIHSQGII-HRDLKPVNIFLDSNGNVKIGDFGLaTSNKLNVELAtqdiNKSTSAALGssgdltgnvgtALYVAPE 192
                         170       180
                  ....*....|....*....|....*...
gi 161076872  728 LLRDayRPGRGSQKGDVYSFGILLYEMI 755
Cdd:cd14046   193 VQSG--TKSTYNEKVDMYSLGIIFFEMC 218
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
581-816 1.00e-14

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


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 75.34  E-value: 1.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMK-----KIHKKSVDitrSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVL-----ANEDlh 650
Cdd:cd14009    18 GEVVAIKeisrkKLNKKLQE---NLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDLSQYIrkrgrLPEA-- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  651 ldhmFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSR---WVCQISDFGLhelkAGQEEPNKseleLKRALC---- 723
Cdd:cd14009    93 ----VARHFMQQLASGLKFLRSKNII-HRDLKPQNLLLSTSgddPVLKIADFGF----ARSLQPAS----MAETLCgspl 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  724 -MAPELLR----DAyrpgrgsqKGDVYSFGILLYEMIGRKGPWgdTAYSKEEIIQFVKCPEmlqhGVFRPALT-HTHLDI 797
Cdd:cd14009   160 yMAPEILQfqkyDA--------KADLWSVGAILFEMLVGKPPF--RGSNHVQLLRNIERSD----AVIPFPIAaQLSPDC 225
                         250
                  ....*....|....*....
gi 161076872  798 PDYIRKCLCQcwdeDPEVR 816
Cdd:cd14009   226 KDLLRRLLRR----DPAER 240
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
581-825 1.15e-14

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


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 75.25  E-value: 1.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSV--DITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLED-VLANEDLHLD---HM 654
Cdd:cd14003    25 GEKVAIKIIDKSKLkeEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEYASGGELFDyIVNNGRLSEDearRF 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  655 FISslvsdILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSelelkralC-----MAPELL 729
Cdd:cd14003   105 FQQ-----LISAVDYCHSNGIV-HRDLKLENILLDKNGNLKIIDFGLSNEFRGGSLLKTF--------CgtpayAAPEVL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  730 RDAYRPGRgsqKGDVYSFGILLYEMIGRKGPWGDTAYSK-EEIIQFVKCPEmlqhgvfrpaltHTHL--DIPDYIRKCLc 806
Cdd:cd14003   171 LGRKYDGP---KADVWSLGVILYAMLTGYLPFDDDNDSKlFRKILKGKYPI------------PSHLspDARDLIRRML- 234
                         250
                  ....*....|....*....
gi 161076872  807 qcwDEDPEVRPDIRLVRMH 825
Cdd:cd14003   235 ---VVDPSKRITIEEILNH 250
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
557-828 1.23e-14

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: 75.58  E-value: 1.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  557 ICRQSILVVGEPNKRSFTNIalFRGN-----------IVAMKKIHKKSVDITR-SIRKELKLMREVRHENIINFIGASTD 624
Cdd:cd05049     2 IKRDTIVLKRELGEGAFGKV--FLGEcynlepeqdkmLVAVKTLKDASSPDARkDFEREAELLTNLQHENIVKFYGVCTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  625 HGSVIIFTTYCARGSLEDVLANEDLHLDHMF----------ISSLV---SDILKGMIYLHDSEIIsHGNLRSSNCLIDSR 691
Cdd:cd05049    80 GDPLLMVFEYMEHGDLNKFLRSHGPDAAFLAsedsapgeltLSQLLhiaVQIASGMVYLASQHFV-HRDLATRNCLVGTN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  692 WVCQISDFGLHE-------LKAGqeepNKSELELKralCMAPELLRdaYRpgRGSQKGDVYSFGILLYEMIGR-KGPWgd 763
Cdd:cd05049   159 LVVKIGDFGMSRdiystdyYRVG----GHTMLPIR---WMPPESIL--YR--KFTTESDVWSFGVVLWEIFTYgKQPW-- 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161076872  764 TAYSKEEIIQFVKCPEMLQhgvfRPAlththlDIPDYIRKCLCQCWDEDPEVRPDIRLVRMHLKE 828
Cdd:cd05049   226 FQLSNTEVIECITQGRLLQ----RPR------TCPSEVYAVMLGCWKREPQQRLNIKDIHKRLQE 280
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
584-819 1.83e-14

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: 75.06  E-value: 1.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDITRSIRKELKLMREV-RHENIINFIGASTDHGS----VIIFTTYCaRGSLEDVLAN-------EDLHL 651
Cdd:cd13985    28 YALKRMYFNDEEQLRVAIKEIEIMKRLcGHPNIVQYYDSAILSSEgrkeVLLLMEYC-PGSLVDILEKsppsplsEEEVL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  652 DHMFisslvsDILKGMIYLH-DSEIISHGNLRSSNCLIDSRWVCQISDFG----LHELKAGQEEPNKSELELKR---ALC 723
Cdd:cd13985   107 RIFY------QICQAVGHLHsQSPPIIHRDIKIENILFSNTGRFKLCDFGsattEHYPLERAEEVNIIEEEIQKnttPMY 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  724 MAPELLrDAYRPGRGSQKGDVYSFGILLYEMIGRKGPWGDTAYSKeeiIQFVKCPEMLQHGvFRPALThthldipDYIRK 803
Cdd:cd13985   181 RAPEMI-DLYSKKPIGEKADIWALGCLLYKLCFFKLPFDESSKLA---IVAGKYSIPEQPR-YSPELH-------DLIRH 248
                         250
                  ....*....|....*.
gi 161076872  804 CLcqcwDEDPEVRPDI 819
Cdd:cd13985   249 ML----TPDPAERPDI 260
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
584-820 1.92e-14

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: 76.21  E-value: 1.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDITRS-IRKELKLMREV-RHENIINFIGASTDHGSVIIFTTYCARGSLEDVL-ANEDLHLDHMF----- 655
Cdd:cd05100    47 VAVKMLKDDATDKDLSdLVSEMEMMKMIgKHKNIINLLGACTQDGPLYVLVEYASKGNLREYLrARRPPGMDYSFdtckl 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  656 ------ISSLVS---DILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL----HELKAGQEEPNkSELELKral 722
Cdd:cd05100   127 peeqltFKDLVScayQVARGMEYLASQKCI-HRDLAARNVLVTEDNVMKIADFGLardvHNIDYYKKTTN-GRLPVK--- 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  723 CMAPELLRDAYRpgrgSQKGDVYSFGILLYEmIGRKGPWGDTAYSKEEIIQFVKcpemLQHGVFRPAlTHTHlDIPDYIR 802
Cdd:cd05100   202 WMAPEALFDRVY----THQSDVWSFGVLLWE-IFTLGGSPYPGIPVEELFKLLK----EGHRMDKPA-NCTH-ELYMIMR 270
                         250
                  ....*....|....*...
gi 161076872  803 kclcQCWDEDPEVRPDIR 820
Cdd:cd05100   271 ----ECWHAVPSQRPTFK 284
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
602-817 2.01e-14

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: 74.66  E-value: 2.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  602 KELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSDILKGMIYLHDSEIIsHGNL 681
Cdd:cd05085    42 SEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGGDFLSFLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCI-HRDL 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  682 RSSNCLIDSRWVCQISDFGLHElkagQEEP---NKSELELKRALCMAPEllrdAYRPGRGSQKGDVYSFGILLYE----- 753
Cdd:cd05085   121 AARNCLVGENNALKISDFGMSR----QEDDgvySSSGLKQIPIKWTAPE----ALNYGRYSSESDVWSFGILLWEtfslg 192
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161076872  754 MIGRKGPWGDTAYSKEEIIQFVKCPemlQHgvfrpalththldIPDYIRKCLCQCWDEDPEVRP 817
Cdd:cd05085   193 VCPYPGMTNQQAREQVEKGYRMSAP---QR-------------CPEDIYKIMQRCWDYNPENRP 240
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
560-761 2.85e-14

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: 75.14  E-value: 2.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  560 QSILVVGEPNKR--------------SFTNIALFRGNIVAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDH 625
Cdd:cd06656     9 RSIVSVGDPKKKytrfekigqgasgtVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  626 GSVIIFTTYCARGSLEDVLAneDLHLDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelk 705
Cdd:cd06656    89 DELWVVMEYLAGGSLTDVVT--ETCMDEGQIAAVCRECLQALDFLHSNQVI-HRDIKSDNILLGMDGSVKLTDFGF---- 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 161076872  706 AGQEEPNKSELE--LKRALCMAPELL-RDAYRPgrgsqKGDVYSFGILLYEMIGRKGPW 761
Cdd:cd06656   162 CAQITPEQSKRStmVGTPYWMAPEVVtRKAYGP-----KVDIWSLGIMAIEMVEGEPPY 215
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
584-839 2.99e-14

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: 75.00  E-value: 2.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDITRS-IRKELKLMREV-RHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANE------------DL 649
Cdd:cd05099    47 VAVKMLKDNATDKDLAdLISEMELMKLIgKHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARrppgpdytfditKV 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  650 HLDHMFISSLVS---DILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL----HELKAGQEEPNkSELELKral 722
Cdd:cd05099   127 PEEQLSFKDLVScayQVARGMEYLESRRCI-HRDLAARNVLVTEDNVMKIADFGLargvHDIDYYKKTSN-GRLPVK--- 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  723 CMAPELLRD-AYrpgrgSQKGDVYSFGILLYEMIGRKG-PWGDTAYskEEIIQFVKcpemLQHGVFRPAlththlDIPDY 800
Cdd:cd05099   202 WMAPEALFDrVY-----THQSDVWSFGILMWEIFTLGGsPYPGIPV--EELFKLLR----EGHRMDKPS------NCTHE 264
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 161076872  801 IRKCLCQCWDEDPEVRPDIRLVRMHLKELQAGLKPNIFD 839
Cdd:cd05099   265 LYMLMRECWHAVPTQRPTFKQLVEALDKVLAAVSEEYLD 303
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
583-847 3.02e-14

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: 74.06  E-value: 3.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  583 IVAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVL-ANEDLHLDHMFISSLVS 661
Cdd:cd14057    22 VAKILKVRDVTTRISRDFNEEYPRLRIFSHPNVLPVLGACNSPPNLVVISQYMPYGSLYNVLhEGTGVVVDQSQAVKFAL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  662 DILKGMIYLHDSE-IISHGNLRSSNCLIDSRWVCQISdfgLHELKAGQEEPNKseleLKRALCMAPELLRDAYRPgRGSQ 740
Cdd:cd14057   102 DIARGMAFLHTLEpLIPRHHLNSKHVMIDEDMTARIN---MADVKFSFQEPGK----MYNPAWMAPEALQKKPED-INRR 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  741 KGDVYSFGILLYEMIGRKGPWGDtaYSKEEIIQFVkcpemlqhgvfrpALTHTHLDIPDYIRKCLCQ----CWDEDPEVR 816
Cdd:cd14057   174 SADMWSFAILLWELVTREVPFAD--LSNMEIGMKI-------------ALEGLRVTIPPGISPHMCKlmkiCMNEDPGKR 238
                         250       260       270
                  ....*....|....*....|....*....|.
gi 161076872  817 PDirlvrmhlkelqaglkpniFDNMLSIMEK 847
Cdd:cd14057   239 PK-------------------FDMIVPILEK 250
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
581-820 5.09e-14

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: 73.21  E-value: 5.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIhkksvDITRSIRK-------ELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVL-ANEDLHLD 652
Cdd:cd08529    25 GRVYALKQI-----DISRMSRKmreeaidEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEYAENGDLHSLIkSQRGRPLP 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  653 HMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEepNKSELELKRALCMAPELLRD- 731
Cdd:cd08529   100 EDQIWKFFIQTLLGLSHLHSKKIL-HRDIKSMNIFLDKGDNVKIGDLGVAKILSDTT--NFAQTIVGTPYYLSPELCEDk 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  732 AYrpgrgSQKGDVYSFGILLYEMIGRKGPWgDTAYSKEEIIQFVKcpemlqhGVFRPALTHTHLDIPDYIRKCLCQcwde 811
Cdd:cd08529   177 PY-----NEKSDVWALGCVLYELCTGKHPF-EAQNQGALILKIVR-------GKYPPISASYSQDLSQLIDSCLTK---- 239

                  ....*....
gi 161076872  812 DPEVRPDIR 820
Cdd:cd08529   240 DYRQRPDTT 248
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
560-761 5.32e-14

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: 73.99  E-value: 5.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  560 QSILVVGEPNKR--------------SFTNIALFRGNIVAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDH 625
Cdd:cd06654    10 RSIVSVGDPKKKytrfekigqgasgtVYTAMDVATGQEVAIRQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  626 GSVIIFTTYCARGSLEDVLAneDLHLDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelk 705
Cdd:cd06654    90 DELWVVMEYLAGGSLTDVVT--ETCMDEGQIAAVCRECLQALEFLHSNQVI-HRDIKSDNILLGMDGSVKLTDFGF---- 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 161076872  706 AGQEEPNKSELE--LKRALCMAPELL-RDAYRPgrgsqKGDVYSFGILLYEMIGRKGPW 761
Cdd:cd06654   163 CAQITPEQSKRStmVGTPYWMAPEVVtRKAYGP-----KVDIWSLGIMAIEMIEGEPPY 216
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
581-816 6.41e-14

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: 73.66  E-value: 6.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVDITRS-IRKELKLMREVRH---ENIINFIGASTDHGSVIIFTTYCARGSLEDVLanEDLHLDHMFI 656
Cdd:cd06917    26 GRVVALKVLNLDTDDDDVSdIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSLWIIMDYCEGGSIRTLM--RAGPIAERYI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  657 SSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkAGQEEPNKSelelKRALC------MAPELLR 730
Cdd:cd06917   104 AVIMREVLVALKFIHKDGII-HRDIKAANILVTNTGNVKLCDFGV----AASLNQNSS----KRSTFvgtpywMAPEVIT 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  731 DayrpGRG-SQKGDVYSFGILLYEMIgrkgpWGDTAYSKEEIIQFV-----KCPEMLQHGVFRPALThthldipDYIRKC 804
Cdd:cd06917   175 E----GKYyDTKADIWSLGITTYEMA-----TGNPPYSDVDALRAVmlipkSKPPRLEGNGYSPLLK-------EFVAAC 238
                         250
                  ....*....|..
gi 161076872  805 LcqcwDEDPEVR 816
Cdd:cd06917   239 L----DEEPKDR 246
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
581-701 6.58e-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: 73.76  E-value: 6.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKI---HKKSVD--ITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCArGSLEDVLANEDLHLDHMF 655
Cdd:cd07841    25 GRIVAIKKIklgERKEAKdgINFTALREIKLLQELKHPNIIGLLDVFGHKSNINLVFEFME-TDLEKVIKDKSIVLTPAD 103
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 161076872  656 ISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL 701
Cdd:cd07841   104 IKSYMLMTLRGLEYLHSNWIL-HRDLKPNNLLIASDGVLKLADFGL 148
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
610-816 7.20e-14

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: 73.53  E-value: 7.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  610 VRHENIINFIgASTDHGSVI-----IFTTYCARGSLEDVLANEDLHLDHMfiSSLVSDILKGMIYLHD----------SE 674
Cdd:cd14140    46 MKHENLLQFI-AAEKRGSNLemelwLITAFHDKGSLTDYLKGNIVSWNEL--CHIAETMARGLSYLHEdvprckgeghKP 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  675 IISHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRALCMAPELLRDAYRPGRGS-QKGDVYSFGILLYE 753
Cdd:cd14140   123 AIAHRDFKSKNVLLKNDLTAVLADFGLAVRFEPGKPPGDTHGQVGTRRYMAPEVLEGAINFQRDSfLRIDMYAMGLVLWE 202
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161076872  754 MIGR----KGPWGDTAYSKEEIIQFVKCPEMLQ----HGVFRPALTHTHLDIPDYIRKCLC--QCWDEDPEVR 816
Cdd:cd14140   203 LVSRckaaDGPVDEYMLPFEEEIGQHPSLEDLQevvvHKKMRPVFKDHWLKHPGLAQLCVTieECWDHDAEAR 275
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
580-827 7.58e-14

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: 73.51  E-value: 7.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  580 RGNIVAMKKIhkKSVDITRS---IRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLH------ 650
Cdd:cd05090    33 HAQLVAIKTL--KDYNNPQQwneFQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFEFMNQGDLHEFLIMRSPHsdvgcs 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  651 ----------LDHMFISSLVSDILKGMIYLhDSEIISHGNLRSSNCLIDSRWVCQISDFGL-HELKAGQ--EEPNKSELE 717
Cdd:cd05090   111 sdedgtvkssLDHGDFLHIAIQIAAGMEYL-SSHFFVHKDLAARNILVGEQLHVKISDLGLsREIYSSDyyRVQNKSLLP 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  718 LKralCMAPEllrdAYRPGRGSQKGDVYSFGILLYEMI--GRKGPWGdtaYSKEEIIQFVK------CPEmlqhgvfrpa 789
Cdd:cd05090   190 IR---WMPPE----AIMYGKFSSDSDIWSFGVVLWEIFsfGLQPYYG---FSNQEVIEMVRkrqllpCSE---------- 249
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 161076872  790 lththlDIPDYIRKCLCQCWDEDPEVRPDIRLVRMHLK 827
Cdd:cd05090   250 ------DCPPRMYSLMTECWQEIPSRRPRFKDIHARLR 281
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
580-755 8.25e-14

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: 73.52  E-value: 8.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  580 RGNIVAMKKIHKKSVD--ITRSIRKELKLMREVR-HENIINFIGASTDHGSVIIFTTYCARgSLEDVLANEDLHLDHMFI 656
Cdd:cd07832    24 TGETVALKKVALRKLEggIPNQALREIKALQACQgHPYVVKLRDVFPHGTGFVLVFEYMLS-SLSEVLRDEERPLTEAQV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  657 SSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRALcMAPELLrdayrpg 736
Cdd:cd07832   103 KRYMRMLLKGVAYMHANRIM-HRDLKPANLLISSTGVLKIADFGLARLFSEEDPRLYSHQVATRWY-RAPELL------- 173
                         170       180
                  ....*....|....*....|...
gi 161076872  737 RGSQK----GDVYSFGILLYEMI 755
Cdd:cd07832   174 YGSRKydegVDLWAVGCIFAELL 196
PBP1_taste_receptor cd06363
ligand-binding domain of the T1R taste receptor; Ligand-binding domain of the T1R taste ...
64-244 8.49e-14

ligand-binding domain of the T1R taste receptor; Ligand-binding domain of the T1R taste receptor. The T1R is a member of the family C receptors within the G-protein coupled receptor superfamily, which also includes the metabotropic glutamate receptors, GABAb receptors, the calcium-sensing receptor (CaSR), the V2R pheromone receptors, and a small group of uncharacterized orphan receptors.


Pssm-ID: 380586 [Multi-domain]  Cd Length: 418  Bit Score: 75.04  E-value: 8.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   64 LAIEDVNKNPNLLPGKKLAFKPVDigHKMSAYRVKP-LRAMTQMREAG-------------VTAFIGPD--ESCTTEALL 127
Cdd:cd06363    50 FAVEEINNSSDLLPGVTLGYEIFD--TCSDAVNFRPtLSFLSQNGSHDievqcnytnyqprVVAVIGPDssELALTTAKL 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  128 ASAWNTPMLSFKCSDPIVSNKSTFHTFARTLAPASKVSKSVISLLNAFHWNKFSIVVSSKPiWGSDVARAIQELAEARNF 207
Cdd:cd06363   128 LGFFLMPQISYGASSEELSNKLLYPSFLRTVPSDKYQVEAMVQLLQEFGWNWVAFLGSDDE-YGQDGLQLFSEKAANTGI 206
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 161076872  208 TISHFKYISDYIPTTKTLSQIDKIIEETYATTrIYVF 244
Cdd:cd06363   207 CVAYQGLIPTDTDPKPKYQDILKKINQTKVNV-VVVF 242
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
584-817 8.80e-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: 72.76  E-value: 8.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSV---DITRSIRKELKLMREVRHENIINFIGASTDHgSVIIFTTYCARGSLEDVLAnedLHLDHMFISSLV 660
Cdd:cd05040    26 VAVKCLKSDVLsqpNAMDDFLKEVNAMHSLDHPNLIRLYGVVLSS-PLMMVTELAPLGSLLDRLR---KDQGHFLISTLC 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 S---DILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKR--ALCmAPELLRdaYRp 735
Cdd:cd05040   102 DyavQIANGMAYLESKRFI-HRDLAARNILLASKDKVKIGDFGLMRALPQNEDHYVMQEHRKVpfAWC-APESLK--TR- 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  736 gRGSQKGDVYSFGILLYEMI--GRKgPWgdTAYSKEEIIQFV-KCPEMLQhgvfRPAlththlDIPDYIRKCLCQCWDED 812
Cdd:cd05040   177 -KFSHASDVWMFGVTLWEMFtyGEE-PW--LGLNGSQILEKIdKEGERLE----RPD------DCPQDIYNVMLQCWAHK 242

                  ....*
gi 161076872  813 PEVRP 817
Cdd:cd05040   243 PADRP 247
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
598-850 1.00e-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: 73.49  E-value: 1.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  598 RSIRKELKLMREV-RHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANED-LHLDHMF--------------ISSLVS 661
Cdd:cd05089    47 RDFAGELEVLCKLgHHPNIINLLGACENRGYLYIAIEYAPYGNLLDFLRKSRvLETDPAFakehgtastltsqqLLQFAS 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  662 DILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHElkaGQEEPNKSELELKRALCMAPELLRDAYRpgrgSQK 741
Cdd:cd05089   127 DVAKGMQYLSEKQFI-HRDLAARNVLVGENLVSKIADFGLSR---GEEVYVKKTMGRLPVRWMAIESLNYSVY----TTK 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  742 GDVYSFGILLYEMIGrkgpWGDTAYSKeeiiqfVKCPEM---LQHGvFRpalTHTHLDIPDYIRKCLCQCWDEDPEVRPD 818
Cdd:cd05089   199 SDVWSFGVLLWEIVS----LGGTPYCG------MTCAELyekLPQG-YR---MEKPRNCDDEVYELMRQCWRDRPYERPP 264
                         250       260       270
                  ....*....|....*....|....*....|..
gi 161076872  819 IRLVRMHLKELQAGLKPNIfdNMlSIMEKYAY 850
Cdd:cd05089   265 FSQISVQLSRMLEARKAYV--NM-ALFENFTY 293
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
585-753 1.02e-13

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: 72.34  E-value: 1.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  585 AMKKI---HKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCArGSLEDVLANEDlHLDHMFISSLVS 661
Cdd:cd14050    30 AVKRSrsrFRGEKDRKRKLEEVERHEKLGEHPNCVRFIKAWEEKGILYIQTELCD-TSLQQYCEETH-SLPESEVWNILL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  662 DILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL-HELKAGqeepNKSELELKRALCMAPELLRdayrpGRGSQ 740
Cdd:cd14050   108 DLLKGLKHLHDHGLI-HLDIKPANIFLSKDGVCKLGDFGLvVELDKE----DIHDAQEGDPRYMAPELLQ-----GSFTK 177
                         170
                  ....*....|...
gi 161076872  741 KGDVYSFGILLYE 753
Cdd:cd14050   178 AADIFSLGITILE 190
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
581-758 1.04e-13

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: 72.98  E-value: 1.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVD----ITrSIRkELKLMREVRHENIINFIGASTDH------GSVIIFTTYCARgSLEDVLANEDLH 650
Cdd:cd07840    24 GELVALKKIRMENEKegfpIT-AIR-EIKLLQKLDHPNVVRLKEIVTSKgsakykGSIYMVFEYMDH-DLTGLLDNPEVK 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  651 LDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkAGQEEPNKSELELKRALCM---APE 727
Cdd:cd07840   101 FTESQIKCYMKQLLEGLQYLHSNGIL-HRDIKGSNILINNDGVLKLADFGL----ARPYTKENNADYTNRVITLwyrPPE 175
                         170       180       190
                  ....*....|....*....|....*....|.
gi 161076872  728 LLRDAYRPGRGSqkgDVYSFGILLYEMIGRK 758
Cdd:cd07840   176 LLLGATRYGPEV---DMWSVGCILAELFTGK 203
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
584-805 1.49e-13

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: 71.94  E-value: 1.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVD---ITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDvLANEDLHLDHMFISSLV 660
Cdd:cd14162    28 VAIKIVSKKKAPedyLQKFLPREIEVIKGLKHPNLICFYEAIETTSRVYIIMELAENGDLLD-YIRKNGALPEPQARRWF 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHdSEIISHGNLRSSNCLIDSRWVCQISDFGlheLKAGQEEPNKSELELKRALC-----MAPELLR-DAYR 734
Cdd:cd14162   107 RQLVAGVEYCH-SKGVVHRDLKCENLLLDKNNNLKITDFG---FARGVMKTKDGKPKLSETYCgsyayASPEILRgIPYD 182
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161076872  735 PgrgsQKGDVYSFGILLYEMIGRKGPWGDTAYSKeeIIQFVkcpemlQHGVFRPALTHTHLDIPDYIRKCL 805
Cdd:cd14162   183 P----FLSDIWSMGVVLYTMVYGRLPFDDSNLKV--LLKQV------QRRVVFPKNPTVSEECKDLILRML 241
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
584-829 1.63e-13

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


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 72.69  E-value: 1.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDIT-RSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVL---------------ANE 647
Cdd:cd05045    33 VAVKMLKENASSSElRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRSFLresrkvgpsylgsdgNRN 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  648 DLHLDH-----MFISSLVS---DILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkagQEEPNKSELELK 719
Cdd:cd05045   113 SSYLDNpderaLTMGDLISfawQISRGMQYLAEMKLV-HRDLAARNVLVAEGRKMKISDFGL------SRDVYEEDSYVK 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  720 RAL------CMAPELLRDAYRpgrgSQKGDVYSFGILLYEMIGRKG-PWGDTAyskeeiiqfvkcPEMLqhgvFRPALTH 792
Cdd:cd05045   186 RSKgripvkWMAIESLFDHIY----TTQSDVWSFGVLLWEIVTLGGnPYPGIA------------PERL----FNLLKTG 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 161076872  793 THLDIPD----YIRKCLCQCWDEDPEVRPDIRLVRMHLKEL 829
Cdd:cd05045   246 YRMERPEncseEMYNLMLTCWKQEPDKRPTFADISKELEKM 286
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
598-817 2.26e-13

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: 71.88  E-value: 2.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  598 RSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSDILKGMIYLHDSEIIs 677
Cdd:cd05064    51 RGFLAEALTLGQFDHSNIVRLEGVITRGNTMMIVTEYMSNGALDSFLRKHEGQLVAGQLMGMLPGLASGMKYLSEMGYV- 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  678 HGNLRSSNCLIDSRWVCQISDFGlhELKAGQEEPNKSELELKR-ALCMAPEllrdAYRPGRGSQKGDVYSFGILLYEMIG 756
Cdd:cd05064   130 HKGLAAHKVLVNSDLVCKISGFR--RLQEDKSEAIYTTMSGKSpVLWAAPE----AIQYHHFSSASDVWSFGIVMWEVMS 203
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161076872  757 rkgpWGDTAY---SKEEIIQFVkcpemlQHGVFRPALTHThldiPDYIRKCLCQCWDEDPEVRP 817
Cdd:cd05064   204 ----YGERPYwdmSGQDVIKAV------EDGFRLPAPRNC----PNLLHQLMLDCWQKERGERP 253
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
581-817 2.38e-13

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: 71.68  E-value: 2.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIhKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVL--ANEDLhLDHMFISS 658
Cdd:cd05052    31 NLTVAVKTL-KEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYGNLLDYLreCNREE-LNAVVLLY 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  659 LVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHEL--------KAGQEEPNKselelkralCMAPELLr 730
Cdd:cd05052   109 MATQIASAMEYLEKKNFI-HRDLAARNCLVGENHLVKVADFGLSRLmtgdtytaHAGAKFPIK---------WTAPESL- 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  731 dAYRpgRGSQKGDVYSFGILLYEMigrkGPWGDTAYSKEEIIQFVkcpEMLQHG--VFRPAlththlDIPDYIRKCLCQC 808
Cdd:cd05052   178 -AYN--KFSIKSDVWAFGVLLWEI----ATYGMSPYPGIDLSQVY---ELLEKGyrMERPE------GCPPKVYELMRAC 241

                  ....*....
gi 161076872  809 WDEDPEVRP 817
Cdd:cd05052   242 WQWNPSDRP 250
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
581-758 2.68e-13

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: 72.35  E-value: 2.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKI--H--KKSVDITrSIRkELKLMREVRHENIINFI--------GASTDHGSVIIFTTYCARgSLEDVLANED 648
Cdd:cd07866    33 GRVVALKKIlmHneKDGFPIT-ALR-EIKILKKLKHPNVVPLIdmaverpdKSKRKRGSVYMVTPYMDH-DLSGLLENPS 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  649 LHLDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQ-EEPNKSELELKRALC---- 723
Cdd:cd07866   110 VKLTESQIKCYMLQLLEGINYLHENHIL-HRDIKAANILIDNQGILKIADFGLARPYDGPpPNPKGGGGGGTRKYTnlvv 188
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 161076872  724 ----MAPELLRDAYRPGRGSqkgDVYSFGILLYEMIGRK 758
Cdd:cd07866   189 trwyRPPELLLGERRYTTAV---DIWGIGCVFAEMFTRR 224
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
583-827 3.31e-13

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: 71.59  E-value: 3.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  583 IVAMKKIHKKS-VDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHL-------DHM 654
Cdd:cd05091    38 AVAIKTLKDKAeGPLREEFRHEAMLRSRLQHPNIVCLLGVVTKEQPMSMIFSYCSHGDLHEFLVMRSPHSdvgstddDKT 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  655 FISSL--------VSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL-HELKAGQ--EEPNKSELELKralC 723
Cdd:cd05091   118 VKSTLepadflhiVTQIAAGMEYLSSHHVV-HKDLATRNVLVFDKLNVKISDLGLfREVYAADyyKLMGNSLLPIR---W 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  724 MAPEllrdAYRPGRGSQKGDVYSFGILLYEMIGRkGPWGDTAYSKEEIIQFVK------CPEmlqhgvfrpalththlDI 797
Cdd:cd05091   194 MSPE----AIMYGKFSIDSDIWSYGVVLWEVFSY-GLQPYCGYSNQDVIEMIRnrqvlpCPD----------------DC 252
                         250       260       270
                  ....*....|....*....|....*....|
gi 161076872  798 PDYIRKCLCQCWDEDPEVRPDIRLVRMHLK 827
Cdd:cd05091   253 PAWVYTLMLECWNEFPSRRPRFKDIHSRLR 282
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
581-761 3.37e-13

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 72.55  E-value: 3.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKI---HKKSVdiTRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANedlhlDHMFIS 657
Cdd:PLN00034   99 GRLYALKVIygnHEDTV--RRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLEGTHIA-----DEQFLA 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  658 SLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSelELKRALCMAPELLRDAYRPGR 737
Cdd:PLN00034  172 DVARQILSGIAYLHRRHIV-HRDIKPSNLLINSAKNVKIADFGVSRILAQTMDPCNS--SVGTIAYMSPERINTDLNHGA 248
                         170       180       190
                  ....*....|....*....|....*....|...
gi 161076872  738 -GSQKGDVYSFGILLYEM--------IGRKGPW 761
Cdd:PLN00034  249 yDGYAGDIWSLGVSILEFylgrfpfgVGRQGDW 281
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
603-820 3.39e-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: 71.97  E-value: 3.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  603 ELKLMREV-RHENIINFIGASTDHGSVIIFTTYCARGSLEDVL-ANEDLHLDHMFISSLVSD--------------ILKG 666
Cdd:cd05101    79 EMEMMKMIgKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLrARRPPGMEYSYDINRVPEeqmtfkdlvsctyqLARG 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  667 MIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL----HELKAGQEEPNkSELELKralCMAPELLRDAYRpgrgSQKG 742
Cdd:cd05101   159 MEYLASQKCI-HRDLAARNVLVTENNVMKIADFGLardiNNIDYYKKTTN-GRLPVK---WMAPEALFDRVY----THQS 229
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161076872  743 DVYSFGILLYEMIGRKG-PWgdTAYSKEEIIQFVKcpemLQHGVFRPAlththlDIPDYIRKCLCQCWDEDPEVRPDIR 820
Cdd:cd05101   230 DVWSFGVLMWEIFTLGGsPY--PGIPVEELFKLLK----EGHRMDKPA------NCTNELYMMMRDCWHAVPSQRPTFK 296
PBP1_NPR_C cd06386
ligand-binding domain of type C natriuretic peptide receptor; Ligand-binding domain of type C ...
125-435 4.97e-13

ligand-binding domain of type C natriuretic peptide receptor; Ligand-binding domain of type C natriuretic peptide receptor (NPR-C). NPR-C is found in atrial, mesentery, placenta, lung, kidney, venous tissue, aortic smooth muscle, and aortic endothelial cells. The affinity of NPR-C for natriuretic peptides is ANP>CNP>BNP. The extracellular domain of NPR-C is about 30% identical to NPR-A and NPR-B. However, unlike the cyclase-linked receptors, it contains only 37 intracellular amino acids and no guanylyl cyclase activity. Major function of NPR-C is to clear natriuretic peptides from the circulation or extracellular surroundings through constitutive receptor-mediated internalization and degradation.


Pssm-ID: 380609 [Multi-domain]  Cd Length: 391  Bit Score: 72.20  E-value: 4.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  125 ALLASAWNTPMLSFKCSDPIVSNKSTFHTFARTLAPA-SKVSKSVISLLNAFHWNKFSIVVSSKPIWGSD--VARAIQEL 201
Cdd:cd06386    89 ARLASHWNLPMLSAGALAAGFSHKDSEYSHLTRVAPAyAKMGEMFLALFRHHHWSRAFLVYSDDKLERNCyfTLEGVHEV 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  202 AEARNFTISHFKYISdyiptTKTLSqIDKIIEETYATTRIYVFIgehiAMVDFVRGLQ---NRRLLESGDYIVVSVddEI 278
Cdd:cd06386   169 FQEEGLHTSIYSFDE-----TKDLD-LEEIVRNIQASERVVIMC----ASSDTIRSIMlvaHRHGMTNGDYAFFNI--EL 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  279 YDSNRRVNimernylDPYIRKEKSKSLDKISFRSVIKISMTYPQNPHIRDICSKIKDYARKTPFLVPyhqrvfDNISVPI 358
Cdd:cd06386   237 FNSSSYGN-------GSWKRGDKHDFEAKQAYSSLQTVTLLRTVKPEFEKFSMEVKSSVQKQGLNDE------DYVNMFV 303
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161076872  359 YGLHlyDSVMIYVRAITEVLRLGGDIYDGNLVMSHIFNRSYHSIQGfDVYIDSNGDAEGNYTVITLQN-DVGSGASIG 435
Cdd:cd06386   304 EGFH--DAILLYALALHEVLRNGYSKKDGGKIIQQTWNRTFEGIAG-QVSIDANGDRYGDFSVIAMTDvEAGTQEVIG 378
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
585-817 5.23e-13

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: 70.89  E-value: 5.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  585 AMKKIHKKSVDITRS-----IRKELKLMREVRHENIINFIG-ASTDHGSVIIFTTYCARgSLEDVL-ANEDLHLDHM--- 654
Cdd:cd14001    32 AVKKINSKCDKGQRSlyqerLKEEAKILKSLNHPNIVGFRAfTKSEDGSLCLAMEYGGK-SLNDLIeERYEAGLGPFpaa 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  655 FISSLVSDILKGMIYLHDSEIISHGNLRSSNCLIDSRW-VCQISDFG----LHELKAGQEEPNK----SElelkraLCMA 725
Cdd:cd14001   111 TILKVALSIARALEYLHNEKKILHGDIKSGNVLIKGDFeSVKLCDFGvslpLTENLEVDSDPKAqyvgTE------PWKA 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  726 PELLRDAyrpGRGSQKGDVYSFGILLYEMIGRKGP-----WGDTAYSKEEiiqfvkCPEM-----LQHGVF--RPALTHT 793
Cdd:cd14001   185 KEALEEG---GVITDKADIFAYGLVLWEMMTLSVPhlnllDIEDDDEDES------FDEDeedeeAYYGTLgtRPALNLG 255
                         250       260
                  ....*....|....*....|....*
gi 161076872  794 HLDIP-DYIRKCLCQCWDEDPEVRP 817
Cdd:cd14001   256 ELDDSyQKVIELFYACTQEDPKDRP 280
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
581-820 5.24e-13

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: 71.11  E-value: 5.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKS-VDITRSIRKELKLMREVRHENIINFIGASTDHG--SVIIFTTYCARGSLEDVLANEDLHLDHMFIS 657
Cdd:cd05079    33 GEQVAVKSLKPESgGNHIADLKKEIEILRNLYHENIVKYKGICTEDGgnGIKLIMEFLPSGSLKEYLPRNKNKINLKQQL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  658 SLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKR-ALCMAPELLRDA--YR 734
Cdd:cd05079   113 KYAVQICKGMDYLGSRQYV-HRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVKDDLDSpVFWYAPECLIQSkfYI 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  735 pgrgsqKGDVYSFGILLYEMIgrkgPWGDTAYSKEEIIQFVKCPEMLQHGVFRPALTHTH-------LDIPDYIRKCLCQ 807
Cdd:cd05079   192 ------ASDVWSFGVTLYELL----TYCDSESSPMTLFLKMIGPTHGQMTVTRLVRVLEEgkrlprpPNCPEEVYQLMRK 261
                         250
                  ....*....|...
gi 161076872  808 CWDEDPEVRPDIR 820
Cdd:cd05079   262 CWEFQPSKRTTFQ 274
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
584-764 5.77e-13

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: 70.29  E-value: 5.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSV---DITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGS-LEDVLANEDLHLD---HMFi 656
Cdd:cd14080    30 VACKIIDKKKApkdFLEKFLPRELEILRKLRHPNIIQVYSIFERGSKVFIFMEYAEHGDlLEYIQKRGALSESqarIWF- 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  657 sslvSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkaGQEEPNKSELELKRALC-----MAPELLRD 731
Cdd:cd14080   109 ----RQLALAVQYLHSLDIA-HRDLKCENILLDSNNNVKLSDFGF-----ARLCPDDDGDVLSKTFCgsaayAAPEILQG 178
                         170       180       190
                  ....*....|....*....|....*....|....
gi 161076872  732 -AYRPgrgsQKGDVYSFGILLYEMIGRKGPWGDT 764
Cdd:cd14080   179 iPYDP----KKYDIWSLGVILYIMLCGSMPFDDS 208
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
583-761 6.02e-13

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: 70.41  E-value: 6.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  583 IVAMKKIHKKSVDITR-----SIRKELKLMREVRHENIINFIGASTD-HGSVIIFTTYCARGSLEDVLAnEDLHLDHMFI 656
Cdd:cd13994    22 LYAVKEYRRRDDESKRkdyvkRLTSEYIISSKLHHPNIVKVLDLCQDlHGKWCLVMEYCPGGDLFTLIE-KADSLSLEEK 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  657 SSLVSDILKGMIYLHDSEIiSHGNLRSSNCLIDSRWVCQISDFGLHE-LKAGQEepnkSELELKRALC-----MAPELLR 730
Cdd:cd13994   101 DCFFKQILRGVAYLHSHGI-AHRDLKPENILLDEDGVLKLTDFGTAEvFGMPAE----KESPMSAGLCgsepyMAPEVFT 175
                         170       180       190
                  ....*....|....*....|....*....|.
gi 161076872  731 DAYRPGRGsqkGDVYSFGILLYEMIGRKGPW 761
Cdd:cd13994   176 SGSYDGRA---VDVWSCGIVLFALFTGRFPW 203
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
610-830 6.48e-13

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: 70.84  E-value: 6.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  610 VRHENIINFIGASTDHGSVII----FTTYCARGSLEDVLANEDLHLDHMfiSSLVSDILKGMIYLHD---------SEII 676
Cdd:cd14141    46 MKHENILQFIGAEKRGTNLDVdlwlITAFHEKGSLTDYLKANVVSWNEL--CHIAQTMARGLAYLHEdipglkdghKPAI 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  677 SHGNLRSSNCLIDSRWVCQISDFGLH-ELKAGQEEPNK-SELELKRAlcMAPELLRDAYRPGRGS-QKGDVYSFGILLYE 753
Cdd:cd14141   124 AHRDIKSKNVLLKNNLTACIADFGLAlKFEAGKSAGDThGQVGTRRY--MAPEVLEGAINFQRDAfLRIDMYAMGLVLWE 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  754 MIGR----KGPWGDTAYS-KEEIIQFVKCPEMLQ---HGVFRPALTHTHLDIPDYIRKC--LCQCWDEDPEVRPDIRLVR 823
Cdd:cd14141   202 LASRctasDGPVDEYMLPfEEEVGQHPSLEDMQEvvvHKKKRPVLRECWQKHAGMAMLCetIEECWDHDAEARLSAGCVE 281

                  ....*..
gi 161076872  824 MHLKELQ 830
Cdd:cd14141   282 ERIIQMQ 288
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
581-817 8.22e-13

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


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 69.97  E-value: 8.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIH-KKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLanEDLHLDHMFISSL 659
Cdd:cd06609    26 NQVVAIKVIDlEEAEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIMEYCGGGSVLDLL--KPGPLDETYIAFI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  660 VSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkAGQEEPNKSelelKR------ALCMAPELLRD-A 732
Cdd:cd06609   104 LREVLLGLEYLHSEGKI-HRDIKAANILLSEEGDVKLADFGV----SGQLTSTMS----KRntfvgtPFWMAPEVIKQsG 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  733 YrpgrgSQKGDVYSFGILLYEMIGRKGPWGDtaYSKEEIIQFV-KC-PEMLQHGVFRPALThthldipDYIRKCLCqcwd 810
Cdd:cd06609   175 Y-----DEKADIWSLGITAIELAKGEPPLSD--LHPMRVLFLIpKNnPPSLEGNKFSKPFK-------DFVELCLN---- 236

                  ....*..
gi 161076872  811 EDPEVRP 817
Cdd:cd06609   237 KDPKERP 243
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
579-816 8.95e-13

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: 70.16  E-value: 8.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  579 FRGNIVAMKKIhkksvditrSIRKELKLMREV--------RHENIINFIGA-STDHGS---VIIFTTYCARGSLEDVLAN 646
Cdd:cd14143    16 WRGEDVAVKIF---------SSREERSWFREAeiyqtvmlRHENILGFIAAdNKDNGTwtqLWLVSDYHEHGSLFDYLNR 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  647 EDLHLDHMFisSLVSDILKGMIYLHdSEI--------ISHGNLRSSNCLIDSRWVCQISDFGL---HELKAGQEE-PNKS 714
Cdd:cd14143    87 YTVTVEGMI--KLALSIASGLAHLH-MEIvgtqgkpaIAHRDLKSKNILVKKNGTCCIADLGLavrHDSATDTIDiAPNH 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  715 ELELKRAlcMAPELLRDAYRPGR--GSQKGDVYSFGILLYEMIGR----------KGPWGDTAYSKEEIIQF--VKCPEM 780
Cdd:cd14143   164 RVGTKRY--MAPEVLDDTINMKHfeSFKRADIYALGLVFWEIARRcsiggihedyQLPYYDLVPSDPSIEEMrkVVCEQK 241
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 161076872  781 LQHGVfrPALTHTHlDIPDYIRKCLCQCWDEDPEVR 816
Cdd:cd14143   242 LRPNI--PNRWQSC-EALRVMAKIMRECWYANGAAR 274
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
583-760 1.15e-12

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: 70.45  E-value: 1.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  583 IVAMKKIH---KKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCArGSLEDVLANEDLHLDHMFISSL 659
Cdd:cd06633    48 VVAIKKMSysgKQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEYCL-GSASDLLEVHKKPLQEVEIAAI 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  660 VSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGlhelKAGQEEPNKSelELKRALCMAPELLRdAYRPGRGS 739
Cdd:cd06633   127 THGALQGLAYLHSHNMI-HRDIKAGNILLTEPGQVKLADFG----SASIASPANS--FVGTPYWMAPEVIL-AMDEGQYD 198
                         170       180
                  ....*....|....*....|.
gi 161076872  740 QKGDVYSFGILLYEMIGRKGP 760
Cdd:cd06633   199 GKVDIWSLGITCIELAERKPP 219
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
583-820 1.24e-12

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: 70.04  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  583 IVAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVL-----------------A 645
Cdd:cd05094    37 LVAVKTLKDPTLAARKDFQREAELLTNLQHDHIVKFYGVCGDGDPLIMVFEYMKHGDLNKFLrahgpdamilvdgqprqA 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  646 NEDLHLDHMFisSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRALCMA 725
Cdd:cd05094   117 KGELGLSQML--HIATQIASGMVYLASQHFV-HRDLATRNCLVGANLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMP 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  726 PELLrdAYRpgRGSQKGDVYSFGILLYEMIGR-KGPWgdTAYSKEEIIQFVKCPEMLQhgvfRPALThthldiPDYIRKC 804
Cdd:cd05094   194 PESI--MYR--KFTTESDVWSFGVILWEIFTYgKQPW--FQLSNTEVIECITQGRVLE----RPRVC------PKEVYDI 257
                         250
                  ....*....|....*.
gi 161076872  805 LCQCWDEDPEVRPDIR 820
Cdd:cd05094   258 MLGCWQREPQQRLNIK 273
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
567-817 1.24e-12

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: 70.04  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  567 EPNKrsFTNIAlfrgniVAMKKIHKKSVDITRSIrKELKLMREV-RHENIINFIGASTDHGSVIIFTTYCARGSLEDVLA 645
Cdd:cd05098    41 KPNR--VTKVA------VKMLKSDATEKDLSDLI-SEMEMMKMIgKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQ 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  646 -----------NED-LHLDHMFISSLVS---DILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL----HELKA 706
Cdd:cd05098   112 arrppgmeycyNPShNPEEQLSSKDLVScayQVARGMEYLASKKCI-HRDLAARNVLVTEDNVMKIADFGLardiHHIDY 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  707 GQEEPNkSELELKralCMAPELLRDAYRpgrgSQKGDVYSFGILLYEMIGRKG-PWgdTAYSKEEIIQFVKcpemLQHGV 785
Cdd:cd05098   191 YKKTTN-GRLPVK---WMAPEALFDRIY----THQSDVWSFGVLLWEIFTLGGsPY--PGVPVEELFKLLK----EGHRM 256
                         250       260       270
                  ....*....|....*....|....*....|..
gi 161076872  786 FRPALTHTHLdipdYIRkcLCQCWDEDPEVRP 817
Cdd:cd05098   257 DKPSNCTNEL----YMM--MRDCWHAVPSQRP 282
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
603-816 1.26e-12

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: 70.08  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  603 ELKLMRevrHENIINFIGAS---TDHGSV--IIFTTYCARGSLEDVLANEDLhlDHMFISSLVSDILKGMIYLHdSEI-- 675
Cdd:cd14054    42 ELPLME---HSNILRFIGADerpTADGRMeyLLVLEYAPKGSLCSYLRENTL--DWMSSCRMALSLTRGLAYLH-TDLrr 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  676 -------ISHGNLRSSNCLIDSRWVCQISDFGL--------HELKAGQEEPNKSELELKRALCMAPELLRDA--YRPGRG 738
Cdd:cd14054   116 gdqykpaIAHRDLNSRNVLVKADGSCVICDFGLamvlrgssLVRGRPGAAENASISEVGTLRYMAPEVLEGAvnLRDCES 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  739 SQK-GDVYSFGILLYEMI--------GRKGPWGDTAYSKE-------EIIQFVKCpEMLQHGVFRPALTHTHLDiPDYIR 802
Cdd:cd14054   196 ALKqVDVYALGLVLWEIAmrcsdlypGESVPPYQMPYEAElgnhptfEDMQLLVS-REKARPKFPDAWKENSLA-VRSLK 273
                         250
                  ....*....|....
gi 161076872  803 KCLCQCWDEDPEVR 816
Cdd:cd14054   274 ETIEDCWDQDAEAR 287
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
590-819 1.58e-12

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: 69.27  E-value: 1.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  590 HKKSVDITRSIRkELKLMREVRHENIINFIGA-STDHGSVIIFTTYCARGSLedvlaneDLHL-DHMFIS-----SLVSD 662
Cdd:cd13990    42 EKKQNYIKHALR-EYEIHKSLDHPRIVKLYDVfEIDTDSFCTVLEYCDGNDL-------DFYLkQHKSIPerearSIIMQ 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  663 ILKGMIYL--HDSEIIsHGNLRSSNCLIDSRWVC---QISDFGLHELkAGQEEPNKSELELKRALC-----MAPELLRDA 732
Cdd:cd13990   114 VVSALKYLneIKPPII-HYDLKPGNILLHSGNVSgeiKITDFGLSKI-MDDESYNSDGMELTSQGAgtywyLPPECFVVG 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  733 YRPGRGSQKGDVYSFGILLYEMI-GRKgPWGDTaySKEEIIQFVKCPEMLQHGVFrPALTHTHLDIPDYIRKCLCQcwde 811
Cdd:cd13990   192 KTPPKISSKVDVWSVGVIFYQMLyGRK-PFGHN--QSQEAILEENTILKATEVEF-PSKPVVSSEAKDFIRRCLTY---- 263

                  ....*...
gi 161076872  812 DPEVRPDI 819
Cdd:cd13990   264 RKEDRPDV 271
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
584-817 1.64e-12

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


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 69.37  E-value: 1.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDIT-RSIRKELKLMREVRHENIINFIGASTDHgSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSD 662
Cdd:cd05057    39 VAIKVLREETGPKAnEEILDEAYVMASVDHPHLVRLLGICLSS-QVQLITQLMPLGCLLDYVRNHRDNIGSQLLLNWCVQ 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  663 ILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSE---LELKralCMAPELLRDayrpGRGS 739
Cdd:cd05057   118 IAKGMSYLEEKRLV-HRDLAARNVLVKTPNHVKITDFGLAKLLDVDEKEYHAEggkVPIK---WMALESIQY----RIYT 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  740 QKGDVYSFGILLYEMI--GRKgPWgdtayskeEIIQFVKCPEMLQHGVFRPALTHTHLDIpdYIrkCLCQCWDEDPEVRP 817
Cdd:cd05057   190 HKSDVWSYGVTVWELMtfGAK-PY--------EGIPAVEIPDLLEKGERLPQPPICTIDV--YM--VLVKCWMIDAESRP 256
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
581-701 2.27e-12

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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: 69.05  E-value: 2.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVD--ITRS-IRkELKLMREVRHENIINFIGASTDHGSVIIFTTYCARgSLEDVLANEDLHLDHMFIS 657
Cdd:cd07829    24 GEIVALKKIRLDNEEegIPSTaLR-EISLLKELKHPNIVKLLDVIHTENKLYLVFEYCDQ-DLKKYLDKRPGPLPPNLIK 101
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 161076872  658 SLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL 701
Cdd:cd07829   102 SIMYQLLRGLAYCHSHRIL-HRDLKPQNLLINRDGVLKLADFGL 144
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
583-876 2.33e-12

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: 69.28  E-value: 2.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  583 IVAMKKIH---KKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCArGSLEDVLANEDLHLDHMFISSL 659
Cdd:cd06634    42 VVAIKKMSysgKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEYCL-GSASDLLEVHKKPLQEVEIAAI 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  660 VSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAgqeePNKSelELKRALCMAPELLRdAYRPGRGS 739
Cdd:cd06634   121 THGALQGLAYLHSHNMI-HRDVKAGNILLTEPGLVKLGDFGSASIMA----PANS--FVGTPYWMAPEVIL-AMDEGQYD 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  740 QKGDVYSFGILLYEMIGRKGP-WGDTAYSKEEIIQFVKCPeMLQHGVFRpalththldipDYIRKCLCQCWDEDPEVRPD 818
Cdd:cd06634   193 GKVDVWSLGITCIELAERKPPlFNMNAMSALYHIAQNESP-ALQSGHWS-----------EYFRNFVDSCLQKIPQDRPT 260
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 161076872  819 IRLVRMHlKELQAGLKPNIfdnmlsIMEKYAYNLEGlVQERTNLLYEEKKKtdmLLYQ 876
Cdd:cd06634   261 SDVLLKH-RFLLRERPPTV------IMDLIQRTKDA-VRELDNLQYRKMKK---ILFQ 307
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
581-758 2.35e-12

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


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 69.48  E-value: 2.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHK---KSVDITRSIRkELKLMREVRHENIINFI-----GASTDHGSVIIFTTYcARGSLEDVL-ANEDLHL 651
Cdd:cd07834    25 GRKVAIKKISNvfdDLIDAKRILR-EIKILRHLKHENIIGLLdilrpPSPEEFNDVYIVTEL-METDLHKVIkSPQPLTD 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  652 DHmfISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkAGQEEPNKSELELKRALCM----APE 727
Cdd:cd07834   103 DH--IQYFLYQILRGLKYLHSAGVI-HRDLKPSNILVNSNCDLKICDFGL----ARGVDPDEDKGFLTEYVVTrwyrAPE 175
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 161076872  728 LLrdayrpgrGSQKG-----DVYSFGILLYEMIGRK 758
Cdd:cd07834   176 LL--------LSSKKytkaiDIWSVGCIFAELLTRK 203
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
598-817 2.98e-12

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: 68.16  E-value: 2.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  598 RSIRKELKLMREVRHENIINFIGAS------TDHGSVIIFTTYCARGSLEDVLANEDlHLDHMFISSLVSDILKGMIYLH 671
Cdd:cd14012    43 QLLEKELESLKKLRHPNLVSYLAFSierrgrSDGWKVYLLTEYAPGGSLSELLDSVG-SVPLDTARRWTLQLLEALEYLH 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  672 DSEIIsHGNLRSSNCLIDSRW---VCQISDFGL-----HELKAGQEEPNKSELELkralcmAPELLRDAYRPGRgsqKGD 743
Cdd:cd14012   122 RNGVV-HKSLHAGNVLLDRDAgtgIVKLTDYSLgktllDMCSRGSLDEFKQTYWL------PPELAQGSKSPTR---KTD 191
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161076872  744 VYSFGILLYEMIgrkgpwgdtaySKEEIIQFVKCPemlqHGVFRPALTHTHLDipDYIRKCLCQcwdeDPEVRP 817
Cdd:cd14012   192 VWDLGLLFLQML-----------FGLDVLEKYTSP----NPVLVSLDLSASLQ--DFLSKCLSL----DPKKRP 244
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
581-757 3.48e-12

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: 68.62  E-value: 3.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHkksVDITRSIR----KELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLaNEDLHLDHMFI 656
Cdd:cd06615    26 GLIMARKLIH---LEIKPAIRnqiiRELKVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVL-KKAGRIPENIL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  657 SSLVSDILKGMIYLHDSEIISHGNLRSSNCLIDSRWVCQISDFG----LHELKAGQEEPNKSElelkralcMAPELLrda 732
Cdd:cd06615   102 GKISIAVLRGLTYLREKHKIMHRDVKPSNILVNSRGEIKLCDFGvsgqLIDSMANSFVGTRSY--------MSPERL--- 170
                         170       180
                  ....*....|....*....|....*....
gi 161076872  733 yrpgRGSQ---KGDVYSFGILLYEM-IGR 757
Cdd:cd06615   171 ----QGTHytvQSDIWSLGLSLVEMaIGR 195
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
602-823 3.52e-12

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: 67.88  E-value: 3.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  602 KELKLMREVRHENIINFIGAS-TDHGSVIIFTTYCARGSLEDVLANEDlhlDHMFISSLVS---DILKGMIYLHDSEIIs 677
Cdd:cd05058    45 KEGIIMKDFSHPNVLSLLGIClPSEGSPLVVLPYMKHGDLRNFIRSET---HNPTVKDLIGfglQVAKGMEYLASKKFV- 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  678 HGNLRSSNCLIDSRWVCQISDFGL------HELKAGQEEPNkSELELKralCMAPELLRDAyrpgRGSQKGDVYSFGILL 751
Cdd:cd05058   121 HRDLAARNCMLDESFTVKVADFGLardiydKEYYSVHNHTG-AKLPVK---WMALESLQTQ----KFTTKSDVWSFGVLL 192
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161076872  752 YEMIGRKGPWGDTAYSKEEIIQFVKCPEMLQhgvfrPALThthldiPDYIRKCLCQCWDEDPEVRPDIR-LVR 823
Cdd:cd05058   193 WELMTRGAPPYPDVDSFDITVYLLQGRRLLQ-----PEYC------PDPLYEVMLSCWHPKPEMRPTFSeLVS 254
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
583-876 3.64e-12

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: 68.92  E-value: 3.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  583 IVAMKKIH---KKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCArGSLEDVLANEDLHLDHMFISSL 659
Cdd:cd06635    52 VVAIKKMSysgKQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEYCL-GSASDLLEVHKKPLQEIEIAAI 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  660 VSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGlhelKAGQEEPNKSelELKRALCMAPELLRdAYRPGRGS 739
Cdd:cd06635   131 THGALQGLAYLHSHNMI-HRDIKAGNILLTEPGQVKLADFG----SASIASPANS--FVGTPYWMAPEVIL-AMDEGQYD 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  740 QKGDVYSFGILLYEMIGRKGPWGDtayskeeiiqfVKCPEMLQHGVFRPALTHTHLDIPDYIRKCLCQCWDEDPEVRPDI 819
Cdd:cd06635   203 GKVDVWSLGITCIELAERKPPLFN-----------MNAMSALYHIAQNESPTLQSNEWSDYFRNFVDSCLQKIPQDRPTS 271
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 161076872  820 RLVRMHLKELQAglKPNifdnmlSIMEKYAYNLEGLVQERTNLLYEEKKKtdmLLYQ 876
Cdd:cd06635   272 EELLKHMFVLRE--RPE------TVLIDLIQRTKDAVRELDNLQYRKMKK---LLFQ 317
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
611-757 3.91e-12

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: 68.62  E-value: 3.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  611 RHENIINFIGAS-TDHGS---VIIFTTYCARGSLEDVLANEDLhlDHMFISSLVSDILKGMIYLHdSEI--------ISH 678
Cdd:cd14142    57 RHENILGFIASDmTSRNSctqLWLITHYHENGSLYDYLQRTTL--DHQEMLRLALSAASGLVHLH-TEIfgtqgkpaIAH 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  679 GNLRSSNCLIDSRWVCQISDFGL---HELKAGQEEP-NKSELELKRAlcMAPELLR--------DAYRpgrgsqKGDVYS 746
Cdd:cd14142   134 RDLKSKNILVKSNGQCCIADLGLavtHSQETNQLDVgNNPRVGTKRY--MAPEVLDetintdcfESYK------RVDIYA 205
                         170
                  ....*....|.
gi 161076872  747 FGILLYEMIGR 757
Cdd:cd14142   206 FGLVLWEVARR 216
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
583-760 4.00e-12

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: 67.86  E-value: 4.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  583 IVAMKKIH---KKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCArGSLEDVLANEDLHLDHMFISSL 659
Cdd:cd06607    28 VVAIKKMSysgKQSTEKWQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVMEYCL-GSASDIVEVHKKPLQEVEIAAI 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  660 VSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAgqeePNKSelELKRALCMAPELLRdAYRPGRGS 739
Cdd:cd06607   107 CHGALQGLAYLHSHNRI-HRDVKAGNILLTEPGTVKLADFGSASLVC----PANS--FVGTPYWMAPEVIL-AMDEGQYD 178
                         170       180
                  ....*....|....*....|.
gi 161076872  740 QKGDVYSFGILLYEMIGRKGP 760
Cdd:cd06607   179 GKVDVWSLGITCIELAERKPP 199
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
583-829 4.88e-12

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: 68.14  E-value: 4.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  583 IVAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVL------------ANEDLH 650
Cdd:cd05093    37 LVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLrahgpdavlmaeGNRPAE 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  651 LDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRALCMAPELLr 730
Cdd:cd05093   117 LTQSQMLHIAQQIAAGMVYLASQHFV-HRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESI- 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  731 dAYRpgRGSQKGDVYSFGILLYEMIGR-KGPWgdTAYSKEEIIQFVKCPEMLQhgvfRPALThthldiPDYIRKCLCQCW 809
Cdd:cd05093   195 -MYR--KFTTESDVWSLGVVLWEIFTYgKQPW--YQLSNNEVIECITQGRVLQ----RPRTC------PKEVYDLMLGCW 259
                         250       260
                  ....*....|....*....|
gi 161076872  810 DEDPEVRPDIRLVRMHLKEL 829
Cdd:cd05093   260 QREPHMRLNIKEIHSLLQNL 279
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
578-816 5.54e-12

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: 67.38  E-value: 5.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  578 LFRGNIVAMKKIHKKSVD-------ITRSIRKELKLMREV-RHENIINFIGASTDHGSVIIFTTYCARGSL-EDVLANED 648
Cdd:cd13993    22 LRTGRKYAIKCLYKSGPNskdgndfQKLPQLREIDLHRRVsRHPNIITLHDVFETEVAIYIVLEYCPNGDLfEAITENRI 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  649 LHLDHMFISSLVSDILKGMIYLHdSEIISHGNLRSSNCLID-SRWVCQISDFGLhelkaGQEEPNKSELELKRALCMAPE 727
Cdd:cd13993   102 YVGKTELIKNVFLQLIDAVKHCH-SLGIYHRDIKPENILLSqDEGTVKLCDFGL-----ATTEKISMDFGVGSEFYMAPE 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  728 LLRDAYRPGRG--SQKGDVYSFGILLYEMIGRKGPWgdTAYSKEEIIqfvkcpeMLQHGVFRPALTHTHLDIPDYIRKCL 805
Cdd:cd13993   176 CFDEVGRSLKGypCAAGDIWSLGIILLNLTFGRNPW--KIASESDPI-------FYDYYLNSPNLFDVILPMSDDFYNLL 246
                         250
                  ....*....|.
gi 161076872  806 CQCWDEDPEVR 816
Cdd:cd13993   247 RQIFTVNPNNR 257
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
593-831 5.98e-12

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: 67.64  E-value: 5.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  593 SVDITRSIRkELKLMREVRHENIINFIGAS------------------TDHGSVIIFTtycargsLEDVLANEDLHLDHM 654
Cdd:cd05074    52 SSDIEEFLR-EAACMKEFDHPNVIKLIGVSlrsrakgrlpipmvilpfMKHGDLHTFL-------LMSRIGEEPFTLPLQ 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  655 FISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL-HELKAGQ--EEPNKSELELKralCMAPELLRD 731
Cdd:cd05074   124 TLVRFMIDIASGMEYLSSKNFI-HRDLAARNCMLNENMTVCVADFGLsKKIYSGDyyRQGCASKLPVK---WLALESLAD 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  732 AYRpgrgSQKGDVYSFGILLYEMIGRkgpwGDTAYS---KEEIIQFVKCPEMLQhgvfRPalththLDIPDYIRKCLCQC 808
Cdd:cd05074   200 NVY----TTHSDVWAFGVTMWEIMTR----GQTPYAgveNSEIYNYLIKGNRLK----QP------PDCLEDVYELMCQC 261
                         250       260
                  ....*....|....*....|...
gi 161076872  809 WDEDPEVRPDIRLVRMHLKELQA 831
Cdd:cd05074   262 WSPEPKCRPSFQHLRDQLELIWG 284
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
580-828 6.42e-12

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: 67.69  E-value: 6.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  580 RGNIVAMKKIHKksvDITRSIR----KELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDL------ 649
Cdd:cd05097    43 QPVLVAVKMLRA---DVTKTARndflKEIKIMSRLKNPNIIRLLGVCVSDDPLCMITEYMENGDLNQFLSQREIestfth 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  650 --HLDHMFISSLV---SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL-HELKAGQEEPNKSELELK-RAL 722
Cdd:cd05097   120 anNIPSVSIANLLymaVQIASGMKYLASLNFV-HRDLATRNCLVGNHYTIKIADFGMsRNLYSGDYYRIQGRAVLPiRWM 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  723 CMAPELLrdayrpGRGSQKGDVYSFGILLYEM--IGRKGPWgdTAYSKEEIIQfvKCPEMLQHGVFRPALTHTHLdIPDY 800
Cdd:cd05097   199 AWESILL------GKFTTASDVWAFGVTLWEMftLCKEQPY--SLLSDEQVIE--NTGEFFRNQGRQIYLSQTPL-CPSP 267
                         250       260
                  ....*....|....*....|....*...
gi 161076872  801 IRKCLCQCWDEDPEVRPDIRLVRMHLKE 828
Cdd:cd05097   268 VFKLMMRCWSRDIKDRPTFNKIHHFLRE 295
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
581-753 7.19e-12

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: 67.45  E-value: 7.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVDITRSIR--KELKLMREVR---HENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLH--LDH 653
Cdd:cd14052    26 GKVYAVKKLKPNYAGAKDRLRrlEEVSILRELTldgHDNIVQLIDSWEYHGHLYIQTELCENGSLDVFLSELGLLgrLDE 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  654 MFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEpnkSELELKRALcMAPELLRDA- 732
Cdd:cd14052   106 FRVWKILVELSLGLRFIHDHHFV-HLDLKPANVLITFEGTLKIGDFGMATVWPLIRG---IEREGDREY-IAPEILSEHm 180
                         170       180
                  ....*....|....*....|.
gi 161076872  733 YrpgrgSQKGDVYSFGILLYE 753
Cdd:cd14052   181 Y-----DKPADIFSLGLILLE 196
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
602-817 7.48e-12

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: 67.41  E-value: 7.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  602 KELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVL------ANEDLHLDHMFISSLVSDILKGMIYLHDSEI 675
Cdd:cd05036    58 MEALIMSKFNHPNIVRCIGVCFQRLPRFILLELMAGGDLKSFLrenrprPEQPSSLTMLDLLQLAQDVAKGCRYLEENHF 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  676 IsHGNLRSSNCLI---DSRWVCQISDFGL--------HELKAGqeepnKSELELKralCMAPEllrdAYRPGRGSQKGDV 744
Cdd:cd05036   138 I-HRDIAARNCLLtckGPGRVAKIGDFGMardiyradYYRKGG-----KAMLPVK---WMPPE----AFLDGIFTSKTDV 204
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161076872  745 YSFGILLYEMIGrkgpWGDTAY---SKEEIIQFVKCPEMLQhgvfRPAlththlDIPDYIRKCLCQCWDEDPEVRP 817
Cdd:cd05036   205 WSFGVLLWEIFS----LGYMPYpgkSNQEVMEFVTSGGRMD----PPK------NCPGPVYRIMTQCWQHIPEDRP 266
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
584-795 9.90e-12

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: 66.96  E-value: 9.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDITRSIR-KELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLhLDHMFISSLVSD 662
Cdd:cd14202    31 VAVKCINKKNLAKSQTLLgKEIKILKELKHENIVALYDFQEIANSVYLVMEYCNGGDLADYLHTMRT-LSEDTIRLFLQQ 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  663 ILKGMIYLHDSEIIsHGNLRSSNCLI--------DSRWVC-QISDFGLHELKAGQeepnkselELKRALC-----MAPEL 728
Cdd:cd14202   110 IAGAMKMLHSKGII-HRDLKPQNILLsysggrksNPNNIRiKIADFGFARYLQNN--------MMAATLCgspmyMAPEV 180
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161076872  729 LRDAYRPGrgsqKGDVYSFGILLYEMIGRKGPWgdTAYSKEEIIQFVKCPEMLQHGVfrPALTHTHL 795
Cdd:cd14202   181 IMSQHYDA----KADLWSIGTIIYQCLTGKAPF--QASSPQDLRLFYEKNKSLSPNI--PRETSSHL 239
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
581-755 1.04e-11

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: 66.39  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVDITRSI---RKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEdLHLDHMFIS 657
Cdd:cd05123    18 GKLYAMKVLRKKEIIKRKEVehtLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGELFSHLSKE-GRFPEERAR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  658 SLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkagqEEPNKSELELKRALC-----MAPELLRda 732
Cdd:cd05123    97 FYAAEIVLALEYLHSLGII-YRDLKPENILLDSDGHIKLTDFGL-------AKELSSDGDRTYTFCgtpeyLAPEVLL-- 166
                         170       180
                  ....*....|....*....|....
gi 161076872  733 yrpGRGSQKG-DVYSFGILLYEMI 755
Cdd:cd05123   167 ---GKGYGKAvDWWSLGVLLYEML 187
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
580-755 1.14e-11

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: 67.44  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  580 RGNIVAMKKIHKKSVDITRSIR--KELKLMREVRHENIINFIGASTDHGSVIIFttycargslEDV-----LANEDLH-- 650
Cdd:cd07850    24 TGQNVAIKKLSRPFQNVTHAKRayRELVLMKLVNHKNIIGLLNVFTPQKSLEEF---------QDVylvmeLMDANLCqv 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  651 ----LDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGqeepnkselelkrALCMAP 726
Cdd:cd07850    95 iqmdLDHERMSYLLYQMLCGIKHLHSAGII-HRDLKPSNIVVKSDCTLKILDFGLARTAGT-------------SFMMTP 160
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 161076872  727 ELLRDAYRP-----GRG-SQKGDVYSFGILLYEMI 755
Cdd:cd07850   161 YVVTRYYRApevilGMGyKENVDIWSVGCIMGEMI 195
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
568-817 1.16e-11

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 66.51  E-value: 1.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  568 PNKRSFTNI--ALFRGNIVAMKKIHKKSVdiTRSIRKELKLMREVRHENIINFIGASTDHGSVIIftTYCARGSLEDVLA 645
Cdd:cd14068     2 LGDGGFGSVyrAVYRGEDVAVKIFNKHTS--FRLLRQELVVLSHLHHPSLVALLAAGTAPRMLVM--ELAPKGSLDALLQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  646 NEDLHLDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLI-----DSRWVCQISDFGLHE------LKAGQEEPNks 714
Cdd:cd14068    78 QDNASLTRTLQHRIALHVADGLRYLHSAMII-YRDLKPHNVLLftlypNCAIIAKIADYGIAQyccrmgIKTSEGTPG-- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  715 elelkralCMAPELLRD--AYrpgrgSQKGDVYSFGILLYEMIGrkgpwgdtaySKEEIIQFVKCP----EMLQHGVFRP 788
Cdd:cd14068   155 --------FRAPEVARGnvIY-----NQQADVYSFGLLLYDILT----------CGERIVEGLKFPnefdELAIQGKLPD 211
                         250       260
                  ....*....|....*....|....*....
gi 161076872  789 ALTHTHLDIPDYIRKCLCQCWDEDPEVRP 817
Cdd:cd14068   212 PVKEYGCAPWPGVEALIKDCLKENPQCRP 240
PBP1_mGluR cd06362
ligand binding domain of metabotropic glutamate receptors (mGluR); Ligand binding domain of ...
65-425 1.17e-11

ligand binding domain of metabotropic glutamate receptors (mGluR); Ligand binding domain of the metabotropic glutamate receptors (mGluR), which are members of the family C of G-protein-coupled receptors that transduce extracellular signals into G-protein activation and ultimately into cellular responses. mGluRs bind to glutamate and function as an excitatory neurotransmitter; they are involved in learning, memory, anxiety, and the perception of pain. Eight subtypes of mGluRs have been cloned so far, and are classified into three groups according to their sequence similarities, transduction mechanisms, and pharmacological profiles. Group I is composed of mGlu1R and mGlu5R that both stimulate PLC hydrolysis. Group II includes mGlu2R and mGlu3R, which inhibit adenylyl cyclase, as do mGlu4R, mGlu6R, mGlu7R, and mGlu8R, which form group III.


Pssm-ID: 380585 [Multi-domain]  Cd Length: 460  Bit Score: 68.47  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   65 AIEDVNKNPNLLPGKKLAFKPVDIGHKMSA-----------------------YRVKPLRAMTQMREAGVTAFIGPDESC 121
Cdd:cd06362    39 AIDEINSRPDLLPNITLGFVILDDCSSDTTaleqalhfirdsllsqesagfcqCSDDPPNLDESFQFYDVVGVIGAESSS 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  122 TTEAL--LASAWNTPMLSFKCSDPIVSNKSTFHTFARTLAPASKVSKSVISLLNAFHWNKFSIVVSSKPiWGSDVARAIQ 199
Cdd:cd06362   119 VSIQVanLLRLFKIPQISYASTSDELSDKERYPYFLRTVPSDSFQAKAIVDILLHFNWTYVSVVYSEGS-YGEEGYKAFK 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  200 ELAEARNFTISHfkyiSDYIPTTKTLSQIDKIIEETYATTRIYVfigehiaMVDFVRGLQNRRLLE-------SGDYIVV 272
Cdd:cd06362   198 KLARKAGICIAE----SERISQDSDEKDYDDVIQKLLQKKNARV-------VVLFADQEDIRGLLRaakrlgaSGRFIWL 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  273 -----SVDDEIYDSNRRV--NIMernYLDPYIRKEKS-----KSLDKISFRsvikismtypQNPHIRDI------CSkiK 334
Cdd:cd06362   267 gsdgwGTNIDDLKGNEDValGAL---TVQPYSEEVPRfddyfKSLTPSNNT----------RNPWFREFwqelfqCS--F 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  335 DYARKTPFLVPYHQRVFDNISVPIYGLH-LYDSVMIYVRAITEVLR-----------LGGDIYDGNLVMSHIFNRSYHSI 402
Cdd:cd06362   332 RPSRENSCNDDKLLINKSEGYKQESKVSfVIDAVYAFAHALHKMHKdlcpgdtglcqDLMKCIDGSELLEYLLNVSFTGE 411
                         410       420
                  ....*....|....*....|...
gi 161076872  403 QGFDVYIDSNGDAEGNYTVITLQ 425
Cdd:cd06362   412 AGGEIRFDENGDGPGRYDIMNFQ 434
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
583-827 1.30e-11

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: 66.53  E-value: 1.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  583 IVAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANE--------------- 647
Cdd:cd05092    37 LVAVKALKEATESARQDFQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYMRHGDLNRFLRSHgpdakildggegqap 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  648 -DLHLDHMFisSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHE-------LKAGqeepNKSELELK 719
Cdd:cd05092   117 gQLTLGQML--QIASQIASGMVYLASLHFV-HRDLATRNCLVGQGLVVKIGDFGMSRdiystdyYRVG----GRTMLPIR 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  720 ralCMAPELLrdAYRpgRGSQKGDVYSFGILLYEMIGR-KGPWgdTAYSKEEIIQFVKCPEMLQhgvfRPALThthldiP 798
Cdd:cd05092   190 ---WMPPESI--LYR--KFTTESDIWSFGVVLWEIFTYgKQPW--YQLSNTEAIECITQGRELE----RPRTC------P 250
                         250       260
                  ....*....|....*....|....*....
gi 161076872  799 DYIRKCLCQCWDEDPEVRPDIRLVRMHLK 827
Cdd:cd05092   251 PEVYAIMQGCWQREPQQRHSIKDIHSRLQ 279
PHA02988 PHA02988
hypothetical protein; Provisional
534-826 1.41e-11

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 66.69  E-value: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  534 DMKDVTVINLGEYNNPTNknifqICRQSILVVGEPNKRSFTNiALFRGNIVAM---KKIHKKSVDITRSIRKELKLMREV 610
Cdd:PHA02988    2 NIITRSYINDIKCIESDD-----IDKYTSVLIKENDQNSIYK-GIFNNKEVIIrtfKKFHKGHKVLIDITENEIKNLRRI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  611 RHENIIN----FIGASTDHGSVIIFTTYCARGSLEDVLANEDlHLDHMFISSLVSDILKGMIYLHDSEIISHGNLRSSNC 686
Cdd:PHA02988   76 DSNNILKiygfIIDIVDDLPRLSLILEYCTRGYLREVLDKEK-DLSFKTKLDMAIDCCKGLYNLYKYTNKPYKNLTSVSF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  687 LIDSRWVCQISDFGLHELKagqeepnkSELELKRALCMA---PELLRDAYRPGrgSQKGDVYSFGILLYEMIGRKGPWGD 763
Cdd:PHA02988  155 LVTENYKLKIICHGLEKIL--------SSPPFKNVNFMVyfsYKMLNDIFSEY--TIKDDIYSLGVVLWEIFTGKIPFEN 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161076872  764 TAYskEEIIQFVkcpeMLQHGVFRpalthTHLDIPDYIRKCLCQCWDEDPEVRPDIRLVRMHL 826
Cdd:PHA02988  225 LTT--KEIYDLI----INKNNSLK-----LPLDCPLEIKCIVEACTSHDSIKRPNIKEILYNL 276
PBP1_sensory_GC_DEF-like cd06371
ligand-binding domain of membrane guanylyl cyclases (GC-D, GC-E, and GC-F) that are ...
64-422 1.46e-11

ligand-binding domain of membrane guanylyl cyclases (GC-D, GC-E, and GC-F) that are specifically expressed in sensory tissues; This group includes the ligand-binding domain of membrane guanylyl cyclases (GC-D, GC-E, and GC-F) that are specifically expressed in sensory tissues. They share a similar topology with an N-terminal extracellular ligand-binding domain, a single transmembrane domain, and a C-terminal cytosolic region that contains kinase-like and catalytic domains. GC-D is specifically expressed in a subpopulation of olfactory sensory neurons. GC-E and GC-F are colocalized within the same photoreceptor cells of the retina and have important roles in phototransduction. Unlike the other family members, GC-E and GC-F have no known extracellular ligands. Instead, they are activated under low calcium conditions by guanylyl cyclase activating proteins called GCAPs. GC-D expressing neurons have been implicated in pheromone detection and GC-D is phylogenetically more similar to the Ca2+-regulated GC-E and GC-F than to receptor GC-A, -B and -C which are activated by peptide ligands. Moreover, these olfactory GCs and retinal GCs share characteristic sequence similarity in a regulatory domain that is involved in the binding of GCAPs, suggesting GC-D activity may be regulated by an unknown extracellular ligand and intracellular Ca2+. Rodent GC-D-expressing neurons have been implicated in pheromone detection and were recently shown to respond to atmospheric CO2 which is an olfactory stimulus for many invertebrates and regulates some insect innate behavior, such as the location of food and hosts.


Pssm-ID: 380594 [Multi-domain]  Cd Length: 379  Bit Score: 67.72  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   64 LAIEDVNKNPNLLPGKKLAFKPVDIGHKMSayrvKPLRAMTQMrEAGVTAFIGPDE--SCTTEALLASAWNTPMLSFKCS 141
Cdd:cd06371    25 LAVSRINKDPSLDLGYWFDYVILPEDCETS----KALAAFSSA-EGRASGFVGPVNpgYCEAASLLAQEWDKALFSWGCV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  142 DPivsNKSTFHTFARTLAPASKVsksVISLLNAFHWNKFSIVVSSKPIWgsdVARAiQELAEA-RNFTIShfkyisdyIP 220
Cdd:cd06371   100 NH---ELNSYPTFARTLPPPADV---LYTVLRYFRWAHVAVVSSPQDLW---VETG-RELASAlRARGLP--------VG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  221 TTKTLSQIDKIIEETYATT----RIYVFIgehiaMV---DFVRGLQNRRLLE--------SGDYIVVSVDDEIYDSNRRV 285
Cdd:cd06371   162 LVTSMEPSDSGAREALKRIrdadRVRVVI-----MCmhsVLIGGEEQRTLLEaahdmgltDGSYVFVPYDTLLYSLPYKH 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  286 nimernylDPYIRKEKSKSLDKiSFRSVIKISMTYPQNPhIRDICSKIKDYaRKTPFLVPYHQrvfdnISvPIYGLhLYD 365
Cdd:cd06371   237 --------EPYAVLRNNSKLRR-AYDAVLTITMESPEGS-FYEAFRRAQER-GELPSDLDPEQ-----VS-PLFGT-IYN 298
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 161076872  366 SVMIYVRAITEVLRLGGDIYDGNLVmSHIFNRSYHsiqGF--DVYIDSNGDAEGNYTVI 422
Cdd:cd06371   299 SIYLLAGAVENARAAGGGVSGASLA-RHARNAQFP---GFnqLLRTDSGGNGQPSYVIL 353
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
583-817 1.52e-11

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: 66.39  E-value: 1.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  583 IVAMKKIHKK-SVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVS 661
Cdd:cd05050    37 MVAVKMLKEEaSADMQADFQREAALMAEFDHPNIVKLLGVCAVGKPMCLLFEYMAYGDLNEFLRHRSPRAQCSLSHSTSS 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  662 ---------------------DILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKR 720
Cdd:cd05050   117 arkcglnplplscteqlciakQVAAGMAYLSERKFV-HRDLATRNCLVGENMVVKIADFGLSRNIYSADYYKASENDAIP 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  721 ALCMAPELLRDAyrpgRGSQKGDVYSFGILLYEMIGrkgpWGDTAY---SKEEIIQFVK------CPEmlqhgvfrpalt 791
Cdd:cd05050   196 IRWMPPESIFYN----RYTTESDVWAYGVVLWEIFS----YGMQPYygmAHEEVIYYVRdgnvlsCPD------------ 255
                         250       260
                  ....*....|....*....|....*.
gi 161076872  792 HTHLDIPDYIRKclcqCWDEDPEVRP 817
Cdd:cd05050   256 NCPLELYNLMRL----CWSKLPSDRP 277
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
581-755 1.77e-11

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: 66.83  E-value: 1.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHK--KSVDITRSIRKELKLMREVRHENIIN----FIGASTDhgsvIIFTTYCARGSLEDVLANEDlhLDHM 654
Cdd:cd07856    35 GQNVAVKKIMKpfSTPVLAKRTYRELKLLKHLRHENIISlsdiFISPLED----IYFVTELLGTDLHRLLTSRP--LEKQ 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  655 FISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkAGQEEPNKSELELKRALcMAPELLRdAYR 734
Cdd:cd07856   109 FIQYFLYQILRGLKYVHSAGVI-HRDLKPSNILVNENCDLKICDFGL----ARIQDPQMTGYVSTRYY-RAPEIML-TWQ 181
                         170       180
                  ....*....|....*....|.
gi 161076872  735 pgRGSQKGDVYSFGILLYEMI 755
Cdd:cd07856   182 --KYDVEVDIWSAGCIFAEML 200
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
584-825 1.98e-11

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: 65.78  E-value: 1.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVD---ITRSIRKELKLMREVRHENIINF--IGASTDhGSVIIFTTYCARGSLEDVLANEDLHLDHMfISS 658
Cdd:cd14163    28 VAIKIIDKSGGPeefIQRFLPRELQIVERLDHKNIIHVyeMLESAD-GKIYLVMELAEDGDVFDCVLHGGPLPEHR-AKA 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  659 LVSDILKGMIYLHDSEIiSHGNLRSSNCLIDSRWVcQISDFGLHELKAgqeepnKSELELKRALC-----MAPELLRDAy 733
Cdd:cd14163   106 LFRQLVEAIRYCHGCGV-AHRDLKCENALLQGFTL-KLTDFGFAKQLP------KGGRELSQTFCgstayAAPEVLQGV- 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  734 rpGRGSQKGDVYSFGILLYEMIGRKGPWGDTayskeeiiqfvKCPEML---QHGVFRPalthTHLDIPDYIRKCLCQCWD 810
Cdd:cd14163   177 --PHDSRKGDIWSMGVVLYVMLCAQLPFDDT-----------DIPKMLcqqQKGVSLP----GHLGVSRTCQDLLKRLLE 239
                         250
                  ....*....|....*
gi 161076872  811 EDPEVRPDIRLVRMH 825
Cdd:cd14163   240 PDMVLRPSIEEVSWH 254
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
583-825 1.98e-11

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: 66.23  E-value: 1.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  583 IVAMKKIH-KKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLhlDHMFISSLVS 661
Cdd:cd06642    31 VVAIKIIDlEEAEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGGGSALDLLKPGPL--EETYIATILR 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  662 DILKGMIYLHdSEIISHGNLRSSNCLIDSRWVCQISDFGLhelkAGQeepnKSELELKR------ALCMAPELLR-DAYr 734
Cdd:cd06642   109 EILKGLDYLH-SERKIHRDIKAANVLLSEQGDVKLADFGV----AGQ----LTDTQIKRntfvgtPFWMAPEVIKqSAY- 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  735 pgrgSQKGDVYSFGILLYEMIGRKGPWGDTAYSKEEIIQFVKCPEMLQHGVFRPalththldIPDYIRKCLcqcwDEDPE 814
Cdd:cd06642   179 ----DFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNSPPTLEGQHSKP--------FKEFVEACL----NKDPR 242
                         250
                  ....*....|.
gi 161076872  815 VRPDIRLVRMH 825
Cdd:cd06642   243 FRPTAKELLKH 253
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
603-763 2.02e-11

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: 65.87  E-value: 2.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  603 ELKLMREVRHENIINFIGASTDHG--SVIIFTTYCARGSLEDVLANEDLhLDHMFISSLVSDILKGMIYLHdSEIISHGN 680
Cdd:cd06651    59 EIQLLKNLQHERIVQYYGCLRDRAekTLTIFMEYMPGGSVKDQLKAYGA-LTESVTRKYTRQILEGMSYLH-SNMIVHRD 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  681 LRSSNCLIDSRWVCQISDFGLHE-LKAGQEEPNKSELELKRALCMAPELLRdayrpGRG-SQKGDVYSFGILLYEMIGRK 758
Cdd:cd06651   137 IKGANILRDSAGNVKLGDFGASKrLQTICMSGTGIRSVTGTPYWMSPEVIS-----GEGyGRKADVWSLGCTVVEMLTEK 211

                  ....*
gi 161076872  759 GPWGD 763
Cdd:cd06651   212 PPWAE 216
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
583-817 2.17e-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: 65.95  E-value: 2.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  583 IVAMKKIHKKSVDITRS-IRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVL--------ANEDLHLDH 653
Cdd:cd05046    37 LVLVKALQKTKDENLQSeFRRELDMFRKLSHKNVVRLLGLCREAEPHYMILEYTDLGDLKQFLratkskdeKLKPPPLST 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  654 MFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkagQEEPNKSELELKRALC-----MAPEL 728
Cdd:cd05046   117 KQKVALCTQIALGMDHLSNARFV-HRDLAARNCLVSSQREVKVSLLSL------SKDVYNSEYYKLRNALiplrwLAPEA 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  729 LRDayrpGRGSQKGDVYSFGILLYEMIGR-KGPWGDTaySKEEIIQfvkcpeMLQHGVFRPALthtHLDIPDYIRKCLCQ 807
Cdd:cd05046   190 VQE----DDFSTKSDVWSFGVLMWEVFTQgELPFYGL--SDEEVLN------RLQAGKLELPV---PEGCPSRLYKLMTR 254
                         250
                  ....*....|
gi 161076872  808 CWDEDPEVRP 817
Cdd:cd05046   255 CWAVNPKDRP 264
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
581-758 3.23e-11

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: 66.24  E-value: 3.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVDIT---RSIRkELKLMREVRHENIInfigASTDhgsviIFTTYCARGSLEDV-----LANEDLH-- 650
Cdd:cd07855    30 GQKVAIKKIPNAFDVVTtakRTLR-ELKILRHFKHDNII----AIRD-----ILRPKVPYADFKDVyvvldLMESDLHhi 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  651 --------LDHmfISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRAL 722
Cdd:cd07855   100 ihsdqpltLEH--IRYFLYQLLRGLKYIHSANVI-HRDLKPSNLLVNENCELKIGDFGMARGLCTSPEEHKYFMTEYVAT 176
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 161076872  723 --CMAPELLrdaYRPGRGSQKGDVYSFGILLYEMIGRK 758
Cdd:cd07855   177 rwYRAPELM---LSLPEYTQAIDMWSVGCIFAEMLGRR 211
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
581-754 3.60e-11

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


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 65.78  E-value: 3.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIH---KKSVDITRsIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANedlH----LDH 653
Cdd:cd08216    25 NTLVAVKKINlesDSKEDLKF-LQQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPLMAYGSCRDLLKT---HfpegLPE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  654 MFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISdfGLHE----LKAGQ------EEPNKSELELKRAlc 723
Cdd:cd08216   101 LAIAFILRDVLNALEYIHSKGYI-HRSVKASHILISGDGKVVLS--GLRYaysmVKHGKrqrvvhDFPKSSEKNLPWL-- 175
                         170       180       190
                  ....*....|....*....|....*....|.
gi 161076872  724 mAPELLRDAYRpGRGsQKGDVYSFGILLYEM 754
Cdd:cd08216   176 -SPEVLQQNLL-GYN-EKSDIYSVGITACEL 203
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
585-831 3.77e-11

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: 65.39  E-value: 3.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  585 AMKKIHKKSVDITRSIRKELKLMREVRHENIIN-----FIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHM---FI 656
Cdd:cd13986    29 ALKKILCHSKEDVKEAMREIENYRLFNHPNILRlldsqIVKEAGGKKEVYLLLPYYKRGSLQDEIERRLVKGTFFpedRI 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  657 SSLVSDILKGMIYLHDSEIIS--HGNLRSSNCLIDSRWVCQISDFG-----------LHELKAGQEEPNKSELELKRAlc 723
Cdd:cd13986   109 LHIFLGICRGLKAMHEPELVPyaHRDIKPGNVLLSEDDEPILMDLGsmnparieiegRREALALQDWAAEHCTMPYRA-- 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  724 maPELLrdAYRPGRG-SQKGDVYSFGILLYEMIGRKGPWgDTAYSKEEIIQFVKCpemlqHGVFRPALTHTH-LDIPDYI 801
Cdd:cd13986   187 --PELF--DVKSHCTiDEKTDIWSLGCTLYALMYGESPF-ERIFQKGDSLALAVL-----SGNYSFPDNSRYsEELHQLV 256
                         250       260       270
                  ....*....|....*....|....*....|
gi 161076872  802 RKCLCQcwdeDPEVRPDIRLVRMHLKELQA 831
Cdd:cd13986   257 KSMLVV----NPAERPSIDDLLSRVHDLIP 282
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
581-755 4.69e-11

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: 65.03  E-value: 4.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMK--KIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDlHLDHMFISS 658
Cdd:cd07833    26 GEIVAIKkfKESEDDEDVKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFEYVERTLLELLEASPG-GLPPDAVRS 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  659 LVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRALcMAPELLRDAYRPGRG 738
Cdd:cd07833   105 YIWQLLQAIAYCHSHNII-HRDIKPENILVSESGVLKLCDFGFARALTARPASPLTDYVATRWY-RAPELLVGDTNYGKP 182
                         170
                  ....*....|....*..
gi 161076872  739 SqkgDVYSFGILLYEMI 755
Cdd:cd07833   183 V---DVWAIGCIMAELL 196
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
581-825 4.84e-11

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: 64.58  E-value: 4.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSV---DITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLAN-------EDLH 650
Cdd:cd14081    26 GQKVAIKIVNKEKLskeSVLMKVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLEYVSGGELFDYLVKkgrltekEARK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  651 LDHMFISSLVsdilkgmiYLHdSEIISHGNLRSSNCLIDSRWVCQISDFGLHELkagqeEPNKSELELKralC-----MA 725
Cdd:cd14081   106 FFRQIISALD--------YCH-SHSICHRDLKPENLLLDEKNNIKIADFGMASL-----QPEGSLLETS---CgsphyAC 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  726 PELLR-DAYRpGRgsqKGDVYSFGILLYEMIGRKGPWGDTaySKEEIIQFVKcpemlqHGVFR-PAltHTHLDIPDYIRK 803
Cdd:cd14081   169 PEVIKgEKYD-GR---KADIWSCGVILYALLVGALPFDDD--NLRQLLEKVK------RGVFHiPH--FISPDAQDLLRR 234
                         250       260
                  ....*....|....*....|..
gi 161076872  804 CLcqcwDEDPEVRPDIRLVRMH 825
Cdd:cd14081   235 ML----EVNPEKRITIEEIKKH 252
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
584-825 6.57e-11

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: 64.42  E-value: 6.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVD---ITRSIRKELKLMREVRHENIIN-FIGASTDHGSVIIFTTYCARGSLEDVLANEdLHLDHMFISSL 659
Cdd:cd14165    29 VAIKIIDKKKAPddfVEKFLPRELEILARLNHKSIIKtYEIFETSDGKVYIVMELGVQGDLLEFIKLR-GALPEDVARKM 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  660 VSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEpnkSELELKRALC-----MAPELLRD-AY 733
Cdd:cd14165   108 FHQLSSAIKYCHELDIV-HRDLKCENLLLDKDFNIKLTDFGFSKRCLRDEN---GRIVLSKTFCgsaayAAPEVLQGiPY 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  734 RPgrgsQKGDVYSFGILLYEMIGRKGPWGDTAYSKEEIIQfvkcpemLQHGVFRPALTHTHLDIPDYIRKCLCqcwdEDP 813
Cdd:cd14165   184 DP----RIYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQ-------KEHRVRFPRSKNLTSECKDLIYRLLQ----PDV 248
                         250
                  ....*....|..
gi 161076872  814 EVRPDIRLVRMH 825
Cdd:cd14165   249 SQRLCIDEVLSH 260
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
581-825 6.65e-11

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: 64.27  E-value: 6.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVDITR------SIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDlHLDHM 654
Cdd:cd14194    30 GLQYAAKFIKKRRTKSSRrgvsreDIEREVSILKEIQHPNVITLHEVYENKTDVILILELVAGGELFDFLAEKE-SLTEE 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  655 FISSLVSDILKGMIYLHdSEIISHGNLRSSNCLIDSRWV----CQISDFGL-HELKAGQEEPN---KSELelkralcMAP 726
Cdd:cd14194   109 EATEFLKQILNGVYYLH-SLQIAHFDLKPENIMLLDRNVpkprIKIIDFGLaHKIDFGNEFKNifgTPEF-------VAP 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  727 ELLRdaYRPgrGSQKGDVYSFGILLYEMIGRKGPW-GDTaysKEEIIQFVKCpemLQHGVFRPALTHTHLDIPDYIRKCL 805
Cdd:cd14194   181 EIVN--YEP--LGLEADMWSIGVITYILLSGASPFlGDT---KQETLANVSA---VNYEFEDEYFSNTSALAKDFIRRLL 250
                         250       260
                  ....*....|....*....|
gi 161076872  806 CQcwdeDPEVRPDIRLVRMH 825
Cdd:cd14194   251 VK----DPKKRMTIQDSLQH 266
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
581-830 6.95e-11

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: 64.23  E-value: 6.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVDITRSIRKELKLMREVR-HENIINFIGASTDHGS-----VIIFTTYCARGSLEDVLaNEdlHLDHM 654
Cdd:cd14037    28 GNRAALKRVYVNDEHDLNVCKREIEIMKRLSgHKNIVGYIDSSANRSGngvyeVLLLMEYCKGGGVIDLM-NQ--RLQTG 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  655 F----ISSLVSDILKGMIYLH--DSEIIsHGNLRSSNCLIDSRWVCQISDFG-----------LHELKAGQEEPNKSELE 717
Cdd:cd14037   105 LteseILKIFCDVCEAVAAMHylKPPLI-HRDLKVENVLISDSGNYKLCDFGsattkilppqtKQGVTYVEEDIKKYTTL 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  718 LKRAlcmaPELLrDAYRPGRGSQKGDVYSFGILLYEMIGRKGPWGdtayskeeiiqfvkcpemlQHGVFrpALTHTHLDI 797
Cdd:cd14037   184 QYRA----PEMI-DLYRGKPITEKSDIWALGCLLYKLCFYTTPFE-------------------ESGQL--AILNGNFTF 237
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 161076872  798 PDYIR-----KCLCQ-CWDEDPEVRPDIRLVRMHLKELQ 830
Cdd:cd14037   238 PDNSRyskrlHKLIRyMLEEDPEKRPNIYQVSYEAFELA 276
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
598-817 8.16e-11

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. 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: 64.43  E-value: 8.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  598 RSIRKELKLMREV-RHENIINFIGASTDH-GSVIIFTTYCARGSLEDVL----------------------ANEDLHLDH 653
Cdd:cd05054    55 KALMTELKILIHIgHHLNVVNLLGACTKPgGPLMVIVEFCKFGNLSNYLrskreefvpyrdkgardveeeeDDDELYKEP 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  654 MFISSLVS---DILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLheLKAGQEEPN-----KSELELKralCMA 725
Cdd:cd05054   135 LTLEDLICysfQVARGMEFLASRKCI-HRDLAARNILLSENNVVKICDFGL--ARDIYKDPDyvrkgDARLPLK---WMA 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  726 PELLRDAYRpgrgSQKGDVYSFGILLYEMIGRKGPWGDTAYSKEEIIQfvkcpeMLQHGVFRPALTHThldiPDYIRKCL 805
Cdd:cd05054   209 PESIFDKVY----TTQSDVWSFGVLLWEIFSLGASPYPGVQMDEEFCR------RLKEGTRMRAPEYT----TPEIYQIM 274
                         250
                  ....*....|..
gi 161076872  806 CQCWDEDPEVRP 817
Cdd:cd05054   275 LDCWHGEPKERP 286
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
581-757 1.03e-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: 64.31  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHkksVDITRSIR----KELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDlHLDHMFI 656
Cdd:cd06650    30 GLVMARKLIH---LEIKPAIRnqiiRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKKAG-RIPEQIL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  657 SSLVSDILKGMIYLHDSEIISHGNLRSSNCLIDSRWVCQISDFGLhelkAGQEEPNKSELELKRALCMAPELLRDAYRpg 736
Cdd:cd06650   106 GKVSIAVIKGLTYLREKHKIMHRDVKPSNILVNSRGEIKLCDFGV----SGQLIDSMANSFVGTRSYMSPERLQGTHY-- 179
                         170       180
                  ....*....|....*....|..
gi 161076872  737 rgSQKGDVYSFGILLYEM-IGR 757
Cdd:cd06650   180 --SVQSDIWSMGLSLVEMaVGR 199
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
584-758 1.14e-10

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


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 64.70  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHK---KSVDITRSIRkELKLMREVRHENIInfigASTDhgsvIIFTTycARGSLEDV-----LANEDLhldHMF 655
Cdd:cd07858    33 VAIKKIANafdNRIDAKRTLR-EIKLLRHLDHENVI----AIKD----IMPPP--HREAFNDVyivyeLMDTDL---HQI 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  656 ISS---LVSD--------ILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEpNKSELELKRALcM 724
Cdd:cd07858    99 IRSsqtLSDDhcqyflyqLLRGLKYIHSANVL-HRDLKPSNLLLNANCDLKICDFGLARTTSEKGD-FMTEYVVTRWY-R 175
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 161076872  725 APELLR--DAYrpgrgSQKGDVYSFGILLYEMIGRK 758
Cdd:cd07858   176 APELLLncSEY-----TTAIDVWSVGCIFAELLGRK 206
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
610-816 1.21e-10

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: 63.65  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  610 VRHENIINFIGASTD-HGSV---IIFTTYCARGSLEDVLANEDLHLDHMFisSLVSDILKGMIYLHDsEI--------IS 677
Cdd:cd14144    46 MRHENILGFIAADIKgTGSWtqlYLITDYHENGSLYDFLRGNTLDTQSML--KLAYSAACGLAHLHT-EIfgtqgkpaIA 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  678 HGNLRSSNCLIDSRWVCQISDFGL-----HELKAGQEEPNkSELELKRAlcMAPELLRDAYRPGRGS--QKGDVYSFGIL 750
Cdd:cd14144   123 HRDIKSKNILVKKNGTCCIADLGLavkfiSETNEVDLPPN-TRVGTKRY--MAPEVLDESLNRNHFDayKMADMYSFGLV 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  751 LYEMIGR----------KGPWGDTAYSKE--EIIQFVKCPEMlqhgvFRPalththlDIP------DYIR---KCLCQCW 809
Cdd:cd14144   200 LWEIARRcisggiveeyQLPYYDAVPSDPsyEDMRRVVCVER-----RRP-------SIPnrwssdEVLRtmsKLMSECW 267

                  ....*..
gi 161076872  810 DEDPEVR 816
Cdd:cd14144   268 AHNPAAR 274
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
583-773 1.22e-10

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: 63.08  E-value: 1.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  583 IVAMKKIHKKSVD--ITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLedvlanedlhldHMFISS-- 658
Cdd:cd14121    23 VVAVKCVSKSSLNkaSTENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGGDL------------SRFIRSrr 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  659 ---------LVSDILKGMIYLHDSEiISHGNLRSSNCLIDSRW--VCQISDFGLHE-LKAGQEEPNkseleLKRA-LCMA 725
Cdd:cd14121    91 tlpestvrrFLQQLASALQFLREHN-ISHMDLKPQNLLLSSRYnpVLKLADFGFAQhLKPNDEAHS-----LRGSpLYMA 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 161076872  726 PE-LLRDAYRPgrgsqKGDVYSFGILLYEMIGRKGPWGDTAYSK-EEIIQ 773
Cdd:cd14121   165 PEmILKKKYDA-----RVDLWSVGVILYECLFGRAPFASRSFEElEEKIR 209
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
581-755 1.23e-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: 63.23  E-value: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIhkksvDITRSIRKEL-----KLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHmf 655
Cdd:cd06648    32 GRQVAVKKM-----DLRKQQRRELlfnevVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQ-- 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  656 ISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHElKAGQEEPNKSELeLKRALCMAPELL-RDAYR 734
Cdd:cd06648   105 IATVCRAVLKALSFLHSQGVI-HRDIKSDSILLTSDGRVKLSDFGFCA-QVSKEVPRRKSL-VGTPYWMAPEVIsRLPYG 181
                         170       180
                  ....*....|....*....|.
gi 161076872  735 PgrgsqKGDVYSFGILLYEMI 755
Cdd:cd06648   182 T-----EVDIWSLGIMVIEMV 197
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
606-833 1.43e-10

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: 63.62  E-value: 1.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  606 LMREVRHENIINFIGAST-DHGSVIIFTTYCARGSLE-------DVLANEDLHLDHMFISSLVSDILKGMIYLHDSEIIs 677
Cdd:cd05043    60 LLYGLSHQNLLPILHVCIeDGEKPMVLYPYMNWGNLKlflqqcrLSEANNPQALSTQQLVHMALQIACGMSYLHRRGVI- 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  678 HGNLRSSNCLIDSRWVCQISDFGL---------HELKAGQEEPNKselelkralCMAPE-LLRDAYrpgrgSQKGDVYSF 747
Cdd:cd05043   139 HKDIAARNCVIDDELQVKITDNALsrdlfpmdyHCLGDNENRPIK---------WMSLEsLVNKEY-----SSASDVWSF 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  748 GILLYEMIgrkgPWGDTAYskEEIIQFvKCPEMLQHGvFRPAlthTHLDIPDYIRKCLCQCWDEDPEVRPDIRLVRMHLK 827
Cdd:cd05043   205 GVLLWELM----TLGQTPY--VEIDPF-EMAAYLKDG-YRLA---QPINCPDELFAVMACCWALDPEERPSFQQLVQCLT 273

                  ....*.
gi 161076872  828 ELQAGL 833
Cdd:cd05043   274 DFHAQL 279
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
581-755 1.75e-10

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: 63.05  E-value: 1.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSV----DITRsIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANE----DLHLD 652
Cdd:cd14161    27 GRLVAIKSIRKDRIkdeqDLLH-IRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEYASRGDLYDYISERqrlsELEAR 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  653 HMFisslvSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQeepnkselELKRALC-----MAPE 727
Cdd:cd14161   106 HFF-----RQIVSAVHYCHANGIV-HRDLKLENILLDANGNIKIADFGLSNLYNQD--------KFLQTYCgsplyASPE 171
                         170       180
                  ....*....|....*....|....*...
gi 161076872  728 LLRDayRPGRGSQKgDVYSFGILLYEMI 755
Cdd:cd14161   172 IVNG--RPYIGPEV-DSWSLGVLLYILV 196
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
588-833 2.27e-10

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: 62.72  E-value: 2.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  588 KIHKKSVDITRSIRKELK-------LMREVRHENIINFIGA------STDHGSVIIFTTYCARGSLEDVL-----ANEDL 649
Cdd:cd05075    29 KVAVKTMKIAICTRSEMEdflseavCMKEFDHPNVMRLIGVclqnteSEGYPSPVVILPFMKHGDLHSFLlysrlGDCPV 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  650 HLDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRALCMAPELL 729
Cdd:cd05075   109 YLPTQMLVKFMTDIASGMEYLSSKNFI-HRDLAARNCMLNENMNVCVADFGLSKKIYNGDYYRQGRISKMPVKWIAIESL 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  730 RDAYRpgrgSQKGDVYSFGILLYEMIGRkgpwGDTAY---SKEEIIQFVKCPEMLQhgvfRPAlththlDIPDYIRKCLC 806
Cdd:cd05075   188 ADRVY----TTKSDVWSFGVTMWEIATR----GQTPYpgvENSEIYDYLRQGNRLK----QPP------DCLDGLYELMS 249
                         250       260
                  ....*....|....*....|....*..
gi 161076872  807 QCWDEDPEVRPDIRLVRMHLKELQAGL 833
Cdd:cd05075   250 SCWLLNPKDRPSFETLRCELEKILKDL 276
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
562-825 2.48e-10

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: 62.94  E-value: 2.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  562 ILVVGEPNKRSFTNIALFR----GNIVAMKKIHKKSVDIT-RSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCA 636
Cdd:cd06622     3 IEVLDELGKGNYGSVYKVLhrptGVTMAMKEIRLELDESKfNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  637 RGSLEDVLA--NEDLHLDHMFISSLVSDILKGMIYLHDSEIISHGNLRSSNCLIDSRWVCQISDFGLhelkAGQEEPNKS 714
Cdd:cd06622    83 AGSLDKLYAggVATEGIPEDVLRRITYAVVKGLKFLKEEHNIIHRDVKPTNVLVNGNGQVKLCDFGV----SGNLVASLA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  715 ELELKRALCMAPELLRDAYRPGRG--SQKGDVYSFGILLYEMIGRKGPWGDTAYSK--EEIIQFVKCPEmlqhgvfrPAL 790
Cdd:cd06622   159 KTNIGCQSYMAPERIKSGGPNQNPtyTVQSDVWSLGLSILEMALGRYPYPPETYANifAQLSAIVDGDP--------PTL 230
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 161076872  791 THTHL-DIPDYIRKCLcqcwDEDPEVRPDIRLVRMH 825
Cdd:cd06622   231 PSGYSdDAQDFVAKCL----NKIPNRRPTYAQLLEH 262
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
603-833 2.60e-10

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: 62.64  E-value: 2.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  603 ELKLMREVRHENIINFIGASTDHGS--------VIIFTTYcarGSLEDVLANEDLHLDHMFIS-----SLVSDILKGMIY 669
Cdd:cd14204    59 EAACMKDFNHPNVIRLLGVCLEVGSqripkpmvILPFMKY---GDLHSFLLRSRLGSGPQHVPlqtllKFMIDIALGMEY 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  670 LHDSEIIsHGNLRSSNCLI-DSRWVCqISDFGLHELKAGQEEPNKSELELKRALCMAPELLRDAYRpgrgSQKGDVYSFG 748
Cdd:cd14204   136 LSSRNFL-HRDLAARNCMLrDDMTVC-VADFGLSKKIYSGDYYRQGRIAKMPVKWIAVESLADRVY----TVKSDVWAFG 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  749 ILLYEMIGRkgpwGDTAYskeeiiqfvkcPEMLQHGVFRPALTHTHLDIP----DYIRKCLCQCWDEDPEVRPDIRLVRM 824
Cdd:cd14204   210 VTMWEIATR----GMTPY-----------PGVQNHEIYDYLLHGHRLKQPedclDELYDIMYSCWRSDPTDRPTFTQLRE 274

                  ....*....
gi 161076872  825 HLKELQAGL 833
Cdd:cd14204   275 NLEKLLESL 283
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
610-829 3.02e-10

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: 62.75  E-value: 3.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  610 VRHENIINFIGASTD-HGS---VIIFTTYCARGSLEDVLANEDLhlDHMFISSLVSDILKGMIYLHdSEI--------IS 677
Cdd:cd14220    46 MRHENILGFIAADIKgTGSwtqLYLITDYHENGSLYDFLKCTTL--DTRALLKLAYSAACGLCHLH-TEIygtqgkpaIA 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  678 HGNLRSSNCLIDSRWVCQISDFGLH-ELKAGQEE---PNKSELELKRAlcMAPELLRDAYRPG--RGSQKGDVYSFGILL 751
Cdd:cd14220   123 HRDLKSKNILIKKNGTCCIADLGLAvKFNSDTNEvdvPLNTRVGTKRY--MAPEVLDESLNKNhfQAYIMADIYSFGLII 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  752 YEMIGR----------KGPW-----GDTAYSKEEIIQFVKCpemlqhgvFRPALTHtHLDIPDYIR---KCLCQCWDEDP 813
Cdd:cd14220   201 WEMARRcvtggiveeyQLPYydmvpSDPSYEDMREVVCVKR--------LRPTVSN-RWNSDECLRavlKLMSECWAHNP 271
                         250
                  ....*....|....*.
gi 161076872  814 EVRPDIRLVRMHLKEL 829
Cdd:cd14220   272 ASRLTALRIKKTLAKM 287
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
584-820 3.05e-10

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: 62.67  E-value: 3.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDIT-RSIRKELKLMREVRHENIINFIGASTDhGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSD 662
Cdd:cd05111    39 VAIKVIQDRSGRQSfQAVTDHMLAIGSLDHAYIVRLLGICPG-ASLQLVTQLLPLGSLLDHVRQHRGSLGPQLLLNWCVQ 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  663 ILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAgqeePNKSEL---ELKRAL-CMAPEllrdAYRPGRG 738
Cdd:cd05111   118 IAKGMYYLEEHRMV-HRNLAARNVLLKSPSQVQVADFGVADLLY----PDDKKYfysEAKTPIkWMALE----SIHFGKY 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  739 SQKGDVYSFGILLYEMIGrkgpWGDTAYSKeeiIQFVKCPEMLQHGvfrPALTHTHLDIPDyIRKCLCQCWDEDPEVRPD 818
Cdd:cd05111   189 THQSDVWSYGVTVWEMMT----FGAEPYAG---MRLAEVPDLLEKG---ERLAQPQICTID-VYMVMVKCWMIDENIRPT 257

                  ..
gi 161076872  819 IR 820
Cdd:cd05111   258 FK 259
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
581-764 3.59e-10

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: 62.12  E-value: 3.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVDITR------SIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLAnEDLHLDHM 654
Cdd:cd14105    30 GLEYAAKFIKKRRSKASRrgvsreDIEREVSILRQVLHPNIITLHDVFENKTDVVLILELVAGGELFDFLA-EKESLSEE 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  655 FISSLVSDILKGMIYLHDSEiISHGNLRSSNCLIDSRWV----CQISDFGL-HELKAGQEEPNkselelkraLC-----M 724
Cdd:cd14105   109 EATEFLKQILDGVNYLHTKN-IAHFDLKPENIMLLDKNVpiprIKLIDFGLaHKIEDGNEFKN---------IFgtpefV 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 161076872  725 APELLrdAYRPgrGSQKGDVYSFGILLYEMIGRKGPW-GDT 764
Cdd:cd14105   179 APEIV--NYEP--LGLEADMWSIGVITYILLSGASPFlGDT 215
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
581-755 3.64e-10

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: 62.02  E-value: 3.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSV----DITRsIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLaNEDLHLDHMFI 656
Cdd:cd14073    26 GREVAIKSIKKDKIedeqDMVR-IRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEYASGGELYDYI-SERRRLPEREA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  657 SSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELkagqeepnKSELELKRALC-----MAPELLRD 731
Cdd:cd14073   104 RRIFRQIVSAVHYCHKNGVV-HRDLKLENILLDQNGNAKIADFGLSNL--------YSKDKLLQTFCgsplyASPEIVNG 174
                         170       180
                  ....*....|....*....|....
gi 161076872  732 ayRPGRGSQKgDVYSFGILLYEMI 755
Cdd:cd14073   175 --TPYQGPEV-DCWSLGVLLYTLV 195
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
583-817 3.90e-10

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: 62.64  E-value: 3.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  583 IVAMKKIHKKSVDITRS-IRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLH----------- 650
Cdd:cd05096    48 LVAVKILRPDANKNARNdFLKEVKILSRLKDPNIIRLLGVCVDEDPLCMITEYMENGDLNQFLSSHHLDdkeengndavp 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  651 -------LDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL-HELKAGQ--EEPNKSELELKr 720
Cdd:cd05096   128 pahclpaISYSSLLHVALQIASGMKYLSSLNFV-HRDLATRNCLVGENLTIKIADFGMsRNLYAGDyyRIQGRAVLPIR- 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  721 alCMAPELLrdayRPGRGSQKGDVYSFGILLYE--MIGRKGPWGDtaYSKEEII----QFVKcPEMLQHGVFRPALThth 794
Cdd:cd05096   206 --WMAWECI----LMGKFTTASDVWAFGVTLWEilMLCKEQPYGE--LTDEQVIenagEFFR-DQGRQVYLFRPPPC--- 273
                         250       260
                  ....*....|....*....|...
gi 161076872  795 ldiPDYIRKCLCQCWDEDPEVRP 817
Cdd:cd05096   274 ---PQGLYELMLQCWSRDCRERP 293
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
593-850 4.48e-10

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: 62.32  E-value: 4.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  593 SVDITRSIRKELKLM-REVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVL-------ANEDLHLDHMFISSLVS--- 661
Cdd:cd05088    47 SKDDHRDFAGELEVLcKLGHHPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLrksrvleTDPAFAIANSTASTLSSqql 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  662 -----DILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHElkaGQEEPNKSELELKRALCMAPELLRDAYRpg 736
Cdd:cd05088   127 lhfaaDVARGMDYLSQKQFI-HRDLAARNILVGENYVAKIADFGLSR---GQEVYVKKTMGRLPVRWMAIESLNYSVY-- 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  737 rgSQKGDVYSFGILLYEMIGrkgpWGDTAYSKEEIIQFVkcpEMLQHGvFRpalTHTHLDIPDYIRKCLCQCWDEDPEVR 816
Cdd:cd05088   201 --TTNSDVWSYGVLLWEIVS----LGGTPYCGMTCAELY---EKLPQG-YR---LEKPLNCDDEVYDLMRQCWREKPYER 267
                         250       260       270
                  ....*....|....*....|....*....|....
gi 161076872  817 PDIRLVRMHLKELQAGLKPNIfdnMLSIMEKYAY 850
Cdd:cd05088   268 PSFAQILVSLNRMLEERKTYV---NTTLYEKFTY 298
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
581-805 4.66e-10

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


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 61.97  E-value: 4.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLV 660
Cdd:cd06643    30 GILAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAGGAVDAVMLELERPLTEPQIRVVC 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkagqEEPNKSELELKRALC-----MAPELLRDAYRP 735
Cdd:cd06643   110 KQTLEALVYLHENKII-HRDLKAGNILFTLDGDIKLADFGV-------SAKNTRTLQRRDSFIgtpywMAPEVVMCETSK 181
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161076872  736 GRGSQ-KGDVYSFGILLYEMIGRKGPWGDTAySKEEIIQFVKC--PEMLQHGVFRPalththlDIPDYIRKCL 805
Cdd:cd06643   182 DRPYDyKADVWSLGVTLIEMAQIEPPHHELN-PMRVLLKIAKSepPTLAQPSRWSP-------EFKDFLRKCL 246
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
599-825 5.18e-10

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: 61.50  E-value: 5.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  599 SIRKELKLMREVRHENIINFIGASTDH--GSVIIFTTYCArGSLEDVLANEDLH-----LDHMFISSLVSdilkGMIYLH 671
Cdd:cd14119    40 NVKREIQILRRLNHRNVIKLVDVLYNEekQKLYMVMEYCV-GGLQEMLDSAPDKrlpiwQAHGYFVQLID----GLEYLH 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  672 dSEIISHGNLRSSNCLIDSRWVCQISDFGLHElkagqeepnkselelkrALCM-----------------APELLR-DAY 733
Cdd:cd14119   115 -SQGIIHKDIKPGNLLLTTDGTLKISDFGVAE-----------------ALDLfaeddtcttsqgspafqPPEIANgQDS 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  734 RPGRgsqKGDVYSFGILLYEMIGRKGPW-GDTAYSKEEIIQfvKCPemlqhgvfrpalththLDIPDYIRKCLCQ----C 808
Cdd:cd14119   177 FSGF---KVDIWSAGVTLYNMTTGKYPFeGDNIYKLFENIG--KGE----------------YTIPDDVDPDLQDllrgM 235
                         250
                  ....*....|....*..
gi 161076872  809 WDEDPEVRPDIRLVRMH 825
Cdd:cd14119   236 LEKDPEKRFTIEQIRQH 252
PBP1_ABC_transporter_GPCR_C-like cd04509
Family C of G-protein coupled receptors and their close homologs, the type 1 ...
50-275 5.98e-10

Family C of G-protein coupled receptors and their close homologs, the type 1 periplasmic-binding proteins of ATP-binding cassette transporter-like systems; This CD includes members of the family C of G-protein coupled receptors and their close homologs, the type 1 periplasmic-binding proteins of ATP-binding cassette transporter-like systems. The family C GPCR includes glutamate/glycine-gated ion channels such as the NMDA receptor, G-protein-coupled receptors, metabotropic glutamate, GABA-B, calcium sensing, pheromone receptors, and atrial natriuretic peptide-guanylate cyclase receptors. The glutamate receptors that form cation-selective ion channels, iGluR, can be classified into three different subgroups according to their binding-affinity for the agonists NMDA (N-methyl-D-asparate), AMPA (alpha-amino-3-dihydro-5-methyl-3-oxo-4-isoxazolepropionic acid), and kainate. L-glutamate is a major neurotransmitter in the brain of vertebrates and acts through either mGluRs or iGluRs. mGluRs subunits possess seven transmembrane segments and a large N-terminal extracellular domain. ABC-type leucine-isoleucine-valine binding protein (LIVBP) is a bacterial periplasmic binding protein that has homology with the amino-terminal domain of the glutamate-receptor ion channels (iGluRs). The extracellular regions of iGluRs are made of two PBP-like domains in tandem, a LIVBP-like domain that constitutes the N terminus (included in this model) followed by a domain related to lysine-arginine-ornithine-binding protein (LAOBP) that belongs to the type 2 periplasmic binding fold protein superfamily. The uncharacterized periplasmic components of various ABC-type transport systems are also included in this family.


Pssm-ID: 380490  Cd Length: 306  Bit Score: 61.94  E-value: 5.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   50 AEYSQMRVTlgGLPLAIEDVNKNPNLLPGKKLAFKPVD-------------------IGHKMSAYRVKPLRAMTQMREAG 110
Cdd:cd04509    23 AQYGIQRFE--AMEQALDDINADPNLLPNNTLGIVIYDdccdpkqaleqsnkfvndlIQKDTSDVRCTNGEPPVFVKPEG 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  111 VTAFIGPdeSCTTEALLAS----AWNTPMLSFKCSDPIVSNKSTFHTFARTLAPASKVSKSVISLLNAFHWNKFSIvVSS 186
Cdd:cd04509   101 IKGVIGH--LCSSVTIPVSnileLFGIPQITYAATAPELSDDRGYQLFLRVVPLDSDQAPAMADIVKEKVWQYVSI-VHD 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  187 KPIWGSDVARAIQELAEARNFTISHFkyisDYIPTTKTLSQIDKIIEETYAT--TRIYVFIGEHIAMVDFVRglQNRRLL 264
Cdd:cd04509   178 EGQYGEGGARAFQDGLKKGGLCIAFS----DGITAGEKTKDFDRLVARLKKEnnIRFVVYFGYHPEMGQILR--AARRAG 251
                         250
                  ....*....|.
gi 161076872  265 ESGDYIVVSVD 275
Cdd:cd04509   252 LVGKFQFMGSD 262
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
581-817 6.02e-10

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: 61.67  E-value: 6.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKS-VDITRSIRKELKLMREVRHENIINFIGASTDH--GSVIIFTTYCARGSLEDVLAN---EDLHLDHM 654
Cdd:cd06621    26 KTIFALKTITTDPnPDVQKQILRELEINKSCASPYIVKYYGAFLDEqdSSIGIAMEYCEGGSLDSIYKKvkkKGGRIGEK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  655 FISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkAGQEEPNKSELELKRALCMAPELLR-DAY 733
Cdd:cd06621   106 VLGKIAESVLKGLSYLHSRKII-HRDIKPSNILLTRKGQVKLCDFGV----SGELVNSLAGTFTGTSYYMAPERIQgGPY 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  734 rpgrgSQKGDVYSFGILLYEMIGRKGPWgdtaysKEEIIQFVKCPEMLQHGV--FRPALThthlDIPDY-------IRKC 804
Cdd:cd06621   181 -----SITSDVWSLGLTLLEVAQNRFPF------PPEGEPPLGPIELLSYIVnmPNPELK----DEPENgikwsesFKDF 245
                         250
                  ....*....|...
gi 161076872  805 LCQCWDEDPEVRP 817
Cdd:cd06621   246 IEKCLEKDGTRRP 258
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
581-757 6.22e-10

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: 62.00  E-value: 6.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKI----HKKSVDITrSIRkELKLMREVRHENIINFI--------GASTDHGSVIIFTTYCARgSLEDVLANED 648
Cdd:cd07865    37 GQIVALKKVlmenEKEGFPIT-ALR-EIKILQLLKHENVVNLIeicrtkatPYNRYKGSIYLVFEFCEH-DLAGLLSNKN 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  649 LHLDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL----HELKAGQeePNKSELELKRALCM 724
Cdd:cd07865   114 VKFTLSEIKKVMKMLLNGLYYIHRNKIL-HRDMKAANILITKDGVLKLADFGLarafSLAKNSQ--PNRYTNRVVTLWYR 190
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 161076872  725 APELL---RDaYRPgrgsqKGDVYSFGILLYEMIGR 757
Cdd:cd07865   191 PPELLlgeRD-YGP-----PIDMWGAGCIMAEMWTR 220
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
581-701 6.43e-10

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: 61.73  E-value: 6.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVDITRS--IRkELKLMREVRHENIINFIGA-STDHGSVIIFtTYCARgsleDVLANEDLH-----LD 652
Cdd:cd07836    25 GEIVALKEIHLDAEEGTPStaIR-EISLMKELKHENIVRLHDViHTENKLMLVF-EYMDK----DLKKYMDTHgvrgaLD 98
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 161076872  653 HMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL 701
Cdd:cd07836    99 PNTVKSFTYQLLKGIAFCHENRVL-HRDLKPQNLLINKRGELKLADFGL 146
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
581-763 7.05e-10

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: 60.88  E-value: 7.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSV---DITRSIRKELKLMREVRHENIINF--IGASTDHgsVIIFTTYCARGSLEDVLA-NEDLHLD-- 652
Cdd:cd14663    25 GESVAIKIIDKEQVareGMVEQIKREIAIMKLLRHPNIVELheVMATKTK--IFFVMELVTGGELFSKIAkNGRLKEDka 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  653 -HMFisslvSDILKGMIYLHdSEIISHGNLRSSNCLIDSRWVCQISDFGLHELkagqEEPNKSELELkRALC-----MAP 726
Cdd:cd14663   103 rKYF-----QQLIDAVDYCH-SRGVFHRDLKPENLLLDEDGNLKISDFGLSAL----SEQFRQDGLL-HTTCgtpnyVAP 171
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 161076872  727 ELLRdayRPGRGSQKGDVYSFGILLYEMIGRKGPWGD 763
Cdd:cd14663   172 EVLA---RRGYDGAKADIWSCGVILFVLLAGYLPFDD 205
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
573-825 7.54e-10

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: 61.24  E-value: 7.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  573 FTNIALFRGNIVAMKKIH-KKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLanEDLHL 651
Cdd:cd06641    21 FKGIDNRTQKVVAIKIIDlEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSALDLL--EPGPL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  652 DHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkAGQeepnKSELELKR------ALCMA 725
Cdd:cd06641    99 DETQIATILREILKGLDYLHSEKKI-HRDIKAANVLLSEHGEVKLADFGV----AGQ----LTDTQIKRn*fvgtPFWMA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  726 PELLR-DAYrpgrgSQKGDVYSFGILLYEMIGRKGPWGDTAYSKEEIIQFVKCPEMLQhGVFRPALThthldipDYIRKC 804
Cdd:cd06641   170 PEVIKqSAY-----DSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLE-GNYSKPLK-------EFVEAC 236
                         250       260
                  ....*....|....*....|.
gi 161076872  805 LcqcwDEDPEVRPDIRLVRMH 825
Cdd:cd06641   237 L----NKEPSFRPTAKELLKH 253
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
581-758 8.34e-10

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: 62.07  E-value: 8.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVDITRSIR--KELKLMREVRHENIINFIG----ASTDHGSVIIFTTYCARGSLEDVL-ANEDLHLDH 653
Cdd:cd07853    25 GKRVALKKMPNVFQNLVSCKRvfRELKMLCFFKHDNVLSALDilqpPHIDPFEEIYVVTELMQSDLHKIIvSPQPLSSDH 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  654 mfISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkAGQEEPNKSEL---ELKRALCMAPELLR 730
Cdd:cd07853   105 --VKVFLYQILRGLKYLHSAGIL-HRDIKPGNLLVNSNCVLKICDFGL----ARVEEPDESKHmtqEVVTQYYRAPEILM 177
                         170       180
                  ....*....|....*....|....*...
gi 161076872  731 DAYRPGrgsQKGDVYSFGILLYEMIGRK 758
Cdd:cd07853   178 GSRHYT---SAVDIWSVGCIFAELLGRR 202
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
590-817 8.57e-10

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


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 61.13  E-value: 8.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  590 HKKSVDITRSI---RKELKLMREVRHENIINFIGASTdhgSVIIFTTYCAR-GSLEDVLANED-----LHLDHMFISSLV 660
Cdd:cd14067    44 HLRAADAMKNFsefRQEASMLHSLQHPCIVYLIGISI---HPLCFALELAPlGSLNTVLEENHkgssfMPLGHMLTFKIA 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWV-----CQISDFGL-----HELKAGQEEPNKSElelkralcmAPELlr 730
Cdd:cd14067   121 YQIAAGLAYLHKKNII-FCDLKSDNILVWSLDVqehinIKLSDYGIsrqsfHEGALGVEGTPGYQ---------APEI-- 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  731 dayRPG-RGSQKGDVYSFGILLYEMI-GRKGPWGdtayskEEIIQFVKcpeMLQHGVfRPALTHTHLDIPDYIRKCLCQC 808
Cdd:cd14067   189 ---RPRiVYDEKVDMFSYGMVLYELLsGQRPSLG------HHQLQIAK---KLSKGI-RPVLGQPEEVQFFRLQALMMEC 255

                  ....*....
gi 161076872  809 WDEDPEVRP 817
Cdd:cd14067   256 WDTKPEKRP 264
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
579-825 8.78e-10

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


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 61.13  E-value: 8.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  579 FRGNIVAMKKIHKKSVDITRsirKELKLMREV-RHENIINFIGASTDHGSVIIFTTYCArGSLEDVLANEDLHLDHMFIS 657
Cdd:cd13982    23 FDGRPVAVKRLLPEFFDFAD---REVQLLRESdEHPNVIRYFCTEKDRQFLYIALELCA-ASLQDLVESPRESKLFLRPG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  658 ----SLVSDILKGMIYLHDSEIIsHGNLRSSNCLI--DSRWVC---QISDFGL-HELKAGQ----EEPNKSELELKRalc 723
Cdd:cd13982    99 lepvRLLRQIASGLAHLHSLNIV-HRDLKPQNILIstPNAHGNvraMISDFGLcKKLDVGRssfsRRSGVAGTSGWI--- 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  724 mAPELLRDAyRPGRGSQKGDVYSFGILLYEMI-GRKGPWGDTaYSKEEII-----QFVKCPEMLQHGVfrpalththlDI 797
Cdd:cd13982   175 -APEMLSGS-TKRRQTRAVDIFSLGCVFYYVLsGGSHPFGDK-LEREANIlkgkySLDKLLSLGEHGP----------EA 241
                         250       260
                  ....*....|....*....|....*...
gi 161076872  798 PDYIRKCLcqcwDEDPEVRPDIRLVRMH 825
Cdd:cd13982   242 QDLIERMI----DFDPEKRPSAEEVLNH 265
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
581-758 8.87e-10

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


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 61.61  E-value: 8.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIH----KKSVDITrSIRkELKLMREVRHENIINF----IGASTDhgSVIIFTTYCargslEDVLANedlHLD 652
Cdd:cd07845    32 GEIVALKKVRmdneRDGIPIS-SLR-EITLLLNLRHPNIVELkevvVGKHLD--SIFLVMEYC-----EQDLAS---LLD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  653 HM---F----ISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL---HELKAGQEEPNKSELELKral 722
Cdd:cd07845   100 NMptpFsesqVKCLMLQLLRGLQYLHENFII-HRDLKVSNLLLTDKGCLKIADFGLartYGLPAKPMTPKVVTLWYR--- 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 161076872  723 cmAPELLrdayrpgRGSQKG----DVYSFGILLYEMIGRK 758
Cdd:cd07845   176 --APELL-------LGCTTYttaiDMWAVGCILAELLAHK 206
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
584-779 9.57e-10

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


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 61.59  E-value: 9.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDITRSIR--KELKLMREVRHENIINFIGASTDHGSV-----IIFTTYCARGSLEDVLANEDLHLDHmfI 656
Cdd:cd07877    45 VAVKKLSRPFQSIIHAKRtyRELRLLKHMKHENVIGLLDVFTPARSLeefndVYLVTHLMGADLNNIVKCQKLTDDH--V 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  657 SSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHElKAGQEEPNKSELELKRalcmAPELLRDAYRPg 736
Cdd:cd07877   123 QFLIYQILRGLKYIHSADII-HRDLKPSNLAVNEDCELKILDFGLAR-HTDDEMTGYVATRWYR----APEIMLNWMHY- 195
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 161076872  737 rgSQKGDVYSFGILLYEMI-GRK-GPWGDTAYSKEEIIQFVKCPE 779
Cdd:cd07877   196 --NQTVDIWSVGCIMAELLtGRTlFPGTDHIDQLKLILRLVGTPG 238
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
588-819 9.88e-10

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: 60.59  E-value: 9.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  588 KIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSL-------EDVLANEDLHLDhMFISslv 660
Cdd:cd08218    34 NISKMSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYCDGGDLykrinaqRGVLFPEDQILD-WFVQ--- 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 sdILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKagqeepnKSELELKRALC-----MAPELLRDayRP 735
Cdd:cd08218   110 --LCLALKHVHDRKIL-HRDIKSQNIFLTKDGIIKLGDFGIARVL-------NSTVELARTCIgtpyyLSPEICEN--KP 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  736 grGSQKGDVYSFGILLYEMIGRKGPWgDTAYSKEEIIQFVKcpemlqhGVFRPALTHTHLDipdyIRKCLCQCWDEDPEV 815
Cdd:cd08218   178 --YNNKSDIWALGCVLYEMCTLKHAF-EAGNMKNLVLKIIR-------GSYPPVPSRYSYD----LRSLVSQLFKRNPRD 243

                  ....
gi 161076872  816 RPDI 819
Cdd:cd08218   244 RPSI 247
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
580-758 1.13e-09

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


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 61.55  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  580 RGNIVAMKKIH--KKSVDITRSIRkELKLMREVRHENIINFIgastdhgSVIIFTTYCargSLEDV-----LANEDLHL- 651
Cdd:cd07849    29 TGQKVAIKKISpfEHQTYCLRTLR-EIKILLRFKHENIIGIL-------DIQRPPTFE---SFKDVyivqeLMETDLYKl 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  652 --------DHmfISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELkAGQEEPNKSELELKRAL- 722
Cdd:cd07849    98 iktqhlsnDH--IQYFLYQILRGLKYIHSANVL-HRDLKPSNLLLNTNCDLKICDFGLARI-ADPEHDHTGFLTEYVATr 173
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 161076872  723 -CMAPELLRdayrpgrgSQKG-----DVYSFGILLYEMIGRK 758
Cdd:cd07849   174 wYRAPEIML--------NSKGytkaiDIWSVGCILAEMLSNR 207
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
585-819 1.31e-09

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: 60.40  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  585 AMKKIHKKSVDITR------SIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDlHLDHMFISS 658
Cdd:cd14195    34 AAKFIKKRRLSSSRrgvsreEIEREVNILREIQHPNIITLHDIFENKTDVVLILELVSGGELFDFLAEKE-SLTEEEATQ 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  659 LVSDILKGMIYLHdSEIISHGNLRSSNCLIDSRWV----CQISDFGL-HELKAGQEEPNKseleLKRALCMAPELLRdaY 733
Cdd:cd14195   113 FLKQILDGVHYLH-SKRIAHFDLKPENIMLLDKNVpnprIKLIDFGIaHKIEAGNEFKNI----FGTPEFVAPEIVN--Y 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  734 RPgrGSQKGDVYSFGILLYEMIGRKGPW-GDTaysKEEIIQFVKCpemLQHGVFRPALTHTHLDIPDYIRKCLCQcwdeD 812
Cdd:cd14195   186 EP--LGLEADMWSIGVITYILLSGASPFlGET---KQETLTNISA---VNYDFDEEYFSNTSELAKDFIRRLLVK----D 253

                  ....*..
gi 161076872  813 PEVRPDI 819
Cdd:cd14195   254 PKKRMTI 260
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
555-761 1.40e-09

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: 60.82  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  555 FQICRQSILVVGEPNK--RSFTNIALFRGNIVAM-------KKIHKKSVDITRSIRKEL-----KLMREVRHENIINFIG 620
Cdd:cd06658     7 FRAALQLVVSPGDPREylDSFIKIGEGSTGIVCIatekhtgKQVAVKKMDLRKQQRRELlfnevVIMRDYHHENVVDMYN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  621 ASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHmfISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFG 700
Cdd:cd06658    87 SYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQ--IATVCLSVLRALSYLHNQGVI-HRDIKSDSILLTSDGRIKLSDFG 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161076872  701 LHElKAGQEEPNKSELeLKRALCMAPELLRdayRPGRGSQKgDVYSFGILLYEMIGRKGPW 761
Cdd:cd06658   164 FCA-QVSKEVPKRKSL-VGTPYWMAPEVIS---RLPYGTEV-DIWSLGIMVIEMIDGEPPY 218
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
584-827 1.46e-09

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: 59.98  E-value: 1.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVD--ITRSIRKELKLMREVRHENIINFIGAStDHGSVIIFTTYCARGSLEDVLAnEDLHLDHMFISSLVS 661
Cdd:cd05116    25 VAVKILKNEANDpaLKDELLREANVMQQLDNPYIVRMIGIC-EAESWMLVMEMAELGPLNKFLQ-KNRHVTEKNITELVH 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  662 DILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRAL-CMAPELLRdaYRpgRGSQ 740
Cdd:cd05116   103 QVSMGMKYLEESNFV-HRDLAARNVLLVTQHYAKISDFGLSKALRADENYYKAQTHGKWPVkWYAPECMN--YY--KFSS 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  741 KGDVYSFGILLYEMIGrkgpWGDTAYSK---EEIIQFVKCPEMLQhgvfRPAlththlDIPDYIRKCLCQCWDEDPEVRP 817
Cdd:cd05116   178 KSDVWSFGVLMWEAFS----YGQKPYKGmkgNEVTQMIEKGERME----CPA------GCPPEMYDLMKLCWTYDVDERP 243
                         250
                  ....*....|
gi 161076872  818 DIRLVRMHLK 827
Cdd:cd05116   244 GFAAVELRLR 253
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
598-826 1.80e-09

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: 59.97  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  598 RSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLE---------DVLANEDLHLDHMFISSLVSDILKGMI 668
Cdd:cd14206    42 RKFISEAQPYRSLQHPNILQCLGLCTETIPFLLIMEFCQLGDLKrylraqrkaDGMTPDLPTRDLRTLQRMAYEITLGLL 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  669 YLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQE---EPNKSELELKRAlcmAPELLrDAYRPG----RGSQK 741
Cdd:cd14206   122 HLHKNNYI-HSDLALRNCLLTSDLTVRIGDYGLSHNNYKEDyylTPDRLWIPLRWV---APELL-DELHGNlivvDQSKE 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  742 GDVYSFGILLYEMIgrkgPWGDTAY---SKEEIIQFVKCPEMLQHGVFRPALTHThldipDYIRKCLCQCWdEDPEVRPD 818
Cdd:cd14206   197 SNVWSLGVTIWELF----EFGAQPYrhlSDEEVLTFVVREQQMKLAKPRLKLPYA-----DYWYEIMQSCW-LPPSQRPS 266

                  ....*...
gi 161076872  819 IRLVRMHL 826
Cdd:cd14206   267 VEELHLQL 274
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
581-819 1.91e-09

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: 59.82  E-value: 1.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIH-------KKSVDITRSIRK---ELKLMRE-VRHENIINFIGASTDHGSVIIFTTY---CARGSLEDVLAN 646
Cdd:cd08528    26 QTLLALKEINmtnpafgRTEQERDKSVGDiisEVNIIKEqLRHPNIVRYYKTFLENDRLYIVMELiegAPLGEHFSSLKE 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  647 EDLHLDHMFISSLVSDILKGMIYLHDSEIISHGNLRSSNCLIDSRWVCQISDFGLhelkAGQEEPNKSELE--LKRALCM 724
Cdd:cd08528   106 KNEHFTEDRIWNIFVQMVLALRYLHKEKQIVHRDLKPNNIMLGEDDKVTITDFGL----AKQKGPESSKMTsvVGTILYS 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  725 APELLRD-AYrpgrgSQKGDVYSFGILLYEMIGRKGPWgdtaYSKEEIIQFVKCPEmlqhGVFRPALTHTHLD-IPDYIR 802
Cdd:cd08528   182 CPEIVQNePY-----GEKADIWALGCILYQMCTLQPPF----YSTNMLTLATKIVE----AEYEPLPEGMYSDdITFVIR 248
                         250
                  ....*....|....*..
gi 161076872  803 KCLCQcwdeDPEVRPDI 819
Cdd:cd08528   249 SCLTP----DPEARPDI 261
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
580-755 3.09e-09

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: 59.51  E-value: 3.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  580 RGNIVAMKKIHKKsvDITRS-----IRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANED-LHLDH 653
Cdd:cd05580    25 SGKYYALKILKKA--KIIKLkqvehVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVMEYVPGGELFSLLRRSGrFPNDV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  654 -MFISSlvsDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkagqeepNKSELELKRALC-----MAPE 727
Cdd:cd05580   103 aKFYAA---EVVLALEYLHSLDIV-YRDLKPENLLLDSDGHIKITDFGF----------AKRVKDRTYTLCgtpeyLAPE 168
                         170       180
                  ....*....|....*....|....*....
gi 161076872  728 LLRdayrpGRGSQKG-DVYSFGILLYEMI 755
Cdd:cd05580   169 IIL-----SKGHGKAvDWWALGILIYEML 192
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
584-778 4.67e-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: 59.68  E-value: 4.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHK--KSVDITRSIRKELKLMREVRHENIINFI-----GASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHmfI 656
Cdd:cd07878    43 VAVKKLSRpfQSLIHARRTYRELRLLKHMKHENVIGLLdvftpATSIENFNEVYLVTNLMGADLNNIVKCQKLSDEH--V 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  657 SSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHElKAGQEEPNKSELELKRalcmAPELLRDAYRPg 736
Cdd:cd07878   121 QFLIYQLLRGLKYIHSAGII-HRDLKPSNVAVNEDCELRILDFGLAR-QADDEMTGYVATRWYR----APEIMLNWMHY- 193
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 161076872  737 rgSQKGDVYSFGILLYEMIGRKG--PWGDTAYSKEEIIQFVKCP 778
Cdd:cd07878   194 --NQTVDIWSVGCIMAELLKGKAlfPGNDYIDQLKRIMEVVGTP 235
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
603-830 5.56e-09

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: 58.27  E-value: 5.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  603 ELKLMREV-RHENIINFIGASTDHGsviifttYCARGSLEDVLANEDLHLD-HMFISSLVS---------DILKGMIYLH 671
Cdd:cd13975    47 EFHYTRSLpKHERIVSLHGSVIDYS-------YGGGSSIAVLLIMERLHRDlYTGIKAGLSleerlqialDVVEGIRFLH 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  672 dSEIISHGNLRSSNCLIDSRWVCQISDFGLhelkaGQEEPNKSELELKRALCMAPELLRDAYrpgrgSQKGDVYSFGILL 751
Cdd:cd13975   120 -SQGLVHRDIKLKNVLLDKKNRAKITDLGF-----CKPEAMMSGSIVGTPIHMAPELFSGKY-----DNSVDVYAFGILF 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  752 -YEMIGR-KGPWG-DTAYSKEEIIQFVKC---PEMLQhgVFrpalththldiPDYIRKCLCQCWDEDPEVRPDIRLVRMH 825
Cdd:cd13975   189 wYLCAGHvKLPEAfEQCASKDHLWNNVRKgvrPERLP--VF-----------DEECWNLMEACWSGDPSQRPLLGIVQPK 255

                  ....*
gi 161076872  826 LKELQ 830
Cdd:cd13975   256 LQGIM 260
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
582-825 5.60e-09

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


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 58.53  E-value: 5.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  582 NIVAMKKIH-KKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLhlDHMFISSLV 660
Cdd:cd06640    30 QVVAIKIIDlEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGGGSALDLLRAGPF--DEFQIATML 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkAGQ--EEPNKSELELKRALCMAPELL-RDAYrpgr 737
Cdd:cd06640   108 KEILKGLDYLHSEKKI-HRDIKAANVLLSEQGDVKLADFGV----AGQltDTQIKRNTFVGTPFWMAPEVIqQSAY---- 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  738 gSQKGDVYSFGILLYEMIGRKGPWGDTaYSKEEIIQFVKCPEMLQHGVFRPALThthldipDYIRKCLcqcwDEDPEVRP 817
Cdd:cd06640   179 -DSKADIWSLGITAIELAKGEPPNSDM-HPMRVLFLIPKNNPPTLVGDFSKPFK-------EFIDACL----NKDPSFRP 245

                  ....*...
gi 161076872  818 DIRLVRMH 825
Cdd:cd06640   246 TAKELLKH 253
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
581-761 5.63e-09

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: 58.88  E-value: 5.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHmfISSLV 660
Cdd:cd06657    45 GKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQ--IAAVC 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHElKAGQEEPNKSELeLKRALCMAPELL-RDAYRPgrgs 739
Cdd:cd06657   123 LAVLKALSVLHAQGVI-HRDIKSDSILLTHDGRVKLSDFGFCA-QVSKEVPRRKSL-VGTPYWMAPELIsRLPYGP---- 195
                         170       180
                  ....*....|....*....|..
gi 161076872  740 qKGDVYSFGILLYEMIGRKGPW 761
Cdd:cd06657   196 -EVDIWSLGIMVIEMVDGEPPY 216
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
581-839 5.64e-09

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: 58.59  E-value: 5.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIhKKSVDITRSIRKELKL---MREVRHENIINFIGASTDHGSVIIFTTyCARGSLEDVLAN---EDLHLDHM 654
Cdd:cd06617    26 GTIMAVKRI-RATVNSQEQKRLLMDLdisMRSVDCPYTVTFYGALFREGDVWICME-VMDTSLDKFYKKvydKGLTIPED 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  655 FISSLVSDILKGMIYLHDSEIISHGNLRSSNCLIDSRWVCQISDFGLhelkAGQEEpnKSELELKRALC---MAPELLRD 731
Cdd:cd06617   104 ILGKIAVSIVKALEYLHSKLSVIHRDVKPSNVLINRNGQVKLCDFGI----SGYLV--DSVAKTIDAGCkpyMAPERINP 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  732 AYRPGRGSQKGDVYSFGILLYEMIGRKGP---WGDTAyskEEIIQFVKCPE-MLQHGVFRPalththlDIPDYIRKCLcq 807
Cdd:cd06617   178 ELNQKGYDVKSDVWSLGITMIELATGRFPydsWKTPF---QQLKQVVEEPSpQLPAEKFSP-------EFQDFVNKCL-- 245
                         250       260       270
                  ....*....|....*....|....*....|...
gi 161076872  808 cwDEDPEVRPDIR-LVRMHLKELQAGLKPNIFD 839
Cdd:cd06617   246 --KKNYKERPNYPeLLQHPFFELHLSKNTDVAS 276
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
661-838 6.16e-09

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: 58.74  E-value: 6.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLH-ELKAGQeepNKSELELKRALCMAPELLRDAyrpgRGS 739
Cdd:cd05608   112 AQIISGLEHLHQRRII-YRDLKPENVLLDDDGNVRISDLGLAvELKDGQ---TKTKGYAGTPGFMAPELLLGE----EYD 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  740 QKGDVYSFGILLYEMIGRKGPW---GDTAYSKEeiiqfvkcpemLQHGVFRPALTHTHLDIPDyiRKCLCQ-CWDEDPEV 815
Cdd:cd05608   184 YSVDYFTLGVTLYEMIAARGPFrarGEKVENKE-----------LKQRILNDSVTYSEKFSPA--SKSICEaLLAKDPEK 250
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 161076872  816 RPDIR-----LVRMHL-------KELQAGLKPNIF 838
Cdd:cd05608   251 RLGFRdgncdGLRTHPffrdinwRKLEAGILPPPF 285
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
588-828 6.75e-09

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: 58.51  E-value: 6.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  588 KIHKKSVDITRSIRK------ELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVL--------ANEDLHLDH 653
Cdd:cd05062    38 RVAIKTVNEAASMRErieflnEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELMTRGDLKSYLrslrpemeNNPVQAPPS 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  654 MF-ISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRALCMAPELLRDa 732
Cdd:cd05062   118 LKkMIQMAGEIADGMAYLNANKFV-HRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKD- 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  733 yrpGRGSQKGDVYSFGILLYEMIG-RKGPWgdTAYSKEEIIQFVKCPEMLQhgvfRPAlththlDIPDYIRKCLCQCWDE 811
Cdd:cd05062   196 ---GVFTTYSDVWSFGVVLWEIATlAEQPY--QGMSNEQVLRFVMEGGLLD----KPD------NCPDMLFELMRMCWQY 260
                         250
                  ....*....|....*..
gi 161076872  812 DPEVRPDIRLVRMHLKE 828
Cdd:cd05062   261 NPKMRPSFLEIISSIKE 277
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
583-828 6.94e-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: 58.47  E-value: 6.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  583 IVAMKKIHKKSVDITRS-IRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANED-----------LH 650
Cdd:cd05095    48 LVAVKMLRADANKNARNdFLKEIKIMSRLKDPNIIRLLAVCITDDPLCMITEYMENGDLNQFLSRQQpegqlalpsnaLT 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  651 LDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL-HELKAGQEEPNKSELELK-RALCMAPEL 728
Cdd:cd05095   128 VSYSDLRFMAAQIASGMKYLSSLNFV-HRDLATRNCLVGKNYTIKIADFGMsRNLYSGDYYRIQGRAVLPiRWMSWESIL 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  729 LrdayrpGRGSQKGDVYSFGILLYEMIG--RKGPWgdTAYSKEEII----QFVKcPEMLQHGVFRPALThthldiPDYIR 802
Cdd:cd05095   207 L------GKFTTASDVWAFGVTLWETLTfcREQPY--SQLSDEQVIentgEFFR-DQGRQTYLPQPALC------PDSVY 271
                         250       260
                  ....*....|....*....|....*.
gi 161076872  803 KCLCQCWDEDPEVRPDIRLVRMHLKE 828
Cdd:cd05095   272 KLMLSCWRRDTKDRPSFQEIHTLLQE 297
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
603-819 7.18e-09

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: 58.32  E-value: 7.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  603 ELKLMREVRHENIINFIGASTDHGSVIIF--TTYCARGSLEDVLAN---EDLHLDHMFISSLVSDILKGMIYLH----DS 673
Cdd:cd08217    49 EVNILRELKHPNIVRYYDRIVDRANTTLYivMEYCEGGDLAQLIKKckkENQYIPEEFIWKIFTQLLLALYECHnrsvGG 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  674 EIISHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSelELKRALCMAPELLRD-AYrpgrgSQKGDVYSFGILLY 752
Cdd:cd08217   129 GKILHRDLKPANIFLDSDNNVKLGDFGLARVLSHDSSFAKT--YVGTPYYMSPELLNEqSY-----DEKSDIWSLGCLIY 201
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161076872  753 EMIGRKGPWgdTAYSKEEIIQFVKCpemlqhGVFRPalththldIPDY--------IRKCLCQcwdeDPEVRPDI 819
Cdd:cd08217   202 ELCALHPPF--QAANQLELAKKIKE------GKFPR--------IPSRysselnevIKSMLNV----DPDKRPSV 256
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
581-758 7.42e-09

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 59.00  E-value: 7.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKK--IHKKSVDITRSIRK------------ELKLMREVRHENIINFIGASTDHGSVIIFTTYCArGSLEDVLaN 646
Cdd:PTZ00024   34 GKIVAIKKvkIIEISNDVTKDRQLvgmcgihfttlrELKIMNEIKHENIMGLVDVYVEGDFINLVMDIMA-SDLKKVV-D 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  647 EDLHLDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL---------HELKAGQEEPNKSELE 717
Cdd:PTZ00024  112 RKIRLTESQVKCILLQILNGLNVLHKWYFM-HRDLSPANIFINSKGICKIADFGLarrygyppySDTLSKDETMQRREEM 190
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 161076872  718 LKRALCM---APELLRDAyrpGRGSQKGDVYSFGILLYEMIGRK 758
Cdd:PTZ00024  191 TSKVVTLwyrAPELLMGA---EKYHFAVDMWSVGCIFAELLTGK 231
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
588-829 7.69e-09

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: 58.31  E-value: 7.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  588 KIHKKSVDITRSIRKELK-------LMREVRHENIINFIGAS---TDHGSV---IIFTTYCARGSLEDVL-----ANEDL 649
Cdd:cd05035    29 KVAVKTMKVDIHTYSEIEeflseaaCMKDFDHPNVMRLIGVCftaSDLNKPpspMVILPFMKHGDLHSYLlysrlGGLPE 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  650 HLDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL-HELKAGQ--EEPNKSELELKralCMAP 726
Cdd:cd05035   109 KLPLQTLLKFMVDIAKGMEYLSNRNFI-HRDLAARNCMLDENMTVCVADFGLsRKIYSGDyyRQGRISKMPVK---WIAL 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  727 ELLRD-AYRPgrgsqKGDVYSFGILLYEMIGRkgpwGDTAY---SKEEIIQFvkcpemLQHG--VFRPAlththlDIPDY 800
Cdd:cd05035   185 ESLADnVYTS-----KSDVWSFGVTMWEIATR----GQTPYpgvENHEIYDY------LRNGnrLKQPE------DCLDE 243
                         250       260
                  ....*....|....*....|....*....
gi 161076872  801 IRKCLCQCWDEDPEVRPDIRLVRMHLKEL 829
Cdd:cd05035   244 VYFLMYFCWTVDPKDRPTFTKLREVLENI 272
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
581-755 1.34e-08

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


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 58.04  E-value: 1.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHK--KSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTY-----CARGSLEDVLANEDLHLDH 653
Cdd:cd07880    40 GAKVAIKKLYRpfQSELFAKRAYRELRLLKHMKHENVIGLLDVFTPDLSLDRFHDFylvmpFMGTDLGKLMKHEKLSEDR 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  654 mfISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkAGQEEPNKSELELKRALcMAPELLRDAY 733
Cdd:cd07880   120 --IQFLVYQMLKGLKYIHAAGII-HRDLKPGNLAVNEDCELKILDFGL----ARQTDSEMTGYVVTRWY-RAPEVILNWM 191
                         170       180
                  ....*....|....*....|..
gi 161076872  734 RPgrgSQKGDVYSFGILLYEMI 755
Cdd:cd07880   192 HY---TQTVDIWSVGCIMAEML 210
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
585-831 1.53e-08

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


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 57.52  E-value: 1.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  585 AMKKIHKKSVDITRSIRKELKLMREVR-HENIINFIGAST------DHG--SVIIFTTYCaRGSLEDVL----ANEDLHL 651
Cdd:cd14036    29 ALKRLLSNEEEKNKAIIQEINFMKKLSgHPNIVQFCSAASigkeesDQGqaEYLLLTELC-KGQLVDFVkkveAPGPFSP 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  652 DHmfISSLVSDILKGMIYLH-DSEIISHGNLRSSNCLIDSRWVCQISDFGLHELKAgqEEPNKSELELKRALC------- 723
Cdd:cd14036   108 DT--VLKIFYQTCRAVQHMHkQSPPIIHRDLKIENLLIGNQGQIKLCDFGSATTEA--HYPDYSWSAQKRSLVedeitrn 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  724 -----MAPELLrDAYRPGRGSQKGDVYSFGILLYEMIGRKGPWGDTAysKEEII--QFVKCPEMLQHGVFRpalththld 796
Cdd:cd14036   184 ttpmyRTPEMI-DLYSNYPIGEKQDIWALGCILYLLCFRKHPFEDGA--KLRIInaKYTIPPNDTQYTVFH--------- 251
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 161076872  797 ipDYIRKCLcqcwDEDPEVRPDIRLVRMHLKELQA 831
Cdd:cd14036   252 --DLIRSTL----KVNPEERLSITEIVEQLQELAA 280
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
581-701 1.64e-08

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


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 57.43  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVD--ITRSIRKELKLMREVRHENIINFIGASTDHGSVII---FTTYCARGSLEDVLANEdlHLDHMF 655
Cdd:cd07861    25 GQIVAMKKIRLESEEegVPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLvfeFLSMDLKKYLDSLPKGK--YMDAEL 102
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 161076872  656 ISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL 701
Cdd:cd07861   103 VKSYLYQILQGILFCHSRRVL-HRDLKPQNLLIDNKGVIKLADFGL 147
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
565-768 2.00e-08

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: 56.89  E-value: 2.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  565 VGEP-NKRSFTNIALFRGN----IVAMKKIHKKSVD---ITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCA 636
Cdd:cd14116     9 IGRPlGKGKFGNVYLAREKqskfILALKVLFKAQLEkagVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  637 RGSLEDVLaNEDLHLDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFG--LHelkagqeEPNKS 714
Cdd:cd14116    89 LGTVYREL-QKLSKFDEQRTATYITELANALSYCHSKRVI-HRDIKPENLLLGSAGELKIADFGwsVH-------APSSR 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 161076872  715 ELELKRAL-CMAPELLRdayrpGR-GSQKGDVYSFGILLYEMIGRKGPWGDTAYSK 768
Cdd:cd14116   160 RTTLCGTLdYLPPEMIE-----GRmHDEKVDLWSLGVLCYEFLVGKPPFEANTYQE 210
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
584-761 2.30e-08

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: 56.56  E-value: 2.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDITRSIR-KELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVL-ANEDLHLDHMFIssLVS 661
Cdd:cd14201    35 VAIKSINKKNLSKSQILLgKEIKILKELQHENIVALYDVQEMPNSVFLVMEYCNGGDLADYLqAKGTLSEDTIRV--FLQ 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  662 DILKGMIYLHDSEIIsHGNLRSSNCLID---------SRWVCQISDFGLhelkAGQEEPNKSELEL-KRALCMAPELLRD 731
Cdd:cd14201   113 QIAAAMRILHSKGII-HRDLKPQNILLSyasrkkssvSGIRIKIADFGF----ARYLQSNMMAATLcGSPMYMAPEVIMS 187
                         170       180       190
                  ....*....|....*....|....*....|
gi 161076872  732 AYRpgrgSQKGDVYSFGILLYEMIGRKGPW 761
Cdd:cd14201   188 QHY----DAKADLWSIGTVIYQCLVGKPPF 213
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
595-817 2.39e-08

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: 56.66  E-value: 2.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  595 DITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFtTYCARGSLEDVLANEDLHLDHMFISSLVSDILKGMIYLHDSE 674
Cdd:cd05056    49 SVREKFLQEAYIMRQFDHPHIVKLIGVITENPVWIVM-ELAPLGELRSYLQVNKYSLDLASLILYAYQLSTALAYLESKR 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  675 IIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQE--EPNKSELELKralCMAPELLRdaYRpgRGSQKGDVYSFGILLY 752
Cdd:cd05056   128 FV-HRDIAARNVLVSSPDCVKLGDFGLSRYMEDESyyKASKGKLPIK---WMAPESIN--FR--RFTSASDVWMFGVCMW 199
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161076872  753 E--MIGRKgPWgdTAYSKEEIIQFVK------CPEMLQhgvfrPALTHThldipdyirkcLCQCWDEDPEVRP 817
Cdd:cd05056   200 EilMLGVK-PF--QGVKNNDVIGRIEngerlpMPPNCP-----PTLYSL-----------MTKCWAYDPSKRP 253
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
601-819 2.62e-08

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: 56.50  E-value: 2.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  601 RKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSL-------EDVLANEDLhldhmfISSLVSDILKGMIYLHDS 673
Cdd:cd08225    47 KKEVILLAKMKHPNIVTFFASFQENGRLFIVMEYCDGGDLmkrinrqRGVLFSEDQ------ILSWFVQISLGLKHIHDR 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  674 EIIsHGNLRSSNCLIDSR-WVCQISDFGLhelkagQEEPNKSeLELKRALC-----MAPELLRDayRPgrGSQKGDVYSF 747
Cdd:cd08225   121 KIL-HRDIKSQNIFLSKNgMVAKLGDFGI------ARQLNDS-MELAYTCVgtpyyLSPEICQN--RP--YNNKTDIWSL 188
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161076872  748 GILLYEMIGRKGPWGDTAyskeeiiqfvkcpemLQHGVFRPALTHTHLDIPDY---IRKCLCQCWDEDPEVRPDI 819
Cdd:cd08225   189 GCVLYELCTLKHPFEGNN---------------LHQLVLKICQGYFAPISPNFsrdLRSLISQLFKVSPRDRPSI 248
PBP1_NPR_B cd06384
ligand-binding domain of type B natriuretic peptide receptor; Ligand-binding domain of type B ...
62-419 2.87e-08

ligand-binding domain of type B natriuretic peptide receptor; Ligand-binding domain of type B natriuretic peptide receptor (NPR-B). NPR-B is one of three known single membrane-spanning natriuretic peptide receptors that have been identified. Natriuretic peptides are family of structurally related but genetically distinct hormones/paracrine factors that regulate blood volume, blood pressure, ventricular hypertrophy, pulmonary hypertension, fat metabolism, and long bone growth. In mammals there are three natriuretic peptides: ANP, BNP, and CNP. Like NPR-A (or GC-A), NPR-B (or GC-B) is a transmembrane guanylyl cyclase, an enzyme that catalyzes the synthesis of cGMP. NPR-B is the predominant natriuretic peptide receptor in the brain. The rank of order activation of NPR-B by natriuretic peptides is CNP>>ANP>BNP. Homozygous inactivating mutations in human NPR-B cause a form of short-limbed dwarfism known as acromesomelic dysplasia type Maroteaux.


Pssm-ID: 380607 [Multi-domain]  Cd Length: 399  Bit Score: 57.56  E-value: 2.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   62 LPLAIEDVNKNPNLLPGK--KLAFKPVDIGHKMSAYrVKPLRAMTQMREAGVTAFIGPD--ESCTTEALLASAWNTPMLS 137
Cdd:cd06384    24 LRMAVDALQRKGKLLRGYtvNLLFHSSELQGACSEY-VAPLMAVDLKLYHDPDVLFGPGcvYPAASVGRFASHWRLPLIT 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  138 -------FKcsdpivSNKSTFHTFARTLAPASKVSKSVISLLNAFHWNKFSIV------VSSKPIWGsdVARAIQELAEA 204
Cdd:cd06384   103 agavafgFS------SKDEHYRTTVRTGPSAPKLGEFVSHLHSHFNWTSRAALlyhdlkTDDRPYYF--IIEGVFLALDG 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  205 RNFTISHFKYISDyipttkTLSQIDKIIEETYATTRIYVFIGEHIAMVDFVRGLQNRRLlESGDYIVVSVD---DEIYDS 281
Cdd:cd06384   175 ENLTVEHVPYDDQ------ENGDPREAIHFIKANGRIVYICGPLEMLHEIMLQAQRENL-TNGDYVFFYLDvfgESLRDD 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  282 NRRVniMERNYLDpyirkEKSKSLDKiSFRSVIKISMTYPQNPHIRDICSKIKDYARKTpFLVPYHQRVFDNISvpiyGL 361
Cdd:cd06384   248 DTRP--AEKPSSD-----IQWQDLRE-AFKTVLVITYKEPDNPEYQEFQRELIARAKQE-FGVQLNPSLMNLIA----GC 314
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 161076872  362 hLYDSVMIYVRAITEVLRLGGDIYDGNLVMSHIFNRSYHSIQGFdVYIDSNGDAEGNY 419
Cdd:cd06384   315 -FYDGVLLYAQALNETLREGGSQKDGLNIVEKMQDRRFWGVTGL-VSMDKNNDRDTDF 370
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
602-755 3.01e-08

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: 56.43  E-value: 3.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  602 KELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVL--ANEDLHLDHMFISSLVSDILKGMIYLHDSEIIS-- 677
Cdd:cd14160    41 SELEVLLLFQHPNILELAAYFTETEKFCLVYPYMQNGTLFDRLqcHGVTKPLSWHERINILIGIAKAIHYLHNSQPCTvi 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  678 HGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKS---ELELKRALCMAPEllrDAYRPGRGSQKGDVYSFGILLYEM 754
Cdd:cd14160   121 CGNISSANILLDDQMQPKLTDFALAHFRPHLEDQSCTinmTTALHKHLWYMPE---EYIRQGKLSVKTDVYSFGIVIMEV 197

                  .
gi 161076872  755 I 755
Cdd:cd14160   198 L 198
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
584-755 3.50e-08

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


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 56.98  E-value: 3.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDITRSIR--KELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANE--DLHLDHMFISSL 659
Cdd:cd07875    52 VAIKKLSRPFQNQTHAKRayRELVLMKCVNHKNIIGLLNVFTPQKSLEEFQDVYIVMELMDANLCQviQMELDHERMSYL 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  660 VSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHElKAGQeepnkselelkrALCMAPELLRDAYRP---- 735
Cdd:cd07875   132 LYQMLCGIKHLHSAGII-HRDLKPSNIVVKSDCTLKILDFGLAR-TAGT------------SFMMTPYVVTRYYRApevi 197
                         170       180
                  ....*....|....*....|..
gi 161076872  736 -GRGSQKG-DVYSFGILLYEMI 755
Cdd:cd07875   198 lGMGYKENvDIWSVGCIMGEMI 219
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
581-763 3.57e-08

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: 56.21  E-value: 3.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLaNEDLHLDHMFISSLV 660
Cdd:cd06645    36 GELAAIKVIKLEPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEFCGGGSLQDIY-HVTGPLSESQIAYVS 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSelELKRALCMAPELLRdAYRPGRGSQ 740
Cdd:cd06645   115 RETLQGLYYLHSKGKM-HRDIKGANILLTDNGHVKLADFGVSAQITATIAKRKS--FIGTPYWMAPEVAA-VERKGGYNQ 190
                         170       180
                  ....*....|....*....|...
gi 161076872  741 KGDVYSFGILLYEMIGRKGPWGD 763
Cdd:cd06645   191 LCDIWAVGITAIELAELQPPMFD 213
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
650-828 3.93e-08

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: 56.13  E-value: 3.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  650 HLDHMFisSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRALCMAPELL 729
Cdd:cd05061   117 TLQEMI--QMAAEIADGMAYLNAKKFV-HRDLAARNCMVAHDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESL 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  730 RDayrpGRGSQKGDVYSFGILLYEMIG-RKGPWgdTAYSKEEIIQFVkcpeMLQHGVFRPAlththlDIPDYIRKCLCQC 808
Cdd:cd05061   194 KD----GVFTTSSDMWSFGVVLWEITSlAEQPY--QGLSNEQVLKFV----MDGGYLDQPD------NCPERVTDLMRMC 257
                         170       180
                  ....*....|....*....|
gi 161076872  809 WDEDPEVRPDIRLVRMHLKE 828
Cdd:cd05061   258 WQFNPKMRPTFLEIVNLLKD 277
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
581-755 4.08e-08

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: 56.36  E-value: 4.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKsvdiTRSIRKELKLMREVRHENIINFIGASTDHGS------VIIFTTYCArGSLEDVL---ANEDLHL 651
Cdd:cd14137    29 GEVVAIKKVLQD----KRYKNRELQIMRRLKHPNIVKLKYFFYSSGEkkdevyLNLVMEYMP-ETLYRVIrhySKNKQTI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  652 DHMFISSLVSDILKGMIYLHdSEIISHGNLRSSNCLIDSR-WVCQISDFG-LHELKAGqeEPNKSElelkraLCM----A 725
Cdd:cd14137   104 PIIYVKLYSYQLFRGLAYLH-SLGICHRDIKPQNLLVDPEtGVLKLCDFGsAKRLVPG--EPNVSY------ICSryyrA 174
                         170       180       190
                  ....*....|....*....|....*....|..
gi 161076872  726 PELLRDA--YrpgrgSQKGDVYSFGILLYEMI 755
Cdd:cd14137   175 PELIFGAtdY-----TTAIDIWSAGCVLAELL 201
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
583-773 4.73e-08

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


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 55.80  E-value: 4.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  583 IVAMKKIHKKSVDITR-SIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMfISSLVS 661
Cdd:cd14167    30 LVAIKCIAKKALEGKEtSIENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQLVSGGELFDRIVEKGFYTERD-ASKLIF 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  662 DILKGMIYLHDSEIIsHGNLRSSNCL---IDSRWVCQISDFGLHELkagqEEPNkselELKRALC-----MAPELLrdAY 733
Cdd:cd14167   109 QILDAVKYLHDMGIV-HRDLKPENLLyysLDEDSKIMISDFGLSKI----EGSG----SVMSTACgtpgyVAPEVL--AQ 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 161076872  734 RPgrGSQKGDVYSFGILLYEMIGRKGPWGDTAYSK--EEIIQ 773
Cdd:cd14167   178 KP--YSKAVDCWSIGVIAYILLCGYPPFYDENDAKlfEQILK 217
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
596-818 5.11e-08

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


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 55.79  E-value: 5.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  596 ITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANED------LHLDHMFISSLVS-----DIL 664
Cdd:cd14011    45 ILELLKRGVKQLTRLRHPRILTVQHPLEESRESLAFATEPVFASLANVLGERDnmpsppPELQDYKLYDVEIkygllQIS 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  665 KGMIYLHDSEIISHGNLRSSNCLIDSR--W-------VCQISDFGLHELKAGQEEPNKSELELKRALCMAPELLRDAyrp 735
Cdd:cd14011   125 EALSFLHNDVKLVHGNICPESVVINSNgeWklagfdfCISSEQATDQFPYFREYDPNLPPLAQPNLNYLAPEYILSK--- 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  736 gRGSQKGDVYSFGILLYEMIGRkgpwGDTAY-SKEEIIQFVKCPEMLQHgvfrpaLTHTHL-DIPDYIRKCLCQCWDEDP 813
Cdd:cd14011   202 -TCDPASDMFSLGVLIYAIYNK----GKPLFdCVNNLLSYKKNSNQLRQ------LSLSLLeKVPEELRDHVKTLLNVTP 270

                  ....*
gi 161076872  814 EVRPD 818
Cdd:cd14011   271 EVRPD 275
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
596-755 5.15e-08

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: 56.00  E-value: 5.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  596 ITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVL----ANEDLHLDHMFisSLVSDILKGMIYLH 671
Cdd:cd14157    35 TERFFQTEVQICFRCCHPNILPLLGFCVESDCHCLIYPYMPNGSLQDRLqqqgGSHPLPWEQRL--SISLGLLKAVQHLH 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  672 DSEIIsHGNLRSSNCLIDSRWVCQISDFGLHeLKAGQEEPNKSELELKRALCMAPELLRDAYRPGRGSQKGDVYSFGILL 751
Cdd:cd14157   113 NFGIL-HGNIKSSNVLLDGNLLPKLGHSGLR-LCPVDKKSVYTMMKTKVLQISLAYLPEDFVRHGQLTEKVDIFSCGVVL 190

                  ....
gi 161076872  752 YEMI 755
Cdd:cd14157   191 AEIL 194
PBP1_CaSR cd06364
ligand-binding domain of the CaSR calcium-sensing receptor, a member of the family C receptors ...
65-260 5.21e-08

ligand-binding domain of the CaSR calcium-sensing receptor, a member of the family C receptors within the G-protein coupled receptor superfamily; Ligand-binding domain of the CaSR calcium-sensing receptor, which is a member of the family C receptors within the G-protein coupled receptor superfamily. CaSR provides feedback control of extracellular calcium homeostasis by responding sensitively to acute fluctuations in extracellular ionized Ca2+ concentration. This ligand-binding domain has homology to the bacterial leucine-isoleucine-valine binding protein (LIVBP) and a leucine binding protein (LBP). CaSR is widely expressed in mammalian tissues and is active in tissues that are not directly involved in extracellular calcium homeostasis. Moreover, CaSR responds to aromatic, aliphatic, and polar amino acids, but not to positively charged or branched chain amino acids, which suggests that changes in plasma amino acid levels are likely to modulate whole body calcium metabolism. Additionally, the family C GPCRs includes at least two receptors with broad-spectrum amino acid-sensing properties: GPRC6A which recognizes basic and various aliphatic amino acids, its gold-fish homolog the 5.24 chemoreceptor, and a specific taste receptor (T1R) which responds to aliphatic, polar, charged, and branched amino acids, but not to aromatic amino acids.


Pssm-ID: 380587 [Multi-domain]  Cd Length: 473  Bit Score: 56.88  E-value: 5.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   65 AIEDVNKNPNLLPGKKLAFKPVD----IGHKMSAyrvkplrAMTQMreAGVTAFIgPDESCTTEALLA-------SA--- 130
Cdd:cd06364    45 AIEEINNSPDLLPNITLGYRIYDscatISKALRA-------ALALV--NGQEETN-LDERCSGGPPVAavigesgSTlsi 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  131 --------WNTPMLSFKCSDPIVSNKSTFHTFARTLAPASKVSKSVISLLNAFHWNkFSIVVSSKPIWGSDVARAIQELA 202
Cdd:cd06364   115 avartlglFYIPQVSYFASCACLSDKKQFPSFLRTIPSDYYQSRALAQLVKHFGWT-WVGAIASDDDYGRNGIKAFLEEA 193
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161076872  203 EARNFTISHfkyiSDYIPTTKTLSQIDKIIEETYATTR--IYVFIGE---HIAMVDFVRglQN 260
Cdd:cd06364   194 EKLGICIAF----SETIPRTYSQEKILRIVEVIKKSTAkvIVVFSSEgdlEPLIKELVR--QN 250
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
584-800 6.00e-08

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


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 56.25  E-value: 6.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDITRSIR--KELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANE--DLHLDHMFISSL 659
Cdd:cd07874    45 VAIKKLSRPFQNQTHAKRayRELVLMKCVNHKNIISLLNVFTPQKSLEEFQDVYLVMELMDANLCQviQMELDHERMSYL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  660 VSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHElKAGQeepnkselelkrALCMAPELLRDAYRP---- 735
Cdd:cd07874   125 LYQMLCGIKHLHSAGII-HRDLKPSNIVVKSDCTLKILDFGLAR-TAGT------------SFMMTPYVVTRYYRApevi 190
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161076872  736 -GRGSQKG-DVYSFGILLYEMIGRK--GPWGDTAYSKEEIIQFV--KCPEMLQHgvFRPALTHTHLDIPDY 800
Cdd:cd07874   191 lGMGYKENvDIWSVGCIMGEMVRHKilFPGRDYIDQWNKVIEQLgtPCPEFMKK--LQPTVRNYVENRPKY 259
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
595-752 6.13e-08

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: 55.44  E-value: 6.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  595 DITRSIRKELKLMREV-RHENII---NFIGASTdhgsvIIFTTY--CARGSLEDVLaNEDLHLDHMFISSLVSDILKGMI 668
Cdd:cd14093    50 ELREATRREIEILRQVsGHPNIIelhDVFESPT-----FIFLVFelCRKGELFDYL-TEVVTLSEKKTRRIMRQLFEAVE 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  669 YLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLH-ELKAGqeepnkselELKRALC-----MAPELLR---DAYRPGRGs 739
Cdd:cd14093   124 FLHSLNIV-HRDLKPENILLDDNLNVKISDFGFAtRLDEG---------EKLRELCgtpgyLAPEVLKcsmYDNAPGYG- 192
                         170
                  ....*....|...
gi 161076872  740 QKGDVYSFGILLY 752
Cdd:cd14093   193 KEVDMWACGVIMY 205
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
598-829 7.15e-08

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: 55.76  E-value: 7.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  598 RSIRKELKLMREVRHE-NIINFIGASTDHGS-VIIFTTYCARGSLEDVL------------------------------- 644
Cdd:cd05103    55 RALMSELKILIHIGHHlNVVNLLGACTKPGGpLMVIVEFCKFGNLSAYLrskrsefvpyktkgarfrqgkdyvgdisvdl 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  645 --------------------------------ANEDLHLDHMFISSLVS---DILKGMIYLHDSEIIsHGNLRSSNCLID 689
Cdd:cd05103   135 krrldsitssqssassgfveekslsdveeeeaGQEDLYKDFLTLEDLICysfQVAKGMEFLASRKCI-HRDLAARNILLS 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  690 SRWVCQISDFGLheLKAGQEEPN-----KSELELKralCMAPELLRDAYRpgrgSQKGDVYSFGILLYEMIGrkgpWGDT 764
Cdd:cd05103   214 ENNVVKICDFGL--ARDIYKDPDyvrkgDARLPLK---WMAPETIFDRVY----TIQSDVWSFGVLLWEIFS----LGAS 280
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161076872  765 AYSKEEIIQFVKCpeMLQHGvfrpalthTHLDIPDY----IRKCLCQCWDEDPEVRPDIRLVRMHLKEL 829
Cdd:cd05103   281 PYPGVKIDEEFCR--RLKEG--------TRMRAPDYttpeMYQTMLDCWHGEPSQRPTFSELVEHLGNL 339
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
581-763 8.42e-08

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


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 55.03  E-value: 8.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLaNEDLHLDHMFISSLV 660
Cdd:cd06646    34 GELAAVKIIKLEPGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICMEYCGGGSLQDIY-HVTGPLSELQIAYVC 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHdSEIISHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSelELKRALCMAPELLRdAYRPGRGSQ 740
Cdd:cd06646   113 RETLQGLAYLH-SKGKMHRDIKGANILLTDNGDVKLADFGVAAKITATIAKRKS--FIGTPYWMAPEVAA-VEKNGGYNQ 188
                         170       180
                  ....*....|....*....|...
gi 161076872  741 KGDVYSFGILLYEMIGRKGPWGD 763
Cdd:cd06646   189 LCDIWAVGITAIELAELQPPMFD 211
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
583-820 8.80e-08

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: 54.79  E-value: 8.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  583 IVAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSvIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSD 662
Cdd:cd05037    32 EVLLKVLDSDHRDISESFFETASLMSQISHKHLVKLYGVCVADEN-IMVQEYVRYGPLDKYLRRMGNNVPLSWKLQVAKQ 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  663 ILKGMIYLHDSEIIsHGNLRSSNCLidsrwVCQ-----------ISDFGLHELKAGQEEPnkseleLKRALCMAPELLRD 731
Cdd:cd05037   111 LASALHYLEDKKLI-HGNVRGRNIL-----LARegldgyppfikLSDPGVPITVLSREER------VDRIPWIAPECLRN 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  732 AyrPGRGSQKGDVYSFGILLYEMIGRkGPWGDTAYSKEEIIQFVKcpemlqhgvfrpalTHTHLDIPDY--IRKCLCQCW 809
Cdd:cd05037   179 L--QANLTIAADKWSFGTTLWEICSG-GEEPLSALSSQEKLQFYE--------------DQHQLPAPDCaeLAELIMQCW 241
                         250
                  ....*....|.
gi 161076872  810 DEDPEVRPDIR 820
Cdd:cd05037   242 TYEPTKRPSFR 252
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
584-757 9.31e-08

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: 54.87  E-value: 9.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKS---VDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLV 660
Cdd:cd14186    29 VAIKMIDKKAmqkAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLEMCHNGEMSRYLKNRKKPFTEDEARHFM 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHdSEIISHGNLRSSNCLIDSRWVCQISDFGLH-ELKAGQEE-------PNKselelkralcMAPELlrdA 732
Cdd:cd14186   109 HQIVTGMLYLH-SHGILHRDLTLSNLLLTRNMNIKIADFGLAtQLKMPHEKhftmcgtPNY----------ISPEI---A 174
                         170       180
                  ....*....|....*....|....*.
gi 161076872  733 YRPGRGSQkGDVYSFGILLYE-MIGR 757
Cdd:cd14186   175 TRSAHGLE-SDVWSLGCMFYTlLVGR 199
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
661-816 1.22e-07

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


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 54.46  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLH-ELKAGQeepnKSELELKRALCMAPELLRD--AYrpgr 737
Cdd:cd05577   102 AEIICGLEHLHNRFIV-YRDLKPENILLDDHGHVRISDLGLAvEFKGGK----KIKGRVGTHGYMAPEVLQKevAY---- 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  738 gSQKGDVYSFGILLYEMIGRKGPWGD--TAYSKEEIIQFVK-CPEMLQHGvFRPALThthldipDYIRKCLCQcwdeDPE 814
Cdd:cd05577   173 -DFSVDWFALGCMLYEMIAGRSPFRQrkEKVDKEELKRRTLeMAVEYPDS-FSPEAR-------SLCEGLLQK----DPE 239

                  ..
gi 161076872  815 VR 816
Cdd:cd05577   240 RR 241
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
603-820 1.25e-07

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: 54.69  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  603 ELKLMREVRHENIINFIGASTDhGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSDILKGMIYLHDSEIIsHGNLR 682
Cdd:cd05110    59 EALIMASMDHPHLVRLLGVCLS-PTIQLVTQLMPHGCLLDYVHEHKDNIGSQLLLNWCVQIAKGMMYLEERRLV-HRDLA 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  683 SSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRALCMAPELLRdaYRpgRGSQKGDVYSFGILLYEMIGRKGPWG 762
Cdd:cd05110   137 ARNVLVKSPNHVKITDFGLARLLEGDEKEYNADGGKMPIKWMALECIH--YR--KFTHQSDVWSYGVTIWELMTFGGKPY 212
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 161076872  763 DTAYSKEeiiqfvkCPEMLQHGVFRPALTHTHLDIpdYIrkCLCQCWDEDPEVRPDIR 820
Cdd:cd05110   213 DGIPTRE-------IPDLLEKGERLPQPPICTIDV--YM--VMVKCWMIDADSRPKFK 259
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
572-768 1.56e-07

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: 54.23  E-value: 1.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  572 SFTNIALFR----GNIVAMKKIHKKSVDITRSIRKELKLMREVRHENIINF--IGASTDHGSVIIftTYCARGSLEDVLA 645
Cdd:cd14166    15 AFSEVYLVKqrstGKLYALKCIKKSPLSRDSSLENEIAVLKRIKHENIVTLedIYESTTHYYLVM--QLVSGGELFDRIL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  646 NEDLHLDHMfISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLI---DSRWVCQISDFGLHELkagqeepnkSELELKRAL 722
Cdd:cd14166    93 ERGVYTEKD-ASRVINQVLSAVKYLHENGIV-HRDLKPENLLYltpDENSKIMITDFGLSKM---------EQNGIMSTA 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 161076872  723 C-----MAPELLrdAYRPgrGSQKGDVYSFGILLYEMIGRKGPWGDTAYSK 768
Cdd:cd14166   162 CgtpgyVAPEVL--AQKP--YSKAVDCWSIGVITYILLCGYPPFYEETESR 208
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
576-827 1.91e-07

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: 53.80  E-value: 1.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  576 IALFRGNIVAMK----KIHKKSVDIT---------RSIRKEL----KLMREVRHENIINFIGAStDHGSVIIFTTYCARG 638
Cdd:cd05115    10 VELGSGNFGCVKkgvyKMRKKQIDVAikvlkqgneKAVRDEMmreaQIMHQLDNPYIVRMIGVC-EAEALMLVMEMASGG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  639 SLEDVLANEDLHLDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELEL 718
Cdd:cd05115    89 PLNKFLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFV-HRDLAARNVLLVNQHYAKISDFGLSKALGADDSYYKARSAG 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  719 KRAL-CMAPELLRdaYRpgRGSQKGDVYSFGILLYEMIGrkgpWGDTAYSK---EEIIQFVKCPEMLQHgvfrPAlthth 794
Cdd:cd05115   168 KWPLkWYAPECIN--FR--KFSSRSDVWSYGVTMWEAFS----YGQKPYKKmkgPEVMSFIEQGKRMDC----PA----- 230
                         250       260       270
                  ....*....|....*....|....*....|...
gi 161076872  795 lDIPDYIRKCLCQCWDEDPEVRPDIRLVRMHLK 827
Cdd:cd05115   231 -ECPPEMYALMSDCWIYKWEDRPNFLTVEQRMR 262
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
603-817 2.24e-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: 54.47  E-value: 2.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  603 ELKLMREV-RHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANE----------------------DLHLDHMFI--- 656
Cdd:cd05106    91 ELKILSHLgQHKNIVNLLGACTHGGPVLVITEYCCYGDLLNFLRKKaetflnfvmalpeisetssdykNITLEKKYIrsd 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  657 -----------------SSLVSD---------------------------ILKGMIYLHDSEIIsHGNLRSSNCLIDSRW 692
Cdd:cd05106   171 sgfssqgsdtyvemrpvSSSSSQssdskdeedtedswpldlddllrfssqVAQGMDFLASKNCI-HRDVAARNVLLTDGR 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  693 VCQISDFGL---------HELKAGQEEPNKselelkralCMAPELLRDAYRpgrgSQKGDVYSFGILLYEMIGR-KGPWG 762
Cdd:cd05106   250 VAKICDFGLardimndsnYVVKGNARLPVK---------WMAPESIFDCVY----TVQSDVWSYGILLWEIFSLgKSPYP 316
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 161076872  763 DTAYSKeeiiQFVKcpeMLQHGVfrpalthtHLDIPDY----IRKCLCQCWDEDPEVRP 817
Cdd:cd05106   317 GILVNS----KFYK---MVKRGY--------QMSRPDFappeIYSIMKMCWNLEPTERP 360
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
581-755 2.26e-07

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: 53.97  E-value: 2.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKK-IHKKSVDITRSIR-KELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDvLANEDLHLDHMFISS 658
Cdd:cd07846    26 GQIVAIKKfLESEDDKMVKKIAmREIKMLKQLRHENLVNLIEVFRRKKRWYLVFEFVDHTVLDD-LEKYPNGLDESRVRK 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  659 LVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKraLCMAPELLRDAYRPGRG 738
Cdd:cd07846   105 YLFQILRGIDFCHSHNII-HRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYVATR--WYRAPELLVGDTKYGKA 181
                         170
                  ....*....|....*..
gi 161076872  739 SqkgDVYSFGILLYEMI 755
Cdd:cd07846   182 V---DVWAVGCLVTEML 195
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
584-755 2.28e-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: 54.26  E-value: 2.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDITRSIR--KELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLH--LDHMFISSL 659
Cdd:cd07876    49 VAVKKLSRPFQNQTHAKRayRELVLLKCVNHKNIISLLNVFTPQKSLEEFQDVYLVMELMDANLCQVIHmeLDHERMSYL 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  660 VSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQeepnkselelkraLCMAPELLRDAYRP---- 735
Cdd:cd07876   129 LYQMLCGIKHLHSAGII-HRDLKPSNIVVKSDCTLKILDFGLARTACTN-------------FMMTPYVVTRYYRApevi 194
                         170       180
                  ....*....|....*....|..
gi 161076872  736 -GRGSQKG-DVYSFGILLYEMI 755
Cdd:cd07876   195 lGMGYKENvDIWSVGCIMGELV 216
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
581-701 2.53e-07

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


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 53.83  E-value: 2.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVD---ITRSIRkELKLMREVRHENIInfigastdhgsviifttycargSLEDVLANE---------- 647
Cdd:cd07835    24 GEIVALKKIRLETEDegvPSTAIR-EISLLKELNHPNIV----------------------RLLDVVHSEnklylvfefl 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161076872  648 --DL--HLDH--------MFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL 701
Cdd:cd07835    81 dlDLkkYMDSspltgldpPLIKSYLYQLLQGIAFCHSHRVL-HRDLKPQNLLIDTEGALKLADFGL 145
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
584-774 2.55e-07

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: 53.53  E-value: 2.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDITRSI-RKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLA-----NEDLhldhmfIS 657
Cdd:cd14120    22 VAIKCITKKNLSKSQNLlGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGDLADYLQakgtlSEDT------IR 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  658 SLVSDILKGMIYLHDSEIIsHGNLRSSNCLID---------SRWVCQISDFGLHE-LKAGQeepnkseleLKRALC---- 723
Cdd:cd14120    96 VFLQQIAAAMKALHSKGIV-HRDLKPQNILLShnsgrkpspNDIRLKIADFGFARfLQDGM---------MAATLCgspm 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 161076872  724 -MAPELLR----DAyrpgrgsqKGDVYSFGILLYEMIGRKGPWgdTAYSKEEIIQF 774
Cdd:cd14120   166 yMAPEVIMslqyDA--------KADLWSIGTIVYQCLTGKAPF--QAQTPQELKAF 211
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
581-755 2.83e-07

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: 53.28  E-value: 2.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVD----ITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDlHLDHMFI 656
Cdd:cd14070    27 GEKVAIKVIDKKKAKkdsyVTKNLRREGRIQQMIRHPNITQLLDILETENSYYLVMELCPGGNLMHRIYDKK-RLEEREA 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  657 SSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRALCMAPELL-RDAYRP 735
Cdd:cd14070   106 RRYIRQLVSAVEHLHRAGVV-HRDLKIENLLLDENDNIKLIDFGLSNCAGILGYSDPFSTQCGSPAYAAPELLaRKKYGP 184
                         170       180
                  ....*....|....*....|
gi 161076872  736 grgsqKGDVYSFGILLYEMI 755
Cdd:cd14070   185 -----KVDVWSIGVNMYAML 199
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
584-820 2.95e-07

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: 53.87  E-value: 2.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHK-KSVDITRSIRKELKLMREVRHENIINFIGASTDhGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSD 662
Cdd:cd05108    39 VAIKELREaTSPKANKEILDEAYVMASVDNPHVCRLLGICLT-STVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQ 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  663 ILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRALCMAPE-LLRDAYrpgrgSQK 741
Cdd:cd05108   118 IAKGMNYLEDRRLV-HRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALEsILHRIY-----THQ 191
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161076872  742 GDVYSFGILLYEMIgrkgPWGDTAYSKeeiIQFVKCPEMLQHGVFRPALTHTHLDIPDYIRKclcqCWDEDPEVRPDIR 820
Cdd:cd05108   192 SDVWSYGVTVWELM----TFGSKPYDG---IPASEISSILEKGERLPQPPICTIDVYMIMVK----CWMIDADSRPKFR 259
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
587-833 3.32e-07

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


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 53.45  E-value: 3.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  587 KKIHKKSVDITRSIRKEL-----KLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHmfISSLVS 661
Cdd:cd06659    47 RQVAVKMMDLRKQQRRELlfnevVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGGALTDIVSQTRLNEEQ--IATVCE 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  662 DILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHElKAGQEEPNKSELeLKRALCMAPE-LLRDAYrpgrgSQ 740
Cdd:cd06659   125 AVLQALAYLHSQGVI-HRDIKSDSILLTLDGRVKLSDFGFCA-QISKDVPKRKSL-VGTPYWMAPEvISRCPY-----GT 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  741 KGDVYSFGILLYEMIGrkgpwGDTAYSKEEIIQFVK----CPEmlqhgvfrPALTHTHLDIP---DYIRKCLCQcwdeDP 813
Cdd:cd06659   197 EVDIWSLGIMVIEMVD-----GEPPYFSDSPVQAMKrlrdSPP--------PKLKNSHKASPvlrDFLERMLVR----DP 259
                         250       260
                  ....*....|....*....|
gi 161076872  814 EVRPDIRLVRMHLKELQAGL 833
Cdd:cd06659   260 QERATAQELLDHPFLLQTGL 279
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
610-757 4.58e-07

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: 53.13  E-value: 4.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  610 VRHENIINFIGASTD-HGS---VIIFTTYCARGSLEDVLANEDLHLDHMFisSLVSDILKGMIYLHdSEI--------IS 677
Cdd:cd14219    56 MRHENILGFIAADIKgTGSwtqLYLITDYHENGSLYDYLKSTTLDTKAML--KLAYSSVSGLCHLH-TEIfstqgkpaIA 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  678 HGNLRSSNCLIDSRWVCQISDFGLH-ELKAGQEE---PNKSELELKRAlcMAPELLRDAYRPGRGSQ--KGDVYSFGILL 751
Cdd:cd14219   133 HRDLKSKNILVKKNGTCCIADLGLAvKFISDTNEvdiPPNTRVGTKRY--MPPEVLDESLNRNHFQSyiMADMYSFGLIL 210

                  ....*.
gi 161076872  752 YEMIGR 757
Cdd:cd14219   211 WEVARR 216
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
581-701 4.82e-07

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: 53.45  E-value: 4.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKK--------IHKKsvditRSIRkELKLMREVRHENIINFIGASTDHGSVIIFT-----TYCARGSLEDVLANE 647
Cdd:cd07851    40 GRKVAIKKlsrpfqsaIHAK-----RTYR-ELRLLKHMKHENVIGLLDVFTPASSLEDFQdvylvTHLMGADLNNIVKCQ 113
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 161076872  648 DLHLDHmfISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL 701
Cdd:cd07851   114 KLSDDH--IQFLVYQILRGLKYIHSAGII-HRDLKPSNLAVNEDCELKILDFGL 164
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
603-755 4.95e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 53.34  E-value: 4.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  603 ELKLMREVRHENIIN-----FIGASTdhgsVIIFTTYcaRGSLEDVLANEDLHLDHMFISSLVSDILKGMIYLHDSEIIs 677
Cdd:PHA03209  107 EAMLLQNVNHPSVIRmkdtlVSGAIT----CMVLPHY--SSDLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQRII- 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  678 HGNLRSSNCLIDS-RWVCqISDFGLHELK---------AGQEEPNkselelkralcmAPELL-RDAYrpgrgSQKGDVYS 746
Cdd:PHA03209  180 HRDVKTENIFINDvDQVC-IGDLGAAQFPvvapaflglAGTVETN------------APEVLaRDKY-----NSKADIWS 241

                  ....*....
gi 161076872  747 FGILLYEMI 755
Cdd:PHA03209  242 AGIVLFEML 250
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
602-817 7.26e-07

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: 52.20  E-value: 7.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  602 KELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHL----DHMFISSLVSDILKGMIYLHDSEIIs 677
Cdd:cd05042    44 KEGQPYRILQHPNILQCLGQCVEAIPYLLVMEFCDLGDLKAYLRSEREHErgdsDTRTLQRMACEVAAGLAHLHKLNFV- 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  678 HGNLRSSNCLIDSRWVCQISDFGLHELKAGQ---EEPNKSELELKRAlcmAPELL---RDAYRPGRGSQKGDVYSFGILL 751
Cdd:cd05042   123 HSDLALRNCLLTSDLTVKIGDYGLAHSRYKEdyiETDDKLWFPLRWT---APELVtefHDRLLVVDQTKYSNIWSLGVTL 199
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161076872  752 YEMIgRKGPWGDTAYSKEEIIQFVKCPEMLQhgVFRPALthtHLDIPDYIRKCLCQCWdEDPEVRP 817
Cdd:cd05042   200 WELF-ENGAQPYSNLSDLDVLAQVVREQDTK--LPKPQL---ELPYSDRWYEVLQFCW-LSPEQRP 258
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
581-825 7.37e-07

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


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 51.91  E-value: 7.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSvDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLAN-----EDLHldHMF 655
Cdd:cd14665    25 KELVAVKYIERGE-KIDENVQREIINHRSLRHPNIVRFKEVILTPTHLAIVMEYAAGGELFERICNagrfsEDEA--RFF 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  656 ISSLVSdilkGMIYLHDSEiISHGNLRSSNCLIDSRWV--CQISDFGLHELKAGQEEPNKSeleLKRALCMAPE-LLRDA 732
Cdd:cd14665   102 FQQLIS----GVSYCHSMQ-ICHRDLKLENTLLDGSPAprLKICDFGYSKSSVLHSQPKST---VGTPAYIAPEvLLKKE 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  733 YrpgrGSQKGDVYSFGILLYEMIGRKGPWGDtaysKEEiiqfvkcPEMLQHGVFRpaLTHTHLDIPDYI------RKCLC 806
Cdd:cd14665   174 Y----DGKIADVWSCGVTLYVMLVGAYPFED----PEE-------PRNFRKTIQR--ILSVQYSIPDYVhispecRHLIS 236
                         250
                  ....*....|....*....
gi 161076872  807 QCWDEDPEVRPDIRLVRMH 825
Cdd:cd14665   237 RIFVADPATRITIPEIRNH 255
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
580-710 7.66e-07

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


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 51.83  E-value: 7.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  580 RGNIVAMKKIHKKSVDIT-------------RSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLAN 646
Cdd:cd14108    12 RGAFSYLRRVKEKSSDLSfaakfipvrakkkTSARRELALLAELDHKSIVRFHDAFEKRRVVIIVTELCHEELLERITKR 91
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161076872  647 EDLHLDHmfISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLI--DSRWVCQISDFG-LHELKAGQEE 710
Cdd:cd14108    92 PTVCESE--VRSYMRQLLEGIEYLHQNDVL-HLDLKPENLLMadQKTDQVRICDFGnAQELTPNEPQ 155
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
584-825 7.73e-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: 7.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSV---DITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLED-VLANEdlHLDHMFISSL 659
Cdd:cd14076    34 VAIKLIRRDTQqenCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYIGIVLEFVSGGELFDyILARR--RLKDSVACRL 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  660 VSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkAGQEEPNKSELelKRALC-----MAPELL-RDAY 733
Cdd:cd14076   112 FAQLISGVAYLHKKGVV-HRDLKLENLLLDKNRNLVITDFGF----ANTFDHFNGDL--MSTSCgspcyAAPELVvSDSM 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  734 RPGRgsqKGDVYSFGILLYEMIGRKGPWGDTAYSK--EEIIQFVKcpemlqhgvfrpALTHTHLDIPDYI----RKCLCQ 807
Cdd:cd14076   185 YAGR---KADIWSCGVILYAMLAGYLPFDDDPHNPngDNVPRLYR------------YICNTPLIFPEYVtpkaRDLLRR 249
                         250
                  ....*....|....*...
gi 161076872  808 CWDEDPEVRPDIRLVRMH 825
Cdd:cd14076   250 ILVPNPRKRIRLSAIMRH 267
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
598-816 8.97e-07

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


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 52.00  E-value: 8.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  598 RSIRKELKLMREVRHENIINFI----GASTDHGSVIIFTTYCARGSLEDVLANEDLhLDHMFISSLVSDILKGMIYLHD- 672
Cdd:cd14032    45 QRFKEEAEMLKGLQHPNIVRFYdfweSCAKGKRCIVLVTELMTSGTLKTYLKRFKV-MKPKVLRSWCRQILKGLLFLHTr 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  673 SEIISHGNLRSSNCLIDS-RWVCQISDFGLHELKagqeEPNKSELELKRALCMAPELLRDAYrpgrgSQKGDVYSFGILL 751
Cdd:cd14032   124 TPPIIHRDLKCDNIFITGpTGSVKIGDLGLATLK----RASFAKSVIGTPEFMAPEMYEEHY-----DESVDVYAFGMCM 194
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161076872  752 YEMIGRKGPWGDTAySKEEIIQFVKCpemlqhGVFRPALTHTH-LDIPDYIRKCLCQCWDEDPEVR 816
Cdd:cd14032   195 LEMATSEYPYSECQ-NAAQIYRKVTC------GIKPASFEKVTdPEIKEIIGECICKNKEERYEIK 253
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
584-825 9.56e-07

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


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 51.78  E-value: 9.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKK--SVD-ITRSIRKELKLMREVRHENIIN-FIGASTDHGSVIIFTTYCARGSLEDVlanedlHLDHMFISSL 659
Cdd:cd14164    28 VAIKIVDRRraSPDfVQKFLPRELSILRRVNHPNIVQmFECIEVANGRLYIVMEAAATDLLQKI------QEVHHIPKDL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  660 VSDILKGMI----YLHDSEIIsHGNLRSSNCLI--DSRWVcQISDFGLHelKAGQEEPNKSELELKRALCMAPE-LLRDA 732
Cdd:cd14164   102 ARDMFAQMVgavnYLHDMNIV-HRDLKCENILLsaDDRKI-KIADFGFA--RFVEDYPELSTTFCGSRAYTPPEvILGTP 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  733 YRPgrgsQKGDVYSFGILLYEMIGRKGPWGDTayskeeiiqFVKCPEMLQHGVFRPalthTHLDIPDYIRKCLCQCWDED 812
Cdd:cd14164   178 YDP----KKYDVWSLGVVLYVMVTGTMPFDET---------NVRRLRLQQRGVLYP----SGVALEEPCRALIRTLLQFN 240
                         250
                  ....*....|...
gi 161076872  813 PEVRPDIRLVRMH 825
Cdd:cd14164   241 PSTRPSIQQVAGN 253
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
581-784 1.11e-06

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


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 51.46  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVDITrSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHlDHMFISSLV 660
Cdd:cd14110    28 GQMLAAKIIPYKPEDKQ-LVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGPELLYNLAERNSY-SEAEVTDYL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFG-LHELKAGQEEPNKSELELkrALCMAPELLRDAyrpGRGS 739
Cdd:cd14110   106 WQILSAVDYLHSRRIL-HLDLRSENMIITEKNLLKIVDLGnAQPFNQGKVLMTDKKGDY--VETMAPELLEGQ---GAGP 179
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 161076872  740 QKgDVYSFGILLYEMIG------RKGPWGDTAYSKEEIIQFVKCPEMLQHG 784
Cdd:cd14110   180 QT-DIWAIGVTAFIMLSadypvsSDLNWERDRNIRKGKVQLSRCYAGLSGG 229
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
581-816 1.22e-06

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: 51.43  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLV 660
Cdd:cd14114    27 GNNFAAKFIMTPHESDKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFLSGGELFERIAAEHYKMSEAEVINYM 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWV--CQISDFGLhelkAGQEEPNKS-ELELKRALCMAPELlrdAYRPGR 737
Cdd:cd14114   107 RQVCEGLCHMHENNIV-HLDIKPENIMCTTKRSneVKLIDFGL----ATHLDPKESvKVTTGTAEFAAPEI---VEREPV 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  738 GSQKgDVYSFGILLYEMIGRKGPWGdtAYSKEEIIQFVK-CPEMLQHGVFrpalTHTHLDIPDYIRKCLCQcwdeDPEVR 816
Cdd:cd14114   179 GFYT-DMWAVGVLSYVLLSGLSPFA--GENDDETLRNVKsCDWNFDDSAF----SGISEEAKDFIRKLLLA----DPNKR 247
PBP1_mGluR_groupII cd06375
ligand binding domain of the group II metabotropic glutamate receptor; Ligand binding domain ...
65-264 1.28e-06

ligand binding domain of the group II metabotropic glutamate receptor; Ligand binding domain of the group II metabotropic glutamate receptor, a family that contains mGlu2R and mGlu3R, all of which inhibit adenylyl cyclase. The metabotropic glutamate receptor is a member of the family C of G-protein-coupled receptors that transduce extracellular signals into G-protein activation and ultimately into intracellular responses. The mGluRs are classified into three groups which comprise eight subtypes


Pssm-ID: 380598 [Multi-domain]  Cd Length: 462  Bit Score: 52.52  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   65 AIEDVNKNPNLLPGKKLAFKPVDIGHKMSAYRVKPL---RA-MTQMREAG------------------VTAFIGPDESCT 122
Cdd:cd06375    43 AIDRINRDPHLLPGVRLGVHILDTCSRDTYALEQSLefvRAsLTKVDDSEymcpddgsyaiqedsplpIAGVIGGSYSSV 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  123 T--EALLASAWNTPMLSFKCSDPIVSNKSTFHTFARTLAPASKVSKSVISLLNAFHWNKFSiVVSSKPIWGSDVARAIQE 200
Cdd:cd06375   123 SiqVANLLRLFQIPQISYASTSAKLSDKSRYDYFARTVPPDFYQAKAMAEILRFFNWTYVS-TVASEGDYGETGIEAFEQ 201
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161076872  201 LAEARNFTIShfkyISDYIPTTKTLSQIDKIIEETY--ATTRIYVFigehiamvdFVRGLQNRRLL 264
Cdd:cd06375   202 EARLRNICIA----TAEKVGRSADRKSFDGVIRELLqkPNARVVVL---------FTRSDDARELL 254
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
581-758 1.31e-06

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: 51.46  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVD----ITrSIRkELKLMREVRHENIINF--IGASTDHGSVIIFTTYcargsLEDVLanEDLhLDHM 654
Cdd:cd07843    30 GEIVALKKLKMEKEKegfpIT-SLR-EINILLKLQHPNIVTVkeVVVGSNLDKIYMVMEY-----VEHDL--KSL-METM 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  655 ---F----ISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkAGQ-EEPNKSELELKRALCM-A 725
Cdd:cd07843   100 kqpFlqseVKCLMLQLLSGVAHLHDNWIL-HRDLKTSNLLLNNRGILKICDFGL----AREyGSPLKPYTQLVVTLWYrA 174
                         170       180       190
                  ....*....|....*....|....*....|...
gi 161076872  726 PELLRDAyrpGRGSQKGDVYSFGILLYEMIGRK 758
Cdd:cd07843   175 PELLLGA---KEYSTAIDMWSVGCIFAELLTKK 204
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
583-817 1.34e-06

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: 51.93  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  583 IVAMKKIHK-KSVDITRSIRKELKLMREVRHE-NIINFIGASTDHGS-VIIFTTYCARGSLEDVL--------ANED--L 649
Cdd:cd14207    39 VVAVKMLKEgATASEYKALMTELKILIHIGHHlNVVNLLGACTKSGGpLMVIVEYCKYGNLSNYLkskrdffvTNKDtsL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  650 HLDHM------------------------FISS------------------------------LVS---DILKGMIYLHD 672
Cdd:cd14207   119 QEELIkekkeaeptggkkkrlesvtssesFASSgfqedkslsdveeeeedsgdfykrpltmedLISysfQVARGMEFLSS 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  673 SEIIsHGNLRSSNCLIDSRWVCQISDFGL-HELKAGQEEPNKSE--LELKralCMAPELLRDAYRpgrgSQKGDVYSFGI 749
Cdd:cd14207   199 RKCI-HRDLAARNILLSENNVVKICDFGLaRDIYKNPDYVRKGDarLPLK---WMAPESIFDKIY----STKSDVWSYGV 270
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161076872  750 LLYEMIGrkgpWGDTAYSKEEIIQ--FVKcpemLQHGvfrpalthTHLDIPDY----IRKCLCQCWDEDPEVRP 817
Cdd:cd14207   271 LLWEIFS----LGASPYPGVQIDEdfCSK----LKEG--------IRMRAPEFatseIYQIMLDCWQGDPNERP 328
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
602-826 1.36e-06

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: 51.14  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  602 KELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVL----ANEDLHLDHMFISSLVSDILKGMIYLHDSEIIs 677
Cdd:cd05087    46 EEAQPYRALQHTNLLQCLAQCAEVTPYLLVMEFCPLGDLKGYLrscrAAESMAPDPLTLQRMACEVACGLLHLHRNNFV- 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  678 HGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRALCMAPELLRDAYRP---GRGSQKGDVYSFGILLYEM 754
Cdd:cd05087   125 HSDLALRNCLLTADLTVKIGDYGLSHCKYKEDYFVTADQLWVPLRWIAPELVDEVHGNllvVDQTKQSNVWSLGVTIWEL 204
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161076872  755 IGRKG-PWGDtaYSKEEIIQFVKCPEMLQhgVFRPALthtHLDIPDYIRKCLCQCWDEdPEVRPDIRLVRMHL 826
Cdd:cd05087   205 FELGNqPYRH--YSDRQVLTYTVREQQLK--LPKPQL---KLSLAERWYEVMQFCWLQ-PEQRPTAEEVHLLL 269
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
627-820 1.50e-06

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: 51.18  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  627 SVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKA 706
Cdd:cd05109    82 TVQLVTQLMPYGCLLDYVRENKDRIGSQDLLNWCVQIAKGMSYLEEVRLV-HRDLAARNVLVKSPNHVKITDFGLARLLD 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  707 GQEEPNKSELELKRALCMAPE-LLRDayrpgRGSQKGDVYSFGILLYEMIgrkgPWGDTAYskeEIIQFVKCPEMLQHGV 785
Cdd:cd05109   161 IDETEYHADGGKVPIKWMALEsILHR-----RFTHQSDVWSYGVTVWELM----TFGAKPY---DGIPAREIPDLLEKGE 228
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 161076872  786 FRPALTHTHLDIpdYIrkCLCQCWDEDPEVRPDIR 820
Cdd:cd05109   229 RLPQPPICTIDV--YM--IMVKCWMIDSECRPRFR 259
PBP1_pheromone_receptor cd06365
Ligand-binding domain of the V2R pheromone receptor, a member of the family C receptors within ...
65-254 1.86e-06

Ligand-binding domain of the V2R pheromone receptor, a member of the family C receptors within the G-protein coupled receptor superfamily; Ligand-binding domain of the V2R pheromone receptor, a member of the family C receptors within the G-protein coupled receptor superfamily, which also includes the metabotropic glutamate receptor, the GABAb receptor, the calcium-sensing receptor (CaSR), the T1R taste receptor, and a small group of uncharacterized orphan receptors.


Pssm-ID: 380588 [Multi-domain]  Cd Length: 464  Bit Score: 51.88  E-value: 1.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   65 AIEDVNKNPNLLPGKKLAFKPVDIGHKMSAYRVKPLRAMTQMREA----------GVTAFIG-PDESCT-TEALLASAWN 132
Cdd:cd06365    45 AIEEINKNPDLLPNITLGFHIYDSCSSERLALESSLSILSGNSEPipnyscreqrKLVAFIGdLSSSTSvAMARILGLYK 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  133 TPMLSFKCSDPIVSNKSTFHTFARTLAPASKVSKSVISLLNAFHWNKFSIVVsskpiwgSDVARAIQELAEARNFTISH- 211
Cdd:cd06365   125 YPQISYGAFDPLLSDKVQFPSFYRTVPSDTSQSLAIVQLLKHFGWTWVGLII-------SDDDYGEQFSQDLKKEMEKNg 197
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 161076872  212 -----FKYISDYIPTTKTLSQIDKIIEEtyaTTRIYVFIGEHIAMVDF 254
Cdd:cd06365   198 icvafVEKIPTNSSLKRIIKYINQIIKS---SANVIIIYGDTDSLLEL 242
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
581-763 1.91e-06

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


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 50.91  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVDITRS---------IRKELKLMREV------RHENI---INFIGASTDHgsVIIFTTYCARGSLED 642
Cdd:cd14077    26 GEKCAIKIIPRASNAGLKKerekrlekeISRDIRTIREAalssllNHPHIcrlRDFLRTPNHY--YMLFEYVDGGQLLDY 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  643 VLANEDLHLDHMfiSSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAgqeepNKSELelkRAL 722
Cdd:cd14077   104 IISHGKLKEKQA--RKFARQIASALDYLHRNSIV-HRDLKIENILISKSGNIKIIDFGLSNLYD-----PRRLL---RTF 172
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 161076872  723 C-----MAPELLRDayRPGRGSQKgDVYSFGILLYEMIGRKGPWGD 763
Cdd:cd14077   173 CgslyfAAPELLQA--QPYTGPEV-DVWSFGVVLYVLVCGKVPFDD 215
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
581-752 2.11e-06

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: 50.46  E-value: 2.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSV--DITRsIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLED-VLANEDLHLDH--MF 655
Cdd:cd14078    28 GEKVAIKIMDKKALgdDLPR-VKTEIEALKNLSHQHICRLYHVIETDNKIFMVLEYCPGGELFDyIVAKDRLSEDEarVF 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  656 ISSLVSDIlkgmIYLHdSEIISHGNLRSSNCLIDSRWVCQISDFGL-HELKAGQeepnKSELElkrALC-----MAPELL 729
Cdd:cd14078   107 FRQIVSAV----AYVH-SQGYAHRDLKPENLLLDEDQNLKLIDFGLcAKPKGGM----DHHLE---TCCgspayAAPELI 174
                         170       180
                  ....*....|....*....|...
gi 161076872  730 RDayRPGRGSqKGDVYSFGILLY 752
Cdd:cd14078   175 QG--KPYIGS-EADVWSMGVLLY 194
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
602-830 2.42e-06

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: 50.41  E-value: 2.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  602 KELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVL---ANEDLHLDHMFISSLVSDILKGMIYLHDSEIIsH 678
Cdd:cd08228    51 KEIDLLKQLNHPNVIKYLDSFIEDNELNIVLELADAGDLSQMIkyfKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVM-H 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  679 GNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELelKRALCMAPELLRD-AYrpgrgSQKGDVYSFGILLYEMIGR 757
Cdd:cd08228   130 RDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLV--GTPYYMSPERIHEnGY-----NFKSDIWSLGCLLYEMAAL 202
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161076872  758 KGP-WGDtaysKEEIIQFVKCPEMLQHgvfrPALTHTHLDipDYIRKCLCQCWDEDPEVRPDIRLVRMHLKELQ 830
Cdd:cd08228   203 QSPfYGD----KMNLFSLCQKIEQCDY----PPLPTEHYS--EKLRELVSMCIYPDPDQRPDIGYVHQIAKQMH 266
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
600-825 2.62e-06

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


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 50.73  E-value: 2.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  600 IRKELKLMREVRHENIINFI----GASTDHGSVIIftTYCARGSLEDVLANEDLHLDHMFIssLVSDILKGMIYLHDSEI 675
Cdd:cd14199    72 VYQEIAILKKLDHPNVVKLVevldDPSEDHLYMVF--ELVKQGPVMEVPTLKPLSEDQARF--YFQDLIKGIEYLHYQKI 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  676 IsHGNLRSSNCLIDSRWVCQISDFGLhelkAGQEEPNKSELE--LKRALCMAPELLRDAYRPGRGsQKGDVYSFGILLYE 753
Cdd:cd14199   148 I-HRDVKPSNLLVGEDGHIKIADFGV----SNEFEGSDALLTntVGTPAFMAPETLSETRKIFSG-KALDVWAMGVTLYC 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  754 MIgrkgpWGDTAYSKEEII--------QFVKCPEmlQHgvfrpalththlDIPDYIRKCLCQCWDEDPEVRPDIRLVRMH 825
Cdd:cd14199   222 FV-----FGQCPFMDERILslhskiktQPLEFPD--QP------------DISDDLKDLLFRMLDKNPESRISVPEIKLH 282
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
598-817 2.69e-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: 50.75  E-value: 2.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  598 RSIRKELKLMREV-RHENIINFIGASTD-HGSVIIFTTYCARGSLEDVL------------------------------- 644
Cdd:cd05102    55 KALMSELKILIHIgNHLNVVNLLGACTKpNGPLMVIVEFCKYGNLSNFLrakregfspyrersprtrsqvrsmveavrad 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  645 --------------------ANEDLHLDHMFISSLVSDIL--------KGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQI 696
Cdd:cd05102   135 rrsrqgsdrvasftestsstNQPRQEVDDLWQSPLTMEDLicysfqvaRGMEFLASRKCI-HRDLAARNILLSENNVVKI 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  697 SDFGLheLKAGQEEPN-----KSELELKralCMAPELLRDAYRpgrgSQKGDVYSFGILLYEMIGrkgpWGDTAYSKEEI 771
Cdd:cd05102   214 CDFGL--ARDIYKDPDyvrkgSARLPLK---WMAPESIFDKVY----TTQSDVWSFGVLLWEIFS----LGASPYPGVQI 280
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 161076872  772 IQ-FVKcpeMLQHGvfrpalthTHLDIPDY----IRKCLCQCWDEDPEVRP 817
Cdd:cd05102   281 NEeFCQ---RLKDG--------TRMRAPEYatpeIYRIMLSCWHGDPKERP 320
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
596-817 3.31e-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: 50.25  E-value: 3.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  596 ITRSIRKELKL----------------MREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHL----DHMF 655
Cdd:cd05086    24 VARVVVKELKAsanpkeqddflqqgepYYILQHPNILQCVGQCVEAIPYLLVFEFCDLGDLKTYLANQQEKLrgdsQIML 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  656 ISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRALCMAPELL---RDA 732
Cdd:cd05086   104 LQRMACEIAAGLAHMHKHNFL-HSDLALRNCYLTSDLTVKVGDYGIGFSRYKEDYIETDDKKYAPLRWTAPELVtsfQDG 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  733 YRPGRGSQKGDVYSFGILLYEMIGRKG-PWGDTAySKEEIIQFVKCPEMlqhGVFRPalthtHLDIP--DYIRKCLCQCW 809
Cdd:cd05086   183 LLAAEQTKYSNIWSLGVTLWELFENAAqPYSDLS-DREVLNHVIKERQV---KLFKP-----HLEQPysDRWYEVLQFCW 253

                  ....*...
gi 161076872  810 dEDPEVRP 817
Cdd:cd05086   254 -LSPEKRP 260
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
638-818 3.42e-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: 50.78  E-value: 3.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  638 GSLEDVLANEDLHLDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL-HELKAGQEEPNKSE- 715
Cdd:cd05107   223 RTRRDTLINESPALSYMDLVGFSYQVANGMEFLASKNCV-HRDLAARNVLICEGKLVKICDFGLaRDIMRDSNYISKGSt 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  716 -LELKralCMAPE-LLRDAYrpgrgSQKGDVYSFGILLYEMIGRKG-PWGDTAYSKeeiiQFVKCpemLQHGVFRPALTH 792
Cdd:cd05107   302 fLPLK---WMAPEsIFNNLY-----TTLSDVWSFGILLWEIFTLGGtPYPELPMNE----QFYNA---IKRGYRMAKPAH 366
                         170       180
                  ....*....|....*....|....*.
gi 161076872  793 THLDIPDYIRKClcqcWDEDPEVRPD 818
Cdd:cd05107   367 ASDEIYEIMQKC----WEEKFEIRPD 388
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
565-755 3.48e-06

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: 49.86  E-value: 3.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  565 VGEP-NKRSFTNIALFRGN----IVAMKKIHKKSVD---ITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCA 636
Cdd:cd14117    10 IGRPlGKGKFGNVYLAREKqskfIVALKVLFKSQIEkegVEHQLRREIEIQSHLRHPNILRLYNYFHDRKRIYLILEYAP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  637 RGSLEDVLANEDlHLDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFG--LHelkagqeEPNKS 714
Cdd:cd14117    90 RGELYKELQKHG-RFDEQRTATFMEELADALHYCHEKKVI-HRDIKPENLLMGYKGELKIADFGwsVH-------APSLR 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 161076872  715 elelKRALCMAPELLRDAYRPGRG-SQKGDVYSFGILLYEMI 755
Cdd:cd14117   161 ----RRTMCGTLDYLPPEMIEGRThDEKVDLWCIGVLCYELL 198
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
578-825 4.42e-06

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


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 50.03  E-value: 4.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  578 LFRGNIVAMKKIHKKSVDITRSIR---KELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLAN---EDLHL 651
Cdd:cd08229    46 LLDGVPVALKKVQIFDLMDAKARAdciKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGDLSRMIKHfkkQKRLI 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  652 DHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELelKRALCMAPELLRD 731
Cdd:cd08229   126 PEKTVWKYFVQLCSALEHMHSRRVM-HRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLV--GTPYYMSPERIHE 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  732 -AYrpgrgSQKGDVYSFGILLYEMIGRKGP-WGDtaysKEEIIQFVKCPEMLQHgvfrPALTHTHLDipDYIRKCLCQCW 809
Cdd:cd08229   203 nGY-----NFKSDIWSLGCLLYEMAALQSPfYGD----KMNLYSLCKKIEQCDY----PPLPSDHYS--EELRQLVNMCI 267
                         250       260
                  ....*....|....*....|.
gi 161076872  810 DEDPEVRPDIRLV-----RMH 825
Cdd:cd08229   268 NPDPEKRPDITYVydvakRMH 288
PK_MADML cd14035
Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to ...
587-817 6.06e-06

Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. MADML has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. It may play an important role in embryonic eye development. The MADML 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: 270937 [Multi-domain]  Cd Length: 263  Bit Score: 49.15  E-value: 6.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  587 KKIHKKSVDITRSIRKELKLmreVRHENIINF----IGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSL--- 659
Cdd:cd14035    32 KKAFKAHEDKIKTMFENLTL---VDHPNIVKFhkywLDVKDNHARVVFITEYVSSGSLKQFLKKTKKNHKTMNARAWkrw 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  660 VSDILKGMIYLHDSEI-ISHGNLRSSNCLIDSRWVCQIS----DFGLHEL-KAGQEEPNKSELELKRALCMAPellrday 733
Cdd:cd14035   109 CTQILSALSYLHSCEPpIIHGNLTSDTIFIQHNGLIKIGsvwhRLFVNVLpEGGVRGPLRQEREELRNLHFFP------- 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  734 rPGRGSQKG----DVYSFGILLYEM-IGRKGPWGDTAYSKEEIIQFVKcpemlqhgvfrpalthtHLDIPDyIRKCLCQC 808
Cdd:cd14035   182 -PEYGSCEDgtavDIFSFGMCALEMaVLEIQANGDTRVSEEAIARARH-----------------SLEDPN-MREFILSC 242

                  ....*....
gi 161076872  809 WDEDPEVRP 817
Cdd:cd14035   243 LRHNPCKRP 251
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
581-773 6.33e-06

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


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 49.66  E-value: 6.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVD-ITRSIRKELKLMREVRHENIINF--IGASTDHGSVIIftTYCARGSLEDVLANEDLHLDHMfIS 657
Cdd:cd14168    35 GKLFAVKCIPKKALKgKESSIENEIAVLRKIKHENIVALedIYESPNHLYLVM--QLVSGGELFDRIVEKGFYTEKD-AS 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  658 SLVSDILKGMIYLHDSEIIsHGNLRSSNCLI---DSRWVCQISDFGLHELKAGQeepnkselELKRALC-----MAPELL 729
Cdd:cd14168   112 TLIRQVLDAVYYLHRMGIV-HRDLKPENLLYfsqDEESKIMISDFGLSKMEGKG--------DVMSTACgtpgyVAPEVL 182
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 161076872  730 rdAYRPgrGSQKGDVYSFGILLYEMIGRKGPWGDTAYSK--EEIIQ 773
Cdd:cd14168   183 --AQKP--YSKAVDCWSIGVIAYILLCGYPPFYDENDSKlfEQILK 224
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
580-761 6.40e-06

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: 49.24  E-value: 6.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  580 RGNIVAMKKIHKKSVDITRSIRkELKLMREVR-HENIINFIGASTDHGSVIIFTT-YCARGSLEDVLANEdLHLDHMFIS 657
Cdd:cd13987    17 SGTKMALKFVPKPSTKLKDFLR-EYNISLELSvHPHIIKTYDVAFETEDYYVFAQeYAPYGDLFSIIPPQ-VGLPEERVK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  658 SLVSDILKGMIYLHDSEIIsHGNLRSSNCLI---DSRWVcQISDFGLHElKAGQEEPNKSELelkrALCMAPELLrDAYR 734
Cdd:cd13987    95 RCAAQLASALDFMHSKNLV-HRDIKPENVLLfdkDCRRV-KLCDFGLTR-RVGSTVKRVSGT----IPYTAPEVC-EAKK 166
                         170       180
                  ....*....|....*....|....*....
gi 161076872  735 PGR--GSQKGDVYSFGILLYEMIGRKGPW 761
Cdd:cd13987   167 NEGfvVDPSIDVWAFGVLLFCCLTGNFPW 195
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
599-825 6.75e-06

Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. This subfamily is composed of NRBP1, also called MLF1-adaptor molecule (MADM), and MADML. NRBP1 was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking. MADML (for MADM-Like) has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. The NRBP1-like 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: 270886 [Multi-domain]  Cd Length: 256  Bit Score: 49.07  E-value: 6.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  599 SIRKELKLMRE-----------VRHENIINFIGASTD----HGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSL---V 660
Cdd:cd13984    30 SERKIFKAQEEkiravfdnliqLDHPNIVKFHRYWTDvqeeKARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKSWkrwC 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEI-ISHGNLRSSNCLIDSRwvcqisdfGLheLKAGQEEPN------KSELELKRAL-CMAPEllrda 732
Cdd:cd13984   110 TQILSALSYLHSCDPpIIHGNLTCDTIFIQHN--------GL--IKIGSVAPDaihnhvKTCREEHRNLhFFAPE----- 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  733 Y-RPGRGSQKGDVYSFGILLYEMIGRK-GPWGDTAYSKEEIIQfvKCPEMLQHGVFRpalththldipDYIRKCLcqcwD 810
Cdd:cd13984   175 YgYLEDVTTAVDIYSFGMCALEMAALEiQSNGEKVSANEEAII--RAIFSLEDPLQK-----------DFIRKCL----S 237
                         250
                  ....*....|....*
gi 161076872  811 EDPEVRPDIRLVRMH 825
Cdd:cd13984   238 VAPQDRPSARDLLFH 252
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
585-763 7.53e-06

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


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 49.07  E-value: 7.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  585 AMKKIHKKSvDITRSIRKELKLMREVRHENIINFIGASTDHGSVII----------FTTYCARGSLEDVLANEDLHLdhm 654
Cdd:cd14087    30 AIKMIETKC-RGREVCESELNVLRRVRHTNIIQLIEVFETKERVYMvmelatggelFDRIIAKGSFTERDATRVLQM--- 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  655 fisslvsdILKGMIYLHdSEIISHGNLRSSNCL-----IDSRWVcqISDFGLHELKAGQEEpnkselELKRALCMAPE-- 727
Cdd:cd14087   106 --------VLDGVKYLH-GLGITHRDLKPENLLyyhpgPDSKIM--ITDFGLASTRKKGPN------CLMKTTCGTPEyi 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 161076872  728 ----LLRDAYrpgrgSQKGDVYSFGILLYEMIGRKGPWGD 763
Cdd:cd14087   169 apeiLLRKPY-----TQSVDMWAVGVIAYILLSGTMPFDD 203
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
655-822 9.47e-06

putative serine/threonine kinase; Provisional


Pssm-ID: 165211 [Multi-domain]  Cd Length: 294  Bit Score: 48.79  E-value: 9.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  655 FISSLVSDILKGMIYLHdSEIISHGNLRSSNCLIDSRWVCQISDFGL--HELKAGQE-EPNKSELELKRALCMAPELlrD 731
Cdd:PHA02882  127 LIKNIMKDMLTTLEYIH-EHGISHGDIKPENIMVDGNNRGYIIDYGIasHFIIHGKHiEYSKEQKDLHRGTLYYAGL--D 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  732 AYRPGRGSQKGDVYSFGILLYEMIGRKGPWGDTAYSKeEIIQFVKCPEMLQHGVFRPALTHTHLDIPDYIRKCLCQCWDE 811
Cdd:PHA02882  204 AHNGACVTRRGDLESLGYCMLKWAGIKLPWKGFGHNG-NLIHAAKCDFIKRLHEGKIKIKNANKFIYDFIECVTKLSYEE 282
                         170
                  ....*....|.
gi 161076872  812 DPEVRPDIRLV 822
Cdd:PHA02882  283 KPDYDALIKIF 293
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
583-792 1.12e-05

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: 48.45  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  583 IVAMKKIH--KKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEdVLANEDLHLDHMFISSLV 660
Cdd:cd07848    28 IVAIKKFKdsEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVEKNMLE-LLEEMPNGVPPEKVRSYI 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSELELKRALcMAPELLRDAYRpgrgSQ 740
Cdd:cd07848   107 YQLIKAIHWCHKNDIV-HRDIKPENLLISHNDVLKLCDFGFARNLSEGSNANYTEYVATRWY-RSPELLLGAPY----GK 180
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161076872  741 KGDVYSFGILLYEMI-GRKGPWGDTAYSKEEIIQFVKCP---EMLQ--------HGVFRPALTH 792
Cdd:cd07848   181 AVDMWSVGCILGELSdGQPLFPGESEIDQLFTIQKVLGPlpaEQMKlfysnprfHGLRFPAVNH 244
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
572-755 1.43e-05

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: 48.55  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  572 SFTNIALFR-------GNIVAMKKIHKKSVDITRSIRK--ELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLED 642
Cdd:cd05582     7 SFGKVFLVRkitgpdaGTLYAMKVLKKATLKVRDRVRTkmERDILADVNHPFIVKLHYAFQTEGKLYLILDFLRGGDLFT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  643 VLANEdlhldHMFISSLV----SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHelKAGQEEPNKSElel 718
Cdd:cd05582    87 RLSKE-----VMFTEEDVkfylAELALALDHLHSLGII-YRDLKPENILLDEDGHIKLTDFGLS--KESIDHEKKAY--- 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 161076872  719 krALC-----MAPELLRdayRPGRgSQKGDVYSFGILLYEMI 755
Cdd:cd05582   156 --SFCgtveyMAPEVVN---RRGH-TQSADWWSFGVLMFEML 191
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
588-781 1.65e-05

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: 47.91  E-value: 1.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  588 KIHKKSVDITRSIRkELKLMREVRHENIINFIGASTDHGSVIIFTTYCArgslEDVL---ANEDLHLDHMfISSLVSDIL 664
Cdd:cd14112    36 KIFEVSDEASEAVR-EFESLRTLQHENVQRLIAAFKPSNFAYLVMEKLQ----EDVFtrfSSNDYYSEEQ-VATTVRQIL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  665 KGMIYLHdSEIISHGNLRSSNCLIDSR--WVCQISDFGLHElKAGQEEPNKSELELKRAlcmAPELLRDayRPGRGSQKg 742
Cdd:cd14112   110 DALHYLH-FKGIAHLDVQPDNIMFQSVrsWQVKLVDFGRAQ-KVSKLGKVPVDGDTDWA---SPEFHNP--ETPITVQS- 181
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 161076872  743 DVYSFGILLYEMIGRKGPW---GDTAYSKEEIIQFVKC-PEML 781
Cdd:cd14112   182 DIWGLGVLTFCLLSGFHPFtseYDDEEETKENVIFVKCrPNLI 224
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
585-817 1.72e-05

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: 47.66  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  585 AMKKIH-KKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANE--DLHLDHMFISSLVS 661
Cdd:cd08219    29 AMKEIRlPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYCDGGDLMQKIKLQrgKLFPEDTILQWFVQ 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  662 DILkGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAgqeEPNKSELE-LKRALCMAPELLRD-AYrpgrgS 739
Cdd:cd08219   109 MCL-GVQHIHEKRVL-HRDIKSKNIFLTQNGKVKLGDFGSARLLT---SPGAYACTyVGTPYYVPPEIWENmPY-----N 178
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161076872  740 QKGDVYSFGILLYEMIGRKGPWGDTAYsKEEIIQFVKcpemlqhGVFRPALTHTHLDIPDYIRkclcQCWDEDPEVRP 817
Cdd:cd08219   179 NKSDIWSLGCILYELCTLKHPFQANSW-KNLILKVCQ-------GSYKPLPSHYSYELRSLIK----QMFKRNPRSRP 244
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
592-775 1.77e-05

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


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 47.81  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  592 KSVDITRSIRKELK-LMREV------RHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANedlHLDHMFISSLVS--- 661
Cdd:cd08221    31 KEVNLSRLSEKERRdALNEIdilsllNHDNIITYYNHFLDGESLFIEMEYCNGGNLHDKIAQ---QKNQLFPEEVVLwyl 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  662 -DILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHelKAGQEEPNKSELELKRALCMAPELLR-DAYrpgrgS 739
Cdd:cd08221   108 yQIVSAVSHIHKAGIL-HRDIKTLNIFLTKADLVKLGDFGIS--KVLDSESSMAESIVGTPYYMSPELVQgVKY-----N 179
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 161076872  740 QKGDVYSFGILLYEMIGRK-----------------GPWGD--TAYSkEEIIQFV 775
Cdd:cd08221   180 FKSDIWAVGCVLYELLTLKrtfdatnplrlavkivqGEYEDidEQYS-EEIIQLV 233
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
573-700 1.88e-05

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: 45.51  E-value: 1.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  573 FTNIALFRGNIVAMKKIHKKSVDITRSIRKELKLMREVR-HE-NIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLh 650
Cdd:cd13968    10 FWAEGECTTIGVAVKIGDDVNNEEGEDLESEMDILRRLKgLElNIPKVLVTEDVDGPNILLMELVKGGTLIAYTQEEEL- 88
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 161076872  651 lDHMFISSLVSDILKGMIYLHdSEIISHGNLRSSNCLIDSRWVCQISDFG 700
Cdd:cd13968    89 -DEKDVESIMYQLAECMRLLH-SFHLIHRDLNNDNILLSEDGNVKLIDFG 136
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
658-835 2.04e-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: 48.48  E-value: 2.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  658 SLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL-HELKAGQEEPNKSELELKRALcMAPELLRDAYRpg 736
Cdd:cd05105   241 SFTYQVARGMEFLASKNCV-HRDLAARNVLLAQGKIVKICDFGLaRDIMHDSNYVSKGSTFLPVKW-MAPESIFDNLY-- 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  737 rgSQKGDVYSFGILLYEMIGrkgpWGDTAYskeeiiqfvkcPEMLQHGVFRPALTHTH-LDIPDY----IRKCLCQCWDE 811
Cdd:cd05105   317 --TTLSDVWSYGILLWEIFS----LGGTPY-----------PGMIVDSTFYNKIKSGYrMAKPDHatqeVYDIMVKCWNS 379
                         170       180
                  ....*....|....*....|....
gi 161076872  812 DPEVRPDIRlvrmHLKELQAGLKP 835
Cdd:cd05105   380 EPEKRPSFL----HLSDIVESLLP 399
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
661-788 2.22e-05

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: 47.77  E-value: 2.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLheLKAGQEEPNKSelelkRALC-----MAPELLrdAYRP 735
Cdd:cd05587   104 AEIAVGLFFLHSKGII-YRDLKLDNVMLDAEGHIKIADFGM--CKEGIFGGKTT-----RTFCgtpdyIAPEII--AYQP 173
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 161076872  736 GRGSQkgDVYSFGILLYEMIGRKGPW-GDtaySKEEIIQFVkcpemLQHGVFRP 788
Cdd:cd05587   174 YGKSV--DWWAYGVLLYEMLAGQPPFdGE---DEDELFQSI-----MEHNVSYP 217
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
595-825 2.42e-05

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


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 47.70  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  595 DITRSIRKELKLMREVR-HENIINFIGA-----STDHGSVIIFTTYCARGSLEDV---LANEDLHLDHMFISSLVSDILK 665
Cdd:cd06638    56 DIDEEIEAEYNILKALSdHPNVVKFYGMyykkdVKNGDQLWLVLELCNGGSVTDLvkgFLKRGERMEEPIIAYILHEALM 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  666 GMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLH-ELKAGQEEPNKSeleLKRALCMAPEL------LRDAYrpgrg 738
Cdd:cd06638   136 GLQHLHVNKTI-HRDVKGNNILLTTEGGVKLVDFGVSaQLTSTRLRRNTS---VGTPFWMAPEViaceqqLDSTY----- 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  739 SQKGDVYSFGILLYEMIGRKGPWGDTayskEEIIQFVKCPEMLQHGVFRPALTHThlDIPDYIRKCLCQcwdeDPEVRPD 818
Cdd:cd06638   207 DARCDVWSLGITAIELGDGDPPLADL----HPMRALFKIPRNPPPTLHQPELWSN--EFNDFIRKCLTK----DYEKRPT 276

                  ....*..
gi 161076872  819 IRLVRMH 825
Cdd:cd06638   277 VSDLLQH 283
HNOBA pfam07701
Heme NO binding associated; The HNOBA domain is found associated with the HNOB domain and ...
857-886 3.04e-05

Heme NO binding associated; The HNOBA domain is found associated with the HNOB domain and pfam00211 in soluble cyclases and signalling proteins. The HNOB domain is predicted to function as a heme-dependent sensor for gaseous ligands, and transduce diverse downstream signals, in both bacteria and animals.


Pssm-ID: 462234  Cd Length: 214  Bit Score: 46.41  E-value: 3.04e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 161076872   857 QERTNLLYEEKKKTDMLLYQMLPRPVAELL 886
Cdd:pfam07701  185 EESMRELEEEKKKTDELLYSMLPKSVADRL 214
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
581-758 3.68e-05

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: 47.20  E-value: 3.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHK--KSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYC-----ARGSLEDVLAnedLHLDH 653
Cdd:cd07879    40 GEKVAIKKLSRpfQSEIFAKRAYRELTLLKHMQHENVIGLLDVFTSAVSGDEFQDFYlvmpyMQTDLQKIMG---HPLSE 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  654 MFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHElKAGQEEPNKSELELKRalcmAPELLRDAY 733
Cdd:cd07879   117 DKVQYLVYQMLCGLKYIHSAGII-HRDLKPGNLAVNEDCELKILDFGLAR-HADAEMTGYVVTRWYR----APEVILNWM 190
                         170       180
                  ....*....|....*....|....*
gi 161076872  734 RPgrgSQKGDVYSFGILLYEMIGRK 758
Cdd:cd07879   191 HY---NQTVDIWSVGCIMAEMLTGK 212
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
662-825 4.47e-05

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


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 46.58  E-value: 4.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  662 DILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGqeepnkSELELKRAL----CMAPELLrdayRPGR 737
Cdd:cd14118   123 DIVLGIEYLHYQKII-HRDIKPSNLLLGDDGHVKIADFGVSNEFEG------DDALLSSTAgtpaFMAPEAL----SESR 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  738 GSQKG---DVYSFGILLYEMIgrkgpWGDTAYSKEEIIQF--------VKCPEmlqhgvfRPALTHthlDIPDYIRKCLc 806
Cdd:cd14118   192 KKFSGkalDIWAMGVTLYCFV-----FGRCPFEDDHILGLhekiktdpVVFPD-------DPVVSE---QLKDLILRML- 255
                         170
                  ....*....|....*....
gi 161076872  807 qcwDEDPEVRPDIRLVRMH 825
Cdd:cd14118   256 ---DKNPSERITLPEIKEH 271
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
602-820 4.89e-05

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: 46.98  E-value: 4.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  602 KELKLMREVRHENIINFIGA-STDHGSVIIFTTYCARGSLEDVLANEDLhLDHMFISSLVSDILKGMIYLHD-SEIISHG 679
Cdd:cd14041    59 REYRIHKELDHPRIVKLYDYfSLDTDSFCTVLEYCEGNDLDFYLKQHKL-MSEKEARSIIMQIVNALKYLNEiKPPIIHY 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  680 NLRSSNCLIDSRWVC---QISDFGLHELKAGQEEPNKSELELKRALC-----MAPELLRDAYRPGRGSQKGDVYSFGILL 751
Cdd:cd14041   138 DLKPGNILLVNGTACgeiKITDFGLSKIMDDDSYNSVDGMELTSQGAgtywyLPPECFVVGKEPPKISNKVDVWSVGVIF 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  752 YEMIGRKGPWGDTAySKEEIIQ---FVKCPEmlqhgVFRPALTHTHLDIPDYIRKCLC---------QCWDEDPEVRPDI 819
Cdd:cd14041   218 YQCLYGRKPFGHNQ-SQQDILQentILKATE-----VQFPPKPVVTPEAKAFIRRCLAyrkedridvQQLACDPYLLPHI 291

                  .
gi 161076872  820 R 820
Cdd:cd14041   292 R 292
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
597-763 7.02e-05

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: 46.27  E-value: 7.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  597 TRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHM--FISSlvsDILKGMIYLHDSE 674
Cdd:cd05612    45 EQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLMEYVPGGELFSYLRNSGRFSNSTglFYAS---EIVCALEYLHSKE 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  675 IIsHGNLRSSNCLIDSRWVCQISDFGLhelkagqeepNKSELELKRALCMAPELLRDAYRPGRGSQKG-DVYSFGILLYE 753
Cdd:cd05612   122 IV-YRDLKPENILLDKEGHIKLTDFGF----------AKKLRDRTWTLCGTPEYLAPEVIQSKGHNKAvDWWALGILIYE 190
                         170
                  ....*....|
gi 161076872  754 MIGRKGPWGD 763
Cdd:cd05612   191 MLVGYPPFFD 200
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
661-788 7.27e-05

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: 46.15  E-value: 7.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHElkagqeePNKSELELKRALC-----MAPELLrdAYRP 735
Cdd:cd05616   108 AEIAIGLFFLQSKGII-YRDLKLDNVMLDSEGHIKIADFGMCK-------ENIWDGVTTKTFCgtpdyIAPEII--AYQP 177
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 161076872  736 GRGSQkgDVYSFGILLYEMIGRKGPWgdTAYSKEEIIQfvkcpEMLQHGVFRP 788
Cdd:cd05616   178 YGKSV--DWWAFGVLLYEMLAGQAPF--EGEDEDELFQ-----SIMEHNVAYP 221
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
581-825 7.38e-05

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


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 45.92  E-value: 7.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIhKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLAN-----EDlhLDHMF 655
Cdd:cd14662    25 KELVAVKYI-ERGLKIDENVQREIINHRSLRHPNIIRFKEVVLTPTHLAIVMEYAAGGELFERICNagrfsED--EARYF 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  656 ISSLVSdilkGMIYLHDSEiISHGNLRSSNCLIDSRWV--CQISDFGLHELKAGQEEPNKSeleLKRALCMAPELL-RDA 732
Cdd:cd14662   102 FQQLIS----GVSYCHSMQ-ICHRDLKLENTLLDGSPAprLKICDFGYSKSSVLHSQPKST---VGTPAYIAPEVLsRKE 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  733 YrpgrGSQKGDVYSFGILLYEMIGRKGPWGDTAYSKEeiiqfvkcpemlqhgvFRPALTH---THLDIPDYI------RK 803
Cdd:cd14662   174 Y----DGKVADVWSCGVTLYVMLVGAYPFEDPDDPKN----------------FRKTIQRimsVQYKIPDYVrvsqdcRH 233
                         250       260
                  ....*....|....*....|..
gi 161076872  804 CLCQCWDEDPEVRPDIRLVRMH 825
Cdd:cd14662   234 LLSRIFVANPAKRITIPEIKNH 255
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
584-770 8.77e-05

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: 45.72  E-value: 8.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKsVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMfISSLVSDI 663
Cdd:cd14115    21 VAVKFVSKK-MKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLLDYLMNHDELMEEK-VAFYIRDI 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  664 LKGMIYLHDSEIiSHGNLRSSNCLIDSRW------------VCQIS-DFGLHELKAGQEepnkselelkralCMAPELLR 730
Cdd:cd14115    99 MEALQYLHNCRV-AHLDIKPENLLIDLRIpvprvklidledAVQISgHRHVHHLLGNPE-------------FAAPEVIQ 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 161076872  731 DAyrpgRGSQKGDVYSFGILLYEMIGRKGPWGDTaySKEE 770
Cdd:cd14115   165 GT----PVSLATDIWSIGVLTYVMLSGVSPFLDE--SKEE 198
PBP1_iGluR_NMDA_NR1 cd06379
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an ...
65-244 9.03e-05

N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an essential channel-forming subunit of the NMDA receptor; N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the NR1, an essential channel-forming subunit of the NMDA receptor. The ionotropic N-methyl-D-asparate (NMDA) subtype of glutamate receptor serves critical functions in neuronal development, functioning, and degeneration in the mammalian central nervous system. The functional NMDA receptor is a heterotetramer ccomposed of two NR1 and two NR2 (A, B, C, and D) or of NR3 (A and B) subunits. The receptor controls a cation channel that is highly permeable to monovalent ions and calcium and exhibits voltage-dependent inhibition by magnesium. Dual agonists, glutamate and glycine, are required for efficient activation of the NMDA receptor. When co-expressed with NR1, the NR3 subunits form receptors that are activated by glycine alone and therefore can be classified as excitatory glycine receptors. NR1/NR3 receptors are calcium-impermeable and unaffected by ligands acting at the NR2 glutamate-binding site


Pssm-ID: 380602  Cd Length: 364  Bit Score: 46.18  E-value: 9.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   65 AIEDVNKNPNLLPGKKLAFKPvdIGHKMSAYRVKpLRAMTQMREAGVTAFI------GPDESCTTEALLASAWNTPMLSF 138
Cdd:cd06379    21 AVNEVNAHSHLPRKITLNATS--ITLDPNPIRTA-LSVCEDLIASQVYAVIvshpptPSDLSPTSVSYTAGFYRIPVIGI 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  139 KCSDPIVSNKSTFHTFARTLAPASKVSKSVISLLNAFHWNKFSIVVSSkpiwgSDVARAIQE----LAEARNFTIShfKY 214
Cdd:cd06379    98 SARDSAFSDKNIHVSFLRTVPPYSHQADVWAEMLRHFEWKQVIVIHSD-----DQDGRALLGrletLAETKDIKIE--KV 170
                         170       180       190
                  ....*....|....*....|....*....|
gi 161076872  215 IsDYIPTTKTLSQIDKIIEEtyATTRIYVF 244
Cdd:cd06379   171 I-EFEPGEKNFTSLLEEMKE--LQSRVILL 197
PBP1_GABAb_receptor_plant cd19990
periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close ...
64-384 1.07e-04

periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close homologs in other plants; This group includes the ligand-binding domain of Arabidopsis thaliana glutamate receptors, which have sequence similarity with animal ionotropic glutamate receptor and its close homologs in other plants. The ligand-binding domain of GABAb receptors are metabotropic transmembrane receptors for gamma-aminobutyric acid (GABA). GABA is the major inhibitory neurotransmitter in the mammalian CNS and, like glutamate and other transmitters, acts via both ligand gated ion channels (GABAa receptors) and G-protein coupled receptors (GABAb receptor or GABAbR). GABAa receptors are members of the ionotropic receptor superfamily which includes alpha-adrenergic and glycine receptors. The GABAb receptor is a member of a receptor superfamily which includes the mGlu receptors. The GABAb receptor is coupled to G alpha-i proteins, and activation causes a decrease in calcium, an increase in potassium membrane conductance, and inhibition of cAMP formation. The response is thus inhibitory and leads to hyperpolarization and decreased neurotransmitter release, for example.


Pssm-ID: 380645 [Multi-domain]  Cd Length: 373  Bit Score: 46.07  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   64 LAIEDVNKNPNLLPGKklafkpVDIGHKMSayRVKPLRAMTQ----MREAGVTAFIGPDESCTTE--ALLASAWNTPMLS 137
Cdd:cd19990    22 MAVSDFNSDSSSYGTK------LVLHVRDS--KGDPLQAASAaldlIKNKKVEAIIGPQTSEEASfvAELGNKAQVPIIS 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  138 FKCSDPIVSN-KSTFhtFARTLAPASKVSKSVISLLNAFHWNKFSIVVSSKPIWGSdvarAIQELAEA---RNFTISHFK 213
Cdd:cd19990    94 FSATSPTLSSlRWPF--FIRMTHNDSSQMKAIAAIVQSYGWRRVVLIYEDDDYGSG----IIPYLSDAlqeVGSRIEYRV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  214 YISDYIPTTKTLSQIDKIIEEtyaTTRIYVFigeHIAMVDFVRGLQNRRLLE--SGDYIVVsVDDEIydsnrrvnimeRN 291
Cdd:cd19990   168 ALPPSSPEDSIEEELIKLKSM---QSRVFVV---HMSSLLASRLFQEAKKLGmmEKGYVWI-VTDGI-----------TN 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  292 YLDpyirkekskSLDKISFRS---VIKISMTYPQNPHIRDICSKikdyaRKTPFLVPYHQRVFDNISvpIYGLHLYDSVM 368
Cdd:cd19990   230 LLD---------SLDSSTISSmqgVIGIKTYIPESSEFQDFKAR-----FRKKFRSEYPEEENAEPN--IYALRAYDAIW 293
                         330
                  ....*....|....*.
gi 161076872  369 IYVRAITEVLRLGGDI 384
Cdd:cd19990   294 ALAHAVEKLNSSGGNI 309
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
633-822 1.09e-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: 46.05  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  633 TYCARGSLEDVLANEDLHLDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL---------HE 703
Cdd:cd05104   193 SYVDQDVTSEILEEDELALDTEDLLSFSYQVAKGMEFLASKNCI-HRDLAARNILLTHGRITKICDFGLardirndsnYV 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  704 LKAGQEEPNKselelkralCMAPELLRDAYRpgrgSQKGDVYSFGILLYEMIGrkgpWGDTAYSKEEI-IQFVKcpeMLQ 782
Cdd:cd05104   272 VKGNARLPVK---------WMAPESIFECVY----TFESDVWSYGILLWEIFS----LGSSPYPGMPVdSKFYK---MIK 331
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 161076872  783 HGVFRPALTHTHLDIPDYIRkclcQCWDEDPEVRPDIRLV 822
Cdd:cd05104   332 EGYRMDSPEFAPSEMYDIMR----SCWDADPLKRPTFKQI 367
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
584-757 1.22e-04

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: 45.54  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDITRSIRKELKLMREVRHENIIN-----FIGASTDHGSVIIFTTY--------CARGSLEDVLANEDLH 650
Cdd:cd07854    33 VAVKKIVLTDPQSVKHALREIKIIRRLDHDNIVKvyevlGPSGSDLTEDVGSLTELnsvyivqeYMETDLANVLEQGPLS 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  651 LDHmfISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSR-WVCQISDFGLHELkAGQEEPNKSELE--LKRALCMAPE 727
Cdd:cd07854   113 EEH--ARLFMYQLLRGLKYIHSANVL-HRDLKPANVFINTEdLVLKIGDFGLARI-VDPHYSHKGYLSegLVTKWYRSPR 188
                         170       180       190
                  ....*....|....*....|....*....|.
gi 161076872  728 LLrdaYRPGRGSQKGDVYSFGILLYEM-IGR 757
Cdd:cd07854   189 LL---LSPNNYTKAIDMWAAGCIFAEMlTGK 216
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
581-800 1.24e-04

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: 45.19  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIH--KKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARG--SLEDVLANEDLHLDhmFI 656
Cdd:cd07860    25 GEVVALKKIRldTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQDlkKFMDASALTGIPLP--LI 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  657 SSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLheLKAGQEEPNKSELELKRALCMAPELLRDA--Yr 734
Cdd:cd07860   103 KSYLFQLLQGLAFCHSHRVL-HRDLKPQNLLINTEGAIKLADFGL--ARAFGVPVRTYTHEVVTLWYRAPEILLGCkyY- 178
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161076872  735 pgrgSQKGDVYSFGILLYEMIGRKGPW-GDTayskeEIIQFVKCPEML--QHGVFRPALThthlDIPDY 800
Cdd:cd07860   179 ----STAVDIWSLGCIFAEMVTRRALFpGDS-----EIDQLFRIFRTLgtPDEVVWPGVT----SMPDY 234
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
602-780 1.75e-04

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: 44.61  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  602 KELKLMREVRHENIINFIGA--ST--DHGSVIIFTTYCARGSLEDVLAN-EDLHLDhmFISSLVSDILKGMIYLHD-SEI 675
Cdd:cd14033    49 EEVEMLKGLQHPNIVRFYDSwkSTvrGHKCIILVTELMTSGTLKTYLKRfREMKLK--LLQRWSRQILKGLHFLHSrCPP 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  676 ISHGNLRSSNCLIDS-RWVCQISDFGLHELKAGQEEpnKSELELKRAlcMAPELLRDAYrpgrgSQKGDVYSFGILLYEM 754
Cdd:cd14033   127 ILHRDLKCDNIFITGpTGSVKIGDLGLATLKRASFA--KSVIGTPEF--MAPEMYEEKY-----DEAVDVYAFGMCILEM 197
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 161076872  755 IGRKGPWGD-----------TAYSKEEIIQFVKCPEM 780
Cdd:cd14033   198 ATSEYPYSEcqnaaqiyrkvTSGIKPDSFYKVKVPEL 234
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
663-754 1.76e-04

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: 44.90  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  663 ILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLheLKAGQEEPNKSelelkRALC-----MAPE-LLRDAYrpG 736
Cdd:cd05570   105 ICLALQFLHERGII-YRDLKLDNVLLDAEGHIKIADFGM--CKEGIWGGNTT-----STFCgtpdyIAPEiLREQDY--G 174
                          90
                  ....*....|....*...
gi 161076872  737 RGSqkgDVYSFGILLYEM 754
Cdd:cd05570   175 FSV---DWWALGVLLYEM 189
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
580-763 1.79e-04

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 45.19  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  580 RGNIVAMKKIHK------KSVDitrSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVL------ANE 647
Cdd:PTZ00263   42 TGEYYAIKCLKKreilkmKQVQ---HVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEFVVGGELFTHLrkagrfPND 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  648 DLHLDHmfisslvSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkagqeepNKSELELKRALCMAPE 727
Cdd:PTZ00263  119 VAKFYH-------AELVLAFEYLHSKDII-YRDLKPENLLLDNKGHVKVTDFGF----------AKKVPDRTFTLCGTPE 180
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 161076872  728 LLRDAYRPGRGSQKG-DVYSFGILLYEMIGRKGPWGD 763
Cdd:PTZ00263  181 YLAPEVIQSKGHGKAvDWWTMGVLLYEFIAGYPPFFD 217
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
660-837 1.81e-04

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: 45.07  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  660 VSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEepNKSElelkrALC-----MAPELLRDAyr 734
Cdd:cd05592   102 GAEIICGLQFLHSRGII-YRDLKLDNVLLDREGHIKIADFGMCKENIYGE--NKAS-----TFCgtpdyIAPEILKGQ-- 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  735 pgRGSQKGDVYSFGILLYEMIGRKGPWgdtayskeeiiqfvkcpemlqHGVFRPALTHTHL-DIPDYIR-------KCLC 806
Cdd:cd05592   172 --KYNQSVDWWSFGVLLYEMLIGQSPF---------------------HGEDEDELFWSICnDTPHYPRwltkeaaSCLS 228
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 161076872  807 QCWDEDPEVR--------PDIR---------LVRMHLKELQAGLKPNI 837
Cdd:cd05592   229 LLLERNPEKRlgvpecpaGDIRdhpffktidWDKLERREIDPPFKPKV 276
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
661-760 1.87e-04

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: 44.65  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHdSEIISHGNLRSSNCLIDSRWVCQISDFGLH-ELKAGqeepnkselELKRALC-----MAPELLRDAyr 734
Cdd:cd05605   109 AEITCGLEHLH-SERIVYRDLKPENILLDDHGHVRISDLGLAvEIPEG---------ETIRGRVgtvgyMAPEVVKNE-- 176
                          90       100
                  ....*....|....*....|....*.
gi 161076872  735 pgRGSQKGDVYSFGILLYEMIGRKGP 760
Cdd:cd05605   177 --RYTFSPDWWGLGCLIYEMIEGQAP 200
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
581-765 2.76e-04

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


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 44.25  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKS-VDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMfISSL 659
Cdd:cd14088    26 GKLYTCKKFLKRDgRKVRKAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLELATGREVFDWILDQGYYSERD-TSNV 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  660 VSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQ---ISDFGLHELKAGQ-EEPNKSELELkralcmAPELL-RDAY- 733
Cdd:cd14088   105 IRQVLEAVAYLHSLKIV-HRNLKLENLVYYNRLKNSkivISDFHLAKLENGLiKEPCGTPEYL------APEVVgRQRYg 177
                         170       180       190
                  ....*....|....*....|....*....|..
gi 161076872  734 RPgrgsqkGDVYSFGILLYEMIGRKGPWGDTA 765
Cdd:cd14088   178 RP------VDCWAIGVIMYILLSGNPPFYDEA 203
PBP1_mGluR_groupIII cd06376
ligand-binding domain of the group III metabotropic glutamate receptor; Ligand-binding domain ...
65-247 2.93e-04

ligand-binding domain of the group III metabotropic glutamate receptor; Ligand-binding domain of the group III metabotropic glutamate receptor, a family which contains mGlu4R, mGluR6R, mGluR7, and mGluR8; all of which inhibit adenylyl cyclase. The metabotropic glutamate receptor is a member of the family C of G-protein-coupled receptors that transduce extracellular signals into G-protein activation and ultimately into intracellular responses. The mGluRs are classified into three groups which comprise eight subtypes.


Pssm-ID: 380599 [Multi-domain]  Cd Length: 467  Bit Score: 44.79  E-value: 2.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   65 AIEDVNKNPNLLPG-------------------KKLAFKPVDIGHKMSAYRVKPLRAMTQMREAGVTAFIGPDEScTTEA 125
Cdd:cd06376    43 ALDQINSDPDLLPNvtlgarildtcsrdtyaleQSLTFVQALIQKDTSDVRCTNGDPPVFVKPEKVVGVIGASAS-SVSI 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  126 LLASA---WNTPMLSFKCSDPIVSNKSTFHTFARTLAPASKVSKSVISLLNAFHWNKFSIVVSSKPIWGSDVARAIQELA 202
Cdd:cd06376   122 MVANIlrlFQIPQISYASTAPELSDDRRYDFFSRVVPPDSFQAQAMVDIVKALGWNYVSTLASEGNYGEKGVESFVQISR 201
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 161076872  203 EARNFTISHfkyiSDYIPTTKTLSQIDKIIE---ETYATTRIYVFIGE 247
Cdd:cd06376   202 EAGGVCIAQ----SEKIPRERRTGDFDKIIKrllETPNARAVVIFADE 245
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
600-775 2.97e-04

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: 44.08  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  600 IRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSDILKGMIYLHdSEIISHG 679
Cdd:cd14104    43 VKKEISILNIARHRNILRLHESFESHEELVMIFEFISGVDIFERITTARFELNEREIVSYVRQVCEALEFLH-SKNIGHF 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  680 NLRSSNCLIDSR--WVCQISDFG-LHELKAGQeepnKSELELKRALCMAPELLRDAYRpgrgSQKGDVYSFGILLYEMIG 756
Cdd:cd14104   122 DIRPENIIYCTRrgSYIKIIEFGqSRQLKPGD----KFRLQYTSAEFYAPEVHQHESV----STATDMWSLGCLVYVLLS 193
                         170
                  ....*....|....*....
gi 161076872  757 RKGPWgdTAYSKEEIIQFV 775
Cdd:cd14104   194 GINPF--EAETNQQTIENI 210
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
581-763 3.18e-04

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: 43.84  E-value: 3.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLV 660
Cdd:cd14191    27 KKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMVSGGELFERIIDEDFELTERECIKYM 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEIIsHGNLRSSN--CLIDSRWVCQISDFGLHELkagQEEPNKSELELKRALCMAPELLRdaYRPgrG 738
Cdd:cd14191   107 RQISEGVEYIHKQGIV-HLDLKPENimCVNKTGTKIKLIDFGLARR---LENAGSLKVLFGTPEFVAPEVIN--YEP--I 178
                         170       180
                  ....*....|....*....|....*.
gi 161076872  739 SQKGDVYSFGILLYEMIGRKGPW-GD 763
Cdd:cd14191   179 GYATDMWSIGVICYILVSGLSPFmGD 204
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
669-754 3.70e-04

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: 43.93  E-value: 3.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  669 YLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQeepnkselelKRALCMAPELLRDAYRPGRGSQKG-DVYSF 747
Cdd:cd14209   116 YLHSLDLI-YRDLKPENLLIDQQGYIKVTDFGFAKRVKGR----------TWTLCGTPEYLAPEIILSKGYNKAvDWWAL 184

                  ....*..
gi 161076872  748 GILLYEM 754
Cdd:cd14209   185 GVLIYEM 191
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
661-788 4.01e-04

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: 44.22  E-value: 4.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHElkagqeePNKSELELKRALC-----MAPELLrdAYRP 735
Cdd:cd05615   118 AEISVGLFFLHKKGII-YRDLKLDNVMLDSEGHIKIADFGMCK-------EHMVEGVTTRTFCgtpdyIAPEII--AYQP 187
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 161076872  736 -GRGSqkgDVYSFGILLYEMIGRKGPWgdTAYSKEEIIQfvkcpEMLQHGVFRP 788
Cdd:cd05615   188 yGRSV---DWWAYGVLLYEMLAGQPPF--DGEDEDELFQ-----SIMEHNVSYP 231
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
581-761 4.12e-04

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: 44.14  E-value: 4.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIHK-------KSVDITRSIRKELKLMREVRHENIINFigASTDHGSVIIFTTYCARGSLEDVLANEDlHLDH 653
Cdd:cd05614    28 NKLYAMKVLRKaalvqkaKTVEHTRTERNVLEHVRQSPFLVTLHY--AFQTDAKLHLILDYVSGGELFTHLYQRD-HFSE 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  654 MFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLhelkagQEEPNKSELELKRALC-----MAPEL 728
Cdd:cd05614   105 DEVRFYSGEIILALEHLHKLGIV-YRDIKLENILLDSEGHVVLTDFGL------SKEFLTEEKERTYSFCgtieyMAPEI 177
                         170       180       190
                  ....*....|....*....|....*....|...
gi 161076872  729 LRDayRPGRGsQKGDVYSFGILLYEMIGRKGPW 761
Cdd:cd05614   178 IRG--KSGHG-KAVDWWSLGILMFELLTGASPF 207
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
588-773 4.14e-04

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: 43.78  E-value: 4.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  588 KIHKKSVditRSIRKELK-LMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDlHLDHMFISSLVSDILKG 666
Cdd:cd14091    31 KIIDKSK---RDPSEEIEiLLRYGQHPNIITLRDVYDDGNSVYLVTELLRGGELLDRILRQK-FFSEREASAVMKTLTKT 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  667 MIYLHDSEIIsHGNLRSSNCL-------IDSrwvCQISDFGLhelkAGQeepnkseLELKRALCM---------APELLR 730
Cdd:cd14091   107 VEYLHSQGVV-HRDLKPSNILyadesgdPES---LRICDFGF----AKQ-------LRAENGLLMtpcytanfvAPEVLK 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 161076872  731 ----DAyrpgrgsqKGDVYSFGILLYEMIGRKGPW----GDTAyskEEIIQ 773
Cdd:cd14091   172 kqgyDA--------ACDIWSLGVLLYTMLAGYTPFasgpNDTP---EVILA 211
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
583-763 5.19e-04

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: 43.42  E-value: 5.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  583 IVAMKKIHKKSVDiTRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDlHLDHMFISSLVSD 662
Cdd:cd14113    34 AVATKFVNKKLMK-RDQVTHELGVLQSLQHPQLVGLLDTFETPTSYILVLEMADQGRLLDYVVRWG-NLTEEKIRFYLRE 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  663 ILKGMIYLHDSEiISHGNLRSSNCLID---SRWVCQISDFG----------LHELKAGQEepnkselelkralCMAPEL- 728
Cdd:cd14113   112 ILEALQYLHNCR-IAHLDLKPENILVDqslSKPTIKLADFGdavqlnttyyIHQLLGSPE-------------FAAPEIi 177
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 161076872  729 LRDAYrpgrgSQKGDVYSFGILLYEMIGRKGPWGD 763
Cdd:cd14113   178 LGNPV-----SLTSDLWSIGVLTYVLLSGVSPFLD 207
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
573-755 5.83e-04

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: 43.37  E-value: 5.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  573 FTNIALFRgNIVAMKKIHKKSVDITRSIR------KELKLMREVRHENIINFIGASTD-----HGSVIIFTTYCARGSLE 641
Cdd:cd14039     6 FGNVCLYQ-NQETGEKIAIKSCRLELSVKnkdrwcHEIQIMKKLNHPNVVKACDVPEEmnflvNDVPLLAMEYCSGGDLR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  642 DVLANED--LHLDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCL---IDSRWVCQISDFGL-HELKAGqeepnkse 715
Cdd:cd14039    85 KLLNKPEncCGLKESQVLSLLSDIGSGIQYLHENKII-HRDLKPENIVlqeINGKIVHKIIDLGYaKDLDQG-------- 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 161076872  716 lelkrALC---------MAPELLRD-AYrpgrgSQKGDVYSFGILLYEMI 755
Cdd:cd14039   156 -----SLCtsfvgtlqyLAPELFENkSY-----TVTVDYWSFGTMVFECI 195
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
574-763 7.06e-04

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. The STRAD-beta subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 43.32  E-value: 7.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  574 TNIALFR----GNIVAMKKIHKKSVDITR--SIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANE 647
Cdd:cd08226    14 TSVYLARhtptGTLVTVKITNLDNCSEEHlkALQNEVVLSHFFRHPNIMTHWTVFTEGSWLWVISPFMAYGSARGLLKTY 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  648 DLH-LDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISdfGLHELKAGQEEPNKSEL-----ELKRA 721
Cdd:cd08226    94 FPEgMNEALIGNILYGAIKALNYLHQNGCI-HRSVKASHILISGDGLVSLS--GLSHLYSMVTNGQRSKVvydfpQFSTS 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 161076872  722 LC--MAPELLRD---AYrpgrgSQKGDVYSFGILLYEMIGRKGPWGD 763
Cdd:cd08226   171 VLpwLSPELLRQdlhGY-----NVKSDIYSVGITACELARGQVPFQD 212
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
602-805 8.13e-04

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


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 42.74  E-value: 8.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  602 KELKLMREVRHENIINFIGA-STDHGSVIIFTTYCARGSLEDVLANEDLhLDHMFISSLVSDILKGMIYLHD-SEIISHG 679
Cdd:cd14040    59 REYRIHKELDHPRIVKLYDYfSLDTDTFCTVLEYCEGNDLDFYLKQHKL-MSEKEARSIVMQIVNALRYLNEiKPPIIHY 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  680 NLRSSNCLIDSRWVC---QISDFGLHEL----KAGQEEPNKSELELKRALCMAPELLRDAYRPGRGSQKGDVYSFGILLY 752
Cdd:cd14040   138 DLKPGNILLVDGTACgeiKITDFGLSKImdddSYGVDGMDLTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFF 217
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 161076872  753 EMIGRKGPWGDTAySKEEIIQ---FVKCPEmLQHGVfRPALTHthlDIPDYIRKCL 805
Cdd:cd14040   218 QCLYGRKPFGHNQ-SQQDILQentILKATE-VQFPV-KPVVSN---EAKAFIRRCL 267
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
611-761 9.19e-04

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: 42.30  E-value: 9.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  611 RHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDlHLDHMFISSLVSDILKGMIYLHDSEIISHgNLRSSNCLIDS 690
Cdd:cd13995    54 RHENIAELYGALLWEETVHLFMEAGEGGSVLEKLESCG-PMREFEIIWVTKHVLKGLDFLHSKNIIHH-DIKPSNIVFMS 131
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161076872  691 RWVCQIsDFGLH-ELKAGQEEPNkselELK-RALCMAPELLRdayrpGRG-SQKGDVYSFGILLYEMIGRKGPW 761
Cdd:cd13995   132 TKAVLV-DFGLSvQMTEDVYVPK----DLRgTEIYMSPEVIL-----CRGhNTKADIYSLGATIIHMQTGSPPW 195
PBP1_GPC6A-like cd06361
ligand-binding domain of the promiscuous L-alpha-amino acid receptor GPRC6A which is a ...
65-235 9.19e-04

ligand-binding domain of the promiscuous L-alpha-amino acid receptor GPRC6A which is a broad-spectrum amino acid-sensing receptor; This family includes the ligand-binding domain of the promiscuous L-alpha-amino acid receptor GPRC6A which is a broad-spectrum amino acid-sensing receptor, and its fish homolog, the 5.24 chemoreceptor. GPRC6A is a member of the family C of G-protein-coupled receptors that transduce extracellular signals into G-protein activation and ultimately into cellular responses.


Pssm-ID: 380584 [Multi-domain]  Cd Length: 401  Bit Score: 43.13  E-value: 9.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   65 AIEDVNKNPnLLPGKKLAFKPVD-----------IGHKMSAY---RVKPLRAMTQMReAGVTAFIGPDESCTTEAL--LA 128
Cdd:cd06361    44 AIEMINNST-LLPGIKLGYEIYDtcsdvtkalqaTLRLLSKFnssNELLECDYTDYV-PPVKAVIGASYSEISIAVarLL 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  129 SAWNTPMLSFKCSDPIVSNKSTFHTFARTLAPASKVSKSVISLLNAFHWNKFSIVVSSkpiwgSDVARAIQEL----AEA 204
Cdd:cd06361   122 NLQLIPQISYESSAPILSDKLRFPSFLRTVPSDFHQTKAMAKLISHFGWNWVGIIYTD-----DDYGRSALESfiiqAEA 196
                         170       180       190
                  ....*....|....*....|....*....|.
gi 161076872  205 RNFTIShFKYIsdyIPTTKTLSQIDKIIEET 235
Cdd:cd06361   197 ENVCIA-FKEV---LPAYLSDPTMNVRINDT 223
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
581-817 9.33e-04

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: 42.74  E-value: 9.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  581 GNIVAMKKIhKKSVDITRSIRKELKL---MREVRHENIINFIGASTDHGSVIIfttyCAR---GSLED----VLANEDLH 650
Cdd:cd06616    31 GTIMAVKRI-RSTVDEKEQKRLLMDLdvvMRSSDCPYIVKFYGALFREGDCWI----CMElmdISLDKfykyVYEVLDSV 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  651 LDHMFISSLVSDILKGMIYLHDSEIISHGNLRSSNCLIDSRWVCQISDFGLhelkAGQEEpnKSELELKRALC---MAPE 727
Cdd:cd06616   106 IPEEILGKIAVATVKALNYLKEELKIIHRDVKPSNILLDRNGNIKLCDFGI----SGQLV--DSIAKTRDAGCrpyMAPE 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  728 LL-----RDAYrpgrgSQKGDVYSFGILLYEMIGRKGPwgdtaYSK-----EEIIQFVKCPEmlqhgvfrPALTHTH--- 794
Cdd:cd06616   180 RIdpsasRDGY-----DVRSDVWSLGITLYEVATGKFP-----YPKwnsvfDQLTQVVKGDP--------PILSNSEere 241
                         250       260
                  ....*....|....*....|....*
gi 161076872  795 --LDIPDYIRKCLCQcwdeDPEVRP 817
Cdd:cd06616   242 fsPSFVNFVNLCLIK----DESKRP 262
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
651-755 1.02e-03

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: 42.47  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  651 LDHMFISSLVSDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEPNKSeleLKRALCMAPELLR 730
Cdd:cd05611    94 LPEDWAKQYIAEVVLGVEDLHQRGII-HRDIKPENLLIDQTGHLKLTDFGLSRNGLEKRHNKKF---VGTPDYLAPETIL 169
                          90       100
                  ....*....|....*....|....*.
gi 161076872  731 dayrpGRG-SQKGDVYSFGILLYEMI 755
Cdd:cd05611   170 -----GVGdDKMSDWWSLGCVIFEFL 190
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
598-763 1.33e-03

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


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 42.02  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  598 RSIRKELKLMREVRHENIINFIGA--STDHGS--VIIFTTYCARGSLEDVLANEDLhLDHMFISSLVSDILKGMIYLHD- 672
Cdd:cd14031    54 QRFKEEAEMLKGLQHPNIVRFYDSweSVLKGKkcIVLVTELMTSGTLKTYLKRFKV-MKPKVLRSWCRQILKGLQFLHTr 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  673 SEIISHGNLRSSNCLIDS-RWVCQISDFGLHELKagqeEPNKSELELKRALCMAPELLRDAYrpgrgSQKGDVYSFGILL 751
Cdd:cd14031   133 TPPIIHRDLKCDNIFITGpTGSVKIGDLGLATLM----RTSFAKSVIGTPEFMAPEMYEEHY-----DESVDVYAFGMCM 203
                         170
                  ....*....|..
gi 161076872  752 YEMIGRKGPWGD 763
Cdd:cd14031   204 LEMATSEYPYSE 215
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
596-763 1.61e-03

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: 41.96  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  596 ITRSIRKELK----LMREVRHENIINFIGA--STDHGS--VIIFTTYCARGSLEDVLANEDLhLDHMFISSLVSDILKGM 667
Cdd:cd14030    63 LSKSERQRFKeeagMLKGLQHPNIVRFYDSweSTVKGKkcIVLVTELMTSGTLKTYLKRFKV-MKIKVLRSWCRQILKGL 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  668 IYLHD-SEIISHGNLRSSNCLIDS-RWVCQISDFGLHELKagqeEPNKSELELKRALCMAPELLRDAYrpgrgSQKGDVY 745
Cdd:cd14030   142 QFLHTrTPPIIHRDLKCDNIFITGpTGSVKIGDLGLATLK----RASFAKSVIGTPEFMAPEMYEEKY-----DESVDVY 212
                         170
                  ....*....|....*...
gi 161076872  746 SFGILLYEMIGRKGPWGD 763
Cdd:cd14030   213 AFGMCMLEMATSEYPYSE 230
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
663-825 1.91e-03

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


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 41.59  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  663 ILKGMIYLHDSEIISHGNLRSSNCLIDSRWVCQISDFGLhelkAGQEEPNKSelELKRALC---MAPELLrDAYRPGRGS 739
Cdd:cd06618   123 IVKALHYLKEKHGVIHRDVKPSNILLDESGNVKLCDFGI----SGRLVDSKA--KTRSAGCaayMAPERI-DPPDNPKYD 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  740 QKGDVYSFGILLYEMIGRKGPW--GDTAYSKEEIIQFVKCPEMLQHGVFRPalththlDIPDYIRKCLCQcwdeDPEVRP 817
Cdd:cd06618   196 IRADVWSLGISLVELATGQFPYrnCKTEFEVLTKILNEEPPSLPPNEGFSP-------DFCSFVDLCLTK----DHRYRP 264

                  ....*...
gi 161076872  818 DIRLVRMH 825
Cdd:cd06618   265 KYRELLQH 272
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
661-761 2.31e-03

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: 41.43  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLheLKAGQEEPNKSELELKRALCMAPELLRDA-YRPGRgs 739
Cdd:cd05590   103 AEITSALMFLHDKGII-YRDLKLDNVLLDHEGHCKLADFGM--CKEGIFNGKTTSTFCGTPDYIAPEILQEMlYGPSV-- 177
                          90       100
                  ....*....|....*....|..
gi 161076872  740 qkgDVYSFGILLYEMIGRKGPW 761
Cdd:cd05590   178 ---DWWAMGVLLYEMLCGHAPF 196
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
661-763 2.87e-03

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: 41.08  E-value: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHdSEIISHGNLRSSNCLIDSRWVCQISDFGLheLKAGQEEPNKSELELKRALCMAPELLRDAyrpgRGSQ 740
Cdd:cd05620   103 AEIVCGLQFLH-SKGIIYRDLKLDNVMLDRDGHIKIADFGM--CKENVFGDNRASTFCGTPDYIAPEILQGL----KYTF 175
                          90       100
                  ....*....|....*....|....
gi 161076872  741 KGDVYSFGILLYEMIGRKGPW-GD 763
Cdd:cd05620   176 SVDWWSFGVLLYEMLIGQSPFhGD 199
pknD PRK13184
serine/threonine-protein kinase PknD;
584-787 3.18e-03

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 41.68  E-value: 3.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKksvDITRSIRKELKLMREVRheniinfIGASTDHGSVIIFTTYCARG-------------SLEDVLAN---- 646
Cdd:PRK13184   30 VALKKIRE---DLSENPLLKKRFLREAK-------IAADLIHPGIVPVYSICSDGdpvyytmpyiegyTLKSLLKSvwqk 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  647 EDLHLDH-------MFISsLVSDILKGMIYLHdSEIISHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEpnkSELELK 719
Cdd:PRK13184  100 ESLSKELaektsvgAFLS-IFHKICATIEYVH-SKGVLHRDLKPDNILLGLFGEVVILDWGAAIFKKLEEE---DLLDID 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  720 ---RALC----------------MAPELLRDAyrpgRGSQKGDVYSFGILLYEMI----------GRKGPWGDTAYSKEE 770
Cdd:PRK13184  175 vdeRNICyssmtipgkivgtpdyMAPERLLGV----PASESTDIYALGVILYQMLtlsfpyrrkkGRKISYRDVILSPIE 250
                         250
                  ....*....|....*..
gi 161076872  771 IIQFVKCPEMLQHGVFR 787
Cdd:PRK13184  251 VAPYREIPPFLSQIAMK 267
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
583-766 3.29e-03

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: 41.05  E-value: 3.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  583 IVAMKKIHkkSVDITRSIrkelkLMReVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVL---ANEDLHlDHMFISSL 659
Cdd:cd05581    39 IIKEKKVK--YVTIEKEV-----LSR-LAHPGIVKLYYTFQDESKLYFVLEYAPNGDLLEYIrkyGSLDEK-CTRFYTAE 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  660 VSDILKgmiYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFG--------LHELKAGQEEPNKSELELKR-------ALCM 724
Cdd:cd05581   110 IVLALE---YLHSKGII-HRDLKPENILLDEDMHIKITDFGtakvlgpdSSPESTKGDADSQIAYNQARaasfvgtAEYV 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 161076872  725 APELLRDayrpGRGSQKGDVYSFGILLYEMIGRKGPW-GDTAY 766
Cdd:cd05581   186 SPELLNE----KPAGKSSDLWALGCIIYQMLTGKPPFrGSNEY 224
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
661-757 4.00e-03

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: 40.80  E-value: 4.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL--HELKAGqeepnkselELKRALC-----MAPELLRDA- 732
Cdd:cd05571   102 AEIVLALGYLHSQGIV-YRDLKLENLLLDKDGHIKITDFGLckEEISYG---------ATTKTFCgtpeyLAPEVLEDNd 171
                          90       100
                  ....*....|....*....|....*.
gi 161076872  733 YrpGRGSqkgDVYSFGILLYEMI-GR 757
Cdd:cd05571   172 Y--GRAV---DWWGLGVVMYEMMcGR 192
PBP1_iGluR_non_NMDA-like cd06368
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the non-NMDA ...
46-213 4.34e-03

N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the non-NMDA (N-methyl-D-aspartate) subtypes of ionotropic glutamate receptors; N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the non-NMDA (N-methyl-D-asparate) subtypes of ionotropic glutamate receptors. While this N-terminal domain belongs to the periplasmic-binding fold type 1 superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type 2. The LIVBP-like domain of iGluRs is thought to play a role in the initial assembly of iGluR subunits, but it is not well understood how this domain is arranged and functions in intact iGluR. Glutamate mediates the majority of excitatory synaptic transmission in the central nervous system via two broad classes of ionotropic receptors, characterized by their response to glutamate agonists: N-methyl-D-aspartate (NMDA) and non-NMDA receptors. NMDA receptors have intrinsically slow kinetics, are highly permeable to Ca2+, and are blocked by extracellular Mg2+ in a voltage-dependent manner. Non-NMDA receptors have faster kinetics, are most often only weakly permeable to Ca2+, and are not blocked by extracellular Mg2+. While non-NMDA receptors typically mediate excitatory synaptic responses at resting membrane potentials, NMDA receptors contribute several forms of synaptic plasticity and are thought to play an important role in the development of synaptic pathways. Non-NMDA receptors include alpha-amino-3-hydroxy-5-methyl-4-isoxazole proprionate (AMPA) and kainate receptors.


Pssm-ID: 380591 [Multi-domain]  Cd Length: 339  Bit Score: 40.81  E-value: 4.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   46 IGFLAEYSQMRVTLGGLPLAIEDVNKNPNLLPGKKLAfkpVDIGHKMSAYRVKPLRAMTQMREAGVTAFIGPDESCTTEA 125
Cdd:cd06368     2 IGAIFNEVNDAHERAAFRYAVERLNTNIVKLAYFRIT---YSIEAIDSNSHFDATDKACDLLEKGVVAIVGPSSSDSNNA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  126 L--LASAWNTPMLSFKCSDPIVSNKSTFHtfartLAPASKVSKSVISLLNAFHWNKFSIVVSSkpiwgSDVARAIQELAE 203
Cdd:cd06368    79 LqsICDALDVPHITVHDDPRLSKSQYSLS-----LYPRNQLSQAVSDLLKYWRWKRFVLVYDD-----DDRLRRLQELLE 148
                         170
                  ....*....|
gi 161076872  204 ARNFTISHFK 213
Cdd:cd06368   149 AARFSKRFVS 158
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
584-822 4.60e-03

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits, common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270662 [Multi-domain]  Cd Length: 266  Bit Score: 40.30  E-value: 4.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  584 VAMKKIHKKSVDITRSIRKELKLMREVRHENIINFIGASTDHGSVIIFTTYCARGSLEDVLANEDLHLDHMFISSLVSDI 663
Cdd:cd05077    39 VILKVLDPSHRDISLAFFETASMMRQVSHKHIVLLYGVCVRDVENIMVEEFVEFGPLDLFMHRKSDVLTTPWKFKVAKQL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  664 LKGMIYLHDSEIIsHGNLRSSNCL-----IDSRW--VCQISDFGLHELKAGQEEpnkselELKRALCMAPELLRDAYRPg 736
Cdd:cd05077   119 ASALSYLEDKDLV-HGNVCTKNILlaregIDGECgpFIKLSDPGIPITVLSRQE------CVERIPWIAPECVEDSKNL- 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  737 rgSQKGDVYSFGILLYEMIGRkgpwGDTAYSKEEIIQfvkcPEMLQHGVFRPALTHThldipDYIRKCLCQCWDEDPEVR 816
Cdd:cd05077   191 --SIAADKWSFGTTLWEICYN----GEIPLKDKTLAE----KERFYEGQCMLVTPSC-----KELADLMTHCMNYDPNQR 255

                  ....*.
gi 161076872  817 PDIRLV 822
Cdd:cd05077   256 PFFRAI 261
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
586-820 5.59e-03

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


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 40.11  E-value: 5.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  586 MKKIH--KKSVDITRSIRKELKLMREVRHENIINFIGASTDH-GSVIIFTTYCARGSLEDVLANED-LHLDHMFISSLVS 661
Cdd:cd08223    30 IKKLNlkNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEGEdGFLYIVMGFCEGGDLYTRLKEQKgVLLEERQVVEWFV 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  662 DILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGLHELKAGQEEpnKSELELKRALCMAPELLRDayRPGrgSQK 741
Cdd:cd08223   110 QIAMALQYMHERNIL-HRDLKTQNIFLTKSNIIKVGDLGIARVLESSSD--MATTLIGTPYYMSPELFSN--KPY--NHK 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  742 GDVYSFGILLYEMIGRKgpwgdTAYSKEEIIQFV------KCPEMLQHgvFRPALThthldipDYIRKCLCQcwdeDPEV 815
Cdd:cd08223   183 SDVWALGCCVYEMATLK-----HAFNAKDMNSLVykilegKLPPMPKQ--YSPELG-------ELIKAMLHQ----DPEK 244

                  ....*
gi 161076872  816 RPDIR 820
Cdd:cd08223   245 RPSVK 249
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
587-776 5.62e-03

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: 40.36  E-value: 5.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  587 KKIHKKS-----VDItrsIRKELKLMREVR-------HENIINFIGASTDHGSVIIFTTYCARGSLedvlanedlhLDH- 653
Cdd:cd14092    24 KCVHKKTgqefaVKI---VSRRLDTSREVQllrlcqgHPNIVKLHEVFQDELHTYLVMELLRGGEL----------LERi 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  654 ----MFISSLVSDILKGMI----YLHDSEIIsHGNLRSSNCL---IDSRWVCQISDFGLHELKAGQEEPNKSELELKRAl 722
Cdd:cd14092    91 rkkkRFTESEASRIMRQLVsavsFMHSKGVV-HRDLKPENLLftdEDDDAEIKIVDFGFARLKPENQPLKTPCFTLPYA- 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 161076872  723 cmAPELLRDAYRPGRGSQKGDVYSFGILLYEMIGRKGPW--GDTAYSKEEIIQFVK 776
Cdd:cd14092   169 --APEVLKQALSTQGYDESCDLWSLGVILYTMLSGQVPFqsPSRNESAAEIMKRIK 222
PBP1_ABC_ligand_binding-like cd06340
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
47-209 6.63e-03

type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in transport of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, their ligand specificity has not been determined experimentally.


Pssm-ID: 380563 [Multi-domain]  Cd Length: 352  Bit Score: 40.23  E-value: 6.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872   47 GFLAEYSQ-MRVtlgGLPLAIEDVNKN---PNLLpGKKLAFKPVDIGHKmsayrvkPLRAMTQM----REAGVTAFIGPD 118
Cdd:cd06340    10 GPLALIGQeAKR---GAELAVDEINAAggiKSLG-GAKIELVVADTQSD-------PEVAASEAerliTQEGVVAIIGAY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  119 ESCTTEAL--LASAWNTPMLSFKCSDPIVSNKsTFHTFARTLAPASKVSKSVISLLNAFH------WNKFSIVVSSKPiW 190
Cdd:cd06340    79 SSSVTLAAsqVAERYGVPFVTASAVADEITER-GFKYVFRTAPTASQFAEDAVDFLKELAkkkgkkIKKVAIIYEDSA-F 156
                         170
                  ....*....|....*....
gi 161076872  191 GSDVARAIQELAEARNFTI 209
Cdd:cd06340   157 GTSVAKGLKKAAKKAGLEV 175
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
661-776 8.94e-03

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: 39.91  E-value: 8.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076872  661 SDILKGMIYLHDSEIIsHGNLRSSNCLIDSRWVCQISDFGL-HELKAGQEEPNkselelkrALC-----MAPE-LLRDAY 733
Cdd:cd05619   113 AEIICGLQFLHSKGIV-YRDLKLDNILLDKDGHIKIADFGMcKENMLGDAKTS--------TFCgtpdyIAPEiLLGQKY 183
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 161076872  734 rpgrgSQKGDVYSFGILLYEMIGRKGPWgdTAYSKEEIIQFVK 776
Cdd:cd05619   184 -----NTSVDWWSFGVLLYEMLIGQSPF--HGQDEEELFQSIR 219
 
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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