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Conserved domains on  [gi|1907082950|ref|XP_036012846|]
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cyclin-dependent kinase 12 isoform X5 [Mus musculus]

Protein Classification

cyclin-dependent kinase( domain architecture ID 10167630)

cyclin-dependent kinase (CDK) is a serine/threonine-protein kinase that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; similar to CDK12 that phosphorylates the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A), thereby acting as a key regulator of transcription elongation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
715-997 0e+00

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 615.66  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  715 WGKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQD 794
Cdd:cd07864      1 WGKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLNHRSVVNLKEIVTDKQD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  795 ALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN--------- 865
Cdd:cd07864     81 ALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNkgqikladf 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 ----------SRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPA 935
Cdd:cd07864    161 glarlynseeSRPYTNKVITLWYRPPELLLGEERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRLCGSPCPA 240
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  936 VWPDVIKLPYFNTMKPKKQYRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd07864    241 VWPDVIKLPYFNTMKPKKQYRRRLREEFSFIPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
THRAP3_BCLAF1 super family cl25810
THRAP3/BCLAF1 family; This family includes thyroid hormone receptor-associated protein 3 ...
214-359 4.81e-03

THRAP3/BCLAF1 family; This family includes thyroid hormone receptor-associated protein 3 (THRAP3), which is a spliceosome component and a subunit of the TRAP complex which plays a role in pre-mRNA splicing and in mRNA decay. It also includes the transcriptional repressor Bcl-2-associated transcription factor 1 (BCLAF1).


The actual alignment was detected with superfamily member pfam15440:

Pssm-ID: 464718  Cd Length: 641  Bit Score: 41.30  E-value: 4.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  214 SPKRRSRSPhRKWSDSSKQDDSPSGASygqdydlsppRSHTSSNYDSYKKSPGSTSRRQSisppyKEPSAYQSSTRSPsp 293
Cdd:pfam15440    7 SPKRRSLSP-RSRSRSHYSDRSSSGRS----------RSSSSRSSSNHSKDPKRSKRWRM-----DDKKHGQKDPRIS-- 68
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  294 ysrrQRSVSPYSRRRSSSYERSGSYSGRSPSPygRRRSSSPFLSKRSLSRSPLPSRKSMKSRSRSP 359
Cdd:pfam15440   69 ----PHGNDHNRSYEHRSPDAKSSEASKSWSP--KRRSPLESVYVYKPSPRPSPERGDSSRRDQYM 128
 
Name Accession Description Interval E-value
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
715-997 0e+00

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 615.66  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  715 WGKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQD 794
Cdd:cd07864      1 WGKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLNHRSVVNLKEIVTDKQD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  795 ALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN--------- 865
Cdd:cd07864     81 ALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNkgqikladf 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 ----------SRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPA 935
Cdd:cd07864    161 glarlynseeSRPYTNKVITLWYRPPELLLGEERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRLCGSPCPA 240
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  936 VWPDVIKLPYFNTMKPKKQYRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd07864    241 VWPDVIKLPYFNTMKPKKQYRRRLREEFSFIPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
723-997 5.45e-78

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 258.23  E-value: 5.45e-78
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950   723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEgFPITAIREIKILRQLVHQSVVNMKEIVTDKQDaldfkkdk 802
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKK-DRERILREIKILKKLKHPNIVRLYDVFEDEDK-------- 71
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950   803 gaFYLVFEYMDH-DLMGLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN---------------- 865
Cdd:smart00220   72 --LYLVMEYCEGgDLFDLLKKR-GRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEdghvkladfglarqld 148
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950   866 -SRPYTNKVITLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANLelaQLELISRLCGSPCPAVWPDVIKlp 944
Cdd:smart00220  149 pGEKLTTFVGTPEYMAPEVLLG-KGYGKAVDIWSLGVILYELLTGKPPFPGDD---QLLELFKKIGKPKPPFPPPEWD-- 222
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1907082950   945 yfntmkpkkqyrrrlreefsfIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:smart00220  223 ---------------------ISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
720-1002 2.89e-70

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 237.79  E-value: 2.89e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  720 VDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIV-TDKQdaldf 798
Cdd:PLN00009     1 MDQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVhSEKR----- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  799 kkdkgaFYLVFEYMDHDLMGLLESGlVHFSEDH--IKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS---------- 866
Cdd:PLN00009    76 ------LYLVFEYLDLDLKKHMDSS-PDFAKNPrlIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRtnalkladfg 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 ---------RPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVW 937
Cdd:PLN00009   149 larafgipvRTFTHEVVTLWYRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRILGTPNEETW 228
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  938 PDVIKLPYFNTMKPKkqyrRRLREEFSFIPS---AALDLLDHMLTLDPSKRCTAEQTLQSDFLKDVEL 1002
Cdd:PLN00009   229 PGVTSLPDYKSAFPK----WPPKDLATVVPTlepAGVDLLSKMLRLDPSKRITARAALEHEYFKDLGD 292
Pkinase pfam00069
Protein kinase domain;
723-997 8.03e-61

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 207.48  E-value: 8.03e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQDaldfkkdk 802
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDN-------- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 gaFYLVFEYMDH-DLMGLLESGlVHFSEDHIKSFMKQLMEGldychkknflhrdikcsnilLNNSRPYTNKVITLWYRPP 881
Cdd:pfam00069   73 --LYLVLEYVEGgSLFDLLSEK-GAFSEREAKFIMKQILEG--------------------LESGSSLTTFVGTPWYMAP 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  882 ElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANlelaqlelisrlcgspcpavwpDVIKLPYFNTMKPkkqyrRRLRE 961
Cdd:pfam00069  130 E-VLGGNPYGPKVDVWSLGCILYELLTGKPPFPGI----------------------NGNEIYELIIDQP-----YAFPE 181
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1907082950  962 EFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:pfam00069  182 LPSNLSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
720-1182 2.23e-35

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 142.07  E-value: 2.23e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  720 VDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLD-----NEKEGFpitaIREIKILRQLVHQSVVNMkeivtdkqd 794
Cdd:COG0515      6 LGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPElaadpEARERF----RREARALARLNHPNIVRV--------- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  795 aLDFKKDKGAFYLVFEYMD-HDLMGLLESGLvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS-RPytnK 872
Cdd:COG0515     73 -YDVGEEDGRPYLVMEYVEgESLADLLRRRG-PLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDgRV---K 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  873 VI---------------------TLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANlelAQLELISRLCGS 931
Cdd:COG0515    148 LIdfgiaralggatltqtgtvvgTPGYMAPEQARG-EPVDPRSDVYSLGVTLYELLTGRPPFDGD---SPAELLRAHLRE 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  932 PCPavwpdviklpyfntmkPKKQYRRRLREEFSfipsaalDLLDHMLTLDPSKRCTAEQTLQSDfLKDVELSKMAPPDLP 1011
Cdd:COG0515    224 PPP----------------PPSELRPDLPPALD-------AIVLRALAKDPEERYQSAAELAAA-LRAVLRSLAAAAAAA 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950 1012 hwqdchELWSKKRRRQRQSGIVIEDPPPSKASRKETTSGTTAEPVKNNSPAPPQPAPVKAEPGPGDAVGLGDITQQLNQS 1091
Cdd:COG0515    280 ------AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAPAAAAAAAAAAAALAAAAAAAAAAAAAALLA 353
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950 1092 ELAVLLNLLQSQTDLSIPQMAQLLNIHSNPEMQQQLEALNQSISALTEASSQQQDSESIAPEESLKEVPSVPVVLPPAEQ 1171
Cdd:COG0515    354 AAAALAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAA 433
                          490
                   ....*....|.
gi 1907082950 1172 TTPEASNTPAD 1182
Cdd:COG0515    434 AAAAAAAAARL 444
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
725-914 9.08e-13

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 72.91  E-value: 9.08e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  725 IIGIIGEGTYGQVYKAKDKDTGELVALKKVRLD-NEKEGFpiTA--IREIKILRQLVHQSVVNMkeivtdkqdaLDFKKD 801
Cdd:NF033483    11 IGERIGRGGMAEVYLAKDTRLDRDVAVKVLRPDlARDPEF--VArfRREAQSAASLSHPNIVSV----------YDVGED 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 KGAFYLVFEYMD-HDLMGLL-ESGLVHFSEdhIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL---------------- 863
Cdd:NF033483    79 GGIPYIVMEYVDgRTLKDYIrEHGPLSPEE--AVEIMIQILSALEHAHRNGIVHRDIKPQNILItkdgrvkvtdfgiara 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  864 --NNSRPYTNKVI-TLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQ 914
Cdd:NF033483   157 lsSTTMTQTNSVLgTVHYLSPEQARG-GTVDARSDIYSLGIVLYEMLTGRPPFD 209
THRAP3_BCLAF1 pfam15440
THRAP3/BCLAF1 family; This family includes thyroid hormone receptor-associated protein 3 ...
214-359 4.81e-03

THRAP3/BCLAF1 family; This family includes thyroid hormone receptor-associated protein 3 (THRAP3), which is a spliceosome component and a subunit of the TRAP complex which plays a role in pre-mRNA splicing and in mRNA decay. It also includes the transcriptional repressor Bcl-2-associated transcription factor 1 (BCLAF1).


Pssm-ID: 464718  Cd Length: 641  Bit Score: 41.30  E-value: 4.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  214 SPKRRSRSPhRKWSDSSKQDDSPSGASygqdydlsppRSHTSSNYDSYKKSPGSTSRRQSisppyKEPSAYQSSTRSPsp 293
Cdd:pfam15440    7 SPKRRSLSP-RSRSRSHYSDRSSSGRS----------RSSSSRSSSNHSKDPKRSKRWRM-----DDKKHGQKDPRIS-- 68
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  294 ysrrQRSVSPYSRRRSSSYERSGSYSGRSPSPygRRRSSSPFLSKRSLSRSPLPSRKSMKSRSRSP 359
Cdd:pfam15440   69 ----PHGNDHNRSYEHRSPDAKSSEASKSWSP--KRRSPLESVYVYKPSPRPSPERGDSSRRDQYM 128
 
Name Accession Description Interval E-value
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
715-997 0e+00

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 615.66  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  715 WGKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQD 794
Cdd:cd07864      1 WGKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLNHRSVVNLKEIVTDKQD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  795 ALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN--------- 865
Cdd:cd07864     81 ALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNkgqikladf 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 ----------SRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPA 935
Cdd:cd07864    161 glarlynseeSRPYTNKVITLWYRPPELLLGEERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRLCGSPCPA 240
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  936 VWPDVIKLPYFNTMKPKKQYRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd07864    241 VWPDVIKLPYFNTMKPKKQYRRRLREEFSFIPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
723-996 4.68e-164

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: 494.39  E-value: 4.68e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKqdalDFKKDK 802
Cdd:cd07840      1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMENEKEGFPITAIREIKLLQKLDHPNVVRLKEIVTSK----GSAKYK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 GAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN----------------- 865
Cdd:cd07840     77 GSIYMVFEYMDHDLTGLLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNdgvlkladfglarpytk 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 --SRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDVIKL 943
Cdd:cd07840    157 enNADYTNRVITLWYRPPELLLGATRYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIFELCGSPTEENWPGVSDL 236
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  944 PYFNTMKPKKQYRRRLREEFS-FIPSAALDLLDHMLTLDPSKRCTAEQTLQSDF 996
Cdd:cd07840    237 PWFENLKPKKPYKRRLREVFKnVIDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
720-996 1.65e-114

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: 362.84  E-value: 1.65e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  720 VDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKqdALDFK 799
Cdd:cd07865     11 VSKYEKLAKIGQGTFGEVFKARHRKTGQIVALKKVLMENEKEGFPITALREIKILQLLKHENVVNLIEICRTK--ATPYN 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 KDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN--------------- 864
Cdd:cd07865     89 RYKGSIYLVFEFCEHDLAGLLSNKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITkdgvlkladfglara 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 -----NSRP--YTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVW 937
Cdd:cd07865    169 fslakNSQPnrYTNRVVTLWYRPPELLLGERDYGPPIDMWGAGCIMAEMWTRSPIMQGNTEQHQLTLISQLCGSITPEVW 248
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  938 PDVIKLPYFNTMKPKKQYRRRLREEFSFIPS--AALDLLDHMLTLDPSKRCTAEQTLQSDF 996
Cdd:cd07865    249 PGVDKLELFKKMELPQGQKRKVKERLKPYVKdpYALDLIDKLLVLDPAKRIDADTALNHDF 309
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
723-997 1.54e-112

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: 356.02  E-value: 1.54e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQdaldfkkdk 802
Cdd:cd07829      1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDNEEEGIPSTALREISLLKELKHPNIVKLLDVIHTEN--------- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 gAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS---------------- 866
Cdd:cd07829     72 -KLYLVFEYCDQDLKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDgvlkladfglarafgi 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 --RPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDVIKLP 944
Cdd:cd07829    151 plRTYTHEVVTLWYRAPEILLGSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIFQILGTPTEESWPGVTKLP 230
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  945 YFNtMKPKKQYRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd07829    231 DYK-PTFPKWPKNDLEKVLPRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
718-996 7.57e-107

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: 341.13  E-value: 7.57e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  718 RCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKqdald 797
Cdd:cd07843      2 RSVDEYEKLNRIEEGTYGVVYRARDKKTGEIVALKKLKMEKEKEGFPITSLREINILLKLQHPNIVTVKEVVVGS----- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 fKKDKgaFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS----------- 866
Cdd:cd07843     77 -NLDK--IYMVMEYVEHDLKSLMETMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRgilkicdfgla 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 -------RPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPD 939
Cdd:cd07843    154 reygsplKPYTQLVVTLWYRAPELLLGAKEYSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIFKLLGTPTEKIWPG 233
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  940 VIKLPYFNTMKPKKQYRRRLREEF--SFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDF 996
Cdd:cd07843    234 FSELPGAKKKTFTKYPYNQLRKKFpaLSLSDNGFDLLNRLLTYDPAKRISAEDALKHPY 292
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
720-993 6.85e-105

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: 336.21  E-value: 6.85e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  720 VDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQDalDFK 799
Cdd:cd07866      7 LRDYEILGKLGEGTFGEVYKARQIKTGRVVALKKILMHNEKDGFPITALREIKILKKLKHPNVVPLIDMAVERPD--KSK 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 KDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-------------- 865
Cdd:cd07866     85 RKRGSVYMVTPYMDHDLSGLLENPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNqgilkiadfglarp 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 ---------------SRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCG 930
Cdd:cd07866    165 ydgpppnpkggggggTRKYTNLVVTRWYRPPELLLGERRYTTAVDIWGIGCVFAEMFTRRPILQGKSDIDQLHLIFKLCG 244
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  931 SPCPAVWPDVIKLPYFNTMKPKKQYRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd07866    245 TPTEETWPGWRSLPGCEGVHSFTNYPRTLEERFGKLGPEGLDLLSKLLSLDPYKRLTASDALE 307
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
718-1010 5.12e-98

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: 317.00  E-value: 5.12e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  718 RCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQdaLD 797
Cdd:cd07845      4 RSVTEFEKLNRIGEGTYGIVYRARDTTSGEIVALKKVRMDNERDGIPISSLREITLLLNLRHPNIVELKEVVVGKH--LD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 fkkdkgAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN------------ 865
Cdd:cd07845     82 ------SIFLVMEYCEQDLASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDkgclkiadfgla 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 ------SRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPD 939
Cdd:cd07845    156 rtyglpAKPMTPKVVTLWYRAPELLLGCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIIQLLGTPNESIWPG 235
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  940 VIKLPYFNTMKPKKQYRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLKDVELSKmaPPDL 1010
Cdd:cd07845    236 FSDLPLVGKFTLPKQPYNNLKHKFPWLSEAGLRLLNFLLMYDPKKRATAEEALESSYFKEKPLPC--EPEM 304
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
722-1011 5.42e-91

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: 297.18  E-value: 5.42e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKE---GFPITAIREIKILRQLVHQSVVnmkeivtdkqDALDF 798
Cdd:cd07841      1 RYEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEakdGINFTALREIKLLQELKHPNII----------GLLDV 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  799 KKDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN------------- 865
Cdd:cd07841     71 FGHKSNINLVFEFMETDLEKVIKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASdgvlkladfglar 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 -----SRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDV 940
Cdd:cd07841    151 sfgspNRKMTHQVVTRWYRAPELLFGARHYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIFEALGTPTEENWPGV 230
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  941 IKLPYFNTMKPKKQYrrRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLKdvELSKMAPP-DLP 1011
Cdd:cd07841    231 TSLPDYVEFKPFPPT--PLKQIFPAASDDALDLLQRLLTLNPNKRITARQALEHPYFS--NDPAPTPPsQLP 298
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
729-993 2.59e-83

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: 274.55  E-value: 2.59e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQDaldfkkdkgaFYLV 808
Cdd:cd07835      7 IGEGTYGVVYKARDKLTGEIVALKKIRLETEDEGVPSTAIREISLLKELNHPNIVRLLDVVHSENK----------LYLV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDHDLMGLLES-GLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS------------------RPY 869
Cdd:cd07835     77 FEFLDLDLKKYMDSsPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEgalkladfglarafgvpvRTY 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  870 TNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDVIKLPYFNTM 949
Cdd:cd07835    157 THEVVTLWYRAPEILLGSKHYSTPVDIWSVGCIFAEMVTRRPLFPGDSEIDQLFRIFRTLGTPDEDVWPGVTSLPDYKPT 236
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1907082950  950 KPKKQyRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd07835    237 FPKWA-RQDLSKVVPSLDEDGLDLLSQMLVYDPAKRISAKAALQ 279
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
723-997 5.45e-78

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 258.23  E-value: 5.45e-78
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950   723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEgFPITAIREIKILRQLVHQSVVNMKEIVTDKQDaldfkkdk 802
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKK-DRERILREIKILKKLKHPNIVRLYDVFEDEDK-------- 71
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950   803 gaFYLVFEYMDH-DLMGLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN---------------- 865
Cdd:smart00220   72 --LYLVMEYCEGgDLFDLLKKR-GRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEdghvkladfglarqld 148
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950   866 -SRPYTNKVITLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANLelaQLELISRLCGSPCPAVWPDVIKlp 944
Cdd:smart00220  149 pGEKLTTFVGTPEYMAPEVLLG-KGYGKAVDIWSLGVILYELLTGKPPFPGDD---QLLELFKKIGKPKPPFPPPEWD-- 222
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1907082950   945 yfntmkpkkqyrrrlreefsfIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:smart00220  223 ---------------------ISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
722-1000 2.51e-73

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: 247.82  E-value: 2.51e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRL--DNekegfPITA---IREIKILRQLVHQSVVNMKEIVTDkQDAL 796
Cdd:cd07834      1 RYELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISNvfDD-----LIDAkriLREIKILRHLKHENIIGLLDILRP-PSPE 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  797 DFKKdkgaFYLVFEYMDHDLMGLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN------------ 864
Cdd:cd07834     75 EFND----VYIVTELMETDLHKVIKSP-QPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNsncdlkicdfgl 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 --------NSRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAV 936
Cdd:cd07834    150 argvdpdeDKGFLTEYVVTRWYRAPELLLSSKKYTKAIDIWSVGCIFAELLTRKPLFPGRDYIDQLNLIVEVLGTPSEED 229
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  937 WPDVIKLPYFNTMK--PKKQyRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLKDV 1000
Cdd:cd07834    230 LKFISSEKARNYLKslPKKP-KKPLSEVFPGASPEAIDLLEKMLVFNPKKRITADEALAHPYLAQL 294
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
723-997 1.18e-72

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 244.49  E-value: 1.18e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLV---HQSVVNMKEIVTDKQDALDFK 799
Cdd:cd07838      1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRVPLSEEGIPLSTIREIALLKQLEsfeHPNVVRLLDVCHGPRTDRELK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 kdkgaFYLVFEYMDHDLMGLLE----SGLvhfSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN---------- 865
Cdd:cd07838     81 -----LTLVFEHVDQDLATYLDkcpkPGL---PPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSdgqvkladfg 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 -SRPYTNK------VITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWP 938
Cdd:cd07838    153 lARIYSFEmaltsvVVTLWYRAPEVLLQSS-YATPVDMWSVGCIFAELFNRRPLFRGSSEADQLGKIFDVIGLPSEEEWP 231
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  939 DVIKLpyfntmkPKKQYRRRLREEF-SFIPS---AALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd07838    232 RNSAL-------PRSSFPSYTPRPFkSFVPEideEGLDLLKKMLTFNPHKRISAFEALQHPYF 287
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
722-992 1.43e-72

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: 244.16  E-value: 1.43e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQL-VHQSVVNMKEIVTDKQDaldfkk 800
Cdd:cd07832      1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEGGIPNQALREIKALQACqGHPYVVKLRDVFPHGTG------ 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 dkgaFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN--------------- 865
Cdd:cd07832     75 ----FVLVFEYMLSSLSEVLRDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISStgvlkiadfglarlf 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 ----SRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDVI 941
Cdd:cd07832    151 seedPRLYSHQVATRWYRAPELLYGSRKYDEGVDLWAVGCIFAELLNGSPLFPGENDIEQLAIVLRTLGTPNEKTWPELT 230
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  942 KLPYFNTMKPKKQYRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTL 992
Cdd:cd07832    231 SLPDYNKITFPESKGIRLEEIFPDCSPEAIDLLKGLLVYNPKKRLSAEEAL 281
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
722-996 3.46e-72

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


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 244.12  E-value: 3.46e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKD--TGELVALKKVRLDNEK-EGFPITAIREIKILRQLVHQSVVNMKEIVTDKQDaldf 798
Cdd:cd07842      1 KYEIEGCIGRGTYGRVYKAKRKNgkDGKEYAIKKFKGDKEQyTGISQSACREIALLRELKHENVVSLVEVFLEHAD---- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  799 kkdkGAFYLVFEYMDHDLMGLL----ESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTNK-- 872
Cdd:cd07842     77 ----KSVYLLFDYAEHDLWQIIkfhrQAKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVMGEGPERGVvk 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  873 -----------------------VITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLE---------LA 920
Cdd:cd07842    153 igdlglarlfnaplkpladldpvVVTIWYRAPELLLGARHYTKAIDIWAIGCIFAELLTLEPIFKGREAkikksnpfqRD 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  921 QLELISRLCGSPCPAVWPDVIKLPYFNTMKPKKQ---YRRRL----REEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd07842    233 QLERIFEVLGTPTEKDWPDIKKMPEYDTLKSDTKastYPNSLlakwMHKHKKPDSQGFDLLRKLLEYDPTKRITAEEALE 312

                   ...
gi 1907082950  994 SDF 996
Cdd:cd07842    313 HPY 315
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
721-997 1.87e-71

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: 241.07  E-value: 1.87e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIvtdkqdaldFKK 800
Cdd:cd07833      1 NKYEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKESEDDEDVKKTALREVKVLRQLRHENIVNLKEA---------FRR 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 dKGAFYLVFEYMDHDLMGLLE---SGLvhfSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS----------- 866
Cdd:cd07833     72 -KGRLYLVFEYVERTLLELLEaspGGL---PPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESgvlklcdfgfa 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 --------RPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWP 938
Cdd:cd07833    148 raltarpaSPLTDYVATRWYRAPELLVGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLYLIQKCLGPLPPSHQE 227
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  939 DVIKLPYFNTMKPKKQYRRRLREE--FSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd07833    228 LFSSNPRFAGVAFPEPSQPESLERryPGKVSSPALDFLKACLRMDPKERLTCDELLQHPYF 288
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
723-996 2.51e-71

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: 240.48  E-value: 2.51e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMkeivtdkqdaLDFKKDK 802
Cdd:cd07860      2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKL----------LDVIHTE 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 GAFYLVFEYMDHDLMGLLESGLVH-FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS--------------- 866
Cdd:cd07860     72 NKLYLVFEFLHQDLKKFMDASALTgIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEgaikladfglarafg 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 ---RPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDVIKL 943
Cdd:cd07860    152 vpvRTYTHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSM 231
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  944 PYFNTMKPKKQyRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDF 996
Cdd:cd07860    232 PDYKPSFPKWA-RQDFSKVVPPLDEDGRDLLSQMLHYDPNKRISAKAALAHPF 283
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
723-997 1.17e-70

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


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 238.59  E-value: 1.17e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVrldneKEGFP----ITAIREIKILRQL-VHQSVVNMKEIVtdkqdald 797
Cdd:cd07830      1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKM-----KKKFYsweeCMNLREVKSLRKLnEHPNIVKLKEVF-------- 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 fkKDKGAFYLVFEYMDHDLMGLLES-GLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN------------ 864
Cdd:cd07830     68 --RENDELYFVFEYMEGNLYQLMKDrKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSgpevvkiadfgl 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 -----NSRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPD 939
Cdd:cd07830    146 areirSRPPYTDYVSTRWYRAPEILLRSTSYSSPVDIWALGCIMAELYTLRPLFPGSSEIDQLYKICSVLGTPTKQDWPE 225
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  940 VIKLPY-----FNTMKPKKQYRrrlreefsFIPSA---ALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd07830    226 GYKLASklgfrFPQFAPTSLHQ--------LIPNAspeAIDLIKDMLRWDPKKRPTASQALQHPYF 283
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
722-992 2.71e-70

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: 237.70  E-value: 2.71e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTdkQDAldfkkd 801
Cdd:cd07861      1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEEGVPSTAIREISLLKELQHPNIVCLEDVLM--QEN------ 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 kgAFYLVFEYMDHDLMGLLES--GLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS------------- 866
Cdd:cd07861     73 --RLYLVFEFLSMDLKKYLDSlpKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKgvikladfglara 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 -----RPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDVI 941
Cdd:cd07861    151 fgipvRVYTHEVVTLWYRAPEVLLGSPRYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIFRILGTPTEDIWPGVT 230
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  942 KLPYFNTMKPKKQyRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTL 992
Cdd:cd07861    231 SLPDYKNTFPKWK-KGSLRTAVKNLDEDGLDLLEKMLIYDPAKRISAKKAL 280
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
720-1002 2.89e-70

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 237.79  E-value: 2.89e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  720 VDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIV-TDKQdaldf 798
Cdd:PLN00009     1 MDQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVhSEKR----- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  799 kkdkgaFYLVFEYMDHDLMGLLESGlVHFSEDH--IKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS---------- 866
Cdd:PLN00009    76 ------LYLVFEYLDLDLKKHMDSS-PDFAKNPrlIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRtnalkladfg 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 ---------RPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVW 937
Cdd:PLN00009   149 larafgipvRTFTHEVVTLWYRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRILGTPNEETW 228
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  938 PDVIKLPYFNTMKPKkqyrRRLREEFSFIPS---AALDLLDHMLTLDPSKRCTAEQTLQSDFLKDVEL 1002
Cdd:PLN00009   229 PGVTSLPDYKSAFPK----WPPKDLATVVPTlepAGVDLLSKMLRLDPSKRITARAALEHEYFKDLGD 292
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
723-997 1.73e-69

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 233.67  E-value: 1.73e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEkegFPITAIREIKILRQL----VHQSVVNMKEIVTDKQDaldf 798
Cdd:cd05118      1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFR---HPKAALREIKLLKHLndveGHPNIVKLLDVFEHRGG---- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  799 kkdkGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN-------------- 864
Cdd:cd05118     74 ----NHLCLVFELMGMNLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINlelgqlkladfgla 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 ---NSRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGspcpavwpdvi 941
Cdd:cd05118    150 rsfTSPPYTPYVATRWYRAPEVLLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRLLG----------- 218
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  942 klpyfntmkpkkqyrrrlreefsfiPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd05118    219 -------------------------TPEALDLLSKMLKYDPAKRITASQALAHPYF 249
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
722-996 1.71e-68

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 232.32  E-value: 1.71e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIV-TDKQdaldfkk 800
Cdd:cd07839      1 KYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLYDVLhSDKK------- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 dkgaFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS-------------- 866
Cdd:cd07839     74 ----LTLVFEYCDQDLKKYFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNgelkladfglaraf 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 ----RPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTK-KPIFQANLELAQLELISRLCGSPCPAVWPDVI 941
Cdd:cd07839    150 gipvRCYSAEVVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAgRPLFPGNDVDDQLKRIFRLLGTPTEESWPGVS 229
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  942 KLPYFntmKPKKQYRR--RLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDF 996
Cdd:cd07839    230 KLPDY---KPYPMYPAttSLVNVVPKLNSTGRDLLQNLLVCNPVQRISAEEALQHPY 283
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
726-997 6.82e-68

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 230.73  E-value: 6.82e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  726 IGIIGEGTYGQVYKAKDKDTGELVALKKVRLdNEKEGFPITAIREIKILRQLVHQSVVNMKEIV-TDKqdaldfkkdkgA 804
Cdd:cd07844      5 LDKLGEGSYATVYKGRSKLTGQLVALKEIRL-EHEEGAPFTAIREASLLKDLKHANIVTLHDIIhTKK-----------T 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  805 FYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN------------------S 866
Cdd:cd07844     73 LTLVFEYLDTDLKQYMDDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISErgelkladfglaraksvpS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 RPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLE-LAQLELISRLCGSPCPAVWPDVIKLPY 945
Cdd:cd07844    153 KTYSNEVVTLWYRPPDVLLGSTEYSTSLDMWGVGCIFYEMATGRPLFPGSTDvEDQLHKIFRVLGTPTEETWPGVSSNPE 232
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  946 FNTMKPKKQYRRRLREEFSFI--PSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd07844    233 FKPYSFPFYPPRPLINHAPRLdrIPHGEELALKFLQYEPKKRISAAEAMKHPYF 286
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
729-993 3.46e-67

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: 228.52  E-value: 3.46e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEkEGFPITAIREIKILRQLVHQSVVNMKEIVTdkqdaldfKKDKgaFYLV 808
Cdd:cd07836      8 LGEGTYATVYKGRNRTTGEIVALKEIHLDAE-EGTPSTAIREISLMKELKHENIVRLHDVIH--------TENK--LMLV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDHDLMGLLESGLVHFSED--HIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS------------------RP 868
Cdd:cd07836     77 FEYMDKDLKKYMDTHGVRGALDpnTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRgelkladfglarafgipvNT 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  869 YTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDVIKLPYFNT 948
Cdd:cd07836    157 FSNEVVTLWYRAPDVLLGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRIMGTPTESTWPGISQLPEYKP 236
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1907082950  949 MKPKKQyRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd07836    237 TFPRYP-PQDLQQLFPHADPLGIDLLHRLLQLNPELRISAHDALQ 280
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
729-1011 1.98e-65

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 225.41  E-value: 1.98e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKE------------GFPITAIREIKILRQLVHQSVVnmkeivtdkqDAL 796
Cdd:PTZ00024    17 LGEGTYGKVEKAYDTLTGKIVAIKKVKIIEISNdvtkdrqlvgmcGIHFTTLRELKIMNEIKHENIM----------GLV 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  797 DFKKDKGAFYLVFEYMDHDLMGLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN----------- 865
Cdd:PTZ00024    87 DVYVEGDFINLVMDIMASDLKKVVDRK-IRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSkgickiadfgl 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 ---------------------SRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLEL 924
Cdd:PTZ00024   166 arrygyppysdtlskdetmqrREEMTSKVVTLWYRAPELLMGAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQLGR 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  925 ISRLCGSPCPAVWPDVIKLPY---FNTMKPKKqyrrrLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLKDVE 1001
Cdd:PTZ00024   246 IFELLGTPNEDNWPQAKKLPLyteFTPRKPKD-----LKTIFPNASDDAIDLLQSLLKLNPLERISAKEALKHEYFKSDP 320
                          330
                   ....*....|
gi 1907082950 1002 LsKMAPPDLP 1011
Cdd:PTZ00024   321 L-PCDPSQLP 329
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
721-996 1.78e-62

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


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 215.47  E-value: 1.78e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILrQLVHQSVVNMKEIVTDKQDaldfKK 800
Cdd:cd07837      1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRLEMEEEGVPSTALREVSLL-QMLSQSIYIVRLLDVEHVE----EN 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DKGAFYLVFEYMDHDLMGLLES---GLVH-FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSR--------- 867
Cdd:cd07837     76 GKPLLYLVFEYLDTDLKKFIDSygrGPHNpLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKgllkiadlg 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  868 ----------PYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVW 937
Cdd:cd07837    156 lgraftipikSYTHEIVTLWYRAPEVLLGSTHYSTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIFRLLGTPNEEVW 235
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  938 PDVIKLP---YFNTMKPKKqyrrrLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDF 996
Cdd:cd07837    236 PGVSKLRdwhEYPQWKPQD-----LSRAVPDLEPEGVDLLTKMLAYDPAKRISAKAALQHPY 292
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
722-997 2.99e-61

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: 213.39  E-value: 2.99e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVR--LDNEKEGfpITAIREIKILRQLVHQSVVNMKEIVTDKQdaldfk 799
Cdd:cd07858      6 KYVPIKPIGRGAYGIVCSAKNSETNEKVAIKKIAnaFDNRIDA--KRTLREIKLLRHLDHENVIAIKDIMPPPH------ 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 kdKGAF---YLVFEYMDHDLMGLLESGLVhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS---------- 866
Cdd:cd07858     78 --REAFndvYIVYELMDTDLHQIIRSSQT-LSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANcdlkicdfgl 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 -RP-------YTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSpcpavwP 938
Cdd:cd07858    155 aRTtsekgdfMTEYVVTRWYRAPELLLNCSEYTTAIDVWSVGCIFAELLGRKPLFPGKDYVHQLKLITELLGS------P 228
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  939 DVIKLPYFNTMKPKK-------QYRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd07858    229 SEEDLGFIRNEKARRyirslpyTPRQSFARLFPHANPLAIDLLEKMLVFDPSKRITVEEALAHPYL 294
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
717-999 4.27e-61

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 213.19  E-value: 4.27e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  717 KRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKV------RLDNEKegfpitAIREIKILRQLV-HQSVVNMKEIV 789
Cdd:cd07852      3 KHILRRYEILKKLGKGAYGIVWKAIDKKTGEVVALKKIfdafrnATDAQR------TFREIMFLQELNdHPNIIKLLNVI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  790 TDKQDaldfkKDkgaFYLVFEYMDHDLMGLLESGLVHfsEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN----- 864
Cdd:cd07852     77 RAEND-----KD---IYLVFEYMETDLHAVIRANILE--DIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNsdcrv 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 -----------------NSRP-YTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELIS 926
Cdd:cd07852    147 kladfglarslsqleedDENPvLTDYVATRWYRAPEILLGSTRYTKGVDMWSVGCILGEMLLGKPLFPGTSTLNQLEKII 226
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  927 RLCGSPCPavwPDV--IKLPYFNTMKPKKQYRRR--LREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLKD 999
Cdd:cd07852    227 EVIGRPSA---EDIesIQSPFAATMLESLPPSRPksLDELFPKASPDALDLLKKLLVFNPNKRLTAEEALRHPYVAQ 300
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
721-996 4.66e-61

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 211.08  E-value: 4.66e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRldnEKEGFPIT---AIREIKILRQLVHQSVVNMKEIvtdkqdald 797
Cdd:cd07847      1 EKYEKLSKIGEGSYGVVFKCRNRETGQIVAIKKFV---ESEDDPVIkkiALREIRMLKQLKHPNLVNLIEV--------- 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 FKKdKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN------------ 865
Cdd:cd07847     69 FRR-KRKLHLVFEYCDHTVLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKqgqiklcdfgfa 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 ---SRP---YTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPD 939
Cdd:cd07847    148 rilTGPgddYTDYVATRWYRAPELLVGDTQYGPPVDVWAIGCVFAELLTGQPLWPGKSDVDQLYLIRKTLGDLIPRHQQI 227
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  940 VIKLPYFNTMK-PKKQYRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDF 996
Cdd:cd07847    228 FSTNQFFKGLSiPEPETREPLESKFPNISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
Pkinase pfam00069
Protein kinase domain;
723-997 8.03e-61

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 207.48  E-value: 8.03e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQDaldfkkdk 802
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDN-------- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 gaFYLVFEYMDH-DLMGLLESGlVHFSEDHIKSFMKQLMEGldychkknflhrdikcsnilLNNSRPYTNKVITLWYRPP 881
Cdd:pfam00069   73 --LYLVLEYVEGgSLFDLLSEK-GAFSEREAKFIMKQILEG--------------------LESGSSLTTFVGTPWYMAP 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  882 ElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANlelaqlelisrlcgspcpavwpDVIKLPYFNTMKPkkqyrRRLRE 961
Cdd:pfam00069  130 E-VLGGNPYGPKVDVWSLGCILYELLTGKPPFPGI----------------------NGNEIYELIIDQP-----YAFPE 181
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1907082950  962 EFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:pfam00069  182 LPSNLSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
726-997 1.97e-60

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


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 209.48  E-value: 1.97e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  726 IGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEkEGFPITAIREIKILRQLVHQSVVNMKEIV-TDKqdaldfkkdkgA 804
Cdd:cd07871     10 LDKLGEGTYATVFKGRSKLTENLVALKEIRLEHE-EGAPCTAIREVSLLKNLKHANIVTLHDIIhTER-----------C 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  805 FYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN------------------S 866
Cdd:cd07871     78 LTLVFEYLDSDLKQYLDNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEkgelkladfglaraksvpT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 RPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDVIKLPYF 946
Cdd:cd07871    158 KTYSNEVVTLWYRPPDVLLGSTEYSTPIDMWGVGCILYEMATGRPMFPGSTVKEELHLIFRLLGTPTEETWPGVTSNEEF 237
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  947 NTMKpKKQYRRR-LREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd07871    238 RSYL-FPQYRAQpLINHAPRLDTDGIDLLSSLLLYETKSRISAEAALRHSYF 288
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
721-997 5.68e-60

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: 209.85  E-value: 5.68e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRlDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVtdKQDALDFKK 800
Cdd:cd07849      5 PRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKIS-PFEHQTYCLRTLREIKILLRFKHENIIGILDIQ--RPPTFESFK 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DkgaFYLVFEYMDHDLMGLLESGlvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN---------------- 864
Cdd:cd07849     82 D---VYIVQELMETDLYKLIKTQ--HLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNtncdlkicdfglaria 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 -----NSRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSP------- 932
Cdd:cd07849    157 dpehdHTGFLTEYVATRWYRAPEIMLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKDYLHQLNLILGILGTPsqedlnc 236
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  933 -CPAVWPDVIK-LPYfntmKPKkqyrRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd07849    237 iISLKARNYIKsLPF----KPK----VPWNKLFPNADPKALDLLDKMLTFNPHKRITVEEALAHPYL 295
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
721-996 5.72e-60

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: 208.05  E-value: 5.72e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIvtdkqdaldFKK 800
Cdd:cd07846      1 EKYENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMVKKIAMREIKMLKQLRHENLVNLIEV---------FRR 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DKgAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS-------------- 866
Cdd:cd07846     72 KK-RWYLVFEFVDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSgvvklcdfgfartl 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 ----RPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDVIK 942
Cdd:cd07846    151 aapgEVYTDYVATRWYRAPELLVGDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIIKCLGNLIPRHQELFQK 230
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  943 LPYFNTMK-PKKQYRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDF 996
Cdd:cd07846    231 NPLFAGVRlPEVKEVEPLERRYPKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
729-1009 2.37e-59

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 206.39  E-value: 2.37e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEkEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQdaldfkkdkgAFYLV 808
Cdd:cd07873     10 LGEGTYATVYKGRSKLTDNLVALKEIRLEHE-EGAPCTAIREVSLLKDLKHANIVTLHDIIHTEK----------SLTLV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN------------------SRPYT 870
Cdd:cd07873     79 FEYLDKDLKQYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINErgelkladfglaraksipTKTYS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  871 NKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDVIKLPYFNTMK 950
Cdd:cd07873    159 NEVVTLWYRPPDILLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFRILGTPTEETWPGILSNEEFKSYN 238
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  951 PKKQYRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLKDVELSKMAPPD 1009
Cdd:cd07873    239 YPKYRADALHNHAPRLDSDGADLLSKLLQFEGRKRISAEEAMKHPYFHSLGERIHKLPD 297
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
722-1000 3.29e-59

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: 205.81  E-value: 3.29e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLD-NEKEgfpitaiREIKILRQLVHQSVVNMKEIVTDKQDaldfKK 800
Cdd:cd14137      5 SYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQDkRYKN-------RELQIMRRLKHPNIVKLKYFFYSSGE----KK 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DKGAFYLVFEYMD---HDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN------------- 864
Cdd:cd14137     74 DEVYLNLVMEYMPetlYRVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDpetgvlklcdfgs 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 --------NSRPYtnkVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCpav 936
Cdd:cd14137    154 akrlvpgePNVSY---ICSRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKVLGTPT--- 227
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  937 wPDVIKlpyfnTMKPKK------QYRRRLREEF--SFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLKDV 1000
Cdd:cd14137    228 -REQIK-----AMNPNYtefkfpQIKPHPWEKVfpKRTPPDAIDLLSKILVYNPSKRLTALEALAHPFFDEL 293
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
721-998 4.50e-56

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: 198.36  E-value: 4.50e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKV--RLDNekegfPITA---IREIKILRQLVHQSVVNMKEIVTDKQDA 795
Cdd:cd07855      5 DRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIpnAFDV-----VTTAkrtLRELKILRHFKHDNIIAIRDILRPKVPY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  796 LDFKKdkgaFYLVFEYMDHDLMGLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN----------- 864
Cdd:cd07855     80 ADFKD----VYVVLDLMESDLHHIIHSD-QPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNencelkigdfg 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 -----------NSRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPC 933
Cdd:cd07855    155 marglctspeeHKYFMTEYVATRWYRAPELMLSLPEYTQAIDMWSVGCIFAEMLGRRQLFPGKNYVHQLQLILTVLGTPS 234
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  934 PAVwpdviklpyFNTMKPKKQYR------RRLREEFS-FIPSA---ALDLLDHMLTLDPSKRCTAEQTLQSDFLK 998
Cdd:cd07855    235 QAV---------INAIGADRVRRyiqnlpNKQPVPWEtLYPKAdqqALDLLSQMLRFDPSERITVAEALQHPFLA 300
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
722-997 3.60e-54

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


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 191.33  E-value: 3.60e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLV---HQSVVNMKEIVTDKQDALDF 798
Cdd:cd07863      1 QYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVQTNEDGLPLSTVREVALLKRLEafdHPNIVRLMDVCATSRTDRET 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  799 KkdkgaFYLVFEYMDHDLMGLLES----GLvhfSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN--------- 865
Cdd:cd07863     81 K-----VTLVFEHVDQDLRTYLDKvpppGL---PAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSggqvkladf 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 --SRPY------TNKVITLWYRPPELLLGEERYTPaIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVW 937
Cdd:cd07863    153 glARIYscqmalTPVVVTLWYRAPEVLLQSTYATP-VDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDW 231
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  938 PDVIKLPYFNtMKPKKQyrrrlREEFSFIP---SAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd07863    232 PRDVTLPRGA-FSPRGP-----RPVQSVVPeieESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
723-993 1.12e-53

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 189.79  E-value: 1.12e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRlDNEKEGFPITAIREIKILRQLV-HQSVVNMKEIVTDKQdaldfkkd 801
Cdd:cd07831      1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMK-KHFKSLEQVNNLREIQALRRLSpHPNILRLIEVLFDRK-------- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 KGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSR-------------- 867
Cdd:cd07831     72 TGRLALVFELMDMNLYELIKGRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDDIlkladfgscrgiys 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  868 --PYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDVIKLPY 945
Cdd:cd07831    152 kpPYTEYISTRWYRAPECLLTDGYYGPKMDIWAVGCVFFEILSLFPLFPGTNELDQIAKIHDVLGTPDAEVLKKFRKSRH 231
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  946 FNTMKPKKQYR--RRLreefsfIPSA---ALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd07831    232 MNYNFPSKKGTglRKL------LPNAsaeGLDLLKKLLAYDPDERITAKQALR 278
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
729-1009 2.75e-52

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 186.74  E-value: 2.75e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEkEGFPITAIREIKILRQLVHQSVVNMKEIV-TDKqdaldfkkdkgAFYL 807
Cdd:cd07872     14 LGEGTYATVFKGRSKLTENLVALKEIRLEHE-EGAPCTAIREVSLLKDLKHANIVTLHDIVhTDK-----------SLTL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN------------------SRPY 869
Cdd:cd07872     82 VFEYLDKDLKQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINErgelkladfglaraksvpTKTY 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  870 TNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDVIKLPYFNTM 949
Cdd:cd07872    162 SNEVVTLWYRPPDVLLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRLLGTPTEETWPGISSNDEFKNY 241
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  950 KPKKQYRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLKDVELSKMAPPD 1009
Cdd:cd07872    242 NFPKYKPQPLINHAPRLDTEGIELLTKFLQYESKKRISAEEAMKHAYFRSLGTRIHSLPE 301
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
721-992 4.11e-52

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: 185.20  E-value: 4.11e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIvtdkqdaldFKK 800
Cdd:cd07848      1 NKFEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEA---------FRR 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 dKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN---------------- 864
Cdd:cd07848     72 -RGKLYLVFEYVEKNMLELLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLIShndvlklcdfgfarnl 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 ---NSRPYTNKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGsPCPavwPDVI 941
Cdd:cd07848    151 segSNANYTEYVATRWYRSPELLLGAP-YGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLG-PLP---AEQM 225
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  942 KL----PYFNTMK-PKKQYRRRL-REEFSFIPSAALDLLDHMLTLDPSKRCTAEQTL 992
Cdd:cd07848    226 KLfysnPRFHGLRfPAVNHPQSLeRRYLGILSGVLLDLMKNLLKLNPTDRYLTEQCL 282
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
721-998 5.51e-52

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: 186.73  E-value: 5.51e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQDALDFKK 800
Cdd:cd07851     15 DRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRPFQSAIHAKRTYRELRLLKHMKHENVIGLLDVFTPASSLEDFQD 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 dkgaFYLVFEYMDHDLMGLLESGlvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN---------------N 865
Cdd:cd07851     95 ----VYLVTHLMGADLNNIVKCQ--KLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNedcelkildfglarhT 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 SRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVwpdVIKLP- 944
Cdd:cd07851    169 DDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMNLVGTPDEEL---LKKISs 245
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  945 -----YFNTMkPKKQyRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLK 998
Cdd:cd07851    246 esarnYIQSL-PQMP-KKDFKEVFSGANPLAIDLLEKMLVLDPDKRITAAEALAHPYLA 302
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
729-997 1.03e-51

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 184.01  E-value: 1.03e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEkEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQdALDFkkdkgafylV 808
Cdd:cd07870      8 LGEGSYATVYKGISRINGQLVALKVISMKTE-EGVPFTAIREASLLKGLKHANIVLLHDIIHTKE-TLTF---------V 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN------------------SRPYT 870
Cdd:cd07870     77 FEYMHTDLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYlgelkladfglaraksipSQTYS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  871 NKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLE-LAQLELISRLCGSPCPAVWPDVIKLPYFNT- 948
Cdd:cd07870    157 SEVVTLWYRPPDVLLGATDYSSALDIWGAGCIFIEMLQGQPAFPGVSDvFEQLEKIWTVLGVPTEDTWPGVSKLPNYKPe 236
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  949 --MKPKKQYRRRLREEFSFIPSAAlDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd07870    237 wfLPCKPQQLRVVWKRLSRPPKAE-DLASQMLMMFPKDRISAQDALLHPYF 286
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
713-999 2.60e-51

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: 184.98  E-value: 2.60e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  713 SDWGKRCVDkfdiIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEgfPITAIREIKILRQLVHQSVVNMKEIV--- 789
Cdd:cd07854      1 FDLGSRYMD----LRPLGCGSNGLVFSAVDSDCDKRVAVKKIVLTDPQS--VKHALREIKIIRRLDHDNIVKVYEVLgps 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  790 -TDKQDALDFKKDKGAFYLVFEYMDHDLMGLLESGLVhfSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN--- 865
Cdd:cd07854     75 gSDLTEDVGSLTELNSVYIVQEYMETDLANVLEQGPL--SEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTedl 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 ---------SR----PYTNK------VITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELI- 925
Cdd:cd07854    153 vlkigdfglARivdpHYSHKgylsegLVTKWYRSPRLLLSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQMQLIl 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  926 ---------SRLCgspCPAVWPDVIKLpyfNTMKPkkqyRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDF 996
Cdd:cd07854    233 esvpvvreeDRNE---LLNVIPSFVRN---DGGEP----RRPLRDLLPGVNPEALDFLEQILTFNPMDRLTAEEALMHPY 302

                   ...
gi 1907082950  997 LKD 999
Cdd:cd07854    303 MSC 305
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
722-998 6.84e-50

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 180.75  E-value: 6.84e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTdKQDALDFKKd 801
Cdd:cd07859      1 RYKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHVSDATRILREIKLLRLLRHPDIVEIKHIML-PPSRREFKD- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 kgaFYLVFEYMDHDLMGLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN----------------- 864
Cdd:cd07859     79 ---IYVVFELMESDLHQVIKAN-DDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANadcklkicdfglarvaf 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 NSRP----YTNKVITLWYRPPELLlGE--ERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWP 938
Cdd:cd07859    155 NDTPtaifWTDYVATRWYRAPELC-GSffSKYTPAIDIWSIGCIFAEVLTGKPLFPGKNVVHQLDLITDLLGTPSPETIS 233
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  939 DVIKLP---YFNTMKPKKQyrRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLK 998
Cdd:cd07859    234 RVRNEKarrYLSSMRKKQP--VPFSQKFPNADPLALRLLERLLAFDPKDRPTAEEALADPYFK 294
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
722-993 9.80e-49

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: 174.24  E-value: 9.80e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVtdkqdaldfkKD 801
Cdd:cd14003      1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVI----------ET 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 KGAFYLVFEYMDH-DLMGLLESgLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN------------SRP 868
Cdd:cd14003     71 ENKIYLVMEYASGgELFDYIVN-NGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKngnlkiidfglsNEF 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  869 YTNKVI-----TLWYRPPELLLGEERYTPAIDVWSCGCILGELftkkpifqanlelaqlelisrLCGspcpavwpdviKL 943
Cdd:cd14003    150 RGGSLLktfcgTPAYAAPEVLLGRKYDGPKADVWSLGVILYAM---------------------LTG-----------YL 197
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  944 PYFNTMKPKKqYRRRLREEF---SFIPSAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd14003    198 PFDDDNDSKL-FRKILKGKYpipSHLSPDARDLIRRMLVVDPSKRITIEEILN 249
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
723-997 8.36e-48

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 174.51  E-value: 8.36e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDT--GELVALKKVRLDNEKEGFPITAIREIKILRQLV-HQSVVNM--KEIVTDkqDALD 797
Cdd:cd07857      2 YELIKELGQGAYGIVCSARNAETseEETVAIKKITNVFSKKILAKRALRELKLLRHFRgHKNITCLydMDIVFP--GNFN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 fkkdkgAFYLVFEYMDHDLMGLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-----------S 866
Cdd:cd07857     80 ------ELYLYEELMEADLHQIIRSG-QPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNAdcelkicdfglA 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 RPY-----------TNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSP--- 932
Cdd:cd07857    153 RGFsenpgenagfmTEYVATRWYRAPEIMLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDYVDQLNQILQVLGTPdee 232
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  933 ------CPAVWPDVIKLPYfntmKPKKQYRRrlreEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd07857    233 tlsrigSPKAQNYIRSLPN----IPKKPFES----IFPNANPLALDLLEKLLAFDPTKRISVEEALEHPYL 295
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
722-993 1.85e-46

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 168.04  E-value: 1.85e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQDaldfkkd 801
Cdd:cd05117      1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKN------- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 kgaFYLVFEYM------DHdlmgLLESGlvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTN-KVI 874
Cdd:cd05117     74 ---LYLVMELCtggelfDR----IVKKG--SFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPiKII 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  875 -------------------TLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRlcGSpcpa 935
Cdd:cd05117    145 dfglakifeegeklktvcgTPYYVAPEVLKG-KGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILK--GK---- 217
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  936 vwpdviklPYFNTmkpkkqyrrrlrEEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd05117    218 --------YSFDS------------PEWKNVSEEAKDLIKRLLVVDPKKRLTAAEALN 255
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
721-1010 2.21e-46

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 169.49  E-value: 2.21e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLdNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQdaldfkk 800
Cdd:cd07869      5 DSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRL-QEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKE------- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 dkgAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN--------------- 865
Cdd:cd07869     77 ---TLTLVFEYVHTDLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDtgelkladfglarak 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 ---SRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELA-QLELISRLCGSPCPAVWPDVI 941
Cdd:cd07869    154 svpSHTYSNEVVTLWYRPPDVLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDIQdQLERIFLVLGTPNEDTWPGVH 233
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  942 KLPYFNTMKPKKQYRRRLRE---EFSFIPSAAlDLLDHMLTLDPSKRCTAEQTLQSDFLKDVelskmaPPDL 1010
Cdd:cd07869    234 SLPHFKPERFTLYSPKNLRQawnKLSYVNHAE-DLASKLLQCFPKNRLSAQAALSHEYFSDL------PPRL 298
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
729-994 2.42e-46

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: 165.91  E-value: 2.42e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEgFPITAIREIKILRQLVHQSVVNMkeivtdkqdaLDFKKDKGAFYLV 808
Cdd:cd00180      1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKK-LLEELLREIEILKKLNHPNIVKL----------YDVFETENFLYLV 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDH-DLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-----------SRPYTNKVI-- 874
Cdd:cd00180     70 MEYCEGgSLKDLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSdgtvkladfglAKDLDSDDSll 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  875 ------TLWYRPPELLLGEERYTPAIDVWSCGCILgelftkkpifqanLELAQLElisrlcgspcpavwpdviklpyfnt 948
Cdd:cd00180    150 kttggtTPPYYAPPELLGGRYYGPKVDIWSLGVIL-------------YELEELK------------------------- 191
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1907082950  949 mkpkkqyrrrlreefsfipsaalDLLDHMLTLDPSKRCTAEQTLQS 994
Cdd:cd00180    192 -----------------------DLIRRMLQYDPKKRPSAKELLEH 214
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
722-993 6.15e-46

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 167.52  E-value: 6.15e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKD-KDTGELVALKKVRLDNEKEGFPITAIREIKILRQLV---HQSVVNMKEIVTDKQDALD 797
Cdd:cd07862      2 QYECVAEIGEGAYGKVFKARDlKNGGRFVALKRVRVQTGEEGMPLSTIREVAVLRHLEtfeHPNVVRLFDVCTVSRTDRE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 FKkdkgaFYLVFEYMDHDLMGLLES----GLvhfSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS------- 866
Cdd:cd07862     82 TK-----LTLVFEHVDQDLTTYLDKvpepGV---PTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSgqiklad 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 ----RPY------TNKVITLWYRPPELLLGEERYTPaIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAV 936
Cdd:cd07862    154 fglaRIYsfqmalTSVVVTLWYRAPEVLLQSSYATP-VDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKILDVIGLPGEED 232
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  937 WPDVIKLPYfNTMKPkkqyrRRLREEFSFIP---SAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd07862    233 WPRDVALPR-QAFHS-----KSAQPIEKFVTdidELGKDLLLKCLTFNPAKRISAYSALS 286
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
723-997 2.59e-45

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 166.57  E-value: 2.59e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRldNEKEgFPITAIREIKILRQLVHQSVVNMKEIVTDKqDALDFKkdk 802
Cdd:cd14210     15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIR--NKKR-FHQQALVEVKILKHLNDNDPDDKHNIVRYK-DSFIFR--- 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 GAFYLVFEYMDHDLMGLLES-GLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTNKVITL----- 876
Cdd:cd14210     88 GHLCIVFELLSINLYELLKSnNFQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKSSIKVIDFgsscf 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  877 ------------WYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSP-------CPAVW 937
Cdd:cd14210    168 egekvytyiqsrFYRAPEVILGLP-YDTAIDMWSLGCILAELYTGYPLFPGENEEEQLACIMEVLGVPpkslidkASRRK 246
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  938 PDVIKL--PYFNTMKPKKQYR---RRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14210    247 KFFDSNgkPRPTTNSKGKKRRpgsKSLAQVLKCDDPSFLDFLKKCLRWDPSERMTPEEALQHPWI 311
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
722-997 2.84e-45

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: 164.56  E-value: 2.84e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEivtdkqdalDFKkD 801
Cdd:cd08215      1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYE---------SFE-E 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 KGAFYLVFEYMDH-DLMGLLE---SGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-----------S 866
Cdd:cd08215     71 NGKLCIVMEYADGgDLAQKIKkqkKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKdgvvklgdfgiS 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 RPYTNKVI-------TLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQA-NLelaqLELISRLCGSPCPAVwp 938
Cdd:cd08215    151 KVLESTTDlaktvvgTPYYLSPELCEN-KPYNYKSDIWALGCVLYELCTLKHPFEAnNL----PALVYKIVKGQYPPI-- 223
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  939 dviklpyfntmkpKKQYRRRLReefsfipsaalDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd08215    224 -------------PSQYSSELR-----------DLVNSMLQKDPEKRPSANEILSSPFI 258
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
729-1008 4.82e-44

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: 163.97  E-value: 4.82e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQDALDFKKdkgaFYLV 808
Cdd:cd07880     23 VGSGAYGTVCSALDRRTGAKVAIKKLYRPFQSELFAKRAYRELRLLKHMKHENVIGLLDVFTPDLSLDRFHD----FYLV 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDHDLMGLLEsgLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS---------------RPYTNKV 873
Cdd:cd07880     99 MPFMGTDLGKLMK--HEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDcelkildfglarqtdSEMTGYV 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  874 ITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDVIKLPYFNTMKPKK 953
Cdd:cd07880    177 VTRWYRAPEVILNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKVTGTPSKEFVQKLQSEDAKNYVKKLP 256
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  954 QYRRR-LREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDF---LKDVELSKMAPP 1008
Cdd:cd07880    257 RFRKKdFRSLLPNANPLAVNVLEKMLVLDAESRITAAEALAHPYfeeFHDPEDETEAPP 315
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
729-1018 5.56e-44

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: 163.53  E-value: 5.56e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQDALDFKKdkgaFYLV 808
Cdd:cd07879     23 VGSGAYGSVCSAIDKRTGEKVAIKKLSRPFQSEIFAKRAYRELTLLKHMQHENVIGLLDVFTSAVSGDEFQD----FYLV 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDHDL---MGLlesglvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS---------------RPYT 870
Cdd:cd07879     99 MPYMQTDLqkiMGH------PLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDcelkildfglarhadAEMT 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  871 NKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVwpdVIKLPYFNTMK 950
Cdd:cd07879    173 GYVVTRWYRAPEVILNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKVTGVPGPEF---VQKLEDKAAKS 249
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  951 PKKQYRRRLREEFSFI-PSA---ALDLLDHMLTLDPSKRCTAEQTLQSDF---LKDVELSKMAPPdlphWQDCHE 1018
Cdd:cd07879    250 YIKSLPKYPRKDFSTLfPKAspqAVDLLEKMLELDVDKRLTATEALEHPYfdsFRDADEETEQQP----YDDSLE 320
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
723-997 2.33e-43

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 158.97  E-value: 2.33e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRldNEKEgFPITAIREIKILRQL------VHQSVVNMKEIVTDKQDAL 796
Cdd:cd14133      1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIK--NNKD-YLDQSLDEIRLLELLnkkdkaDKYHIVRLKDVFYFKNHLC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  797 dfkkdkgafyLVFEYMDHDLMGLLESGLVH-FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTNKVI- 874
Cdd:cd14133     78 ----------IVFELLSQNLYEFLKQNKFQyLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRCQIKIId 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  875 ----------------TLWYRPPELLLGEeRYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPcpavwp 938
Cdd:cd14133    148 fgsscfltqrlysyiqSRYYRAPEVILGL-PYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIP------ 220
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  939 dviklPYFNTMKPKKQyrrrlREEFsfipsaaLDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14133    221 -----PAHMLDQGKAD-----DELF-------VDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
728-997 1.37e-42

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 156.91  E-value: 1.37e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFpITAI-REIKILRQLVHQSVVNMkeivtdkqdaLDFKKDKGAFY 806
Cdd:cd06606      7 LLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEE-LEALeREIRILSSLKHPNIVRY----------LGTERTENTLN 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVFEYMDH-DLMGLLESGLvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS------------------- 866
Cdd:cd06606     76 IFLEYVPGgSLASLLKKFG-KLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDgvvkladfgcakrlaeiat 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 RPYTNKVI-TLWYRPPELLLGEErYTPAIDVWSCGCILGELFT-KKPIFQANLELAQLELISRLCGSPCpavwpdvikLP 944
Cdd:cd06606    155 GEGTKSLRgTPYWMAPEVIRGEG-YGRAADIWSLGCTVIEMATgKPPWSELGNPVAALFKIGSSGEPPP---------IP 224
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  945 yfntmkpkkqyrrrlreefSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd06606    225 -------------------EHLSEEAKDFLRKCLQRDPKKRPTADELLQHPFL 258
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
717-997 4.72e-41

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


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 154.83  E-value: 4.72e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  717 KRCVDKFDIIGI-IGEGTYGQVYKAKDKDTGEL--VALKKVrldnEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQ 793
Cdd:cd07868     12 ERVEDLFEYEGCkVGRGTYGHVYKAKRKDGKDDkdYALKQI----EGTGISMSACREIALLRELKHPNVISLQKVFLSHA 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  794 DAldfkkdkgAFYLVFEYMDHDLMGLLE--------SGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN 865
Cdd:cd07868     88 DR--------KVWLLFDYAEHDLWHIIKfhraskanKKPVQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 SRPYTNKV-------------------------ITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLE-- 918
Cdd:cd07868    160 EGPERGRVkiadmgfarlfnsplkpladldpvvVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQEdi 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  919 -------LAQLELISRLCGSPCPAVWPDVIKLPYFNTMkpKKQYRRRLREEFSFIP----------SAALDLLDHMLTLD 981
Cdd:cd07868    240 ktsnpyhHDQLDRIFNVMGFPADKDWEDIKKMPEHSTL--MKDFRRNTYTNCSLIKymekhkvkpdSKAFHLLQKLLTMD 317
                          330
                   ....*....|....*.
gi 1907082950  982 PSKRCTAEQTLQSDFL 997
Cdd:cd07868    318 PIKRITSEQAMQDPYF 333
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
703-993 6.12e-41

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


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 153.47  E-value: 6.12e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  703 PRYGERRQTESDWGKrcVDKFDIIGIIGEGTYGQVYKAKDKDTGELVA---LKKVRLDNEKegfpitaiREIKILRQLV- 778
Cdd:cd14132      2 PEYWDYENLNVEWGS--QDDYEIIRKIGRGKYSEVFEGINIGNNEKVVikvLKPVKKKKIK--------REIKILQNLRg 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  779 HQSVVNMKEIVTDKQdaldfkkdKGAFYLVFEYMDH-DLMGLLESglvhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIK 857
Cdd:cd14132     72 GPNIVKLLDVVKDPQ--------SKTPSLIFEYVNNtDFKTLYPT----LTDYDIRYYMYELLKALDYCHSKGIMHRDVK 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  858 CSNILLNNSR------------------PYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKK-PIFQANLE 918
Cdd:cd14132    140 PHNIMIDHEKrklrlidwglaefyhpgqEYNVRVASRYYKGPELLVDYQYYDYSLDMWSLGCMLASMIFRKePFFHGHDN 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  919 LAQLELISRLCGSpcpavwpDV---------IKLP-YFNTMKPKKQyRRRLReefSFIPSA--------ALDLLDHMLTL 980
Cdd:cd14132    220 YDQLVKIAKVLGT-------DDlyayldkygIELPpRLNDILGRHS-KKPWE---RFVNSEnqhlvtpeALDLLDKLLRY 288
                          330
                   ....*....|...
gi 1907082950  981 DPSKRCTAEQTLQ 993
Cdd:cd14132    289 DHQERITAKEAMQ 301
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
722-997 1.86e-40

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: 150.43  E-value: 1.86e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPItaIREIKILRQLVHQSVVNMKEIVTDKQDAldfkkd 801
Cdd:cd05122      1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESI--LNEIAILKKCKHPNIVKYYGSYLKKDEL------ 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 kgafYLVFEYMDH-DLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN---------------- 864
Cdd:cd05122     73 ----WIVMEFCSGgSLKDLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTsdgevklidfglsaql 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 NSRPYTNKVI-TLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISR--LCGSPCPAVWPDVI 941
Cdd:cd05122    149 SDGKTRNTFVgTPYWMAPEVIQG-KPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATngPPGLRNPKKWSKEF 227
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  942 KlpyfntmkpkkqyrrrlreefsfipsaalDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd05122    228 K-----------------------------DFLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
729-997 1.93e-40

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


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 152.53  E-value: 1.93e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGEL--VALKKVrldnEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQDAldfkkdkgAFY 806
Cdd:cd07867     10 VGRGTYGHVYKAKRKDGKDEkeYALKQI----EGTGISMSACREIALLRELKHPNVIALQKVFLSHSDR--------KVW 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVFEYMDHDLMGLLE--------SGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTNKV----- 873
Cdd:cd07867     78 LLFDYAEHDLWHIIKfhraskanKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPERGRVkiadm 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  874 --------------------ITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLE---------LAQLEL 924
Cdd:cd07867    158 gfarlfnsplkpladldpvvVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQEdiktsnpfhHDQLDR 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  925 ISRLCGSPCPAVWPDVIKLPYFNTMkpKKQYRRRLREEFSFIP----------SAALDLLDHMLTLDPSKRCTAEQTLQS 994
Cdd:cd07867    238 IFSVMGFPADKDWEDIRKMPEYPTL--QKDFRRTTYANSSLIKymekhkvkpdSKVFLLLQKLLTMDPTKRITSEQALQD 315

                   ...
gi 1907082950  995 DFL 997
Cdd:cd07867    316 PYF 318
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
729-1002 2.34e-40

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: 154.13  E-value: 2.34e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKV-----RLDNEKEGFpitaiREIKILRQLVHQSVVNMKEIVTDKQdaLDFKKDkg 803
Cdd:cd07853      8 IGYGAFGVVWSVTDPRDGKRVALKKMpnvfqNLVSCKRVF-----RELKMLCFFKHDNVLSALDILQPPH--IDPFEE-- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  804 aFYLVFEYMDHDLMGLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN------------------ 865
Cdd:cd07853     79 -IYVVTELMQSDLHKIIVSP-QPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSncvlkicdfglarveepd 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 -SRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSP--------CPAV 936
Cdd:cd07853    157 eSKHMTQEVVTQYYRAPEILMGSRHYTSAVDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLGTPsleamrsaCEGA 236
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  937 WPDVIKlpyfntMKPKKQYRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLKDVEL 1002
Cdd:cd07853    237 RAHILR------GPHKPPSLPVLYTLSSQATHEAVHLLCRMLVFDPDKRISAADALAHPYLDEGRL 296
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
723-998 2.25e-39

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: 147.24  E-value: 2.25e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALK-----KVRLDNEKEGFpitaIREIKILRQLVHQSVVNMkeivtdkqdaLD 797
Cdd:cd14007      2 FEIGKPLGKGKFGNVYLAREKKSGFIVALKvisksQLQKSGLEHQL----RREIEIQSHLRHPNILRL----------YG 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 FKKDKGAFYLVFEYMDH-DLMGLLESgLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL------------- 863
Cdd:cd14007     68 YFEDKKRIYLILEYAPNgELYKELKK-QKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLgsngelkladfgw 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  864 ----NNSRPYTnKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANlelaqlelisrlcgspcpavwpd 939
Cdd:cd14007    147 svhaPSNRRKT-FCGTLDYLPPEMVEGKE-YDYKVDIWSLGVLCYELLVGKPPFESK----------------------- 201
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  940 viklpyfntmKPKKQYRRRLREEFSF---IPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLK 998
Cdd:cd14007    202 ----------SHQETYKRIQNVDIKFpssVSPEAKDLISKLLQKDPSKRLSLEQVLNHPWIK 253
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
729-997 8.34e-39

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: 148.10  E-value: 8.34e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEI-VTDKQDaldfkkdkgaFYL 807
Cdd:cd07856     18 VGMGAFGLVCSARDQLTGQNVAVKKIMKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIfISPLED----------IYF 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYMDHDLMGLLESGLVHfsEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS---------------RPYTNK 872
Cdd:cd07856     88 VTELLGTDLHRLLTSRPLE--KQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENcdlkicdfglariqdPQMTGY 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  873 VITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPcPAvwpDVIK-LPYFNTMK- 950
Cdd:cd07856    166 VSTRYYRAPEIMLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELLGTP-PD---DVINtICSENTLRf 241
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  951 ----PKKQyRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd07856    242 vqslPKRE-RVPFSEKFKNADPDAIDLLEKMLVFDPKKRISAAEALAHPYL 291
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
721-992 6.26e-38

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: 146.34  E-value: 6.26e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQDALDFKK 800
Cdd:cd07877     17 ERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEFND 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 dkgaFYLVFEYMDHDLMGLLESGlvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN---------------N 865
Cdd:cd07877     97 ----VYLVTHLMGADLNNIVKCQ--KLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNedcelkildfglarhT 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 SRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDVIKLPY 945
Cdd:cd07877    171 DDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGAELLKKISSESA 250
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1907082950  946 FNTMKPKKQY-RRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTL 992
Cdd:cd07877    251 RNYIQSLTQMpKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQAL 298
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
722-998 2.64e-37

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: 141.58  E-value: 2.64e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGfpiTAIREIKILRQLVHQSVVNMkeivtdkqdaLDFKKD 801
Cdd:cd06614      1 LYKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQNKE---LIINEILIMKECKHPNIVDY----------YDSYLV 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 KGAFYLVFEYMDH-DLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN--------------- 865
Cdd:cd06614     68 GDELWVVMEYMDGgSLTDIITQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKdgsvkladfgfaaql 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 --SRPYTNKVI-TLWYRPPELLLGEErYTPAIDVWSCGCILgelftkkpifqanLELAQlelisrlcGSPcpavwpdvik 942
Cdd:cd06614    148 tkEKSKRNSVVgTPYWMAPEVIKRKD-YGPKVDIWSLGIMC-------------IEMAE--------GEP---------- 195
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  943 lPYFN----------TMK--PKKQYRRRLREEFsfipsaaLDLLDHMLTLDPSKRCTAEQTLQSDFLK 998
Cdd:cd06614    196 -PYLEepplralfliTTKgiPPLKNPEKWSPEF-------KDFLNKCLVKDPEKRPSAEELLQHPFLK 255
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
729-1008 4.76e-37

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: 143.65  E-value: 4.76e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQDALDFKKdkgaFYLV 808
Cdd:cd07878     23 VGSGAYGSVCSAYDTRLRQKVAVKKLSRPFQSLIHARRTYRELRLLKHMKHENVIGLLDVFTPATSIENFNE----VYLV 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDHDLMGLLEsgLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS---------------RPYTNKV 873
Cdd:cd07878     99 TNLMGADLNNIVK--CQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDcelrildfglarqadDEMTGYV 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  874 ITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDVIK---LPYFNTMK 950
Cdd:cd07878    177 ATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEVVGTPSPEVLKKISSehaRKYIQSLP 256
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  951 PKKQyrRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL---KDVELSKMAPP 1008
Cdd:cd07878    257 HMPQ--QDLKKIFRGANPLAIDLLEKMLVLDSDKRISASEALAHPYFsqyHDPEDEPEAEP 315
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
721-997 1.78e-35

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: 136.23  E-value: 1.78e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKV--RLDNEKEgfpITAIR-EIKILRQLVHQSVVNMkeivtdkQDALD 797
Cdd:cd14002      1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIpkRGKSEKE---LRNLRqEIEILRKLNHPNIIEM-------LDSFE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 FKKDkgaFYLVFEYMDHDLMGLLESGLVhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-----------S 866
Cdd:cd14002     71 TKKE---FVVVTEYAQGELFQILEDDGT-LPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKggvvklcdfgfA 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 RPYTNKVITL-------WYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANlelAQLELISRLCGSPCPavWPD 939
Cdd:cd14002    147 RAMSCNTLVLtsikgtpLYMAPE-LVQEQPYDHTADLWSLGCILYELFVGQPPFYTN---SIYQLVQMIVKDPVK--WPS 220
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  940 viklpyfnTMKPkkqyrrrlreEFSfipsaalDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14002    221 --------NMSP----------EFK-------SFLQGLLNKDPSKRLSWPDLLEHPFV 253
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
720-1182 2.23e-35

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 142.07  E-value: 2.23e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  720 VDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLD-----NEKEGFpitaIREIKILRQLVHQSVVNMkeivtdkqd 794
Cdd:COG0515      6 LGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPElaadpEARERF----RREARALARLNHPNIVRV--------- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  795 aLDFKKDKGAFYLVFEYMD-HDLMGLLESGLvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS-RPytnK 872
Cdd:COG0515     73 -YDVGEEDGRPYLVMEYVEgESLADLLRRRG-PLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDgRV---K 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  873 VI---------------------TLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANlelAQLELISRLCGS 931
Cdd:COG0515    148 LIdfgiaralggatltqtgtvvgTPGYMAPEQARG-EPVDPRSDVYSLGVTLYELLTGRPPFDGD---SPAELLRAHLRE 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  932 PCPavwpdviklpyfntmkPKKQYRRRLREEFSfipsaalDLLDHMLTLDPSKRCTAEQTLQSDfLKDVELSKMAPPDLP 1011
Cdd:COG0515    224 PPP----------------PPSELRPDLPPALD-------AIVLRALAKDPEERYQSAAELAAA-LRAVLRSLAAAAAAA 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950 1012 hwqdchELWSKKRRRQRQSGIVIEDPPPSKASRKETTSGTTAEPVKNNSPAPPQPAPVKAEPGPGDAVGLGDITQQLNQS 1091
Cdd:COG0515    280 ------AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAPAAAAAAAAAAAALAAAAAAAAAAAAAALLA 353
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950 1092 ELAVLLNLLQSQTDLSIPQMAQLLNIHSNPEMQQQLEALNQSISALTEASSQQQDSESIAPEESLKEVPSVPVVLPPAEQ 1171
Cdd:COG0515    354 AAAALAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAA 433
                          490
                   ....*....|.
gi 1907082950 1172 TTPEASNTPAD 1182
Cdd:COG0515    434 AAAAAAAAARL 444
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
722-997 4.73e-35

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: 135.36  E-value: 4.73e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLD--NEKEGFPITAirEIKILRQLVHQSVVNMKEIVTDKQDALdfk 799
Cdd:cd08217      1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGkmSEKEKQQLVS--EVNILRELKHPNIVRYYDRIVDRANTT--- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 kdkgaFYLVFEYMDH-DLMGLLESGLVH---FSEDHIKSFMKQLMEGLDYCHKKN-----FLHRDIKCSNILL---NN-- 865
Cdd:cd08217     76 -----LYIVMEYCEGgDLAQLIKKCKKEnqyIPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFLdsdNNvk 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 ------SRPYTNK-------VITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQANlelAQLELISRLCGSP 932
Cdd:cd08217    151 lgdfglARVLSHDssfaktyVGTPYYMSPELLN-EQSYDEKSDIWSLGCLIYELCALHPPFQAA---NQLELAKKIKEGK 226
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  933 CPAvwpdvikLPYfntmkpkkQYRRRLREefsfipsaaldLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd08217    227 FPR-------IPS--------RYSSELNE-----------VIKSMLNVDPDKRPSVEELLQLPLI 265
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
722-996 2.93e-34

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: 132.71  E-value: 2.93e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDN-EKEGFPITAIREIKILRQLVHQSVVNMkeivtdkqdaLDFKK 800
Cdd:cd14014      1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELaEDEEFRERFLREARALARLSHPNIVRV----------YDVGE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DKGAFYLVFEYMD-HDLMGLLESGLVhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN--------------- 864
Cdd:cd14014     71 DDGRPYIVMEYVEgGSLADLLRERGP-LPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTedgrvkltdfgiara 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 ---NSRPYTNKVI-TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANlelAQLELISRLCGSPCPAVWPDV 940
Cdd:cd14014    150 lgdSGLTQTGSVLgTPAYMAPEQARGGP-VDPRSDIYSLGVVLYELLTGRPPFDGD---SPAAVLAKHLQEAPPPPSPLN 225
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  941 IKLPyfntmkpkkqyrrrlreefsfipsAALD-LLDHMLTLDPSKRCTAEQTLQSDF 996
Cdd:cd14014    226 PDVP------------------------PALDaIILRALAKDPEERPQSAAELLAAL 258
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
722-993 4.24e-34

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 132.60  E-value: 4.24e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALK-----KVRL-DNEKEGFPitaiREIKILRQLVHQSVVNMKEIVTDKQDa 795
Cdd:cd14098      1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKqivkrKVAGnDKNLQLFQ----REINILKSLEHPGIVRLIDWYEDDQH- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  796 ldfkkdkgaFYLVFEYMDH-DLMG-LLESGLVhfSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTNKV 873
Cdd:cd14098     76 ---------IYLVMEYVEGgDLMDfIMAWGAI--PEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPVIVKI 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  874 I-------------------TLWYRPPELLLGEER-----YTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRlc 929
Cdd:cd14098    145 SdfglakvihtgtflvtfcgTMAYLAPEILMSKEQnlqggYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRK-- 222
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  930 GSPCpavwpdviklpyfntMKPKKQYRrrlreefsfIPSAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd14098    223 GRYT---------------QPPLVDFN---------ISEEAIDFILRLLDVDPEKRMTAAQALD 262
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
723-998 4.88e-34

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: 132.33  E-value: 4.88e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEgFPITAIREIKILRQLVHQSVVNMKEivtdkqdALDfkkDK 802
Cdd:cd06623      3 LERVKVLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEE-FRKQLLRELKTLRSCESPYVVKCYG-------AFY---KE 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 GAFYLVFEYMDhdlMGLLESGL---VHFSEDHIKSFMKQLMEGLDYCH-KKNFLHRDIKCSNILLN-------------- 864
Cdd:cd06623     72 GEISIVLEYMD---GGSLADLLkkvGKIPEPVLAYIARQILKGLDYLHtKRHIIHRDIKPSNLLINskgevkiadfgisk 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 ---NSRPYTNK-VITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAvWPDV 940
Cdd:cd06623    149 vleNTLDQCNTfVGTVTYMSPERIQGES-YSYAADIWSLGLTLLECALGKFPFLPPGQPSFFELMQAICDGPPPS-LPAE 226
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  941 IKLPYFNtmkpkkqyrrrlreefSFIpsaaldllDHMLTLDPSKRCTAEQTLQSDFLK 998
Cdd:cd06623    227 EFSPEFR----------------DFI--------SACLQKDPKKRPSAAELLQHPFIK 260
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
729-997 5.99e-33

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: 129.21  E-value: 5.99e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALK---KVRLDNEKEGF--------PITAI-REIKILRQLVHQSVVNMKEiVTDkqdal 796
Cdd:cd14008      1 LGRGSFGKVKLALDTETGQLYAIKifnKSRLRKRREGKndrgkiknALDDVrREIAIMKKLDHPNIVRLYE-VID----- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  797 DFKKDKgaFYLVFEYMDH-DLMGLLE-SGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN---------- 864
Cdd:cd14008     75 DPESDK--LYLVLEYCEGgPVMELDSgDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTadgtvkisdf 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 -------NSRPYTNKVI-TLWYRPPELLLGEERY--TPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRlcgSPCP 934
Cdd:cd14008    153 gvsemfeDGNDTLQKTAgTPAFLAPELCDGDSKTysGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQN---QNDE 229
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  935 AVWPDVIklpyfntmkpkkqyrrrlREEFSfipsaalDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14008    230 FPIPPEL------------------SPELK-------DLLRRMLEKDPEKRITLKEIKEHPWV 267
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
716-998 1.10e-32

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 130.52  E-value: 1.10e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  716 GKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRldnEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKqDA 795
Cdd:cd14226      8 GEKWMDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIK---NKKAFLNQAQIEVRLLELMNKHDTENKYYIVRLK-RH 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  796 LDFKkdkGAFYLVFEYMDHDLMGLLESglVHF---SEDHIKSFMKQLMEGLDYCHKK--NFLHRDIKCSNILLNN----- 865
Cdd:cd14226     84 FMFR---NHLCLVFELLSYNLYDLLRN--TNFrgvSLNLTRKFAQQLCTALLFLSTPelSIIHCDLKPENILLCNpkrsa 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 -------SRPYTNKVI-----TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPc 933
Cdd:cd14226    159 ikiidfgSSCQLGQRIyqyiqSRFYRSPEVLLGLP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGMP- 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  934 PAVWPD--------VIKLP----YFNTMKPKKQYR----RRLRE---------------EFSFIPSAAL---DLLDHMLT 979
Cdd:cd14226    237 PVHMLDqapkarkfFEKLPdgtyYLKKTKDGKKYKppgsRKLHEilgvetggpggrragEPGHTVEDYLkfkDLILRMLD 316
                          330
                   ....*....|....*....
gi 1907082950  980 LDPSKRCTAEQTLQSDFLK 998
Cdd:cd14226    317 YDPKTRITPAEALQHSFFK 335
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
725-997 1.23e-32

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 130.06  E-value: 1.23e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  725 IIGIIGEGTYGQVYKAKDKDTGELVALKKVRldNEKEGFPiTAIREIKILRQLvhqsvvNMKEIVTDKQ---DALDFKKD 801
Cdd:cd14212      3 VLDLLGQGTFGQVVKCQDLKTNKLVAVKVLK--NKPAYFR-QAMLEIAILTLL------NTKYDPEDKHhivRLLDHFMH 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 KGAFYLVFEYMDHDLMGLLESGLVH-FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTNKVI------ 874
Cdd:cd14212     74 HGHLCIVFELLGVNLYELLKQNQFRgLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDSPEIKLIdfgsac 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  875 ----TLW-------YRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSP----------- 932
Cdd:cd14212    154 fenyTLYtyiqsrfYRSPEVLLG-LPYSTAIDMWSLGCIAAELFLGLPLFPGNSEYNQLSRIIEMLGMPpdwmlekgknt 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  933 -----------CPAVW----------------------------PDVI-KLPYFNTMKPKKQYRRRLREEFsfipsaaLD 972
Cdd:cd14212    233 nkffkkvaksgGRSTYrlktpeefeaenncklepgkryfkyktlEDIImNYPMKKSKKEQIDKEMETRLAF-------ID 305
                          330       340
                   ....*....|....*....|....*
gi 1907082950  973 LLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14212    306 FLKGLLEYDPKKRWTPDQALNHPFI 330
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
721-997 1.46e-32

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 129.99  E-value: 1.46e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRlDNEK--EgfpiTAIREIKILRQLVHQSVVNMKEIVTdKQDALDF 798
Cdd:cd14134     12 NRYKILRLLGEGTFGKVLECWDRKRKRYVAVKIIR-NVEKyrE----AAKIEIDVLETLAEKDPNGKSHCVQ-LRDWFDY 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  799 kkdKGAFYLVFEymdhdLMG------LLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSR----- 867
Cdd:cd14134     86 ---RGHMCIVFE-----LLGpslydfLKKNNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDSDyvkvy 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  868 -PYTN-----------KVI-----TLW------------YRPPELLLGEERYTPAiDVWSCGCILGELFTKKPIFQ--AN 916
Cdd:cd14134    158 nPKKKrqirvpkstdiKLIdfgsaTFDdeyhssivstrhYRAPEVILGLGWSYPC-DVWSIGCILVELYTGELLFQthDN 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  917 LElaQLELISRLCGsPCPAVW----PDVIKLPYFNTMK---------------PKKQYRRRLREEFSFIPSaALDLLDHM 977
Cdd:cd14134    237 LE--HLAMMERILG-PLPKRMirraKKGAKYFYFYHGRldwpegsssgrsikrVCKPLKRLMLLVDPEHRL-LFDLIRKM 312
                          330       340
                   ....*....|....*....|
gi 1907082950  978 LTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14134    313 LEYDPSKRITAKEALKHPFF 332
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
729-993 4.68e-31

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: 123.49  E-value: 4.68e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFpITAIR-EIKILRQLVHQSVVnmKEIvtdkqdalDFKKDKGAFYL 807
Cdd:cd06627      8 IGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSD-LKSVMgEIDLLKKLNHPNIV--KYI--------GSVKTKDSLYI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYMDhdlMGLLESGLV---HFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNIL-----------------LNNSR 867
Cdd:cd06627     77 ILEYVE---NGSLASIIKkfgKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILttkdglvkladfgvatkLNEVE 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  868 PYTNKVI-TLWYRPPELLLGEERYTpAIDVWSCGCILGELFTKKPIFqanLELAQLELISRLCGSPCPAVwpdviklpyf 946
Cdd:cd06627    154 KDENSVVgTPYWMAPEVIEMSGVTT-ASDIWSVGCTVIELLTGNPPY---YDLQPMAALFRIVQDDHPPL---------- 219
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1907082950  947 ntmkPKKqyrrrlreefsfIPSAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd06627    220 ----PEN------------ISPELRDFLLQCFQKDPTLRPSAKELLK 250
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
722-997 1.03e-29

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


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 122.12  E-value: 1.03e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRldnEKEGFPITAIREIKILRQLVHQ------SVVNMKEIVTdkqda 795
Cdd:cd14225     44 RYEILEVIGKGSFGQVVKALDHKTNEHVAIKIIR---NKKRFHHQALVEVKILDALRRKdrdnshNVIHMKEYFY----- 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  796 ldFKKDkgaFYLVFEYMDHDLMGLLE-SGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTNKVI 874
Cdd:cd14225    116 --FRNH---LCITFELLGMNLYELIKkNNFQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQSSIKVI 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  875 TL-----------------WYRPPELLLGEeRYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVW 937
Cdd:cd14225    191 DFgsscyehqrvytyiqsrFYRSPEVILGL-PYSMAIDMWSLGCILAELYTGYPLFPGENEVEQLACIMEVLGLPPPELI 269
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  938 PDVIKLPYF--------NTMKPKKQYRRRLREEFSFIPSAA----LDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14225    270 ENAQRRRLFfdskgnprCITNSKGKKRRPNSKDLASALKTSdplfLDFIRRCLEWDPSKRMTPDEALQHEWI 341
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
723-997 1.05e-29

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: 119.68  E-value: 1.05e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFpitaIREIKILRQLVHQSVVnmkeivtdKQDALDFKKDK 802
Cdd:cd06612      5 FDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQEI----IKEISILKQCDSPYIV--------KYYGSYFKNTD 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 gaFYLVFEYMD----HDLMGLLESGLvhfSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN-------------- 864
Cdd:cd06612     73 --LWIVMEYCGagsvSDIMKITNKTL---TEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNeegqakladfgvsg 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 ---NSRPYTNKVI-TLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPifqanlelaqlelisrlcgspcpavwpdv 940
Cdd:cd06612    148 qltDTMAKRNTVIgTPFWMAPEVIQ-EIGYNNKADIWSLGITAIEMAEGKP----------------------------- 197
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  941 iklPYFNT-------MKPKKQyRRRLRE------EFSfipsaalDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd06612    198 ---PYSDIhpmraifMIPNKP-PPTLSDpekwspEFN-------DFVKKCLVKDPEERPSAIQLLQHPFI 256
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
725-997 1.52e-29

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: 119.21  E-value: 1.52e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  725 IIGI-IGEGTYGQVYKA--KDKDTGELVALK----KVRLDNEKEGF-PitaiREIKILRQLVHQSVVNMKEIVtdkqdal 796
Cdd:cd14080      3 RLGKtIGEGSYSKVKLAeyTKSGLKEKVACKiidkKKAPKDFLEKFlP----RELEILRKLRHPNIIQVYSIF------- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  797 dfkKDKGAFYLVFEYMDH-DLmglLESGLVH--FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLnnSRPYTNKV 873
Cdd:cd14080     72 ---ERGSKVFIFMEYAEHgDL---LEYIQKRgaLSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILL--DSNNNVKL 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  874 I----------------------TLWYRPPELLLGEErYTPAI-DVWSCGCIlgeLFTkkpifqanlelaqlelisRLCG 930
Cdd:cd14080    144 SdfgfarlcpdddgdvlsktfcgSAAYAAPEILQGIP-YDPKKyDIWSLGVI---LYI------------------MLCG 201
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  931 SpcpavwpdvikLPyFNTMKPKKQYRRRLREEFSF------IPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14080    202 S-----------MP-FDDSNIKKMLKDQQNRKVRFpssvkkLSPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
707-1000 3.94e-29

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 122.45  E-value: 3.94e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  707 ERRQTESDWGKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDnekegfPITAIREIKILRQLVHQSVVNMK 786
Cdd:PTZ00036    52 EEKMIDNDINRSPNKSYKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVLQD------PQYKNRELLIMKNLNHINIIFLK 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  787 EIVTDKQdaldFKKDKGAFYL--VFEYMDHDLMGLLEsglvHFSEDH-------IKSFMKQLMEGLDYCHKKNFLHRDIK 857
Cdd:PTZ00036   126 DYYYTEC----FKKNEKNIFLnvVMEFIPQTVHKYMK----HYARNNhalplflVKLYSYQLCRALAYIHSKFICHRDLK 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  858 CSNILLNnSRPYTNK-------------------VITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLE 918
Cdd:PTZ00036   198 PQNLLID-PNTHTLKlcdfgsaknllagqrsvsyICSRFYRAPELMLGATNYTTHIDLWSLGCIIAEMILGYPIFSGQSS 276
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  919 LAQLELISRLCGSPCpavwPDVIKL--PYFNTMKPKKQYRRRLREEF-SFIPSAALDLLDHMLTLDPSKRCTAEQTLQSD 995
Cdd:PTZ00036   277 VDQLVRIIQVLGTPT----EDQLKEmnPNYADIKFPDVKPKDLKKVFpKGTPDDAINFISQFLKYEPLKRLNPIEALADP 352

                   ....*
gi 1907082950  996 FLKDV 1000
Cdd:PTZ00036   353 FFDDL 357
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
721-997 5.50e-29

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


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 117.32  E-value: 5.50e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDT-------GELVALKKVRLDNEkegfPITAIREIKILRQLVHQS-VVNMKEIVTDK 792
Cdd:cd14019      1 NKYRIIEKIGEGTFSSVYKAEDKLHdlydrnkGRLVALKHIYPTSS----PSRILNELECLERLGGSNnVSGLITAFRNE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  793 QDALdfkkdkgafyLVFEYMDHD-------LMGLLEsglvhfsedhIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN- 864
Cdd:cd14019     77 DQVV----------AVLPYIEHDdfrdfyrKMSLTD----------IRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNr 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 ----------------NSRP--YTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTK-KPIFQANLELAQLELI 925
Cdd:cd14019    137 etgkgvlvdfglaqreEDRPeqRAPRAGTRGFRAPEVLFKCPHQTTAIDIWSAGVILLSILSGrFPFFFSSDDIDALAEI 216
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  926 SRLCGSPcpavwpdviklpyfntmkpkkqyrrrlreefsfipsAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14019    217 ATIFGSD------------------------------------EAYDLLDKLLELDPSKRITAEEALKHPFF 252
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
728-908 6.95e-29

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 117.25  E-value: 6.95e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950   728 IIGEGTYGQVYKAK----DKDTGELVALKKVRLD---NEKEGFpitaIREIKILRQLVHQSVVNMKEIVTDKQdaldfkk 800
Cdd:smart00219    6 KLGEGAFGEVYKGKlkgkGGKKKVEVAVKTLKEDaseQQIEEF----LREARIMRKLDHPNVVKLLGVCTEEE------- 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950   801 dkgAFYLVFEYMDH-DLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-----------SRP 868
Cdd:smart00219   75 ---PLYIVMEYMEGgDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGEnlvvkisdfglSRD 151
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*....
gi 1907082950   869 YTNKVITL---------WYrPPELLLgEERYTPAIDVWSCGCILGELFT 908
Cdd:smart00219  152 LYDDDYYRkrggklpirWM-APESLK-EGKFTSKSDVWSFGVLLWEIFT 198
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
723-998 1.04e-28

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: 117.32  E-value: 1.04e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALK---KVRLDNEKEGFpiTAIREIKILRQLVHQSVVNMkeivtdkqdALDFk 799
Cdd:cd05581      3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKvldKRHIIKEKKVK--YVTIEKEVLSRLAHPGIVKL---------YYTF- 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 KDKGAFYLVFEYMDH-DLMGLLESgLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL--------------- 863
Cdd:cd05581     71 QDESKLYFVLEYAPNgDLLEYIRK-YGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLdedmhikitdfgtak 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  864 ---NNSRPYTNK-----------------VITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLE 923
Cdd:cd05581    150 vlgPDSSPESTKgdadsqiaynqaraasfVGTAEYVSPE-LLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQ 228
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  924 LISRLCgspcpAVWPDviklpyfntmkpkkqyrrrlreefsFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLK 998
Cdd:cd05581    229 KIVKLE-----YEFPE-------------------------NFPPDAKDLIQKLLVLDPSKRLGVNENGGYDELK 273
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
729-985 1.14e-28

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: 116.46  E-value: 1.14e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPI-TAIREIKILRQLVHQSVVNMKeivtdkqdaLDFKkDKGAFYL 807
Cdd:cd05123      1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVeHTLNERNILERVNHPFIVKLH---------YAFQ-TEEKLYL 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYMDH-DLMGLLESgLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN-------------------NSR 867
Cdd:cd05123     71 VLDYVPGgELFSHLSK-EGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDsdghikltdfglakelssdGDR 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  868 PYTnKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANlelaqlelisrlcgspcpavwpdviklpyfn 947
Cdd:cd05123    150 TYT-FCGTPEYLAPEVLLGKG-YGKAVDWWSLGVLLYEMLTGKPPFYAE------------------------------- 196
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1907082950  948 tmKPKKQYRRRLREEFSF---IPSAALDLLDHMLTLDPSKR 985
Cdd:cd05123    197 --NRKEIYEKILKSPLKFpeyVSPEAKSLISGLLQKDPTKR 235
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
729-943 2.57e-28

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: 115.40  E-value: 2.57e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLD--NEK--EGFpitaIREIKILRQLVHQSVVNMkeivtdkqdaLDFKKDKGA 804
Cdd:cd14009      1 IGRGSFATVWKGRHKQTGEVVAIKEISRKklNKKlqENL----ESEIAILKSIKHPNIVRL----------YDVQKTEDF 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  805 FYLVFEYMD-HDLmglleSGLVH----FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLnnSRPYTNKVI----- 874
Cdd:cd14009     67 IYLVLEYCAgGDL-----SQYIRkrgrLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLL--STSGDDPVLkiadf 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  875 -------------TL----WYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCG----SPC 933
Cdd:cd14009    140 gfarslqpasmaeTLcgspLYMAPEILQF-QKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDAvipfPIA 218
                          250
                   ....*....|
gi 1907082950  934 PAVWPDVIKL 943
Cdd:cd14009    219 AQLSPDCKDL 228
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
729-914 2.74e-28

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: 114.94  E-value: 2.74e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKdtGELVALKKVRLDNE----KEGFpitaIREIKILRQLVHQSVVNMKEIVTDKQDaldfkkdkga 804
Cdd:cd13999      1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDndelLKEF----RREVSILSKLRHPNIVQFIGACLSPPP---------- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  805 FYLVFEYMDH-DLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSrpYTNKVI--------- 874
Cdd:cd13999     65 LCIVTEYMPGgSLYDLLHKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDEN--FTVKIAdfglsrikn 142
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  875 -----------TLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQ 914
Cdd:cd13999    143 sttekmtgvvgTPRWMAPEVLRG-EPYTEKADVYSFGIVLWELLTGEVPFK 192
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
723-994 3.15e-28

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: 115.20  E-value: 3.15e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTdkqdaldfkkDK 802
Cdd:cd08529      2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFV----------DK 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 GAFYLVFEYMDH-DLMGLLESGLVH-FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNI-----------------LL 863
Cdd:cd08529     72 GKLNIVMEYAENgDLHSLIKSQRGRpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIfldkgdnvkigdlgvakIL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  864 NNSRPYTNKVI-TLWYRPPELLlgEER-YTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAvwpdvi 941
Cdd:cd08529    152 SDTTNFAQTIVgTPYYLSPELC--EDKpYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPPISA------ 223
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  942 klPYfntmkpkkqyrrrlreefsfipSAAL-DLLDHMLTLDPSKRCTAEQTLQS 994
Cdd:cd08529    224 --SY----------------------SQDLsQLIDSCLTKDYRQRPDTTELLRN 253
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
729-997 1.14e-27

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 113.80  E-value: 1.14e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDN-EKEGFPITAIREIKILRQLVHQSVVNMKeivtdkqdalDFKKDKGAFYL 807
Cdd:cd14099      9 LGKGGFAKCYEVTDMSTGKVYAGKVVPKSSlTKPKQREKLKSEIKIHRSLKHPNIVKFH----------DCFEDEENVYI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYMDH-DLMGLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS-------------------R 867
Cdd:cd14099     79 LLELCSNgSLMELLKRR-KALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENmnvkigdfglaarleydgeR 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  868 PYT-----NkvitlwYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQAnlelaqlelisrlcgspcpavwPDVik 942
Cdd:cd14099    158 KKTlcgtpN------YIAPEVLEKKKGHSFEVDIWSLGVILYTLLVGKPPFET----------------------SDV-- 207
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  943 lpyfntmkpKKQYRRRLREEFSF-----IPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14099    208 ---------KETYKRIKKNEYSFpshlsISDEAKDLIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
723-993 2.29e-27

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: 112.81  E-value: 2.29e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMkeivtdkqdaLDFKKDK 802
Cdd:cd14069      3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDCPENIKKEVCIQKMLSHKNVVRF----------YGHRREG 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 GAFYLVFEYMDH-DLMGLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS--------------- 866
Cdd:cd14069     73 EFQYLFLEYASGgELFDKIEPD-VGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENdnlkisdfglatvfr 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 -----RPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCIL-----GELFTKKPIfqanlelaqlelisrlcgSPCPAv 936
Cdd:cd14069    152 ykgkeRLLNKMCGTLPYVAPELLAKKKYRAEPVDVWSCGIVLfamlaGELPWDQPS------------------DSCQE- 212
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  937 wpdviklpYFNTMKPKKQYRRrlreEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd14069    213 --------YSDWKENKKTYLT----PWKKIDTAALSLLRKILTENPNKRITIEDIKK 257
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
728-908 3.15e-27

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: 112.26  E-value: 3.15e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950   728 IIGEGTYGQVYKAK----DKDTGELVALKKVRLD---NEKEGFpitaIREIKILRQLVHQSVVNMKEIVTDKQdaldfkk 800
Cdd:smart00221    6 KLGEGAFGEVYKGTlkgkGDGKEVEVAVKTLKEDaseQQIEEF----LREARIMRKLDHPNIVKLLGVCTEEE------- 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950   801 dkgAFYLVFEYMDH-DLMG-LLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-----------SR 867
Cdd:smart00221   75 ---PLMIVMEYMPGgDLLDyLRKNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGEnlvvkisdfglSR 151
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|
gi 1907082950   868 PYTNKVITL---------WYrPPELLLgEERYTPAIDVWSCGCILGELFT 908
Cdd:smart00221  152 DLYDDDYYKvkggklpirWM-APESLK-EGKFTSKSDVWSFGVLLWEIFT 199
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
728-997 5.26e-27

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: 112.09  E-value: 5.26e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVRL-------DNEKEGFPITAIR-EIKILRQLVHQSVVNMkeivtdkqdaLDFK 799
Cdd:cd06629      8 LIGKGTYGRVYLAMNATTGEMLAVKQVELpktssdrADSRQKTVVDALKsEIDTLKDLDHPNIVQY----------LGFE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 KDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL---------------- 863
Cdd:cd06629     78 ETEDYFSIFLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVdlegickisdfgiskk 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  864 -----NNSRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFT-KKP-----IFQANLELAQLelisrlcgSP 932
Cdd:cd06629    158 sddiyGNNGATSMQGSVFWMAPEVIHSQGQGYSAKVDIWSLGCVVLEMLAgRRPwsddeAIAAMFKLGNK--------RS 229
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  933 CPAVWPDVIklpyfntmkpkkqyrrrlreefsfIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd06629    230 APPVPEDVN------------------------LSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
729-1012 7.61e-27

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: 113.28  E-value: 7.61e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQDALDFKKdkgaFYLV 808
Cdd:cd07850      8 IGSGAQGIVCAAYDTVTGQNVAIKKLSRPFQNVTHAKRAYRELVLMKLVNHKNIIGLLNVFTPQKSLEEFQD----VYLV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDHDLMGLLESGLVHfseDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN-----------------NSRPYTN 871
Cdd:cd07850     84 MELMDANLCQVIQMDLDH---ERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKsdctlkildfglartagTSFMMTP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  872 KVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPC--------PAVWPDVIKL 943
Cdd:cd07850    161 YVVTRYYRAPEVILGMG-YKENVDIWSVGCIMGEMIRGTVLFPGTDHIDQWNKIIEQLGTPSdefmsrlqPTVRNYVENR 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  944 PY-----FNTMKPKKQYRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLK------DVElskmAPPDLPH 1012
Cdd:cd07850    240 PKyagysFEELFPDVLFPPDSEEHNKLKASQARDLLSKMLVIDPEKRISVDDALQHPYINvwydpsEVE----APPPAPY 315
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
721-997 8.56e-27

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 111.72  E-value: 8.56e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKV---------RLDNEKegfPITAIREIKILRQLVHQSVVNMKEIVtD 791
Cdd:cd14084      6 KKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIInkrkftigsRREINK---PRNIETEIEILKKLSHPCIIKIEDFF-D 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  792 KQDAldfkkdkgaFYLVFEYMDH-DLMGLLESGLvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYT 870
Cdd:cd14084     82 AEDD---------YYIVLELMEGgELFDRVVSNK-RLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEEC 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  871 ---------NKVI-----------TLWYRPPELLL--GEERYTPAIDVWSCGCILgelFTKkpifqanlelaqlelisrL 928
Cdd:cd14084    152 likitdfglSKILgetslmktlcgTPTYLAPEVLRsfGTEGYTRAVDCWSLGVIL---FIC------------------L 210
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  929 CGSPcpavwpdviklPY---FNTMKPKKQYrrrLREEFSFIPSA-------ALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14084    211 SGYP-----------PFseeYTQMSLKEQI---LSGKYTFIPKAwknvseeAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
729-997 2.19e-26

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 109.80  E-value: 2.19e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEkEGFPITAI----REIKILRQLVHQSVVNMkeivtdkqdaLDFKKDKGA 804
Cdd:cd06632      8 LGSGSFGSVYEGFNGDTGDFFAVKEVSLVDD-DKKSRESVkqleQEIALLSKLRHPNIVQY----------YGTEREEDN 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  805 FYLVFEYMDhdlMGLLESgLVH----FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNnsrpyTNKVITL---- 876
Cdd:cd06632     77 LYIFLEYVP---GGSIHK-LLQrygaFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVD-----TNGVVKLadfg 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  877 -------------------WYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQanlELAQLELISRLCGSPCPAVW 937
Cdd:cd06632    148 makhveafsfaksfkgspyWMAPEVIMQKNSGYGLAVDIWSLGCTVLEMATGKPPWS---QYEGVAAIFKIGNSGELPPI 224
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  938 PDviklpyfnTMKPKkqyrrrlreefsfipsaALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd06632    225 PD--------HLSPD-----------------AKDFIRLCLQRDPEDRPTASQLLEHPFV 259
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
729-997 2.24e-26

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 110.09  E-value: 2.24e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELV--ALKKVR--LDNEKEG-FPITAIREIKILRQLVHQSVVNmkeivtdkqdALD-FKKDK 802
Cdd:cd13994      1 IGKGATSVVRIVTKKNPRSGVlyAVKEYRrrDDESKRKdYVKRLTSEYIISSKLHHPNIVK----------VLDlCQDLH 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 GAFYLVFEYMDH-DLMGLLESGLvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL------------------ 863
Cdd:cd13994     71 GKWCLVMEYCPGgDLFTLIEKAD-SLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLdedgvlkltdfgtaevfg 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  864 ---NNSRPYTNKVI-TLWYRPPELLLGEErYTP-AIDVWSCGCILGELFTKKPIFQAnlelaqlelisrlcgspcpAVWP 938
Cdd:cd13994    150 mpaEKESPMSAGLCgSEPYMAPEVFTSGS-YDGrAVDVWSCGIVLFALFTGRFPWRS-------------------AKKS 209
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  939 DVIKLPYfntMKPKKQYRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd13994    210 DSAYKAY---EKSGDFTNGPYEPIENLLPSECRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
729-1001 4.43e-26

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 109.61  E-value: 4.43e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKV------------RLDNEKEgfpitaireikILRQLVHQSVVNMKEIVTDKQDal 796
Cdd:cd05579      1 ISRGAYGRVYLAKKKSTGDLYAIKVIkkrdmirknqvdSVLAERN-----------ILSQAQNPFVVKLYYSFQGKKN-- 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  797 dfkkdkgaFYLVFEYMDH-DLMGLLESgLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN---------- 865
Cdd:cd05579     68 --------LYLVMEYLPGgDLYSLLEN-VGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDAnghlkltdfg 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 -SR---------------------PYTNKVI-TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANlelAQL 922
Cdd:cd05579    139 lSKvglvrrqiklsiqkksngapeKEDRRIVgTPDYLAPEILLGQG-HGKTVDWWSLGVILYEFLVGIPPFHAE---TPE 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  923 ELISRLCGSPCPavWPDVIKLPYfntmkpkkqyrrrlreefsfipsAALDLLDHMLTLDPSKR---CTAEQTLQSDFLKD 999
Cdd:cd05579    215 EIFQNILNGKIE--WPEDPEVSD-----------------------EAKDLISKLLTPDPEKRlgaKGIEEIKNHPFFKG 269

                   ..
gi 1907082950 1000 VE 1001
Cdd:cd05579    270 ID 271
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
728-997 4.82e-26

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: 109.16  E-value: 4.82e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVRLDN------EKEGFPITAI-REIKILRQLVHQSVVNMkeivtdkqdaLDFKK 800
Cdd:cd06628      7 LIGSGSFGSVYLGMNASSGELMAVKQVELPSvsaenkDRKKSMLDALqREIALLRELQHENIVQY----------LGSSS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS------------RP 868
Cdd:cd06628     77 DANHLNIFLEYVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKggikisdfgiskKL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  869 YTNKVIT------------LWYRPPELLlGEERYTPAIDVWSCGCILGELFTKKPIFQanlELAQLELISRLCGSPCPAV 936
Cdd:cd06628    157 EANSLSTknngarpslqgsVFWMAPEVV-KQTSYTRKADIWSLGCLVVEMLTGTHPFP---DCTQMQAIFKIGENASPTI 232
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  937 WPDviklpyfntmkpkkqyrrrlreefsfIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd06628    233 PSN--------------------------ISSEARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
728-997 5.11e-26

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: 108.93  E-value: 5.11e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVRL-DNEKEGFPITAiREIKILRQLVHQSVVnmkeivtdKQDALDFKKDKgaFY 806
Cdd:cd06626      7 KIGEGTFGKVYTAVNLDTGELMAMKEIRFqDNDPKTIKEIA-DEMKVLEGLDHPNLV--------RYYGVEVHREE--VY 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVFEYMDH-DLMGLLESGLVhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL------------------NNSR 867
Cdd:cd06626     76 IFMEYCQEgTLEELLRHGRI-LDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLdsngliklgdfgsavklkNNTT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  868 PYT-----NKVITLWYRPPELLLGEER--YTPAIDVWSCGCILGELFT-KKPIFQANLELAqlelISRLCGSPCPAVWPD 939
Cdd:cd06626    155 TMApgevnSLVGTPAYMAPEVITGNKGegHGRAADIWSLGCVVLEMATgKRPWSELDNEWA----IMYHVGMGHKPPIPD 230
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  940 viklpyfntmkpkkqyrrrlREEFSfipSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd06626    231 --------------------SLQLS---PEGKDFLSRCLESDPKKRPTASELLDHPFI 265
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
723-997 5.66e-26

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 109.23  E-value: 5.66e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDtGELVALKKVRLDN----EKEGFpitaIREIKILRQLVHQS-VVNMKEI-VTDKQDAL 796
Cdd:cd14131      3 YEILKQLGKGGSSKVYKVLNPK-KKIYALKRVDLEGadeqTLQSY----KNEIELLKKLKGSDrIIQLYDYeVTDEDDYL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  797 dfkkdkgafYLVFEYMDHDLMGLLESGLVH-FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL------------ 863
Cdd:cd14131     78 ---------YMVMECGEIDLATILKKKRPKpIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLvkgrlklidfgi 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  864 -NNSRPYT------NKVITLWYRPPELLL-------GEERY--TPAIDVWSCGCILGELFTKKPIFQanlelaQL-ELIS 926
Cdd:cd14131    149 aKAIQNDTtsivrdSQVGTLNYMSPEAIKdtsasgeGKPKSkiGRPSDVWSLGCILYQMVYGKTPFQ------HItNPIA 222
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  927 RLCGSPCPAVwpdVIKLPyfntmkpkkqyrrrlreefSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14131    223 KLQAIIDPNH---EIEFP-------------------DIPNPDLIDVMKRCLQRDPKKRPSIPELLNHPFL 271
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
722-934 8.13e-26

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


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 111.38  E-value: 8.13e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRldNEKEgFPITAIREIKILRQLVHQSVVNMKEIVtdkqDALDFKKD 801
Cdd:cd14224     66 RYEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVR--NEKR-FHRQAAEEIRILEHLKKQDKDNTMNVI----HMLESFTF 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 KGAFYLVFEYMDHDLMGLLE-SGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL----------------- 863
Cdd:cd14224    139 RNHICMTFELLSMNLYELIKkNKFQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLkqqgrsgikvidfgssc 218
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  864 -NNSRPYTnKVITLWYRPPELLLGEeRYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCP 934
Cdd:cd14224    219 yEHQRIYT-YIQSRFYRAPEVILGA-RYGMPIDMWSFGCILAELLTGYPLFPGEDEGDQLACMIELLGMPPQ 288
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
729-997 1.23e-25

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: 107.72  E-value: 1.23e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKV-RLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQDaldfkkdkgaFYL 807
Cdd:cd14081      9 LGKGQTGLVKLAKHCVTGQKVAIKIVnKEKLSKESVLMKVEREIAIMKLIEHPNVLKLYDVYENKKY----------LYL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYM-DHDLMG-LLESGlvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSR-------------PYTNK 872
Cdd:cd14081     79 VLEYVsGGELFDyLVKKG--RLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNnikiadfgmaslqPEGSL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  873 VIT----LWYRPPELLLGEERYTPAIDVWSCGCILGELFTKK-PIFQANLElaqlELISRLCgspcpavwpdviklpyfn 947
Cdd:cd14081    157 LETscgsPHYACPEVIKGEKYDGRKADIWSCGVILYALLVGAlPFDDDNLR----QLLEKVK------------------ 214
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  948 tmkpkkqyrrrlREEF---SFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14081    215 ------------RGVFhipHFISPDAQDLLRRMLEVNPEKRITIEEIKKHPWF 255
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
722-918 1.37e-25

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: 107.82  E-value: 1.37e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLD--NEKEGFPI---TAIREIKILRQL-VHQSVVNMkeivtdkqda 795
Cdd:cd13993      1 RYQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSgpNSKDGNDFqklPQLREIDLHRRVsRHPNIITL---------- 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  796 LDFKKDKGAFYLVFEYMDH-DLM-GLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS------- 866
Cdd:cd13993     71 HDVFETEVAIYIVLEYCPNgDLFeAITENRIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDegtvklc 150
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  867 ---------RPYTNKVITLWYRPPELL-----LGEERYTPAIDVWSCG-CILGELFTKKPIFQANLE 918
Cdd:cd13993    151 dfglattekISMDFGVGSEFYMAPECFdevgrSLKGYPCAAGDIWSLGiILLNLTFGRNPWKIASES 217
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
716-994 3.02e-25

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: 106.99  E-value: 3.02e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  716 GKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLdNEKEGFPITAIREIKILRQLVHQSVVN-----MKEIVt 790
Cdd:cd13996      1 NSRYLNDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRL-TEKSSASEKVLREVKALAKLNHPNIVRyytawVEEPP- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  791 dkqdaldfkkdkgaFYLVFEYMD-HDLMGLLESGLVHFSEDH--IKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL---- 863
Cdd:cd13996     79 --------------LYIQMELCEgGTLRDWIDRRNSSSKNDRklALELFKQILKGVSYIHSKGIVHRDLKPSNIFLdndd 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  864 -----------------------------NNSRPYTNKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKkpiFQ 914
Cdd:cd13996    145 lqvkigdfglatsignqkrelnnlnnnnnGNTSNNSVGIGTPLYASPEQLDGEN-YNEKADIYSLGIILFEMLHP---FK 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  915 ANLELAQlelisrlcgspcpaVWPDV--IKLPYFNTMKPKKQYrrrlreefsfipsaalDLLDHMLTLDPSKRCTAEQTL 992
Cdd:cd13996    221 TAMERST--------------ILTDLrnGILPESFKAKHPKEA----------------DLIQSLLSKNPEERPSAEQLL 270

                   ..
gi 1907082950  993 QS 994
Cdd:cd13996    271 RS 272
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
728-908 1.30e-24

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: 104.93  E-value: 1.30e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAK---DKDTGELVALKKVRLD---NEKEGFpitaIREIKILRQLVHQSVVNMKEIVTDKQDaldfkkd 801
Cdd:cd00192      2 KLGEGAFGEVYKGKlkgGDGKTVDVAVKTLKEDaseSERKDF----LKEARVMKKLGHPNVVRLLGVCTEEEP------- 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 kgaFYLVFEYMDH-DLMGLL--------ESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN------- 865
Cdd:cd00192     71 ---LYLVMEYMEGgDLLDFLrksrpvfpSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEdlvvkis 147
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  866 ----SRPYTN----------KVITLWYrPPELLLgEERYTPAIDVWSCGCILGELFT 908
Cdd:cd00192    148 dfglSRDIYDddyyrkktggKLPIRWM-APESLK-DGIFTSKSDVWSFGVLLWEIFT 202
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
720-997 1.42e-24

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 105.08  E-value: 1.42e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  720 VDKFDIIGIIGEGTYGQVYKAKDKDTGELVALK--KVRLDNEKEgfpITAirEIKILRQLVHQsvvnmkEIVTDKQDALd 797
Cdd:cd06608      5 AGIFELVEVIGEGTYGKVYKARHKKTGQLAAIKimDIIEDEEEE---IKL--EINILRKFSNH------PNIATFYGAF- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 FKKDK----GAFYLVFEYMDH----DLM-GLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN--- 865
Cdd:cd06608     73 IKKDPpggdDQLWLVMEYCGGgsvtDLVkGLRKKG-KRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEeae 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 --------SRPYTNKVI-------TLWYRPPELLLGEERYTPAI----DVWSCGCILGELFTKKPIFQANLELAQLELIS 926
Cdd:cd06608    152 vklvdfgvSAQLDSTLGrrntfigTPYWMAPEVIACDQQPDASYdarcDVWSLGITAIELADGKPPLCDMHPMRALFKIP 231
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  927 RlcgSPCPavwpdviklpyfnTMKPKKQYRRRLReefsfipsaalDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd06608    232 R---NPPP-------------TLKSPEKWSKEFN-----------DFISECLIKNYEQRPFTEELLEHPFI 275
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
729-997 3.14e-24

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: 106.33  E-value: 3.14e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQDALDFKKdkgaFYLV 808
Cdd:cd07874     25 IGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKSLEEFQD----VYLV 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDHDLMGLLESGLVHfseDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-----------------SRPYTN 871
Cdd:cd07874    101 MELMDANLCQVIQMELDH---ERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSdctlkildfglartagtSFMMTP 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  872 KVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPC--------PAVWPDVIKL 943
Cdd:cd07874    178 YVVTRYYRAPEVILGMG-YKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCpefmkklqPTVRNYVENR 256
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  944 PYFNTMKPKKQYRRRL----REEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd07874    257 PKYAGLTFPKLFPDSLfpadSEHNKLKASQARDLLSKMLVIDPAKRISVDEALQHPYI 314
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
729-1010 4.06e-24

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: 105.88  E-value: 4.06e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQDALDFKKdkgaFYLV 808
Cdd:cd07876     29 IGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKSLEEFQD----VYLV 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDHDLMGLLESGLVHfseDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS--------------------RP 868
Cdd:cd07876    105 MELMDANLCQVIHMELDH---ERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDctlkildfglartactnfmmTP 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  869 YtnkVITLWYRPPELLLGEeRYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPC--------PAVWPDV 940
Cdd:cd07876    182 Y---VVTRYYRAPEVILGM-GYKENVDIWSVGCIMGELVKGSVIFQGTDHIDQWNKVIEQLGTPSaefmnrlqPTVRNYV 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  941 IKLPYFNTMK----------PKKQYRRRLREefsfipSAALDLLDHMLTLDPSKRCTAEQTLQSDFLK---DVELSKMAP 1007
Cdd:cd07876    258 ENRPQYPGISfeelfpdwifPSESERDKLKT------SQARDLLSKMLVIDPDKRISVDEALRHPYITvwyDPAEAEAPP 331

                   ...
gi 1907082950 1008 PDL 1010
Cdd:cd07876    332 PQI 334
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
729-939 4.41e-24

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: 103.35  E-value: 4.41e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAK----DKDTGELVALKKVR---LDNEKEGFpitaIREIKILRQLVHQSVVNMKEIVTDKQDAldfkkd 801
Cdd:pfam07714    7 LGEGAFGEVYKGTlkgeGENTKIKVAVKTLKegaDEEEREDF----LEEASIMKKLDHPNIVKLLGVCTQGEPL------ 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 kgafYLVFEYMDH-DLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-----------SR-- 867
Cdd:pfam07714   77 ----YIVTEYMPGgDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSEnlvvkisdfglSRdi 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  868 ----PYTNKVITL----WYrPPELLLgEERYTPAIDVWSCGCILGELFT--KKPifQANLELAQ-LELISRLCGSPCPAV 936
Cdd:pfam07714  153 ydddYYRKRGGGKlpikWM-APESLK-DGKFTSKSDVWSFGVLLWEIFTlgEQP--YPGMSNEEvLEFLEDGYRLPQPEN 228

                   ...
gi 1907082950  937 WPD 939
Cdd:pfam07714  229 CPD 231
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
728-997 4.71e-24

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: 103.59  E-value: 4.71e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVRL------DNEKEGFPITAIREIKILRQLV-HQSVVNMKeivtdkqdalDFKK 800
Cdd:cd14093     10 ILGRGVSSTVRRCIEKETGQEFAVKIIDItgekssENEAEELREATRREIEILRQVSgHPNIIELH----------DVFE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DKGAFYLVFEYMDH-DLMGLLESgLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS------------- 866
Cdd:cd14093     80 SPTFIFLVFELCRKgELFDYLTE-VVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNlnvkisdfgfatr 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 ----RPYTNKVITLWYRPPELL-----LGEERYTPAIDVWSCGCILGELftkkpifqanlelaqlelisrLCGspCPAVW 937
Cdd:cd14093    159 ldegEKLRELCGTPGYLAPEVLkcsmyDNAPGYGKEVDMWACGVIMYTL---------------------LAG--CPPFW 215
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  938 PDVIKLPYFNTMKPKKQYRRrlrEEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14093    216 HRKQMVMLRNIMEGKYEFGS---PEWDDISDTAKDLISKLLVVDPKKRLTAEEALEHPFF 272
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
723-994 5.33e-24

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 102.85  E-value: 5.33e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRL----DNEKEgfpiTAIREIKILRQLVHQSVVNMKEIVTDKQdaldf 798
Cdd:cd08530      2 FKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLgslsQKERE----DSVNEIRLLASVNHPNIIRYKEAFLDGN----- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  799 kkdkgAFYLVFEYMD-HDLMGLLESGLVH---FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN--------- 865
Cdd:cd08530     73 -----RLCIVMEYAPfGDLSKLISKRKKKrrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAgdlvkigdl 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 ------SRPYTNKVI-TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQAnlELAQlELISRLCGSPCPAVWP 938
Cdd:cd08530    148 giskvlKKNLAKTQIgTPLYAAPEVWKGRP-YDYKSDIWSLGCLLYEMATFRPPFEA--RTMQ-ELRYKVCRGKFPPIPP 223
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  939 dviklpyfntmkpkkQYRRRLREEFSFipsaaldlldhMLTLDPSKRCTAEQTLQS 994
Cdd:cd08530    224 ---------------VYSQDLQQIIRS-----------LLQVNPKKRPSCDKLLQS 253
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
722-997 6.43e-24

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 104.23  E-value: 6.43e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTG-ELVALKKVRlDNEKegFPITAIREIKILRQLVHQSVVNMKEIVTdkqdALDFKK 800
Cdd:cd14135      1 RYRVYGYLGKGVFSNVVRARDLARGnQEVAIKIIR-NNEL--MHKAGLKELEILKKLNDADPDDKKHCIR----LLRHFE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DKGAFYLVFEYMDHDLMGLL--ESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSR----------- 867
Cdd:cd14135     74 HKNHLCLVFESLSMNLREVLkkYGKNVGLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKKntlklcdfgsa 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  868 ---------PYtnkVITLWYRPPELLLGEeRYTPAIDVWSCGCILGELFTKKPIF--QANLELaqLELISRLCGsPCPav 936
Cdd:cd14135    154 sdigeneitPY---LVSRFYRAPEIILGL-PYDYPIDMWSVGCTLYELYTGKILFpgKTNNHM--LKLMMDLKG-KFP-- 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  937 wPDVIK-----LPYFN-----------------------TMKPKKQYRRRLRE-----EFSFIPSAAL-DLLDHMLTLDP 982
Cdd:cd14135    225 -KKMLRkgqfkDQHFDenlnfiyrevdkvtkkevrrvmsDIKPTKDLKTLLIGkqrlpDEDRKKLLQLkDLLDKCLMLDP 303
                          330
                   ....*....|....*
gi 1907082950  983 SKRCTAEQTLQSDFL 997
Cdd:cd14135    304 EKRITPNEALQHPFI 318
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
721-1001 7.17e-24

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 103.78  E-value: 7.17e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLD--NEKEGFPITAI-REIKILRQLVHQSVVNMKEIVTDKqdald 797
Cdd:cd14094      3 DVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAkfTSSPGLSTEDLkREASICHMLKHPHIVELLETYSSD----- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 fkkdkGAFYLVFEYMD-----HDLMGLLESGLVhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL---NNSRPY 869
Cdd:cd14094     78 -----GMLYMVFEFMDgadlcFEIVKRADAGFV-YSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  870 ------------------TNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFqanlelaqlelisrlCGS 931
Cdd:cd14094    152 klggfgvaiqlgesglvaGGRVGTPHFMAPE-VVKREPYGKPVDVWGCGVILFILLSGCLPF---------------YGT 215
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  932 PcPAVWPDVIKLPYfnTMKPKkqyrrrlreEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLKDVE 1001
Cdd:cd14094    216 K-ERLFEGIIKGKY--KMNPR---------QWSHISESAKDLVRRMLMLDPAERITVYEALNHPWIKERD 273
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
721-998 7.97e-24

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: 103.09  E-value: 7.97e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEgfPITAI-REIKILRQLVHQSVVNMKEIVTDkqdalDFK 799
Cdd:cd06609      1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEEAED--EIEDIqQEIQFLSQCDSPYITKYYGSFLK-----GSK 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 kdkgaFYLVFEYMDH-DLMGLLESGLvhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN------------- 865
Cdd:cd06609     74 -----LWIIMEYCGGgSVLDLLKPGP--LDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEegdvkladfgvsg 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 --SRPYTNK---VITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRlcgSPCPavwpdv 940
Cdd:cd06609    147 qlTSTMSKRntfVGTPFWMAPEVIKQSG-YDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPK---NNPP------ 216
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  941 iKLPyfntmkpkkqyrrrlREEFSfipSAALDLLDHMLTLDPSKRCTAEQTLQSDFLK 998
Cdd:cd06609    217 -SLE---------------GNKFS---KPFKDFVELCLNKDPKERPSAKELLKHKFIK 255
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
722-997 1.10e-23

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: 101.96  E-value: 1.10e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDN----EKEGfpitAIREIKILRQLVHQSVVNMkeivtdkqdaLD 797
Cdd:cd08225      1 RYEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKmpvkEKEA----SKKEVILLAKMKHPNIVTF----------FA 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 FKKDKGAFYLVFEYMDH-DLMGLL--ESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNIL------------ 862
Cdd:cd08225     67 SFQENGRLFIVMEYCDGgDLMKRInrQRG-VLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFlskngmvaklgd 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  863 ------LNNSRPYTNKVI-TLWYRPPELLlgEER-YTPAIDVWSCGCILGELFTKKPIFQANlELAQLELisRLCGSpcp 934
Cdd:cd08225    146 fgiarqLNDSMELAYTCVgTPYYLSPEIC--QNRpYNNKTDIWSLGCVLYELCTLKHPFEGN-NLHQLVL--KICQG--- 217
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  935 avwpdviklpYFNTMKPkkQYRRRLREefsfipsaaldLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd08225    218 ----------YFAPISP--NFSRDLRS-----------LISQLFKVSPRDRPSITSILKRPFL 257
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
729-1014 1.21e-23

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: 104.74  E-value: 1.21e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQDALDFKKdkgaFYLV 808
Cdd:cd07875     32 IGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLEEFQD----VYIV 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDHDLMGLLESGLVHfseDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-----------------SRPYTN 871
Cdd:cd07875    108 MELMDANLCQVIQMELDH---ERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSdctlkildfglartagtSFMMTP 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  872 KVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPC--------PAVWPDVIKL 943
Cdd:cd07875    185 YVVTRYYRAPEVILGMG-YKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVIEQLGTPCpefmkklqPTVRTYVENR 263
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  944 PYFNTMKPKKQYRRRL----REEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLK---DVELSKMAPPDLPHWQ 1014
Cdd:cd07875    264 PKYAGYSFEKLFPDVLfpadSEHNKLKASQARDLLSKMLVIDASKRISVDEALQHPYINvwyDPSEAEAPPPKIPDKQ 341
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
722-990 1.27e-23

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: 101.70  E-value: 1.27e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAI-REIKILRQLVHQSVVNMKEIVTDKqdaldfkk 800
Cdd:cd14073      2 RYELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDMVRIrREIEIMSSLNHPHIIRIYEVFENK-------- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DKgaFYLVFEYMDH-DLMGLLESGLVhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-----------SRP 868
Cdd:cd14073     74 DK--IVIVMEYASGgELYDYISERRR-LPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQngnakiadfglSNL 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  869 YT-NKVITLW-----YRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRlcgspcpavwpdvik 942
Cdd:cd14073    151 YSkDKLLQTFcgsplYASPEIVNGTPYQGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISS--------------- 215
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1907082950  943 lpyfntmkpkKQYRRRLReefsfiPSAALDLLDHMLTLDPSKRCTAEQ 990
Cdd:cd14073    216 ----------GDYREPTQ------PSDASGLIRWMLTVNPKRRATIED 247
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
722-996 1.33e-23

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 102.00  E-value: 1.33e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDnEKEGFPITAiREIKILRQLVHQSVVNMKeivtdkqdALDFKKD 801
Cdd:cd06613      1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIKLE-PGDDFEIIQ-QEISMLKECRHPNIVAYF--------GSYLRRD 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 KgaFYLVFEYMD----HDLMGLLEsglvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN------------- 864
Cdd:cd06613     71 K--LWIVMEYCGggslQDIYQVTG----PLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTedgdvkladfgvs 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 ----NSRPYTNKVI-TLWYRPPELLLGEER--YTPAIDVWSCG--CI-LGELftKKPIFqaNLELAQ-LELISRLCGSPc 933
Cdd:cd06613    145 aqltATIAKRKSFIgTPYWMAPEVAAVERKggYDGKCDIWALGitAIeLAEL--QPPMF--DLHPMRaLFLIPKSNFDP- 219
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  934 pavwpdviklpyfntmkPKKQYRRRLREEF-SFIPSAaldlldhmLTLDPSKRCTAEQTLQSDF 996
Cdd:cd06613    220 -----------------PKLKDKEKWSPDFhDFIKKC--------LTKNPKKRPTATKLLQHPF 258
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
729-993 2.46e-23

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 100.81  E-value: 2.46e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALK--KVRLDNEKEgfpitAIREIKILRQLVHQSVVNMKEIVTDKQDALdfkkdkgafy 806
Cdd:cd14006      1 LGRGRFGVVKRCIEKATGREFAAKfiPKRDKKKEA-----VLREISILNQLQHPRIIQLHEAYESPTELV---------- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVFEYMDHdlmGLLESGLVH---FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTNKVI--------- 874
Cdd:cd14006     66 LILELCSG---GELLDRLAErgsLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSPQIKIIdfglarkln 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  875 ----------TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISrlcgspcpavwpdviklp 944
Cdd:cd14006    143 pgeelkeifgTPEFVAPEIVNGEP-VSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANIS------------------ 203
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907082950  945 yfntmkpkkQYRRRLREE-FSFIPSAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd14006    204 ---------ACRVDFSEEyFSSVSQEAKDFIRKLLVKEPRKRPTAQEALQ 244
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
722-994 2.90e-23

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: 100.94  E-value: 2.90e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKvrLDNE---KEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQDaldf 798
Cdd:cd14663      1 RYELGRTLGEGTFAKVKFARNTKTGESVAIKI--IDKEqvaREGMVEQIKREIAIMKLLRHPNIVELHEVMATKTK---- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  799 kkdkgaFYLVFEYMDHdlmGLLESGLV---HFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSR-------- 867
Cdd:cd14663     75 ------IFFVMELVTG---GELFSKIAkngRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGnlkisdfg 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  868 ----PYTNKVITLW--------YRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQAnlelaqlelisrlcgspcpa 935
Cdd:cd14663    146 lsalSEQFRQDGLLhttcgtpnYVAPEVLARRGYDGAKADIWSCGVILFVLLAGYLPFDD-------------------- 205
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  936 vwPDVIKLpyfntmkpkkqYRRRLREEF---SFIPSAALDLLDHMLTLDPSKRCTAEQTLQS 994
Cdd:cd14663    206 --ENLMAL-----------YRKIMKGEFeypRWFSPGAKSLIKRILDPNPSTRITVEQIMAS 254
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
728-997 3.52e-23

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: 100.95  E-value: 3.52e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITaiREIKILRQLVHQSVVNMKEIVTDkqdaldfkkdkGAFYL 807
Cdd:cd06624     15 VLGKGTFGVVYAARDLSTQVRIAIKEIPERDSREVQPLH--EEIALHSRLSHKNIVQYLGSVSE-----------DGFFK 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFeyMDH----DLMGLLES--GLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN------------NSR-- 867
Cdd:cd06624     82 IF--MEQvpggSLSALLRSkwGPLKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNtysgvvkisdfgTSKrl 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  868 ----PYTNKVI-TLWYRPPELL-LGEERYTPAIDVWSCGCILGELFTKKPIFqanLELaqlelisrlcGSPCPAVWpdvi 941
Cdd:cd06624    160 aginPCTETFTgTLQYMAPEVIdKGQRGYGPPADIWSLGCTIIEMATGKPPF---IEL----------GEPQAAMF---- 222
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  942 KLPYFNTMKPkkqyrrrLREEFSfipSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd06624    223 KVGMFKIHPE-------IPESLS---EEAKSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
723-993 4.57e-23

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


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 100.16  E-value: 4.57e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALK---KVRLDNEKegfpITAI-REIKILRQLVHQSVVNMKEIVTDKQdaldf 798
Cdd:cd14071      2 YDIERTIGKGNFAVVKLARHRITKTEVAIKiidKSQLDEEN----LKKIyREVQIMKMLNHPHIIKLYQVMETKD----- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  799 kkdkgAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-----------SR 867
Cdd:cd14071     73 -----MLYLVTEYASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDAnmnikiadfgfSN 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  868 PYTN-KVITLW-----YRPPELLLGEERYTPAIDVWSCGCILGELftkkpifqanlelaqlelisrLCGSpcpavwpdvi 941
Cdd:cd14071    148 FFKPgELLKTWcgsppYAAPEVFEGKEYEGPQLDIWSLGVVLYVL---------------------VCGA---------- 196
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  942 kLPYFNTMKPKKQYR---RRLREEFsFIPSAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd14071    197 -LPFDGSTLQTLRDRvlsGRFRIPF-FMSTDCEHLIRRMLVLDPSKRLTIEQIKK 249
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
725-997 6.63e-23

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 99.65  E-value: 6.63e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  725 IIG-IIGEGTYGQVYKAKDKDTGELVALK---KVRLDNEKEGFPITaiREIKILRQLVHQSVVNMKEIVTDKQDaldfkk 800
Cdd:cd14079      5 ILGkTLGVGSFGKVKLAEHELTGHKVAVKilnRQKIKSLDMEEKIR--REIQILKLFRHPHIIRLYEVIETPTD------ 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 dkgaFYLVFEYM------DHdlmgLLESGlvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNsrpytNKVI 874
Cdd:cd14079     77 ----IFMVMEYVsggelfDY----IVQKG--RLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDS-----NMNV 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  875 TLW----------------------YRPPELLLGEERYTPAIDVWSCGCILGELftkkpifqanlelaqlelisrLCGSp 932
Cdd:cd14079    142 KIAdfglsnimrdgeflktscgspnYAAPEVISGKLYAGPEVDVWSCGVILYAL---------------------LCGS- 199
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  933 cpavwpdvikLPYFNTMKP---KKqyrrrLREEFSFIPS----AALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14079    200 ----------LPFDDEHIPnlfKK-----IKSGIYTIPShlspGARDLIKRMLVVDPLKRITIPEIRQHPWF 256
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
721-997 7.12e-23

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 101.11  E-value: 7.12e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDnekEGFPITAIREIKILRQLVH--------QSVVNMkeivtdk 792
Cdd:cd14136     10 GRYHVVRKLGWGHFSTVWLCWDLQNKRFVALKVVKSA---QHYTEAALDEIKLLKCVREadpkdpgrEHVVQL------- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  793 qdaLDFKKDKGAF----YLVFEYMDHDLMGLLES----GL-VHFsedhIKSFMKQLMEGLDYCHKK-NFLHRDIKCSNIL 862
Cdd:cd14136     80 ---LDDFKHTGPNgthvCMVFEVLGPNLLKLIKRynyrGIpLPL----VKKIARQVLQGLDYLHTKcGIIHTDIKPENVL 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  863 LN------------NS----RPYTNKVITLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQA------NLELA 920
Cdd:cd14136    153 LCiskievkiadlgNAcwtdKHFTEDIQTRQYRSPEVILG-AGYGTPADIWSTACMAFELATGDYLFDPhsgedySRDED 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  921 QLELISRLCGsPCPavwPDVIKL-----PYFN---TMKPKKQYRRR-----LREEFSFIPSAAL---DLLDHMLTLDPSK 984
Cdd:cd14136    232 HLALIIELLG-RIP---RSIILSgkysrEFFNrkgELRHISKLKPWpledvLVEKYKWSKEEAKefaSFLLPMLEYDPEK 307
                          330
                   ....*....|...
gi 1907082950  985 RCTAEQTLQSDFL 997
Cdd:cd14136    308 RATAAQCLQHPWL 320
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
729-997 1.09e-22

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: 99.44  E-value: 1.09e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKV--------RLDNEKEGFPITA-----IREIKILRQLVHQSVVNMKEIVTDKQda 795
Cdd:cd14077      9 IGAGSMGKVKLAKHIRTGEKCAIKIIprasnaglKKEREKRLEKEISrdirtIREAALSSLLNHPHICRLRDFLRTPN-- 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  796 ldfkkdkgAFYLVFEYMDHDLMglLESGLVH--FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRP----- 868
Cdd:cd14077     87 --------HYYMLFEYVDGGQL--LDYIISHgkLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNikiid 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  869 ------YTNKVI------TLWYRPPELLLGeERYT-PAIDVWSCGCILGELftkkpifqanlelaqlelisrLCGspcpa 935
Cdd:cd14077    157 fglsnlYDPRRLlrtfcgSLYFAAPELLQA-QPYTgPEVDVWSFGVVLYVL---------------------VCG----- 209
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  936 vwpdviKLPYFNTMKPKKQYR-RRLREEF-SFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14077    210 ------KVPFDDENMPALHAKiKKGKVEYpSYLSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
729-995 1.43e-22

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: 98.87  E-value: 1.43e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVA---LKKVRL-------DNEKegfpitaiREIKILRQLVHQSVVNMKEIVTDKqdaldf 798
Cdd:cd14119      1 LGEGSYGKVKEVLDTETLCRRAvkiLKKRKLrripngeANVK--------REIQILRRLNHRNVIKLVDVLYNE------ 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  799 kkDKGAFYLVFEYMDHDLMGLL-ESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN------------ 865
Cdd:cd14119     67 --EKQKLYMVMEYCVGGLQEMLdSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTdgtlkisdfgva 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 ---SRPYTNKVITLWY-----RPPELLLGEERYTP-AIDVWSCGCILGELFTKK-PIFQANL-ELaqLELISRlcgspCP 934
Cdd:cd14119    145 ealDLFAEDDTCTTSQgspafQPPEIANGQDSFSGfKVDIWSAGVTLYNMTTGKyPFEGDNIyKL--FENIGK-----GE 217
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  935 AVWPDViklpyfntmkpkkqyrrrlreefsfIPSAALDLLDHMLTLDPSKRCTAEQTLQSD 995
Cdd:cd14119    218 YTIPDD-------------------------VDPDLQDLLRGMLEKDPEKRFTIEQIRQHP 253
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
722-992 1.23e-21

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 95.96  E-value: 1.23e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEivtdkqdalDFKKD 801
Cdd:cd08220      1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQAALNEVKVLSMLHHPNIIEYYE---------SFLED 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 KgAFYLVFEYMDHDLMG--LLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN--------------- 864
Cdd:cd08220     72 K-ALMIVMEYAPGGTLFeyIQQRKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNkkrtvvkigdfgisk 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 --NSRPYTNKVI-TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQA-NLelaqlelisrlcgspcPAVwpdV 940
Cdd:cd08220    151 ilSSKSKAYTVVgTPCYISPELCEGKP-YNQKSDIWALGCVLYELASLKRAFEAaNL----------------PAL---V 210
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  941 IKLPYFNTMKPKKQYRRRLREefsfipsaaldLLDHMLTLDPSKRCTAEQTL 992
Cdd:cd08220    211 LKIMRGTFAPISDRYSEELRH-----------LILSMLHLDPNKRPTLSEIM 251
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
722-993 1.35e-21

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


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 95.86  E-value: 1.35e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVrlDNEK-EGFPITAIREIKILRQLVHQSVVNM-KEIVTDKQdaldfk 799
Cdd:cd14095      1 KYDIGRVIGDGNFAVVKECRDKATDKEYALKII--DKAKcKGKEHMIENEVAILRRVKHPNIVQLiEEYDTDTE------ 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 kdkgaFYLVFEYMDH-DLMGLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLnnsRPYTNKVITL-- 876
Cdd:cd14095     73 -----LYLVMELVKGgDLFDAITSS-TKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLV---VEHEDGSKSLkl 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  877 --------------------WYRPPELLlGEERYTPAIDVWSCGCILGELftkkpifqanlelaqlelisrLCGSPcPAV 936
Cdd:cd14095    144 adfglatevkeplftvcgtpTYVAPEIL-AETGYGLKVDIWAAGVITYIL---------------------LCGFP-PFR 200
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  937 WPDVIKLPYFNTMkpkkqyrrrLREEFSF-------IPSAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd14095    201 SPDRDQEELFDLI---------LAGEFEFlspywdnISDSAKDLISRMLVVDPEKRYSAGQVLD 255
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
723-997 1.58e-21

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


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 95.94  E-value: 1.58e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALK---KVRLDNEKEGFPITAIREIKILRqlvHQSVVNMKEiVTDKQDALdfk 799
Cdd:cd14074      5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKvidKTKLDDVSKAHLFQEVRCMKLVQ---HPNVVRLYE-VIDTQTKL--- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 kdkgafYLVFEYMD----HDLMGLLESGLvhfSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL------------ 863
Cdd:cd14074     78 ------YLILELGDggdmYDYIMKHENGL---NEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfekqglvkltdf 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  864 ---NNSRPYTnKVIT----LWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRlcgspCPAV 936
Cdd:cd14074    149 gfsNKFQPGE-KLETscgsLAYSAPEILLGDEYDAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMD-----CKYT 222
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  937 WPDviklpyfntmkpkkqyrrrlreefsFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14074    223 VPA-------------------------HVSPECKDLIRRMLIRDPKKRASLEEIENHPWL 258
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
728-911 1.69e-21

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 95.89  E-value: 1.69e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVRLDNE-----KEgfpITAI-REIKILRQLVHQSVVNMkeivtdkqdaLDFKKD 801
Cdd:cd06625      7 LLGQGAFGQVYLCYDADTGRELAVKQVEIDPInteasKE---VKALeCEIQLLKNLQHERIVQY----------YGCLQD 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 KGAFYLVFEYMdhdlmgllESGLVHfseDHIKS-----------FMKQLMEGLDYCHKKNFLHRDIKCSNILLNN----- 865
Cdd:cd06625     74 EKSLSIFMEYM--------PGGSVK---DEIKAygaltenvtrkYTRQILEGLAYLHSNMIVHRDIKGANILRDSngnvk 142
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  866 --------------SRPYTNKVI-TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKP 911
Cdd:cd06625    143 lgdfgaskrlqticSSTGMKSVTgTPYWMSPEVINGEG-YGRKADIWSVGCTVVEMLTTKP 202
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
723-992 1.82e-21

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 96.74  E-value: 1.82e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKD-KDTGELVALKKVRL-----DNEKEGFPITAIREIKILRQLVHQSVVNMkeivtdkqdaL 796
Cdd:cd14096      3 YRLINKIGEGAFSNVYKAVPlRNTGKPVAIKVVRKadlssDNLKGSSRANILKEVQIMKRLSHPNIVKL----------L 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  797 DFKKDKGAFYLVFEYMD-----HDLMGLlesglVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLnNSRPYT- 870
Cdd:cd14096     73 DFQESDEYYYIVLELADggeifHQIVRL-----TYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLF-EPIPFIp 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  871 ---------------------------------------NKVI----------TLWYRPPElLLGEERYTPAIDVWSCGC 901
Cdd:cd14096    147 sivklrkadddetkvdegefipgvggggigivkladfglSKQVwdsntktpcgTVGYTAPE-VVKDERYSKKVDMWALGC 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  902 ILGELftkkpifqanlelaqlelisrLCGSPcpavwpdviklPYFN------TMKPKKQYRRRLREEFSFIPSAALDLLD 975
Cdd:cd14096    226 VLYTL---------------------LCGFP-----------PFYDesietlTEKISRGDYTFLSPWWDEISKSAKDLIS 273
                          330
                   ....*....|....*..
gi 1907082950  976 HMLTLDPSKRCTAEQTL 992
Cdd:cd14096    274 HLLTVDPAKRYDIDEFL 290
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
729-946 5.53e-21

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: 94.29  E-value: 5.53e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAI-REIKILRQLVHQSVVNMKE-IVTDKQdaldfkkdkgaFY 806
Cdd:cd14162      8 LGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPEDYLQKFLpREIEVIKGLKHPNLICFYEaIETTSR-----------VY 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVFEYMDH-DLMGLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN---------------NSRPYT 870
Cdd:cd14162     77 IIMELAENgDLLDYIRKN-GALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDknnnlkitdfgfargVMKTKD 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  871 NKVI-------TLWYRPPELLLGEErYTPAI-DVWSCGCIL-----GEL-------------FTKKPIFQANLELAQ--L 922
Cdd:cd14162    156 GKPKlsetycgSYAYASPEILRGIP-YDPFLsDIWSMGVVLytmvyGRLpfddsnlkvllkqVQRRVVFPKNPTVSEecK 234
                          250       260
                   ....*....|....*....|....*.
gi 1907082950  923 ELISRLCgSPCP--AVWPDVIKLPYF 946
Cdd:cd14162    235 DLILRML-SPVKkrITIEEIKRDPWF 259
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
722-916 5.67e-21

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: 94.05  E-value: 5.67e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKV----RLDNEKEGfpiTAIREIKILRQLVHQSVVNMKEIvtdkqdald 797
Cdd:cd06607      2 IFEDLREIGHGSFGAVYYARNKRTSEVVAIKKMsysgKQSTEKWQ---DIIKEVKFLRQLRHPNTIEYKGC--------- 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 FKKDKGAfYLVFEYMDHDLMGLLEsglVH---FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS-------- 866
Cdd:cd06607     70 YLREHTA-WLVMEYCLGSASDIVE---VHkkpLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPgtvkladf 145
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  867 ------RPYTNKVITLWYRPPELLLG--EERYTPAIDVWSCG--CI-LGElfTKKPIFQAN 916
Cdd:cd06607    146 gsaslvCPANSFVGTPYWMAPEVILAmdEGQYDGKVDVWSLGitCIeLAE--RKPPLFNMN 204
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
723-997 6.30e-21

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


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 95.59  E-value: 6.30e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKvrLDNEKEGFPITAIrEIKILRQLVHQSVVNMKEIvtdkqDALDFKKDK 802
Cdd:cd14211      1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKI--LKNHPSYARQGQI-EVSILSRLSQENADEFNFV-----RAYECFQHK 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 GAFYLVFEYMDHDLMGLLESGlvHFSE---DHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN--SRPYTNKVITL- 876
Cdd:cd14211     73 NHTCLVFEMLEQNLYDFLKQN--KFSPlplKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDpvRQPYRVKVIDFg 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  877 -----------------WYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPD 939
Cdd:cd14211    151 sashvskavcstylqsrYYRAPEIILGLP-FCEAIDMWSLGCVIAELFLGWPLYPGSSEYDQIRYISQTQGLPAEHLLNA 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  940 VIKLPYF---NTMKPKKQYRRRLREEF----------------------------SFIPSAAL-----------DLLDHM 977
Cdd:cd14211    230 ATKTSRFfnrDPDSPYPLWRLKTPEEHeaetgikskearkyifnclddmaqvngpSDLEGSELlaekadrrefiDLLKRM 309
                          330       340
                   ....*....|....*....|
gi 1907082950  978 LTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14211    310 LTIDQERRITPGEALNHPFV 329
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
729-990 6.94e-21

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: 93.89  E-value: 6.94e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKA-KDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKeivtdkqdalDFKKDKGAFYL 807
Cdd:cd14121      3 LGSGTYATVYKAyRKSGAREVVAVKCVSKSSLNKASTENLLTEIELLKKLKHPHIVELK----------DFQWDEEHIYL 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYMDH-DLmglleSGLVHFS----EDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTNKV--------I 874
Cdd:cd14121     73 IMEYCSGgDL-----SRFIRSRrtlpESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPVLKLadfgfaqhL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  875 TLW-----------YRPPELLLGeERYTPAIDVWSCGCILGE-LFTKKPIfqANLELAQLEL-ISRlcgspcpavwPDVI 941
Cdd:cd14121    148 KPNdeahslrgsplYMAPEMILK-KKYDARVDLWSVGVILYEcLFGRAPF--ASRSFEELEEkIRS----------SKPI 214
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1907082950  942 KLPyfntmkpkkqyrrrlreEFSFIPSAALDLLDHMLTLDPSKRCTAEQ 990
Cdd:cd14121    215 EIP-----------------TRPELSADCRDLLLRLLQRDPDRRISFEE 246
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
719-993 7.63e-21

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: 93.87  E-value: 7.63e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  719 CVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALK---KVRLdnEKEGFPITAIREIKILRQLVHQSVVNMkeivtdkqda 795
Cdd:cd14116      3 ALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKvlfKAQL--EKAGVEHQLRREVEIQSHLRHPNILRL---------- 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  796 LDFKKDKGAFYLVFEYMDH-DLMGLLESgLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN--------- 865
Cdd:cd14116     71 YGYFHDATRVYLILEYAPLgTVYRELQK-LSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSagelkiadf 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 -------SRPYTNKVITLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANLElaqlelisrlcgspcpavwp 938
Cdd:cd14116    150 gwsvhapSSRRTTLCGTLDYLPPEMIEG-RMHDEKVDLWSLGVLCYEFLVGKPPFEANTY-------------------- 208
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  939 dviklpyfntmkpKKQYRRRLREEFS---FIPSAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd14116    209 -------------QETYKRISRVEFTfpdFVTEGARDLISRLLKHNPSQRPMLREVLE 253
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
722-993 7.81e-21

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 93.87  E-value: 7.81e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLdnekegFPITA-------IREIKILRQLVHQSVVNMkeivtdkqd 794
Cdd:cd08224      1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQI------FEMMDakarqdcLKEIDLLQQLNHPNIIKY--------- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  795 aLDFKKDKGAFYLVFEYMDH-DLMGLLE---SGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN----- 865
Cdd:cd08224     66 -LASFIENNELNIVLELADAgDLSRLIKhfkKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITAngvvk 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 ------SRPYTNK-------VITLWYRPPELLLGEErYTPAIDVWSCGCILGELFT-KKPIFQANLELAQL-ELISRLCG 930
Cdd:cd08224    145 lgdlglGRFFSSKttaahslVGTPYYMSPERIREQG-YDFKSDIWSLGCLLYEMAAlQSPFYGEKMNLYSLcKKIEKCEY 223
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  931 SPCPAvwpdviklpyfntmkpkKQYRRRLReefsfipsaalDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd08224    224 PPLPA-----------------DLYSQELR-----------DLVAACIQPDPEKRPDISYVLD 258
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
723-985 9.10e-21

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 93.47  E-value: 9.10e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALK---KVRLDNEKEGFPItaIREIKILRQLVHQSVVNMKEIVTDKQDaldfk 799
Cdd:cd05578      2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKymnKQKCIEKDSVRNV--LNELEILQELEHPFLVNLWYSFQDEED----- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 kdkgaFYLVFEYMdhdLMGLLE---SGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN----------- 865
Cdd:cd05578     75 -----MYMVVDLL---LGGDLRyhlQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEqghvhitdfni 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 ------SRPYTNKVITLWYRPPELLLGEErYTPAIDVWSCGCILGE-LFTKKPIFQANLELAQLELISRLCGSPC-PAVW 937
Cdd:cd05578    147 atkltdGTLATSTSGTKPYMAPEVFMRAG-YSFAVDWWSLGVTAYEmLRGKRPYEIHSRTSIEEIRAKFETASVLyPAGW 225
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1907082950  938 pdviklpyfntmkpkkqyrrrlreefsfiPSAALDLLDHMLTLDPSKR 985
Cdd:cd05578    226 -----------------------------SEEAIDLINKLLERDPQKR 244
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
722-935 9.50e-21

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: 93.50  E-value: 9.50e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPiTAIREIKILRQLVHQSVVNMKEivtdkqdalDFKKD 801
Cdd:cd08219      1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSSAVE-DSRKEAVLLAKMKHPNIVAFKE---------SFEAD 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 kGAFYLVFEYMDH-DLMGL--LESGLVhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN-----------NSR 867
Cdd:cd08219     71 -GHLYIVMEYCDGgDLMQKikLQRGKL-FPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTqngkvklgdfgSAR 148
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  868 PYTNK-------VITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANlelAQLELISRLCG---SPCPA 935
Cdd:cd08219    149 LLTSPgayactyVGTPYYVPPEIWENMP-YNNKSDIWSLGCILYELCTLKHPFQAN---SWKNLILKVCQgsyKPLPS 222
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
723-943 1.45e-20

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: 93.34  E-value: 1.45e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTG-ELVALKKVRLDN--------EKEGFPITAIREIKILR-QLVHQSVVNMKEIVTDK 792
Cdd:cd08528      2 YAVLELLGSGAFGCVYKVRKKSNGqTLLALKEINMTNpafgrteqERDKSVGDIISEVNIIKeQLRHPNIVRYYKTFLEN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  793 QdaldfkkdkgAFYLVFEYMDHDLMGLLESGL----VHFSEDHIKSFMKQLMEGLDYCHK-KNFLHRDIKCSNILLN--- 864
Cdd:cd08528     82 D----------RLYIVMELIEGAPLGEHFSSLkeknEHFTEDRIWNIFVQMVLALRYLHKeKQIVHRDLKPNNIMLGedd 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 ---------------NSRPYTNKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQAN--LELA------- 920
Cdd:cd08528    152 kvtitdfglakqkgpESSKMTSVVGTILYSCPEIVQNEP-YGEKADIWALGCILYQMCTLQPPFYSTnmLTLAtkiveae 230
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1907082950  921 -----------QLELISRLCGSPCPAVWPDVIKL 943
Cdd:cd08528    231 yeplpegmysdDITFVIRSCLTPDPEARPDIVEV 264
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
725-997 2.98e-20

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: 92.15  E-value: 2.98e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  725 IIGI-IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGF-----PitaiREIKILRQLVHQSVVNMKEIvtdkqdaldF 798
Cdd:cd14165      4 ILGInLGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDFvekflP----RELEILARLNHKSIIKTYEI---------F 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  799 KKDKGAFYLVFEY-MDHDLMGLLESGLVhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-----------S 866
Cdd:cd14165     71 ETSDGKVYIVMELgVQGDLLEFIKLRGA-LPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKdfnikltdfgfS 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 RPY----TNKVI-------TLWYRPPELLLGEErYTPAI-DVWSCGCILGELftkkpifqanlelaqlelisrLCGSpcp 934
Cdd:cd14165    150 KRClrdeNGRIVlsktfcgSAAYAAPEVLQGIP-YDPRIyDIWSLGVILYIM---------------------VCGS--- 204
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  935 avwpdvikLPYfNTMKPKKQYRRRLREEFSFIPSAAL-----DLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14165    205 --------MPY-DDSNVKKMLKIQKEHRVRFPRSKNLtseckDLIYRLLQPDVSQRLCIDEVLSHPWL 263
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
721-1005 3.28e-20

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 92.50  E-value: 3.28e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRL--DNEKEGFpitaIREIKILRQLVHQSVVNMKEIVtdkqdaldF 798
Cdd:cd06611      5 DIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIesEEELEDF----MVEIDILSECKHPNIVGLYEAY--------F 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  799 KKDKgaFYLVFEYMD----HDLMGLLESGLvhfSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL---NNSR---- 867
Cdd:cd06611     73 YENK--LWILIEFCDggalDSIMLELERGL---TEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLtldGDVKladf 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  868 --PYTNK---------VITLWYRPPELLLGE----ERYTPAIDVWSCGCILgelftkkpifqanLELAQLElisrlcgSP 932
Cdd:cd06611    148 gvSAKNKstlqkrdtfIGTPYWMAPEVVACEtfkdNPYDYKADIWSLGITL-------------IELAQME-------PP 207
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  933 CPAVWPDVIKLPYFNTMKPKKQYRRRLREEFSfipsaalDLLDHMLTLDPSKRCTAEQTLQSDFLKDVELSKM 1005
Cdd:cd06611    208 HHELNPMRVLLKILKSEPPTLDQPSKWSSSFN-------DFLKSCLVKDPDDRPTAAELLKHPFVSDQSDNKA 273
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
729-999 3.28e-20

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 92.00  E-value: 3.28e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEK-EGFpitaIREIKILRQL-VHQSVVNMKEIVTDKQDaldfkkdkgafY 806
Cdd:cd13987      1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKlKDF----LREYNISLELsVHPHIIKTYDVAFETED-----------Y 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVFEyMDHDLMGLL------ESGLvhfSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPY----------- 869
Cdd:cd13987     66 YVFA-QEYAPYGDLfsiippQVGL---PEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCRrvklcdfgltr 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  870 ----TNKVITLW--YRPPEL--LLGEERYT--PAIDVWSCGCILGELFTKKPIFQAnlelaqlelisrlCGSPCPAVWPD 939
Cdd:cd13987    142 rvgsTVKRVSGTipYTAPEVceAKKNEGFVvdPSIDVWAFGVLLFCCLTGNFPWEK-------------ADSDDQFYEEF 208
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  940 VIKLPYFNTMKPkKQYRRrlreefsFIPSaALDLLDHMLTLDPSKRCTAEQTLQsdFLKD 999
Cdd:cd13987    209 VRWQKRKNTAVP-SQWRR-------FTPK-ALRMFKKLLAPEPERRCSIKEVFK--YLGD 257
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
722-993 8.05e-20

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 90.66  E-value: 8.05e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIV-TDKqdaldfkk 800
Cdd:cd14072      1 NYRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIeTEK-------- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 dkgAFYLVFEY------MDHdlmgLLESGLVHFSEDHIKsfMKQLMEGLDYCHKKNFLHRDIKCSNILLNN--------- 865
Cdd:cd14072     73 ---TLYLVMEYasggevFDY----LVAHGRMKEKEARAK--FRQIVSAVQYCHQKRIVHRDLKAENLLLDAdmnikiadf 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 --SRPYT--NKVITLW----YRPPELLLGEERYTPAIDVWSCGCIlgeLFTkkpifqanlelaqleLISrlcGSpcpavw 937
Cdd:cd14072    144 gfSNEFTpgNKLDTFCgsppYAAPELFQGKKYDGPEVDVWSLGVI---LYT---------------LVS---GS------ 196
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  938 pdvikLPyFNTMKPKKQYRRRLREEFS---FIPSAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd14072    197 -----LP-FDGQNLKELRERVLRGKYRipfYMSTDCENLLKKFLVLNPSKRGTLEQIMK 249
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
721-993 9.35e-20

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


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 90.51  E-value: 9.35e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALK---KVRLDNEKEgfpiTAIREIKILRQLVHQSVVNMKEIVtdkqdald 797
Cdd:cd14083      3 DKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKcidKKALKGKED----SLENEIAVLRKIKHPNIVQLLDIY-------- 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 fkKDKGAFYLVF------EYMDHdlmgLLESGlvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNiLLNNSRPYTN 871
Cdd:cd14083     71 --ESKSHLYLVMelvtggELFDR----IVEKG--SYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPEN-LLYYSPDEDS 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  872 KVI--------------------TLWYRPPELLlGEERYTPAIDVWSCGCILGELftkkpifqanlelaqlelisrLCGS 931
Cdd:cd14083    142 KIMisdfglskmedsgvmstacgTPGYVAPEVL-AQKPYGKAVDCWSIGVISYIL---------------------LCGY 199
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  932 PcpavwpdviklPYFNTMKPkKQYRRRLREEFSF-------IPSAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd14083    200 P-----------PFYDENDS-KLFAQILKAEYEFdspywddISDSAKDFIRHLMEKDPNKRYTCEQALE 256
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
729-916 1.66e-19

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: 91.25  E-value: 1.66e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKV----RLDNEKEGfpiTAIREIKILRQLVHQSVVNMKEIvtdkqdaldFKKDKGA 804
Cdd:cd06633     29 IGHGSFGAVYFATNSHTNEVVAIKKMsysgKQTNEKWQ---DIIKEVKFLQQLKHPNTIEYKGC---------YLKDHTA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  805 fYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN--------------SRPYT 870
Cdd:cd06633     97 -WLVMEYCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEpgqvkladfgsasiASPAN 175
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1907082950  871 NKVITLWYRPPELLLG--EERYTPAIDVWSCGCILGELFTKKP-IFQAN 916
Cdd:cd06633    176 SFVGTPYWMAPEVILAmdEGQYDGKVDIWSLGITCIELAERKPpLFNMN 224
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
714-997 2.02e-19

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 90.03  E-value: 2.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  714 DW--GKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEK------EGFPITAIREIKILRQLV-HQSVVN 784
Cdd:cd14181      1 DWagAKEFYQKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEVTAERlspeqlEEVRSSTLKEIHILRQVSgHPSIIT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  785 MkeivtdkqdaLDFKKDKGAFYLVFEYMDH-DLMGLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL 863
Cdd:cd14181     81 L----------IDSYESSTFIFLVFDLMRRgELFDYLTEK-VTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  864 NNsrpytNKVITL----------------------WYRPPELL---LGE--ERYTPAIDVWSCGCILGELFTKKPIFQAN 916
Cdd:cd14181    150 DD-----QLHIKLsdfgfschlepgeklrelcgtpGYLAPEILkcsMDEthPGYGKEVDLWACGVILFTLLAGSPPFWHR 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  917 LELAQLELIsrlcgspcpavwpdviklpyfntMKPKKQYRrrlREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDF 996
Cdd:cd14181    225 RQMLMLRMI-----------------------MEGRYQFS---SPEWDDRSSTVKDLISRLLVVDPEIRLTAEQALQHPF 278

                   .
gi 1907082950  997 L 997
Cdd:cd14181    279 F 279
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
728-997 2.08e-19

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 89.92  E-value: 2.08e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVrlDNEKEGFPITAI--REIKILRQLVHQSVVNMKEIvtdkqdaldFKKDKgAF 805
Cdd:cd14097      8 KLGQGSFGVVIEATHKETQTKWAIKKI--NREKAGSSAVKLleREVDILKHVNHAHIIHLEEV---------FETPK-RM 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  806 YLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS------------------- 866
Cdd:cd14097     76 YLVMELCEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSiidnndklnikvtdfglsv 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 -------RPYTNKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWpd 939
Cdd:cd14097    156 qkyglgeDMLQETCGTPIYMAPEVISAHG-YSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTQSVW-- 232
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  940 viklpyfntmkpkkqyrrrlreefSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14097    233 ------------------------QSVSDAAKNVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
721-1001 2.22e-19

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 90.17  E-value: 2.22e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRL------DNEKegfpitAIREIKILRQLVHQSVVNMKEIVTDKqd 794
Cdd:cd14086      1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTkklsarDHQK------LEREARICRLLKHPNIVRLHDSISEE-- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  795 aldfkkdkGAFYLVFEYMDHdlmGLLESGLV---HFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL-------- 863
Cdd:cd14086     73 --------GFHYLVFDLVTG---GELFEDIVareFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskskgaa 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  864 -------------NNSRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFqanLELAQLELISRlcg 930
Cdd:cd14086    142 vkladfglaievqGDQQAWFGFAGTPGYLSPE-VLRKDPYGKPVDIWACGVILYILLVGYPPF---WDEDQHRLYAQ--- 214
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  931 spcpavwpdvIKLPYFNTMKPkkqyrrrlreEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLKDVE 1001
Cdd:cd14086    215 ----------IKAGAYDYPSP----------EWDTVTPEAKDLINQMLTVNPAKRITAAEALKHPWICQRD 265
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
716-997 2.73e-19

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 90.84  E-value: 2.73e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  716 GKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGE-LVALKKVR-LDNEKEGfpitAIREIKILRQLVHQSVVNmKEIVTDKQ 793
Cdd:cd14214      8 GDWLQERYEIVGDLGEGTFGKVVECLDHARGKsQVALKIIRnVGKYREA----ARLEINVLKKIKEKDKEN-KFLCVLMS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  794 DALDFKkdkGAFYLVFEYMDHDLMGLL-ESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS------ 866
Cdd:cd14214     83 DWFNFH---GHMCIAFELLGKNTFEFLkENNFQPYPLPHIRHMAYQLCHALKFLHENQLTHTDLKPENILFVNSefdtly 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 ----------------------------RPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQANLE 918
Cdd:cd14214    160 nesksceeksvkntsirvadfgsatfdhEHHTTIVATRHYRPPEVIL-ELGWAQPCDVWSLGCILFEYYRGFTLFQTHEN 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  919 LAQLELISRLCGsPCPA-VWPDVIKLPYF------------------NTMKPKKQYRRRLREEFSFIpsaaLDLLDHMLT 979
Cdd:cd14214    239 REHLVMMEKILG-PIPShMIHRTRKQKYFykgslvwdenssdgryvsENCKPLMSYMLGDSLEHTQL----FDLLRRMLE 313
                          330
                   ....*....|....*...
gi 1907082950  980 LDPSKRCTAEQTLQSDFL 997
Cdd:cd14214    314 FDPALRITLKEALLHPFF 331
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
722-997 3.89e-19

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 88.60  E-value: 3.89e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALK-----KVRLD---NEKEGFPITAirEIKILRQLVHQSVVNMKEIvtdkq 793
Cdd:cd14004      1 DYTILKEMGEGAYGQVNLAIYKSKGKEVVIKfifkeRILVDtwvRDRKLGTVPL--EIHILDTLNKRSHPNIVKL----- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  794 daLDFKKDKGAFYLVFEymDH----DLMGLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN---- 865
Cdd:cd14004     74 --LDFFEDDEFYYLVME--KHgsgmDLFDFIERK-PNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGngti 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 ------------SRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELftkkpIFQANlelaqlelisrlcgspc 933
Cdd:cd14004    149 klidfgsaayikSGPFDTFVGTIDYAAPEVLRGNPYGGKEQDIWALGVLLYTL-----VFKEN----------------- 206
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  934 pavwpdviklPYFN---TMKPKKQYRRRLREEfsfipsaALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14004    207 ----------PFYNieeILEADLRIPYAVSED-------LIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
729-997 5.38e-19

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


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 88.21  E-value: 5.38e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKvrLDNEKEGFPITAI-REIKILRQLVHQSVVNMKEIV-TDKQdaldfkkdkgaFY 806
Cdd:cd14078     11 IGSGGFAKVKLATHILTGEKVAIKI--MDKKALGDDLPRVkTEIEALKNLSHQHICRLYHVIeTDNK-----------IF 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVFEYMDHdlmGLLESGLV---HFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNsrpYTN-KVI-------- 874
Cdd:cd14078     78 MVLEYCPG---GELFDYIVakdRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDE---DQNlKLIdfglcakp 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  875 -------------TLWYRPPELLLGEERYTPAIDVWSCGCILGELftkkpifqanlelaqlelisrLCGSpcpavwpdvi 941
Cdd:cd14078    152 kggmdhhletccgSPAYAAPELIQGKPYIGSEADVWSMGVLLYAL---------------------LCGF---------- 200
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  942 kLPY--FNTMKPKKQYRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14078    201 -LPFddDNVMALYRKIQSGKYEEPEWLSPSSKLLLDQMLQVDPKKRITVKELLNHPWV 257
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
728-976 5.87e-19

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: 88.64  E-value: 5.87e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVRL----DNEKEGFPITAIREIKILRQLVHQSVVNMkeivtdkqdaLDFKKDKG 803
Cdd:cd06630      7 LLGTGAFSSCYQARDVKTGTLMAVKQVSFcrnsSSEQEEVVEAIREEIRMMARLNHPNIVRM----------LGATQHKS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  804 AFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-------------SRPYT 870
Cdd:cd06630     77 HFNIFVEWMAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDStgqrlriadfgaaARLAS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  871 NK----------VITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDV 940
Cdd:cd06630    157 KGtgagefqgqlLGTIAFMAPEVLRGEQ-YGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFKIASATTPPPIPEH 235
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1907082950  941 IKLPYFNTMkpkkqyRRRLREEFSFIPSAAlDLLDH 976
Cdd:cd06630    236 LSPGLRDVT------LRCLELQPEDRPPAR-ELLKH 264
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
722-915 7.36e-19

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


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 87.94  E-value: 7.36e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEivtdkqdalDFKkD 801
Cdd:cd08218      1 KYVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKEREESRKEVAVLSKMKHPNIVQYQE---------SFE-E 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 KGAFYLVFEYMDH-DLMGLLESGL-VHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNI-----------------L 862
Cdd:cd08218     71 NGNLYIVMDYCDGgDLYKRINAQRgVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIfltkdgiiklgdfgiarV 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  863 LNNSRPYTNKVI-TLWYRPPELLlgEER-YTPAIDVWSCGCILGELFTKKPIFQA 915
Cdd:cd08218    151 LNSTVELARTCIgTPYYLSPEIC--ENKpYNNKSDIWALGCVLYEMCTLKHAFEA 203
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
729-985 1.02e-18

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: 87.77  E-value: 1.02e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEgfPITAIREIKIlrqlvHQSVVNMKEIVTDKQDALDFKKDKGAFYLV 808
Cdd:cd13985      8 LGEGGFSYVYLAHDVNTGRRYALKRMYFNDEEQ--LRVAIKEIEI-----MKRLCGHPNIVQYYDSAILSSEGRKEVLLL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDHDLMGLLESGL-VHFSEDHIKSFMKQLMEGLDYCHKKN--FLHRDIKCSNILLNNSRPYT--------------- 870
Cdd:cd13985     81 MEYCPGSLVDILEKSPpSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKlcdfgsattehyple 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  871 ------------NKVITLWYRPPEL--LLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELaqlelisrlcgspcpAV 936
Cdd:cd13985    161 raeevniieeeiQKNTTPMYRAPEMidLYSKKPIGEKADIWALGCLLYKLCFFKLPFDESSKL---------------AI 225
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1907082950  937 WPDVIKLPYFNTmkpkkqYRRRLReefsfipsaalDLLDHMLTLDPSKR 985
Cdd:cd13985    226 VAGKYSIPEQPR------YSPELH-----------DLIRHMLTPDPAER 257
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
722-995 1.16e-18

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


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 87.29  E-value: 1.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIR----EIKILRQLVHQSVVNMKEIvtdkqdaLD 797
Cdd:cd14005      1 QYEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTEWAMINGPVpvplEIALLLKASKPGVPGVIRL-------LD 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 FKKDKGAFYLVFEYMD--HDLMGLL-ESGlvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN---------- 864
Cdd:cd14005     74 WYERPDGFLLIMERPEpcQDLFDFItERG--ALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINlrtgevklid 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 -------NSRPYTNKVITLWYRPPELLLgEERY--TPAIdVWSCGCILGELftkkpifqanlelaqlelisrLCGspcpa 935
Cdd:cd14005    152 fgcgallKDSVYTDFDGTRVYSPPEWIR-HGRYhgRPAT-VWSLGILLYDM---------------------LCG----- 203
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  936 vwpdviKLPYFNT---MKPKKQYRRRLREEfsfipsaALDLLDHMLTLDPSKRCTAEQTLQSD 995
Cdd:cd14005    204 ------DIPFENDeqiLRGNVLFRPRLSKE-------CCDLISRCLQFDPSKRPSLEQILSHP 253
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
722-903 1.50e-18

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: 86.93  E-value: 1.50e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKdTGELVALKKVRLDNEKEGFPITAIR-EIKILRQLVHQSVVNMKEIVtdkqdaldfkK 800
Cdd:cd14161      4 RYEFLETLGKGTYGRVKKARDS-SGRLVAIKSIRKDRIKDEQDLLHIRrEIEIMSSLNHPHIISVYEVF----------E 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DKGAFYLVFEYMDH-DLMGLLeSGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-----------SRP 868
Cdd:cd14161     73 NSSKIVIVMEYASRgDLYDYI-SERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDAngnikiadfglSNL 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1907082950  869 Y-TNKVITLW-----YRPPELLLGEERYTPAIDVWSCGCIL 903
Cdd:cd14161    152 YnQDKFLQTYcgsplYASPEIVNGRPYIGPEVDSWSLGVLL 192
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
728-916 1.64e-18

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: 87.37  E-value: 1.64e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGEL-VALKKVRLDNEKEGFPITAiREIKILRQLVHQSVVNMkeivtdkqdaLDFKKDKGAFY 806
Cdd:cd14202      9 LIGHGAFAVVFKGRHKEKHDLeVAVKCINKKNLAKSQTLLG-KEIKILKELKHENIVAL----------YDFQEIANSVY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVFEYMDH-DLMGLLESgLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS---RPYTNKV--------- 873
Cdd:cd14202     78 LVMEYCNGgDLADYLHT-MRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSggrKSNPNNIrikiadfgf 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  874 ----------ITL----WYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQAN 916
Cdd:cd14202    157 arylqnnmmaATLcgspMYMAPEVIM-SQHYDAKADLWSIGTIIYQCLTGKAPFQAS 212
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
729-997 1.86e-18

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 86.71  E-value: 1.86e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKD---KDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKqdaldfkkdkGAF 805
Cdd:cd08222      8 LGSGNFGTVYLVSDlkaTADEELKVLKEISVGELQPDETVDANREAKLLSKLDHPAIVKFHDSFVEK----------ESF 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  806 YLVFEY-----MDHDLMGLLESGLVhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN----------SRPY- 869
Cdd:cd08222     78 CIVTEYceggdLDDKISEYKKSGTT-IDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNnvikvgdfgiSRILm 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  870 ------TNKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQ-ANLelaqLELISRLCGSPCPAVwPDvik 942
Cdd:cd08222    157 gtsdlaTTFTGTPYYMSPEVLKHEG-YNSKSDIWSLGCILYEMCCLKHAFDgQNL----LSVMYKIVEGETPSL-PD--- 227
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  943 lpyfntmkpkkQYRRRLReefsfipsaalDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd08222    228 -----------KYSKELN-----------AIYSRMLNKDPALRPSAAEILKIPFI 260
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
721-1004 1.98e-18

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


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 87.39  E-value: 1.98e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEgfPITAIREIKILRQLVHQSVVNMkeivtdkqdaLDFKK 800
Cdd:cd06644     12 EVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEE--LEDYMVEIEILATCNHPYIVKL----------LGAFY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DKGAFYLVFEYMD----HDLMGLLESGLvhfSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN------------ 864
Cdd:cd06644     80 WDGKLWIMIEFCPggavDAIMLELDRGL---TEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTldgdikladfgv 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 ---NSRPYTNK---VITLWYRPPELLLGEER----YTPAIDVWSCGCILGELFTKKPifqANLELAQLELISRLCGSP-- 932
Cdd:cd06644    157 sakNVKTLQRRdsfIGTPYWMAPEVVMCETMkdtpYDYKADIWSLGITLIEMAQIEP---PHHELNPMRVLLKIAKSEpp 233
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  933 ---CPAVWPdviklPYFNtmkpkkqyrrrlreefsfipsaalDLLDHMLTLDPSKRCTAEQTLQSDFLKDVELSK 1004
Cdd:cd06644    234 tlsQPSKWS-----MEFR------------------------DFLKTALDKHPETRPSAAQLLEHPFVSSVTSNR 279
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
729-993 2.34e-18

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: 86.94  E-value: 2.34e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDtGELVALKKVRLDNEKEGFPiTAIREIKILRQLVHQSVVNMkeivtdkqdaLDFKKDKGAFYLV 808
Cdd:cd14066      1 IGSGGFGTVYKGVLEN-GTVVAVKRLNEMNCAASKK-EFLTELEMLGRLRHPNLVRL----------LGYCLESDEKLLV 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDH----DLMGLLESGLVHfSEDHIKSFMKQLMEGLDYCHKKNFL---HRDIKCSNILLN----------------- 864
Cdd:cd14066     69 YEYMPNgsleDRLHCHKGSPPL-PWPQRLKIAKGIARGLEYLHEECPPpiiHGDIKSSNILLDedfepkltdfglarlip 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 --NSRPYTNKVI-TLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDVI 941
Cdd:cd14066    148 psESVSKTSAVKgTIGYLAPEYIRT-GRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRKDLVEWVESKGKEELEDIL 226
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  942 klpyfntmkpkkqyRRRLREEFSFIPSAALDLLD---HMLTLDPSKRCTAEQTLQ 993
Cdd:cd14066    227 --------------DKRLVDDDGVEEEEVEALLRlalLCTRSDPSLRPSMKEVVQ 267
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
721-993 3.32e-18

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: 86.23  E-value: 3.32e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRlDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVtdkqdaldfkK 800
Cdd:cd14167      3 DIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIA-KKALEGKETSIENEIAVLHKIKHPNIVALDDIY----------E 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DKGAFYLVFEYMDHDLM--GLLESGLvhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNiLLNNSRPYTNKVI---- 874
Cdd:cd14167     72 SGGHLYLIMQLVSGGELfdRIVEKGF--YTERDASKLIFQILDAVKYLHDMGIVHRDLKPEN-LLYYSLDEDSKIMisdf 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  875 -----------------TLWYRPPELLlGEERYTPAIDVWSCGCILGELftkkpifqanlelaqlelisrLCGSPcpavw 937
Cdd:cd14167    149 glskiegsgsvmstacgTPGYVAPEVL-AQKPYSKAVDCWSIGVIAYIL---------------------LCGYP----- 201
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  938 pdviklPYFNTmKPKKQYRRRLREEFSF-------IPSAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd14167    202 ------PFYDE-NDAKLFEQILKAEYEFdspywddISDSAKDFIQHLMEKDPEKRFTCEQALQ 257
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
729-916 3.77e-18

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: 85.88  E-value: 3.77e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKD-TGELVALKKVRLDNEKEGFPITAiREIKILRQLVHQSVVNMkeivtdkqdaLDFKKDKGAFYL 807
Cdd:cd14120      1 IGHGAFAVVFKGRHRKkPDLPVAIKCITKKNLSKSQNLLG-KEIKILKELSHENVVAL----------LDCQETSSSVYL 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYMDH-DLMGLLESGLVhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSR---PYTNKV---------- 873
Cdd:cd14120     70 VMEYCNGgDLADYLQAKGT-LSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSgrkPSPNDIrlkiadfgfa 148
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  874 ---------ITL----WYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQAN 916
Cdd:cd14120    149 rflqdgmmaATLcgspMYMAPEVIMSLQ-YDAKADLWSIGTIVYQCLTGKAPFQAQ 203
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
729-996 4.29e-18

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: 85.81  E-value: 4.29e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVrldnEKEGFPITAiREIKILRQLVHQSVVnmkeivtdkqdaldfkkdkgAFY-- 806
Cdd:cd14010      8 IGRGKHSVVYKGRRKGTIEFVAIKCV----DKSKRPEVL-NEVRLTHELKHPNVL--------------------KFYew 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 --------LVFEY-MDHDLMGLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN------------- 864
Cdd:cd14010     63 yetsnhlwLVVEYcTGGDLETLLRQD-GNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDgngtlklsdfgla 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 --------------------NSRPYTNKVI-TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANlELAQL- 922
Cdd:cd14010    142 rregeilkelfgqfsdegnvNKVSKKQAKRgTPYYMAPELFQGGV-HSFASDLWALGCVLYEMFTGKPPFVAE-SFTELv 219
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  923 ELIsrLCGSPcpavwpdviklpyfNTMKPKkqyrrrlreeFSFIPSAA-LDLLDHMLTLDPSKRCTAEQTLQSDF 996
Cdd:cd14010    220 EKI--LNEDP--------------PPPPPK----------VSSKPSPDfKSLLKGLLEKDPAKRLSWDELVKHPF 268
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
729-988 4.87e-18

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: 85.61  E-value: 4.87e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIR-EIKILRQLVHQSVVNMKEIVTDKQDALdfkkdkgafYL 807
Cdd:cd05611      4 ISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTNVKaERAIMMIQGESPYVAKLYYSFQSKDYL---------YL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-----------SRP-YTNK--- 872
Cdd:cd05611     75 VMEYLNGGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQtghlkltdfglSRNgLEKRhnk 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  873 --VITLWYRPPELLLGEERyTPAIDVWSCGCILGELFTKKPIFQANlelaqlelisrlcgSPcPAVWPDVIklpyfntmk 950
Cdd:cd05611    155 kfVGTPDYLAPETILGVGD-DKMSDWWSLGCVIFEFLFGYPPFHAE--------------TP-DAVFDNIL--------- 209
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1907082950  951 pkkqyRRRL---REEFSFIPSAALDLLDHMLTLDPSKRCTA 988
Cdd:cd05611    210 -----SRRInwpEEVKEFCSPEAVDLINRLLCMDPAKRLGA 245
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
721-996 5.10e-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: 85.87  E-value: 5.10e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPiTAIREIKILRQLVHQSVVNMKEIVTDKQDaldfkk 800
Cdd:cd06610      1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKCQTSMD-ELRKEIQAMSQCNHPNVVSYYTSFVVGDE------ 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 dkgaFYLVFEYMD----HDLM--GLLESGlvhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN---------- 864
Cdd:cd06610     74 ----LWLVMPLLSggslLDIMksSYPRGG---LDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGedgsvkiadf 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 ------------NSRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQanlELAQLELISRLCGSP 932
Cdd:cd06610    147 gvsaslatggdrTRKVRKTFVGTPCWMAPEVMEQVRGYDFKADIWSFGITAIELATGAAPYS---KYPPMKVLMLTLQND 223
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  933 CPavwpdviKLPyfnTMKPKKQYRRRLReefsfipsaalDLLDHMLTLDPSKRCTAEQTLQSDF 996
Cdd:cd06610    224 PP-------SLE---TGADYKKYSKSFR-----------KMISLCLQKDPSKRPTAEELLKHKF 266
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
721-1000 1.10e-17

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


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 86.57  E-value: 1.10e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVR----LDNEKEGFpITAIREIkilrqLVHQSvvnmKEIVTDKQDAL 796
Cdd:cd05573      1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRksdmLKREQIAH-VRAERDI-----LADAD----SPWIVRLHYAF 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  797 dfkKDKGAFYLVFEYM-DHDLMGLLESGLVhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN----------- 864
Cdd:cd05573     71 ---QDEDHLYLVMEYMpGGDLMNLLIKYDV-FPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDadghikladfg 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 -----------------------------NSRPYTNK-------VITLWYRPPELLLGEErYTPAIDVWSCGCILGELFT 908
Cdd:cd05573    147 lctkmnksgdresylndsvntlfqdnvlaRRRPHKQRrvraysaVGTPDYIAPEVLRGTG-YGPECDWWSLGVILYEMLY 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  909 KKPIFQA-NLELAQLELISrlcgspcpavWPDVIKLPYFNTMKPKkqyrrrlreefsfipsaALDLLDHMLTlDPSKR-C 986
Cdd:cd05573    226 GFPPFYSdSLVETYSKIMN----------WKESLVFPDDPDVSPE-----------------AIDLIRRLLC-DPEDRlG 277
                          330
                   ....*....|....
gi 1907082950  987 TAEQTLQSDFLKDV 1000
Cdd:cd05573    278 SAEEIKAHPFFKGI 291
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
726-999 1.18e-17

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: 85.43  E-value: 1.18e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  726 IGIIGEGTYGQVYKAKDKDTGELVALKKV--RLDnekegfpitAIREIKILRQLV-HQSVVNMKEIvtdkqdaldfKKDK 802
Cdd:cd14092     11 EEALGDGSFSVCRKCVHKKTGQEFAVKIVsrRLD---------TSREVQLLRLCQgHPNIVKLHEV----------FQDE 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 GAFYLVFEYmdhdLMG--LLE--SGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL-NNSRPYTNKVI--- 874
Cdd:cd14092     72 LHTYLVMEL----LRGgeLLEriRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFtDEDDDAEIKIVdfg 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  875 ----------------TLWYRPPELL---LGEERYTPAIDVWSCGCILGELFTKKPIFQA-NLELAQLELISRLCgspcp 934
Cdd:cd14092    148 farlkpenqplktpcfTLPYAAPEVLkqaLSTQGYDESCDLWSLGVILYTMLSGQVPFQSpSRNESAAEIMKRIK----- 222
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  935 avwpdviklpyfntmkpkkqyrrrlREEFSF-------IPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLKD 999
Cdd:cd14092    223 -------------------------SGDFSFdgeewknVSSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQG 269
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
728-911 1.32e-17

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: 84.68  E-value: 1.32e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVRL-----DNEKEGFPITAIREIKILRQLVHQSVVNMKEIvtdkqdaldFKKDK 802
Cdd:cd13990      7 LLGKGGFSEVYKAFDLVEQRYVACKIHQLnkdwsEEKKQNYIKHALREYEIHKSLDHPRIVKLYDV---------FEIDT 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 GAFYLVFEYMD-HDLMGLL-ESGLVhfSEDHIKSFMKQLMEGLDYC--HKKNFLHRDIKCSNILLNNSRPYTN------- 871
Cdd:cd13990     78 DSFCTVLEYCDgNDLDFYLkQHKSI--PEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSGNVSGEikitdfg 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  872 --KVI------------------TLWYRPPE-LLLGEE--RYTPAIDVWSCGCILGE-LFTKKP 911
Cdd:cd13990    156 lsKIMddesynsdgmeltsqgagTYWYLPPEcFVVGKTppKISSKVDVWSVGVIFYQmLYGRKP 219
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
722-908 1.52e-17

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: 84.20  E-value: 1.52e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIgiIGEGTYGQVYKAKDKDTGELVALKKVRLD----NEKEGFpitaIREIKILRQLVHQSVVNMkeivtdkqdaLD 797
Cdd:cd13983      4 KFNEV--LGRGSFKTVYRAFDTEEGIEVAWNEIKLRklpkAERQRF----KQEIEILKSLKHPNIIKF----------YD 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 --FKKDKGAFYLVFEYMDhdlmglleSG--------LVHFSEDHIKSFMKQLMEGLDYCHKKN--FLHRDIKCSNI---- 861
Cdd:cd13983     68 swESKSKKEVIFITELMT--------SGtlkqylkrFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIfing 139
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  862 --------------LLNNSRPYTnkVI-TLWYRPPELLlgEERYTPAIDVWSCGCILGELFT 908
Cdd:cd13983    140 ntgevkigdlglatLLRQSFAKS--VIgTPEFMAPEMY--EEHYDEKVDIYAFGMCLLEMAT 197
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
721-993 1.62e-17

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 84.88  E-value: 1.62e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPItairEIKILRQLVHQSVVNMKEIVTDKQDaldfkk 800
Cdd:cd14085      3 DFFEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKTVDKKIVRT----EIGVLLRLSHPNIIKLKEIFETPTE------ 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 dkgaFYLVFEYMDHDLM--GLLESGlvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYT-------- 870
Cdd:cd14085     73 ----ISLVLELVTGGELfdRIVEKG--YYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAplkiadfg 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  871 -NKVI-----------TLWYRPPELLLGEErYTPAIDVWSCGCILGELftkkpifqanlelaqlelisrLCGSPcpavwp 938
Cdd:cd14085    147 lSKIVdqqvtmktvcgTPGYCAPEILRGCA-YGPEVDMWSVGVITYIL---------------------LCGFE------ 198
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  939 dviklPYFNTMKPKKQYRRRLREEFSFI-------PSAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd14085    199 -----PFYDERGDQYMFKRILNCDYDFVspwwddvSLNAKDLVKKLIVLDPKKRLTTQQALQ 255
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
723-993 2.33e-17

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


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 83.46  E-value: 2.33e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALK---KVRLDNEKEGFPitaiREIKILRQLVHQSVVNMKEIV-TDKQdaldf 798
Cdd:cd14185      2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKiidKSKLKGKEDMIE----SEILIIKSLSHPNIVKLFEVYeTEKE----- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  799 kkdkgaFYLVFEYMDH-DLM-GLLESglVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN----------- 865
Cdd:cd14185     73 ------IYLILEYVRGgDLFdAIIES--VKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHnpdksttlkla 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 --------SRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANlELAQLELIsrlcgspcpavw 937
Cdd:cd14185    145 dfglakyvTGPIFTVCGTPTYVAPE-ILSEKGYGLEVDMWAAGVILYILLCGFPPFRSP-ERDQEELF------------ 210
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  938 pDVIKLPYFNTMKPKkqyrrrlreeFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd14185    211 -QIIQLGHYEFLPPY----------WDNISEAAKDLISRLLVVDPEKRYTAKQVLQ 255
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
722-863 2.53e-17

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


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 83.66  E-value: 2.53e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPitaiREIKILRQLvhQSVVNMKEIvtdkqdaLDFKKD 801
Cdd:cd14016      1 RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDSKHPQLE----YEAKVYKLL--QGGPGIPRL-------YWFGQE 67
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  802 KGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL 863
Cdd:cd14016     68 GDYNVMVMDLLGPSLEDLFNKCGRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLM 129
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
723-995 2.72e-17

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: 83.96  E-value: 2.72e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPiTAIREIKILRQLVHQSVVNMKeivtdkQDALDfkkdK 802
Cdd:cd14046      8 FEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIKLRSESKNNS-RILREVMLLSRLNHQHVVRYY------QAWIE----R 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 GAFYLVFEYMD-HDLMGLLESGLvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSR-------------- 867
Cdd:cd14046     77 ANLYIQMEYCEkSTLRDLIDSGL-FQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGnvkigdfglatsnk 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  868 ----------------------PYTNKVITLWYRPPELLLGEER-YTPAIDVWSCGCILGELFTKkpiFQANLELAQLEL 924
Cdd:cd14046    156 lnvelatqdinkstsaalgssgDLTGNVGTALYVAPEVQSGTKStYNEKVDMYSLGIIFFEMCYP---FSTGMERVQILT 232
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  925 ISRLCGSPCPavwpdviklPYFNTMKPKKQyrrrlreeFSFIPSaaldLLDHmltlDPSKRCTAEQTLQSD 995
Cdd:cd14046    233 ALRSVSIEFP---------PDFDDNKHSKQ--------AKLIRW----LLNH----DPAKRPSAQELLKSE 278
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
723-993 2.83e-17

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: 83.89  E-value: 2.83e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITaiREIKILRQLVHQSVVNMKeivtdkqdalDFKKDK 802
Cdd:cd14166      5 FIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSSLE--NEIAVLKRIKHENIVTLE----------DIYEST 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 GAFYLVFEYMDHDLM--GLLESGLvhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTNKVITLW--- 877
Cdd:cd14166     73 THYYLVMQLVSGGELfdRILERGV--YTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTPDENSKIMITDFgls 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  878 ----------------YRPPElLLGEERYTPAIDVWSCGCILGELftkkpifqanlelaqlelisrLCGSPcpavwpdvi 941
Cdd:cd14166    151 kmeqngimstacgtpgYVAPE-VLAQKPYSKAVDCWSIGVITYIL---------------------LCGYP--------- 199
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  942 klPYFNTMKpKKQYRRRLREEFSF-------IPSAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd14166    200 --PFYEETE-SRLFEKIKEGYYEFespfwddISESAKDFIRHLLEKNPSKRYTCEKALS 255
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
723-932 2.87e-17

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 84.70  E-value: 2.87e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRldnEKEGFPITAIREIKILRQLVhqsvvnmkeivTDKQDALDFKKDK 802
Cdd:cd14229      2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILK---NHPSYARQGQIEVGILARLS-----------NENADEFNFVRAY 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 GAFY------LVFEYMDHDLMGLLESGlvHFSE---DHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN--SRPYTN 871
Cdd:cd14229     68 ECFQhrnhtcLVFEMLEQNLYDFLKQN--KFSPlplKVIRPILQQVATALKKLKSLGLIHADLKPENIMLVDpvRQPYRV 145
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  872 KVITL------------------WYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSP 932
Cdd:cd14229    146 KVIDFgsashvsktvcstylqsrYYRAPEIILGLP-FCEAIDMWSLGCVIAELFLGWPLYPGALEYDQIRYISQTQGLP 223
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
723-992 2.91e-17

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 83.69  E-value: 2.91e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKegfpitAIREIKILRQLVHQSVV--NMKEIVTDKQDALDFKK 800
Cdd:cd14047      8 FKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVKLNNEK------AEREVKALAKLDHPNIVryNGCWDGFDYDPETSSSN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DKG-AFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFM-----KQLMEGLDYCHKKNFLHRDIKCSNILLN---------- 864
Cdd:cd14047     82 SSRsKTKCLFIQMEFCEKGTLESWIEKRNGEKLDKVLaleifEQITKGVEYIHSKKLIHRDLKPSNIFLVdtgkvkigdf 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 -------NSRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTkkpIFQANLELAQlelisrlcgspcpaVW 937
Cdd:cd14047    162 glvtslkNDGKRTKSKGTLSYMSPE-QISSQDYGKEVDIYALGLILFELLH---VCDSAFEKSK--------------FW 223
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  938 PDVI--KLPyfntmkpkKQYRRRLREEFSFIpsaaldllDHMLTLDPSKRCTAEQTL 992
Cdd:cd14047    224 TDLRngILP--------DIFDKRYKIEKTII--------KKMLSKKPEDRPNASEIL 264
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
721-998 4.09e-17

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: 83.16  E-value: 4.09e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLD-NEKEGFPItaIREIKILRQlvhqsvVNMKEIVTDKQdALdfk 799
Cdd:cd06605      1 DDLEYLGELGEGNGGVVSKVRHRPSGQIMAVKVIRLEiDEALQKQI--LRELDVLHK------CNSPYIVGFYG-AF--- 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 KDKGAFYLVFEYMDHdlmGLLESGL--VHFSEDHIKSFM-KQLMEGLDYCHKK-NFLHRDIKCSNILLN----------- 864
Cdd:cd06605     69 YSEGDISICMEYMDG---GSLDKILkeVGRIPERILGKIaVAVVKGLIYLHEKhKIIHRDVKPSNILVNsrgqvklcdfg 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 ------NSRPYTNkVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKK---PIFQANLELAQLELISRLCGSPCPa 935
Cdd:cd06605    146 vsgqlvDSLAKTF-VGTRSYMAPERISGGK-YTVKSDIWSLGLSLVELATGRfpyPPPNAKPSMMIFELLSYIVDEPPP- 222
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  936 vwpdviKLPyfntmkpkkqyrrrlREEFSfipSAALDLLDHMLTLDPSKRCTAEQTLQSDFLK 998
Cdd:cd06605    223 ------LLP---------------SGKFS---PDFQDFVSQCLQKDPTERPSYKELMEHPFIK 261
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
729-915 5.12e-17

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 82.66  E-value: 5.12e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKE-GFPITAIREIKILRQLVHQSVVNMkeivtdkqdaldFK--KDKGAF 805
Cdd:cd05572      1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQtRQQEHIFSEKEILEECNSPFIVKL------------YRtfKDKKYL 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  806 YLVFEYMD-HDLMGLLESgLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNsRPY-------TNKVI--- 874
Cdd:cd05572     69 YMLMEYCLgGELWTILRD-RGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDS-NGYvklvdfgFAKKLgsg 146
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1907082950  875 --------TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQA 915
Cdd:cd05572    147 rktwtfcgTPEYVAPEIILNKG-YDFSVDYWSLGILLYELLTGRPPFGG 194
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
729-966 5.86e-17

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: 82.81  E-value: 5.86e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAK----DKDTGELVALKKVRLD---NEKEGFPitaiREIKILRQLVHQSVVNMKEiVTDKQDALDFKkd 801
Cdd:cd05038     12 LGEGHFGSVELCRydplGDNTGEQVAVKSLQPSgeeQHMSDFK----REIEILRTLDHEYIVKYKG-VCESPGRRSLR-- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 kgafyLVFEYmdhdlmglLESG-LVHFSEDH--------IKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYT-- 870
Cdd:cd05038     85 -----LIMEY--------LPSGsLRDYLQRHrdqidlkrLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKis 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  871 ----NKVITL----------------WYRPPEllLGEERYTPAIDVWSCGCILGELFTK------------KPIFQANLE 918
Cdd:cd05038    152 dfglAKVLPEdkeyyyvkepgespifWYAPEC--LRESRFSSASDVWSFGVTLYELFTYgdpsqsppalflRMIGIAQGQ 229
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  919 LAQLELISRLCGS---PCPAVWPDVIklpyFNTMKPKKQYRRRLREEFSFI 966
Cdd:cd05038    230 MIVTRLLELLKSGerlPRPPSCPDEV----YDLMKECWEYEPQDRPSFSDL 276
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
729-998 7.68e-17

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: 82.11  E-value: 7.68e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKvrLDNEKEGFPITAIREIKILRQLVHQSVVNM--KEIVTDKqdaldfkkdkgaFY 806
Cdd:cd06648     15 IGEGSTGIVCIATDKSTGRQVAVKK--MDLRKQQRRELLFNEVVIMRDYQHPNIVEMysSYLVGDE------------LW 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVFEYMDHdlmGLLESGLVH--FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS-----------------R 867
Cdd:cd06648     81 VVMEFLEG---GALTDIVTHtrMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDgrvklsdfgfcaqvskeV 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  868 PYTNKVI-TLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPifqanlelaqlelisrlcgspcpavwpdviklPYF 946
Cdd:cd06648    158 PRRKSLVgTPYWMAPE-VISRLPYGTEVDIWSLGIMVIEMVDGEP--------------------------------PYF 204
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  947 NtmKPKKQYRRRLREE-------FSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLK 998
Cdd:cd06648    205 N--EPPLQAMKRIRDNeppklknLHKVSPRLRSFLDRMLVRDPAQRATAAELLNHPFLA 261
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
721-985 9.04e-17

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: 82.63  E-value: 9.04e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKK------VRLDNEKEgfpitAIREIKILRQLVHQSVVNMkeivtdkqd 794
Cdd:cd05580      1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKIlkkakiIKLKQVEH-----VLNEKRILSEVRHPFIVNL--------- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  795 aLDFKKDKGAFYLVFEYMD-HDLMGLL-ESGlvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN------- 865
Cdd:cd05580     67 -LGSFQDDRNLYMVMEYVPgGELFSLLrRSG--RFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSdghikit 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 ---------SRPYTnKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELftkkpifqanlelaqlelisrLCGSPcPav 936
Cdd:cd05580    144 dfgfakrvkDRTYT-LCGTPEYLAPEIILSKG-HGKAVDWWALGILIYEM---------------------LAGYP-P-- 197
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  937 wpdviklpyFNTMKPKKQYRRRL--REEF-SFIPSAALDLLDHMLTLDPSKR 985
Cdd:cd05580    198 ---------FFDENPMKIYEKILegKIRFpSFFDPDAKDLIKRLLVVDLTKR 240
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
721-1013 9.46e-17

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: 82.47  E-value: 9.46e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEgFPITAIREIKILRQLVHQSVVNMKEIVTDKQDaldfkk 800
Cdd:cd06621      1 DKIVELSSLGEGAGGSVTKCRLRNTKTIFALKTITTDPNPD-VQKQILRELEINKSCASPYIVKYYGAFLDEQD------ 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 dkGAFYLVFEYMD----HDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN----------- 865
Cdd:cd06621     74 --SSIGIAMEYCEggslDSIYKKVKKKGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRkgqvklcdfgv 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 SRPYTNKVI-----TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANLE--LAQLELISRLCGSPCPavwp 938
Cdd:cd06621    152 SGELVNSLAgtftgTSYYMAPERIQGGP-YSITSDVWSLGLTLLEVAQNRFPFPPEGEppLGPIELLSYIVNMPNP---- 226
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  939 dviklpyfnTMKPKKQYRRRLREEFSfipsaalDLLDHMLTLDPSKRCTAEQTLQSDFLKDvelSKMAPPDLPHW 1013
Cdd:cd06621    227 ---------ELKDEPENGIKWSESFK-------DFIEKCLEKDGTRRPGPWQMLAHPWIKA---QEKKKVNMAKF 282
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
728-994 1.04e-16

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 81.95  E-value: 1.04e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKkVRLDNEKegfpitAIREIKI-LRQLVHQSVVNMKEIVTDKQDaldfkkDKGAFY 806
Cdd:cd14089      8 VLGLGINGKVLECFHKKTGEKFALK-VLRDNPK------ARREVELhWRASGCPHIVRIIDVYENTYQ------GRKCLL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVFEYMDHdlmGLL-----ESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRP------------- 868
Cdd:cd14089     75 VVMECMEG---GELfsriqERADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPnailkltdfgfak 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  869 --YTNKVI-----TLWYRPPElLLGEERYTPAIDVWSCGCILGELftkkpifqanlelaqlelisrLCGSPcpavwpdvi 941
Cdd:cd14089    152 etTTKKSLqtpcyTPYYVAPE-VLGPEKYDKSCDMWSLGVIMYIL---------------------LCGYP--------- 200
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  942 klPYF--NTMKPKKQYRRRLR--------EEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQS 994
Cdd:cd14089    201 --PFYsnHGLAISPGMKKRIRngqyefpnPEWSNVSEEAKDLIRGLLKTDPSERLTIEEVMNH 261
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
721-916 1.08e-16

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: 81.45  E-value: 1.08e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKV-RLDNEKEGFPITAIREIKILRQLVHQSVVNMkeivtdkqdaLDFK 799
Cdd:cd14186      1 EDFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIdKKAMQKAGMVQRVRNEVEIHCQLKHPSILEL----------YNYF 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 KDKGAFYLVFEyMDHDlmGLLESGLVH----FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN---NSRPYTNK 872
Cdd:cd14186     71 EDSNYVYLVLE-MCHN--GEMSRYLKNrkkpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTrnmNIKIADFG 147
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  873 VITLWYRPPE---LLLGEERY-TPAI----------DVWSCGCILGELFTKKPIFQAN 916
Cdd:cd14186    148 LATQLKMPHEkhfTMCGTPNYiSPEIatrsahglesDVWSLGCMFYTLLVGRPPFDTD 205
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
720-998 1.11e-16

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: 81.83  E-value: 1.11e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  720 VDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKV-RLDNEKEGFPITAIREIKILRQLVHQSVVNMkeivtdkqdaLDF 798
Cdd:cd14117      5 IDDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLfKSQIEKEGVEHQLRREIEIQSHLRHPNILRL----------YNY 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  799 KKDKGAFYLVFEYMDHDLM--GLLESGlvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN------------ 864
Cdd:cd14117     75 FHDRKRIYLILEYAPRGELykELQKHG--RFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGykgelkiadfgw 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 --NSRPYTNKVI--TLWYRPPELLLGEErYTPAIDVWSCGCILGELftkkpifqanlelaqlelisrlcgspcpavwpdV 940
Cdd:cd14117    153 svHAPSLRRRTMcgTLDYLPPEMIEGRT-HDEKVDLWCIGVLCYEL---------------------------------L 198
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  941 IKLPYFNTMKPKKQYRRRLREEFSF---IPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLK 998
Cdd:cd14117    199 VGMPPFESASHTETYRRIVKVDLKFppfLSDGSRDLISKLLRYHPSERLPLKGVMEHPWVK 259
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
722-903 1.24e-16

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: 81.57  E-value: 1.24e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRldnEKEGFPITAIREIKILRQLVHQSVVNMKE-IVTDKQDALDFKK 800
Cdd:cd14665      1 RYELVKDIGSGNFGVARLMRDKQTKELVAVKYIE---RGEKIDENVQREIINHRSLRHPNIVRFKEvILTPTHLAIVMEY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DKGAfyLVFEYmdhdlmgLLESGlvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN---------------- 864
Cdd:cd14665     78 AAGG--ELFER-------ICNAG--RFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDgspaprlkicdfgysk 146
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1907082950  865 ----NSRPYTNkVITLWYRPPELLLGEERYTPAIDVWSCGCIL 903
Cdd:cd14665    147 ssvlHSQPKST-VGTPAYIAPEVLLKKEYDGKIADVWSCGVTL 188
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
728-978 1.40e-16

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


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 81.63  E-value: 1.40e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVRLDNE--KEGFPITAIR-EIKILRQLVHQSVVNMKEIVTDKQDAldfkkdkgA 804
Cdd:cd06652      9 LLGQGAFGRVYLCYDADTGRELAVKQVQFDPEspETSKEVNALEcEIQLLKNLLHERIVQYYGCLRDPQER--------T 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  805 FYLVFEYMDHdlmGLLESGLVHF---SEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS------------RPY 869
Cdd:cd06652     81 LSIFMEYMPG---GSIKDQLKSYgalTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVgnvklgdfgaskRLQ 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  870 T---------NKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQanlELAQLELISRLCGSPCPAVWPDV 940
Cdd:cd06652    158 TiclsgtgmkSVTGTPYWMSPEVISGEG-YGRKADIWSVGCTVVEMLTEKPPWA---EFEAMAAIFKIATQPTNPQLPAH 233
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1907082950  941 IKlpyfntmKPKKQYRRRLREEFSFIPSAAlDLLDHML 978
Cdd:cd06652    234 VS-------DHCRDFLKRIFVEAKLRPSAD-ELLRHTF 263
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
729-997 1.73e-16

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


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 80.73  E-value: 1.73e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALK--KVRLDNEKEgfpiTAIREIKILRQLVHQSVVNMkeivtdkQDALDFKKDkgaFY 806
Cdd:cd14103      1 LGRGKFGTVYRCVEKATGKELAAKfiKCRKAKDRE----DVRNEIEIMNQLRHPRLLQL-------YDAFETPRE---MV 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVFEYM----------DHDLMgLLESGLVHFsedhiksfMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTNKVITL 876
Cdd:cd14103     67 LVMEYVaggelfervvDDDFE-LTERDCILF--------MRQICEGVQYMHKQGILHLDLKPENILCVSRTGNQIKIIDF 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  877 ----WYRP----------PELLLGE----ERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRlcgspcpAVWp 938
Cdd:cd14103    138 glarKYDPdkklkvlfgtPEFVAPEvvnyEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTR-------AKW- 209
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  939 dviklpYFNTmkpkkqyrrrlrEEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14103    210 ------DFDD------------EAFDDISDEAKDFISKLLVKDPRKRMSAAQCLQHPWL 250
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
723-1011 2.08e-16

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


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 83.16  E-value: 2.08e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRldnekegfpitaiREIKILRQLVHQsVVNMKEIVT-DKQDAL----- 796
Cdd:cd05600     13 FQILTQVGQGGYGSVFLARKKDTGEICALKIMK-------------KKVLFKLNEVNH-VLTERDILTtTNSPWLvklly 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  797 DFkKDKGAFYLVFEYM-DHDLMGLL-ESGLVHfsEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS-------- 866
Cdd:cd05600     79 AF-QDPENVYLAMEYVpGGDFRTLLnNSGILS--EEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSghikltdf 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 ----------------------------------------------RPYTNKVI-TLWYRPPELLLGEErYTPAIDVWSC 899
Cdd:cd05600    156 glasgtlspkkiesmkirleevkntafleltakerrniyramrkedQNYANSVVgSPDYMAPEVLRGEG-YDLTVDYWSL 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  900 GCILGELFTKKPIFqanlelaqlelisrlCGSPCPAVWpdvIKLPYFNTM--KPKKQYRrrlREEFSFiPSAALDLLDHM 977
Cdd:cd05600    235 GCILFECLVGFPPF---------------SGSTPNETW---ANLYHWKKTlqRPVYTDP---DLEFNL-SDEAWDLITKL 292
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1907082950  978 LTlDPSKR-CTAEQTLQSDFLKDVELSKM----APPDLP 1011
Cdd:cd05600    293 IT-DPQDRlQSPEQIKNHPFFKNIDWDRLregsKPPFIP 330
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
728-987 2.14e-16

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: 81.25  E-value: 2.14e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALK---KVRLdNEKEGF------------------PITAI-REIKILRQLVHQSVVNM 785
Cdd:cd14118      1 EIGKGSYGIVKLAYNEEDNTLYAMKilsKKKL-LKQAGFfrrppprrkpgalgkpldPLDRVyREIAILKKLDHPNVVKL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  786 KEIVTD-KQDALdfkkdkgafYLVFEymdhdlmgLLESGLVH-------FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIK 857
Cdd:cd14118     80 VEVLDDpNEDNL---------YMVFE--------LVDKGAVMevptdnpLSEETARSYFRDIVLGIEYLHYQKIIHRDIK 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  858 CSNILLNN-----------SRPY-------TNKVITLWYRPPELLLGEERYTP--AIDVWSCGCILGELFTKKPIFQANL 917
Cdd:cd14118    143 PSNLLLGDdghvkiadfgvSNEFegddallSSTAGTPAFMAPEALSESRKKFSgkALDIWAMGVTLYCFVFGRCPFEDDH 222
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  918 ELAQLELISRlcgspcpavwpDVIKLPyfntmkpkkqyrrrlrEEFSFipSAAL-DLLDHMLTLDPSKRCT 987
Cdd:cd14118    223 ILGLHEKIKT-----------DPVVFP----------------DDPVV--SEQLkDLILRMLDKNPSERIT 264
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
729-998 3.06e-16

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: 80.36  E-value: 3.06e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPItaIREIKILRQLVHQSVVNMKE--IVTDKqdaldfkkdkgaFY 806
Cdd:cd06647     15 IGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKELI--INEILVMRENKNPNIVNYLDsyLVGDE------------LW 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVFEYmdhdLMGLLESGLVH---FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN------------------N 865
Cdd:cd06647     81 VVMEY----LAGGSLTDVVTetcMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGmdgsvkltdfgfcaqitpE 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 SRPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISrlcgspcpavwpdviklpy 945
Cdd:cd06647    157 QSKRSTMVGTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIA------------------- 216
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  946 fNTMKPKKQYRRRLREEFSfipsaalDLLDHMLTLDPSKRCTAEQTLQSDFLK 998
Cdd:cd06647    217 -TNGTPELQNPEKLSAIFR-------DFLNRCLEMDVEKRGSAKELLQHPFLK 261
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
721-997 3.33e-16

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: 80.32  E-value: 3.33e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITaiREIKILRQLVHQSVVNMkeivtdkQDALDfkk 800
Cdd:cd14114      2 DHYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVR--KEIQIMNQLHHPKLINL-------HDAFE--- 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DKGAFYLVFEYMDH-DLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTNKVI----- 874
Cdd:cd14114     70 DDNEMVLILEFLSGgELFERIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRSNEVKLIdfgla 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  875 --------------TLWYRPPELLLGEE--RYTpaiDVWSCGCILGELFTKKPIFQANLELAQLELISRlcgspCPAVWP 938
Cdd:cd14114    150 thldpkesvkvttgTAEFAAPEIVEREPvgFYT---DMWAVGVLSYVLLSGLSPFAGENDDETLRNVKS-----CDWNFD 221
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  939 DviklpyfntmkpkkqyrrrlrEEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14114    222 D---------------------SAFSGISEEAKDFIRKLLLADPNKRMTIHQALEHPWL 259
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
728-998 3.76e-16

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 80.60  E-value: 3.76e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKegFPITAI-REIKILRQLVHQSVVNmkeIVTDKQDALdfkkdKG-AF 805
Cdd:cd06917      8 LVGRGSYGAVYRGYHVKTGRVVALKVLNLDTDD--DDVSDIqKEVALLSQLKLGQPKN---IIKYYGSYL-----KGpSL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  806 YLVFEYMDH-DLMGLLESGLVhfSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN------------------NS 866
Cdd:cd06917     78 WIIMDYCEGgSIRTLMRAGPI--AERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTntgnvklcdfgvaaslnqNS 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 RPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFqANLELAQlelisrlcgspcpAVwpdviklpyf 946
Cdd:cd06917    156 SKRSTFVGTPYWMAPEVITEGKYYDTKADIWSLGITTYEMATGNPPY-SDVDALR-------------AV---------- 211
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  947 nTMKPKKQYRRRLREEFSfipSAALDLLDHMLTLDPSKRCTAEQTLQSDFLK 998
Cdd:cd06917    212 -MLIPKSKPPRLEGNGYS---PLLKEFVAACLDEEPKDRLSADELLKSKWIK 259
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
721-1004 4.89e-16

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


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 80.46  E-value: 4.89e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKV--RLDNEKEGFPItairEIKILRQLVHQSVVNMkeivtdkQDALDF 798
Cdd:cd06643      5 DFWEIVGELGDGAFGKVYKAQNKETGILAAAKVIdtKSEEELEDYMV----EIDILASCDHPNIVKL-------LDAFYY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  799 KKDkgaFYLVFEYMD----HDLMGLLESGLvhfSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN---------- 864
Cdd:cd06643     74 ENN---LWILIEFCAggavDAVMLELERPL---TEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTldgdikladf 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 -----NSRPYTNK---VITLWYRPPELLLGEER----YTPAIDVWSCGCILGELFTKKPifqANLELAQLELISRLCGSP 932
Cdd:cd06643    148 gvsakNTRTLQRRdsfIGTPYWMAPEVVMCETSkdrpYDYKADVWSLGVTLIEMAQIEP---PHHELNPMRVLLKIAKSE 224
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  933 CPAVwpdviklpyfntMKPKkqyrrRLREEFSfipsaalDLLDHMLTLDPSKRCTAEQTLQSDFLKDVELSK 1004
Cdd:cd06643    225 PPTL------------AQPS-----RWSPEFK-------DFLRKCLEKNVDARWTTSQLLQHPFVSVLVSNK 272
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
721-997 5.59e-16

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: 79.68  E-value: 5.59e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRldnEKEGFPI--TAIREIKILRQLVHQSVVNMKEIVTDKQDALDF 798
Cdd:cd14088      1 DRYDLGQVIKTEEFCEIFRAKDKTTGKLYTCKKFL---KRDGRKVrkAAKNEINILKMVKHPNILQLVDVFETRKEYFIF 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  799 KkDKGAFYLVFEYmdhdlmgLLESGlvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTNKVI---- 874
Cdd:cd14088     78 L-ELATGREVFDW-------ILDQG--YYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNRLKNSKIVIsdfh 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  875 --------------TLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLElisrlcgspcpavwpdv 940
Cdd:cd14088    148 laklenglikepcgTPEYLAPE-VVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEEDDYE----------------- 209
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  941 iklpyfntMKPKKQYRRRLREEFSF-------IPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14088    210 --------NHDKNLFRKILAGDYEFdspywddISQAAKDLVTRLMEVEQDQRITAEEAISHEWI 265
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
723-1019 9.26e-16

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: 79.60  E-value: 9.26e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVrldnEKEGFPITaiREIKIL-RQLVHQSVVNMKEIVTDKQdaldfkkd 801
Cdd:cd14091      2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKII----DKSKRDPS--EEIEILlRYGQHPNIITLRDVYDDGN-------- 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 kgAFYLVFEYMDhdlmG--LLESGLV--HFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNIL--LNNSRPYTNKVI- 874
Cdd:cd14091     68 --SVYLVTELLR----GgeLLDRILRqkFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILyaDESGDPESLRICd 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  875 -------------------TLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISR-------L 928
Cdd:cd14091    142 fgfakqlraengllmtpcyTANFVAPE-VLKKQGYDAACDIWSLGVLLYTMLAGYTPFASGPNDTPEVILARigsgkidL 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  929 CGspcpavwpdviklPYFNTmkpkkqyrrrlreefsfIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLkdVELSKMAPP 1008
Cdd:cd14091    221 SG-------------GNWDH-----------------VSDSAKDLVRKMLHVDPSQRPTAAQVLQHPWI--RNRDSLPQR 268
                          330
                   ....*....|.
gi 1907082950 1009 DLPHWQDCHEL 1019
Cdd:cd14091    269 QLTDPQDAALV 279
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
725-985 1.02e-15

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: 79.07  E-value: 1.02e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  725 IIG-IIGEGTYGQV-----YKAKDKDTGELVALKKVRLDNEKEGFPITAI-REIKILRQLVHQSVVNMkeivtdkqdaLD 797
Cdd:cd14076      4 ILGrTLGEGEFGKVklgwpLPKANHRSGVQVAIKLIRRDTQQENCQTSKImREINILKGLTHPNIVRL----------LD 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 FKKDKGAFYLVFEYMDHDlmGLLESGLVH--FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRpytNKVIT 875
Cdd:cd14076     74 VLKTKKYIGIVLEFVSGG--ELFDYILARrrLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNR---NLVIT 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  876 LW----------------------YRPPELLLGEERYT-PAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSP 932
Cdd:cd14076    149 DFgfantfdhfngdlmstscgspcYAAPELVVSDSMYAgRKADIWSCGVILYAMLAGYLPFDDDPHNPNGDNVPRLYRYI 228
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  933 C--PAVWPDviklpyfntmkpkkqyrrrlreefsFIPSAALDLLDHMLTLDPSKR 985
Cdd:cd14076    229 CntPLIFPE-------------------------YVTPKARDLLRRILVPNPRKR 258
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
721-1012 1.05e-15

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 80.52  E-value: 1.05e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRldnEKEGFPITAIREIKILRQLVHQSVVNMKEIvtdkqDALDFKK 800
Cdd:cd14227     15 NTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILK---NHPSYARQGQIEVSILARLSTESADDYNFV-----RAYECFQ 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DKGAFYLVFEYMDHDLMGLL-ESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL--NNSRPYTNKVITL- 876
Cdd:cd14227     87 HKNHTCLVFEMLEQNLYDFLkQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvdPSRQPYRVKVIDFg 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  877 -----------------WYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPD 939
Cdd:cd14227    167 sashvskavcstylqsrYYRAPEIILGLP-FCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLPAEYLLSA 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  940 VIKLPYF---NTMKPKKQYRRRLREE----------------FSFIPSAA-----------------------LDLLDHM 977
Cdd:cd14227    246 GTKTTRFfnrDTDSPYPLWRLKTPEDheaetgikskearkyiFNCLDDMAqvnmttdlegsdmlvekadrrefIDLLKKM 325
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1907082950  978 LTLDPSKRCTAEQTLQSDFLKDVELSkmappDLPH 1012
Cdd:cd14227    326 LTIDADKRITPIETLNHPFVTMTHLL-----DFPH 355
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
721-1012 1.13e-15

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


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 80.52  E-value: 1.13e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRldnEKEGFPITAIREIKILRQLVhqsvvnmkeivTDKQDALDFKK 800
Cdd:cd14228     15 NSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILK---NHPSYARQGQIEVSILSRLS-----------SENADEYNFVR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DKGAFY------LVFEYMDHDLMGLL-ESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN--SRPYTN 871
Cdd:cd14228     81 SYECFQhknhtcLVFEMLEQNLYDFLkQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDpvRQPYRV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  872 KVITL------------------WYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPC 933
Cdd:cd14228    161 KVIDFgsashvskavcstylqsrYYRAPEIILGLP-FCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLPA 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  934 PAVWPDVIKLPYFNTMKPKKQY---RRRLREE----------------FSFIPSAA-----------------------L 971
Cdd:cd14228    240 EYLLSAGTKTSRFFNRDPNLGYplwRLKTPEEheletgikskearkyiFNCLDDMAqvnmstdlegtdmlaekadrreyI 319
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1907082950  972 DLLDHMLTLDPSKRCTAEQTLQSDFLKDVELSkmappDLPH 1012
Cdd:cd14228    320 DLLKKMLTIDADKRITPLKTLNHPFVTMTHLL-----DFPH 355
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
718-994 1.15e-15

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 79.09  E-value: 1.15e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  718 RCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVV-------------- 783
Cdd:cd14049      3 RYLNEFEEIARLGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMKVLREVKVLAGLQHPNIVgyhtawmehvqlml 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  784 --NMKEIVTDKQDALDFKKDKGAFYlVFEYMDHDLMGLlesglvhfseDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNI 861
Cdd:cd14049     83 yiQMQLCELSLWDWIVERNKRPCEE-EFKSAPYTPVDV----------DVTTKILQQLLEGVTYIHSMGIVHRDLKPRNI 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  862 LLN-------------------------------NSRPYTNKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFtkK 910
Cdd:cd14049    152 FLHgsdihvrigdfglacpdilqdgndsttmsrlNGLTHTSGVGTCLYAAPEQLEGSH-YDFKSDMYSIGVILLELF--Q 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  911 PiFQANLELAqlELISRLCGSPCPavwpdviklpyfntmkpkKQYRRRLREEFSFIpsaaldllDHMLTLDPSKRCTAEQ 990
Cdd:cd14049    229 P-FGTEMERA--EVLTQLRNGQIP------------------KSLCKRWPVQAKYI--------KLLTSTEPSERPSASQ 279

                   ....
gi 1907082950  991 TLQS 994
Cdd:cd14049    280 LLES 283
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
729-916 1.29e-15

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: 79.71  E-value: 1.29e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKV----RLDNEKEGfpiTAIREIKILRQLVHQSVVNMKEIVTDKQDAldfkkdkga 804
Cdd:cd06635     33 IGHGSFGAVYFARDVRTSEVVAIKKMsysgKQSNEKWQ---DIIKEVKFLQRIKHPNSIEYKGCYLREHTA--------- 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  805 fYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN--------------SRPYT 870
Cdd:cd06635    101 -WLVMEYCLGSASDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEpgqvkladfgsasiASPAN 179
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1907082950  871 NKVITLWYRPPELLLG--EERYTPAIDVWSCGCILGELFTKK-PIFQAN 916
Cdd:cd06635    180 SFVGTPYWMAPEVILAmdEGQYDGKVDVWSLGITCIELAERKpPLFNMN 228
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
721-913 1.43e-15

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


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 79.58  E-value: 1.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDN--EKEgfPITAIR-EIKILRQLVHQSVVNMKEIVTDKQDald 797
Cdd:cd05599      1 EDFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEmlEKE--QVAHVRaERDILAEADNPWVVKLYYSFQDEEN--- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 fkkdkgaFYLVFEYMD-HDLMGLLESGLVhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS---------- 866
Cdd:cd05599     76 -------LYLIMEFLPgGDMMTLLMKKDT-LTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARghiklsdfgl 147
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  867 --------RPYTNkVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIF 913
Cdd:cd05599    148 ctglkkshLAYST-VGTPDYIAPEVFL-QKGYGKECDWWSLGVIMYEMLIGYPPF 200
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
723-997 1.44e-15

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: 78.25  E-value: 1.44e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEivtdkqdalDFKKDK 802
Cdd:cd08223      2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKE---------SFEGED 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 GAFYLVfeymdhdlMGLLESGLVH----------FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL--------- 863
Cdd:cd08223     73 GFLYIV--------MGFCEGGDLYtrlkeqkgvlLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLtksniikvg 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  864 ---------NNSRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANlelAQLELISRLCGSPCP 934
Cdd:cd08223    145 dlgiarvleSSSDMATTLIGTPYYMSPE-LFSNKPYNHKSDVWALGCCVYEMATLKHAFNAK---DMNSLVYKILEGKLP 220
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  935 AvwpdvikLPyfntmkpkKQYRRRLreefsfipsaaLDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd08223    221 P-------MP--------KQYSPEL-----------GELIKAMLHQDPEKRPSVKRILRQPYI 257
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
726-954 1.53e-15

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: 78.79  E-value: 1.53e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  726 IGIIGEGTYGQV----YKAKDKDTGELVALKKVRLDN---EKEGFpitaIREIKILRQLVHQSVVNMKEIVTDKQDAldf 798
Cdd:cd05080      9 IRDLGEGHFGKVslycYDPTNDGTGEMVAVKALKADCgpqHRSGW----KQEIDILKTLYHENIVKYKGCCSEQGGK--- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  799 kkdkgAFYLVFEYMD-HDLMGLLESGLVHFSEdhIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSR-------PYT 870
Cdd:cd05080     82 -----SLQLIMEYVPlGSLRDYLPKHSIGLAQ--LLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRlvkigdfGLA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  871 NKVIT---------------LWYRPPelLLGEERYTPAIDVWSCGCILGELFTK-------KPIFQANLELAQ------- 921
Cdd:cd05080    155 KAVPEgheyyrvredgdspvFWYAPE--CLKEYKFYYASDVWSFGVTLYELLTHcdssqspPTKFLEMIGIAQgqmtvvr 232
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1907082950  922 -LELISRLCGSPCPAVWP-DVIKL------------PYFNTMKPKKQ 954
Cdd:cd05080    233 lIELLERGERLPCPDKCPqEVYHLmkncweteasfrPTFENLIPILK 279
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
729-908 2.01e-15

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: 78.52  E-value: 2.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQV----YKAKDKDTGELVALKKVRLDNEK--EGFPitaiREIKILRQLVHQSVVNMKEIVtdkqdaldFKKDK 802
Cdd:cd14205     12 LGKGNFGSVemcrYDPLQDNTGEVVAVKKLQHSTEEhlRDFE----REIEILKSLQHDNIVKYKGVC--------YSAGR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 GAFYLVFEYMDHdlmGLLESGLVHFSE--DHIK--SFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSR----------- 867
Cdd:cd14205     80 RNLRLIMEYLPY---GSLRDYLQKHKEriDHIKllQYTSQICKGMEYLGTKRYIHRDLATRNILVENENrvkigdfgltk 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  868 --PYTNKVITL---------WYRPPELLlgEERYTPAIDVWSCGCILGELFT 908
Cdd:cd14205    157 vlPQDKEYYKVkepgespifWYAPESLT--ESKFSVASDVWSFGVVLYELFT 206
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
722-903 2.07e-15

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: 77.89  E-value: 2.07e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVrldneKEGFPITA--IREIKILRQLVHQSVVNMKEIV-TDKQDALdf 798
Cdd:cd14662      1 RYELVKDIGSGNFGVARLMRNKETKELVAVKYI-----ERGLKIDEnvQREIINHRSLRHPNIIRFKEVVlTPTHLAI-- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  799 kkdkgafylVFEYM-DHDLMG-LLESGlvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN------------ 864
Cdd:cd14662     74 ---------VMEYAaGGELFErICNAG--RFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDgspaprlkicdf 142
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1907082950  865 --------NSRPYTNkVITLWYRPPELLLGEERYTPAIDVWSCGCIL 903
Cdd:cd14662    143 gyskssvlHSQPKST-VGTPAYIAPEVLSRKEYDGKVADVWSCGVTL 188
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
729-916 2.51e-15

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 78.53  E-value: 2.51e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKV----RLDNEKEGfpiTAIREIKILRQLVHQSVVNMKEIVTDKQDAldfkkdkga 804
Cdd:cd06634     23 IGHGSFGAVYFARDVRNNEVVAIKKMsysgKQSNEKWQ---DIIKEVKFLQKLRHPNTIEYRGCYLREHTA--------- 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  805 fYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS--------------RPYT 870
Cdd:cd06634     91 -WLVMEYCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPglvklgdfgsasimAPAN 169
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1907082950  871 NKVITLWYRPPELLLG--EERYTPAIDVWSCGCILGELFTKK-PIFQAN 916
Cdd:cd06634    170 SFVGTPYWMAPEVILAmdEGQYDGKVDVWSLGITCIELAERKpPLFNMN 218
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
726-997 3.00e-15

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: 77.47  E-value: 3.00e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  726 IGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILrqlvhqSVVNMKEIVTDKQDALDfkkdKGAF 805
Cdd:cd08221      5 VRVLGRGAFGEAVLYRKTEDNSLVVWKEVNLSRLSEKERRDALNEIDIL------SLLNHDNIITYYNHFLD----GESL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  806 YLVFEYMD----HDLMGLLESGLvhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS--------------- 866
Cdd:cd08221     75 FIEMEYCNggnlHDKIAQQKNQL--FPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKAdlvklgdfgiskvld 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 ---RPYTNKVITLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANLELaqlelisRLCGSPCPAVWPDVIkl 943
Cdd:cd08221    153 sesSMAESIVGTPYYMSPELVQG-VKYNFKSDIWAVGCVLYELLTLKRTFDATNPL-------RLAVKIVQGEYEDID-- 222
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  944 pyfntmkpkKQYRRRLREefsfipsaaldLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd08221    223 ---------EQYSEEIIQ-----------LVHDCLHQDPEDRPTAEELLERPLL 256
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
723-1012 3.32e-15

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


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 78.51  E-value: 3.32e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVR----LDNEKEGFP-----ITAIREIKILRQLvhqsvvnmkeivtdkQ 793
Cdd:cd05601      3 FEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKksetLAQEEVSFFeeerdIMAKANSPWITKL---------------Q 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  794 DALdfkKDKGAFYLVFEYM-DHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNIL---------- 862
Cdd:cd05601     68 YAF---QDSENLYLVMEYHpGGDLLSLLSRYDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILidrtghikla 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  863 -------LNNSRPYTNK--VITLWYRPPELLLGEER-----YTPAIDVWSCGCILGELFTKKPIFQAnlelaqlelisrl 928
Cdd:cd05601    145 dfgsaakLSSDKTVTSKmpVGTPDYIAPEVLTSMNGgskgtYGVECDWWSLGIVAYEMLYGKTPFTE------------- 211
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  929 cgspcpavwpDVIKLPYFNTMKPKKQYrrRLREEFSfIPSAALDLLDHMLTlDPSKRCTAEQTLQSDFLKDVELSK---M 1005
Cdd:cd05601    212 ----------DTVIKTYSNIMNFKKFL--KFPEDPK-VSESAVDLIKGLLT-DAKERLGYEGLCCHPFFSGIDWNNlrqT 277

                   ....*..
gi 1907082950 1006 APPDLPH 1012
Cdd:cd05601    278 VPPFVPT 284
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
729-1011 3.74e-15

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


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 77.57  E-value: 3.74e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKV---RLdnEKEGFPITAIREIKILRQLVHQSVVNMkeivtdkqdALDFKKdKGAF 805
Cdd:cd05577      1 LGRGGFGEVCACQVKATGKMYACKKLdkkRI--KKKKGETMALNEKIILEKVSSPFIVSL---------AYAFET-KDKL 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  806 YLVFEYMDH-DL-MGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-----------------S 866
Cdd:cd05577     69 CLVLTLMNGgDLkYHIYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDhghvrisdlglavefkgG 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 RPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLcgspcpaVWPDVIKLPyf 946
Cdd:cd05577    149 KKIKGRVGTHGYMAPEVLQKEVAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEELKRR-------TLEMAVEYP-- 219
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  947 ntmkpkkqyrrrlrEEFSfipSAALDLLDHMLTLDPSKRC-----TAEQTLQSDFLKD-----VELSKMAPPDLP 1011
Cdd:cd05577    220 --------------DSFS---PEARSLCEGLLQKDPERRLgcrggSADEVKEHPFFRSlnwqrLEAGMLEPPFVP 277
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
722-997 4.88e-15

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 77.97  E-value: 4.88e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKD-TGELVALKKVR-LDNEKEGfpitAIREIKILRQLVHQSVVNMKEIVtdkqDALDFK 799
Cdd:cd14213     13 RYEIVDTLGEGAFGKVVECIDHKmGGMHVAVKIVKnVDRYREA----ARSEIQVLEHLNTTDPNSTFRCV----QMLEWF 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 KDKGAFYLVFEymdhdLMGLL------ESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS------- 866
Cdd:cd14213     85 DHHGHVCIVFE-----LLGLStydfikENSFLPFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQSdyvvkyn 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 ---------------------------RPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQANLEL 919
Cdd:cd14213    160 pkmkrdertlknpdikvvdfgsatyddEHHSTLVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSK 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  920 AQLELISRLCGsPCPA-VWPDVIKLPYFN------------------TMKPKKQYRRRLREEFSFIpsaaLDLLDHMLTL 980
Cdd:cd14213    239 EHLAMMERILG-PLPKhMIQKTRKRKYFHhdqldwdehssagryvrrRCKPLKEFMLSQDVDHEQL----FDLIQKMLEY 313
                          330
                   ....*....|....*..
gi 1907082950  981 DPSKRCTAEQTLQSDFL 997
Cdd:cd14213    314 DPAKRITLDEALKHPFF 330
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
714-997 5.42e-15

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 78.13  E-value: 5.42e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  714 DWGKrcvDKFDIIGIIGEGTYGQVYKAKD-KDTGELVALKKVRldnEKEGFPITAIREIKILRQLVHQSVVNmKEIVTDK 792
Cdd:cd14215      8 DWLQ---ERYEIVSTLGEGTFGRVVQCIDhRRGGARVALKIIK---NVEKYKEAARLEINVLEKINEKDPEN-KNLCVQM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  793 QDALDFkkdKGAFYLVFEYMDHDLMGLL-ESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS----- 866
Cdd:cd14215     81 FDWFDY---HGHMCISFELLGLSTFDFLkENNYLPYPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVNSdyelt 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 -----------------------------RPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQANL 917
Cdd:cd14215    158 ynlekkrdersvkstairvvdfgsatfdhEHHSTIVSTRHYRAPEVIL-ELGWSQPCDVWSIGCIIFEYYVGFTLFQTHD 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  918 ELAQLELISRLCGsPCPA-VWPDVIKLPYF---------NT---------MKPKKQYRRRLREEFSFIpsaaLDLLDHML 978
Cdd:cd14215    237 NREHLAMMERILG-PIPSrMIRKTRKQKYFyhgrldwdeNTsagryvrenCKPLRRYLTSEAEEHHQL----FDLIESML 311
                          330
                   ....*....|....*....
gi 1907082950  979 TLDPSKRCTAEQTLQSDFL 997
Cdd:cd14215    312 EYEPSKRLTLAAALKHPFF 330
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
723-994 7.43e-15

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: 76.57  E-value: 7.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRL---DNEKEgfpitAIREIKILRQLVHQSVVNMKE--IVTDKQdald 797
Cdd:cd13986      2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILChskEDVKE-----AMREIENYRLFNHPNILRLLDsqIVKEAG---- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 fkkDKGAFYLVFEYMDH-DLMGLLESGLVH---FSEDHIKSFMKQLMEGLDYCHK---KNFLHRDIKCSNILL------- 863
Cdd:cd13986     73 ---GKKEVYLLLPYYKRgSLQDEIERRLVKgtfFPEDRILHIFLGICRGLKAMHEpelVPYAHRDIKPGNVLLseddepi 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  864 --------------NNSR------PYTNKVITLWYRPPEL--LLGEERYTPAIDVWSCGCILGEL-FTKKPifqanlela 920
Cdd:cd13986    150 lmdlgsmnparieiEGRRealalqDWAAEHCTMPYRAPELfdVKSHCTIDEKTDIWSLGCTLYALmYGESP--------- 220
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  921 qLELISRLCGSPCPAVWPDVIKLPyfntmkPKKQYrrrlreefsfiPSAALDLLDHMLTLDPSKRCTAEQTLQS 994
Cdd:cd13986    221 -FERIFQKGDSLALAVLSGNYSFP------DNSRY-----------SEELHQLVKSMLVVNPAERPSIDDLLSR 276
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
729-913 9.96e-15

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: 75.55  E-value: 9.96e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDtgELVALKKVRLDNEKEGFpitaIREIKILRQLVHQSVVNMKEIVTDKQdaldfkkdkgAFYLV 808
Cdd:cd14058      1 VGRGSFGVVCKARWRN--QIVAVKIIESESEKKAF----EVEVRQLSRVDHPNIIKLYGACSNQK----------PVCLV 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDH-DLMGLLES--GLVHFSEDHIKSFMKQLMEGLDYCHK---KNFLHRDIKCSNILLNN----------------S 866
Cdd:cd14058     65 MEYAEGgSLYNVLHGkePKPIYTAAHAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNggtvlkicdfgtacdiS 144
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1907082950  867 RPYTNKVITLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIF 913
Cdd:cd14058    145 THMTNNKGSAAWMAPEVFEG-SKYSEKCDVFSWGIILWEVITRRKPF 190
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
721-993 1.21e-14

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 76.30  E-value: 1.21e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIG-IIGEGTYGQVYKAKDKDTGELVALKKVrldNEKEGFPITAI-REIKILRQLV-HQSVVNMKEivtdkqdald 797
Cdd:cd14090      1 DLYKLTGeLLGEGAYASVQTCINLYTGKEYAVKII---EKHPGHSRSRVfREVETLHQCQgHPNILQLIE---------- 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 FKKDKGAFYLVFEYMDH-DLMGLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN----------- 865
Cdd:cd14090     68 YFEDDERFYLVFEKMRGgPLLSHIEKR-VHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESmdkvspvkicd 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 ----SRPYTNKVITLWYRPPELL--LGEERY-TPAI---------------DVWSCGCILGELFTKKPIFQANlelaqle 923
Cdd:cd14090    147 fdlgSGIKLSSTSMTPVTTPELLtpVGSAEYmAPEVvdafvgealsydkrcDLWSLGVILYIMLCGYPPFYGR------- 219
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  924 lisrlCGSPCPavW------PDVIKLPYFNTMKPKKQYRRRlreEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd14090    220 -----CGEDCG--WdrgeacQDCQELLFHSIQEGEYEFPEK---EWSHISAEAKDLISHLLVRDASQRYTAEQVLQ 285
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
729-908 1.97e-14

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


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 75.56  E-value: 1.97e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNE-----KEGFPItairEIKILRQLVHQSVVNMKEIvtdkQDALDFKKDKG 803
Cdd:cd13989      1 LGSGGFGYVTLWKHQDTGEYVAIKKCRQELSpsdknRERWCL----EVQIMKKLNHPNVVSARDV----PPELEKLSPND 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  804 AFYLVFEYMDH-DLMGLLE-----SGLvhfSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLnnsRPYTNKVI--- 874
Cdd:cd13989     73 LPLLAMEYCSGgDLRKVLNqpencCGL---KESEVRTLLSDISSAISYLHENRIIHRDLKPENIVL---QQGGGRVIykl 146
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  875 --------------------TLWYRPPElLLGEERYTPAIDVWSCGCILGELFT 908
Cdd:cd13989    147 idlgyakeldqgslctsfvgTLQYLAPE-LFESKKYTCTVDYWSFGTLAFECIT 199
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
728-939 1.99e-14

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 75.06  E-value: 1.99e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVRLD--NEKEGFPITAIR-EIKILRQLVHQSVVNMKEIVTDKQDaldfKKdkga 804
Cdd:cd06653      9 LLGRGAFGEVYLCYDADTGRELAVKQVPFDpdSQETSKEVNALEcEIQLLKNLRHDRIVQYYGCLRDPEE----KK---- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  805 FYLVFEYMDHdlmGLLESGLVHF---SEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPY------TNKVI- 874
Cdd:cd06653     81 LSIFVEYMPG---GSVKDQLKAYgalTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVklgdfgASKRIq 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  875 --------------TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQanlELAQLELISRLCGSPCPAVWPD 939
Cdd:cd06653    158 ticmsgtgiksvtgTPYWMSPEVISGEG-YGRKADVWSVACTVVEMLTEKPPWA---EYEAMAAIFKIATQPTKPQLPD 232
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
725-934 2.07e-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: 75.19  E-value: 2.07e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  725 IIGIIGEGTYGQV-----YKAKDKDTGELVA---LKKVRLDNEKEGFPitaiREIKILRQLVHQSVVNMKEIVTDKqdal 796
Cdd:cd05049      9 LKRELGEGAFGKVflgecYNLEPEQDKMLVAvktLKDASSPDARKDFE----REAELLTNLQHENIVKFYGVCTEG---- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  797 dfkkdkGAFYLVFEYMDH-DLMGLLESG------LVHFSEDHIKSFMKQLME-------GLDYCHKKNFLHRDIKCSNIL 862
Cdd:cd05049     81 ------DPLLMVFEYMEHgDLNKFLRSHgpdaafLASEDSAPGELTLSQLLHiavqiasGMVYLASQHFVHRDLATRNCL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  863 LNN-----------SRP-YTNKvitlWYR------------PPELLLgEERYTPAIDVWSCGCILGELFT--KKPIFQ-A 915
Cdd:cd05049    155 VGTnlvvkigdfgmSRDiYSTD----YYRvgghtmlpirwmPPESIL-YRKFTTESDVWSFGVVLWEIFTygKQPWFQlS 229
                          250       260
                   ....*....|....*....|.
gi 1907082950  916 NLELAQLELISRLCGSP--CP 934
Cdd:cd05049    230 NTEVIECITQGRLLQRPrtCP 250
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
723-992 2.39e-14

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: 74.65  E-value: 2.39e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREikilrqlvhqsvVNMKEIVTDKQDALDFKK-- 800
Cdd:cd14050      3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDRKRKLEE------------VERHEKLGEHPNCVRFIKaw 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 -DKGAFYLVFEYMDHDLMGLLEsGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPY---------- 869
Cdd:cd14050     71 eEKGILYIQTELCDTSLQQYCE-ETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCklgdfglvve 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  870 --TNKVITLW-----YRPPELLLGeeRYTPAIDVWSCGCILGELFTkkpifqaNLELAQlelisrlcGSPcpaVWPDVik 942
Cdd:cd14050    150 ldKEDIHDAQegdprYMAPELLQG--SFTKAADIFSLGITILELAC-------NLELPS--------GGD---GWHQL-- 207
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  943 lpyfntmkpKKQYrrrLREEF-SFIPSAALDLLDHMLTLDPSKRCTAEQTL 992
Cdd:cd14050    208 ---------RQGY---LPEEFtAGLSPELRSIIKLMMDPDPERRPTAEDLL 246
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
721-993 2.67e-14

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: 74.83  E-value: 2.67e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVA---LKKVRLDNEKEGFPITAI-REIKILRQLVHQSVVNMKEIVTDKQDAL 796
Cdd:cd14105      5 DFYDIGEELGSGQFAVVKKCREKSTGLEYAakfIKKRRSKASRRGVSREDIeREVSILRQVLHPNIITLHDVFENKTDVV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  797 dfkkdkgafyLVFEYMD----HDLMGLLESglvhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL--NNSRPYT 870
Cdd:cd14105     85 ----------LILELVAggelFDFLAEKES----LSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLldKNVPIPR 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  871 NKVI-------------------TLWYRPPELLLGEERYTPAiDVWSCGCILGELFTKKPIFQANLELAQLELISRlcgs 931
Cdd:cd14105    151 IKLIdfglahkiedgnefknifgTPEFVAPEIVNYEPLGLEA-DMWSIGVITYILLSGASPFLGDTKQETLANITA---- 225
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  932 pcpavwpdvikLPY-FNtmkpkkqyrrrlREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd14105    226 -----------VNYdFD------------DEYFSNTSELAKDFIRQLLVKDPRKRMTIQESLR 265
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
721-932 2.75e-14

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


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 75.82  E-value: 2.75e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKkvrldnekegfpitAIREIKILR--QLVHqsVVNMKEIVTDKQDALDF 798
Cdd:cd05598      1 SMFEKIKTIGVGAFGEVSLVRKKDTNALYAMK--------------TLRKKDVLKrnQVAH--VKAERDILAEADNEWVV 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  799 K-----KDKGAFYLVFEYM-DHDLMGLL-ESGLvhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN------- 864
Cdd:cd05598     65 KlyysfQDKENLYFVMDYIpGGDLMSLLiKKGI--FEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDrdghikl 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 -------------NSRPYTNK--VITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIF---------------- 913
Cdd:cd05598    143 tdfglctgfrwthDSKYYLAHslVGTPNYIAPEVLL-RTGYTQLCDWWSVGVILYEMLVGQPPFlaqtpaetqlkvinwr 221
                          250       260
                   ....*....|....*....|....*.
gi 1907082950  914 -------QANLELAQLELISRLCGSP 932
Cdd:cd05598    222 ttlkiphEANLSPEAKDLILRLCCDA 247
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
723-995 2.75e-14

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: 74.34  E-value: 2.75e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKK----VRLDNEKEgfpiTAIREIKILRQL-VHQSVVNMkeivtdkqdaLD 797
Cdd:cd13997      2 FHELEQIGSGSFSEVFKVRSKVDGCLYAVKKskkpFRGPKERA----RALREVEAHAALgQHPNIVRY----------YS 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 FKKDKGAFYLVFEYMD-HDLMGLLE--SGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRpyTNK-- 872
Cdd:cd13997     68 SWEEGGHLYIQMELCEnGSLQDALEelSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKG--TCKig 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  873 ---VITLW------------YRPPELLLGEERYTPAIDVWSCGCILgelftkkpifqanLELAqlelisrlCGSPCPAvw 937
Cdd:cd13997    146 dfgLATRLetsgdveegdsrYLAPELLNENYTHLPKADIFSLGVTV-------------YEAA--------TGEPLPR-- 202
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  938 pdviklpyfntmkpKKQYRRRLRE-EFSFIPSAAL-----DLLDHMLTLDPSKRCTAEQTLQSD 995
Cdd:cd13997    203 --------------NGQQWQQLRQgKLPLPPGLVLsqeltRLLKVMLDPDPTRRPTADQLLAHD 252
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
656-997 2.95e-14

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 76.02  E-value: 2.95e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  656 QRTRHLLTDLPLPPElPGGDPSPPDSPEPKAITPPQQPYkkrpkiccprygerrqtesdwgkrcvDKFDIIGIIGEGTYG 735
Cdd:PLN00034    36 QRDPSLAVPLPLPPP-SSSSSSSSSSSASGSAPSAAKSL--------------------------SELERVNRIGSGAGG 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  736 QVYKAKDKDTGELVALKkVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKeivtdkqdalDFKKDKGAFYLVFEYMDHd 815
Cdd:PLN00034    89 TVYKVIHRPTGRLYALK-VIYGNHEDTVRRQICREIEILRDVNHPNVVKCH----------DMFDHNGEIQVLLEFMDG- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  816 lmGLLESGLVHfSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSR------------------PYTNKVITLW 877
Cdd:PLN00034   157 --GSLEGTHIA-DEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKnvkiadfgvsrilaqtmdPCNSSVGTIA 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  878 YRPPELL---LGEERYTP-AIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDVIklpyfntmkpkk 953
Cdd:PLN00034   234 YMSPERIntdLNHGAYDGyAGDIWSLGVSILEFYLGRFPFGVGRQGDWASLMCAICMSQPPEAPATAS------------ 301
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1907082950  954 qyrrrlREEFSFIPSAaldlldhmLTLDPSKRCTAEQTLQSDFL 997
Cdd:PLN00034   302 ------REFRHFISCC--------LQREPAKRWSAMQLLQHPFI 331
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
729-941 3.99e-14

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: 74.02  E-value: 3.99e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLD---NEKEGFpitaIREIKILRQLVHQSVVNMKEIVTDKQdaldfkkdkgAF 805
Cdd:cd05041      3 IGRGNFGDVYRGVLKPDNTEVAVKTCRETlppDLKRKF----LQEARILKQYDHPNIVKLIGVCVQKQ----------PI 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  806 YLVFEYMD-HDLMGLLESglvhfSEDHIKsfMKQLME-------GLDYCHKKNFLHRDIKCSNILL--NN---------S 866
Cdd:cd05041     69 MIVMELVPgGSLLTFLRK-----KGARLT--VKQLLQmcldaaaGMEYLESKNCIHRDLAARNCLVgeNNvlkisdfgmS 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 RPYTNKVITL----------WYRPPELLLGeeRYTPAIDVWSCGCILGELFTKKPIFQANLELAQL-ELISRLCGSPCPA 935
Cdd:cd05041    142 REEEDGEYTVsdglkqipikWTAPEALNYG--RYTSESDVWSFGILLWEIFSLGATPYPGMSNQQTrEQIESGYRMPAPE 219

                   ....*.
gi 1907082950  936 VWPDVI 941
Cdd:cd05041    220 LCPEAV 225
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
722-997 4.08e-14

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK1 binds with high affinity the alternative splicing factor, SRSF1 (serine/arginine-rich splicing factor 1), and regiospecifically phosphorylates 10-12 serines in its RS domain. It plays a role in the regulation of pre-mRNA splicing, chromatin structure, and germ cell development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271118 [Multi-domain]  Cd Length: 349  Bit Score: 75.45  E-value: 4.08e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRldnEKEGFPITAIREIKILRqlvhqSVVNM------KEIVTDKQDA 795
Cdd:cd14216     11 RYHVIRKLGWGHFSTVWLSWDIQGKRFVAMKVVK---SAEHYTETALDEIKLLK-----SVRNSdpndpnREMVVQLLDD 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  796 LDFKKDKGAFY-LVFEYMDHDLMG-LLESGLVHFSEDHIKSFMKQLMEGLDYCHKK-NFLHRDIKCSNILLNNSRPY--- 869
Cdd:cd14216     83 FKISGVNGTHIcMVFEVLGHHLLKwIIKSNYQGLPLPCVKKIIRQVLQGLDYLHTKcRIIHTDIKPENILLSVNEQYirr 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  870 ------------------------------------------TNKVITLWYRPPELLLGEERYTPAiDVWSCGCILGELF 907
Cdd:cd14216    163 laaeatewqrnflvnplepknaeklkvkiadlgnacwvhkhfTEDIQTRQYRSLEVLIGSGYNTPA-DIWSTACMAFELA 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  908 TKKPIFQAN-------------LELAQLELISR---LCGSPCPAVWPDVIKLPYFNTMKPKKQYrRRLREEFSFIPSAA- 970
Cdd:cd14216    242 TGDYLFEPHsgedysrdedhiaLIIELLGKVPRkliVAGKYSKEFFTKKGDLKHITKLKPWGLF-EVLVEKYEWSQEEAa 320
                          330       340
                   ....*....|....*....|....*....
gi 1907082950  971 --LDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14216    321 gfTDFLLPMLELIPEKRATAAECLRHPWL 349
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
725-1013 4.84e-14

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: 74.40  E-value: 4.84e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  725 IIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDnEKEGFPITAIREIKILRQLVHQSVVNMKeivtdkqdaldfkkdkGA 804
Cdd:cd06620      9 TLKDLGAGNGGSVSKVLHIPTGTIMAKKVIHID-AKSSVRKQILRELQILHECHSPYIVSFY----------------GA 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  805 FY-------LVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKK-NFLHRDIKCSNILLNN----------- 865
Cdd:cd06620     72 FLnennniiICMEYMDCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSkgqiklcdfgv 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 SRPYTNKVI-----TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANLELAQ--------LELISRLCGSP 932
Cdd:cd06620    152 SGELINSIAdtfvgTSTYMSPERIQGGK-YSVKSDVWSLGLSIIELALGEFPFAGSNDDDDgyngpmgiLDLLQRIVNEP 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  933 CPavwpdviklpyfntmkpkkqyrrRLREEFSFiPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLKDVElsKMAPPDLPH 1012
Cdd:cd06620    231 PP-----------------------RLPKDRIF-PKDLRDFVDRCLLKDPRERPSPQLLLDHDPFIQAV--RASDVDLRA 284

                   .
gi 1907082950 1013 W 1013
Cdd:cd06620    285 W 285
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
729-911 5.01e-14

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: 73.68  E-value: 5.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFpitaIREIKILRQLVHQSVVNMKEI-VTDKQdaldfkkdkgaFYL 807
Cdd:cd14065      1 LGKGFFGEVYKVTHRETGKVMVMKELKRFDEQRSF----LKEVKLMRRLSHPNILRFIGVcVKDNK-----------LNF 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYMDH-DLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTNKVIT----------- 875
Cdd:cd14065     66 ITEYVNGgTLEELLKSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRNAVVAdfglarempde 145
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  876 ----------------LWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKP 911
Cdd:cd14065    146 ktkkpdrkkrltvvgsPYWMAPEMLRGES-YDEKVDVFSFGIVLCEIIGRVP 196
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
729-993 5.01e-14

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 73.92  E-value: 5.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRL-----DNEKEgfpitAIREIKILRQ-LVHQSVVNMKEIVTDKQDALdfkkdk 802
Cdd:cd14106     16 LGRGKFAVVRKCIHKETGKEYAAKFLRKrrrgqDCRNE-----ILHEIAVLELcKDCPRVVNLHEVYETRSELI------ 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 gafyLVFEYMDHdlmGLLESGLV---HFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTNKVI----- 874
Cdd:cd14106     85 ----LILELAAG---GELQTLLDeeeCLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPLGDIKLcdfgi 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  875 ---------------TLWYRPPELLlgeeRYTP---AIDVWSCGCILGELFTKKPIFQANLELAQLELISRlcgspCPAV 936
Cdd:cd14106    158 srvigegeeireilgTPDYVAPEIL----SYEPislATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQ-----CNLD 228
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  937 WPDviklpyfntmkpkkqyrrrlrEEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd14106    229 FPE---------------------ELFKDVSPLAIDFIKRLLVKDPEKRLTAKECLE 264
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
728-997 6.50e-14

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


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 73.42  E-value: 6.50e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALK-----KVRLDNEKEGFpitaIREIKILRQLVHQSVVNMKEIVTDKQDaldfkkdk 802
Cdd:cd14189      8 LLGKGGFARCYEMTDLATNKTYAVKviphsRVAKPHQREKI----VNEIELHRDLHHKHVVKFSHHFEDAEN-------- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 gaFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS--------------RP 868
Cdd:cd14189     76 --IYIFLELCSRKSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENmelkvgdfglaarlEP 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  869 YTNKVITLW----YRPPELLLgEERYTPAIDVWSCGCILGELftkkpifqanlelaqlelisrLCGSPcPavwpdviklp 944
Cdd:cd14189    154 PEQRKKTICgtpnYLAPEVLL-RQGHGPESDVWSLGCVMYTL---------------------LCGNP-P---------- 200
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  945 yFNTMKPKKQYRRRLREEF---SFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14189    201 -FETLDLKETYRCIKQVKYtlpASLSLPARHLLAGILKRNPGDRLTLDQILEHEFF 255
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
729-998 7.50e-14

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: 73.50  E-value: 7.50e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVA---LKKVRLDNEKEGFPITAI-REIKILRQLVHQSVVNMKEIVTDKQDALdfkkdkga 804
Cdd:cd14195     13 LGSGQFAIVRKCREKGTGKEYAakfIKKRRLSSSRRGVSREEIeREVNILREIQHPNIITLHDIFENKTDVV-------- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  805 fyLVFEYMD----HDLMGLLESglvhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNI-LLNNSRP----------- 868
Cdd:cd14195     85 --LILELVSggelFDFLAEKES----LTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENImLLDKNVPnpriklidfgi 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  869 ---------YTNKVITLWYRPPELLlgeeRYTP---AIDVWSCGCILGELFTKKPIFQANLELAQLELISrlcgspcpAV 936
Cdd:cd14195    159 ahkieagneFKNIFGTPEFVAPEIV----NYEPlglEADMWSIGVITYILLSGASPFLGETKQETLTNIS--------AV 226
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  937 WPDVIKLPYFNTMKPKKQYRRRLreefsfipsaaldlldhmLTLDPSKRCTAEQTLQSDFLK 998
Cdd:cd14195    227 NYDFDEEYFSNTSELAKDFIRRL------------------LVKDPKKRMTIAQSLEHSWIK 270
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
722-998 7.52e-14

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: 73.74  E-value: 7.52e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEgfpITAIREIKILRQLVHQSVVNMKEivtdKQDALDfkkd 801
Cdd:cd14104      1 KYMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGADQ---VLVKKEISILNIARHRNILRLHE----SFESHE---- 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 kgAFYLVFEYMD-HDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTNKVI------ 874
Cdd:cd14104     70 --ELVMIFEFISgVDIFERITTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGSYIKIIefgqsr 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  875 --------TLWYRPPELLLGE----ERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELIsrlcgspCPAVWPdvik 942
Cdd:cd14104    148 qlkpgdkfRLQYTSAEFYAPEvhqhESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENI-------RNAEYA---- 216
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  943 lpyFNTmkpkkqyrrrlrEEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLK 998
Cdd:cd14104    217 ---FDD------------EAFKNISIEALDFVDRLLVKERKSRMTAQEALNHPWLK 257
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
729-997 9.35e-14

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: 73.87  E-value: 9.35e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKvrLDNEKEGFPITAIREIKILRQLVHQSVVNMkeivtdkqdaldFKKdkgafYLV 808
Cdd:cd06659     29 IGEGSTGVVCIAREKHSGRQVAVKM--MDLRKQQRRELLFNEVVIMRDYQHPNVVEM------------YKS-----YLV 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMdHDLMGLLESGL-------VHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL-----------------N 864
Cdd:cd06659     90 GEEL-WVLMEYLQGGAltdivsqTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLtldgrvklsdfgfcaqiS 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 NSRPYTNKVI-TLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQANlelAQLELISRLCGSPCPavwpdviKL 943
Cdd:cd06659    169 KDVPKRKSLVgTPYWMAPEVIS-RCPYGTEVDIWSLGIMVIEMVDGEPPYFSD---SPVQAMKRLRDSPPP-------KL 237
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  944 PYFNTMKPKkqyrrrLReefsfipsaalDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd06659    238 KNSHKASPV------LR-----------DFLERMLVRDPQERATAQELLDHPFL 274
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
729-908 9.37e-14

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


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 73.42  E-value: 9.37e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQV----YKAKDKDTGELVALKKvrLDNEKEGFPITAI-REIKILRQLVHQSVVNMKEIVTDKQDAldfkkdkg 803
Cdd:cd05079     12 LGEGHFGKVelcrYDPEGDNTGEQVAVKS--LKPESGGNHIADLkKEIEILRNLYHENIVKYKGICTEDGGN-------- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  804 AFYLVFEYMDH-DLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRP-------------- 868
Cdd:cd05079     82 GIKLIMEFLPSgSLKEYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQvkigdfgltkaiet 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1907082950  869 ----YTNK----VITLWYrPPELLLGEERYTpAIDVWSCGCILGELFT 908
Cdd:cd05079    162 dkeyYTVKddldSPVFWY-APECLIQSKFYI-ASDVWSFGVTLYELLT 207
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
721-998 1.41e-13

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 72.64  E-value: 1.41e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLD-------NEKEGFPITAIREIKILRQLV-HQSVVNMKeivtdk 792
Cdd:cd14182      3 EKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDITgggsfspEEVQELREATLKEIDILRKVSgHPNIIQLK------ 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  793 qdalDFKKDKGAFYLVFEYMDH-DLMGLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSR---- 867
Cdd:cd14182     77 ----DTYETNTFFFLVFDLMKKgELFDYLTEK-VTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMnikl 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  868 ---------PYTNKVI----TLWYRPPELLL-----GEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELI---S 926
Cdd:cd14182    152 tdfgfscqlDPGEKLRevcgTPGYLAPEIIEcsmddNHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMImsgN 231
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  927 RLCGSPcpaVWPDviklpYFNTMKpkkqyrrrlreefsfipsaalDLLDHMLTLDPSKRCTAEQTLQSDFLK 998
Cdd:cd14182    232 YQFGSP---EWDD-----RSDTVK---------------------DLISRFLVVQPQKRYTAEEALAHPFFQ 274
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
728-998 2.13e-13

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 72.37  E-value: 2.13e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVRldnEKEGFPITAI-REIKILRQLvhQSVVNMKEIVtdkqdalDFKKDKGAFY 806
Cdd:cd14174      9 LLGEGAYAKVQGCVSLQNGKEYAVKIIE---KNAGHSRSRVfREVETLYQC--QGNKNILELI-------EFFEDDTRFY 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNIL----------------------LN 864
Cdd:cd14174     77 LVFEKLRGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILcespdkvspvkicdfdlgsgvkLN 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 NS-RPYTNKVITL-----WYRPPEL--LLGEER--YTPAIDVWSCGCILGELFTKKPIFQANlelaqlelisrlCGSPCP 934
Cdd:cd14174    157 SAcTPITTPELTTpcgsaEYMAPEVveVFTDEAtfYDKRCDLWSLGVILYIMLSGYPPFVGH------------CGTDCG 224
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  935 AVWPDVIKLPYFNTMKPKKQYRRRLRE-EFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLK 998
Cdd:cd14174    225 WDRGEVCRVCQNKLFESIQEGKYEFPDkDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWVQ 289
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
728-997 2.48e-13

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: 71.70  E-value: 2.48e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKdKDTGELVALKKVRLDN------EKEGFPITaiREIKILRQLVHQSVVNMkeIVTDKQDALdfkkd 801
Cdd:cd06631      8 VLGKGAYGTVYCGL-TSTGQLIAVKQVELDTsdkekaEKEYEKLQ--EEVDLLKTLKHVNIVGY--LGTCLEDNV----- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 kgafylVFEYMDHDLMGLLESGLVHFS---EDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL--------------- 863
Cdd:cd06631     78 ------VSIFMEFVPGGSIASILARFGaleEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLmpngviklidfgcak 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  864 ----NNSRPYTNKVI-----TLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPifqanlelaqlelisrlcgsPcp 934
Cdd:cd06631    152 rlciNLSSGSQSQLLksmrgTPYWMAPEVIN-ETGHGRKSDIWSIGCTVFEMATGKP--------------------P-- 208
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  935 avWPDVIKLPYFNTMKPKKQYRRRLREEFSfipSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd06631    209 --WADMNPMAAIFAIGSGRKPVPRLPDKFS---PEARDFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
729-903 2.64e-13

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: 71.56  E-value: 2.64e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVrldnEKEGFPITAI-----REIKILRQLVHQSVVNMKEIVtdkqdaldfKKDKG 803
Cdd:cd14163      8 IGEGTYSKVKEAFSKKHQRKVAIKII----DKSGGPEEFIqrflpRELQIVERLDHKNIIHVYEML---------ESADG 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  804 AFYLVFEYM-DHDLMGLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN----------------- 865
Cdd:cd14163     75 KIYLVMELAeDGDVFDCVLHG-GPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGftlkltdfgfakqlpkg 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1907082950  866 ----SRPYTNKVItlwYRPPELLLGEERYTPAIDVWSCGCIL 903
Cdd:cd14163    154 grelSQTFCGSTA---YAAPEVLQGVPHDSRKGDIWSMGVVL 192
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
729-906 3.29e-13

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


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 72.60  E-value: 3.29e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKV--RLDNEKEGFPITaIREIKIL-RQLVHQS--VVNMKeivtdkqdaLDFKKDKG 803
Cdd:cd05586      1 IGKGTFGQVYQVRKKDTRRIYAMKVLskKVIVAKKEVAHT-IGERNILvRTALDESpfIVGLK---------FSFQTPTD 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  804 aFYLVFEYMDHdlmGLLESGLVH---FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN---------------- 864
Cdd:cd05586     71 -LYLVTDYMSG---GELFWHLQKegrFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDanghialcdfglskad 146
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1907082950  865 -NSRPYTNKVI-TLWYRPPELLLGEERYTPAIDVWSCGCILGEL 906
Cdd:cd05586    147 lTDNKTTNTFCgTTEYLAPEVLLDEKGYTKMVDFWSLGVLVFEM 190
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
728-903 3.87e-13

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 71.29  E-value: 3.87e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVrldnEKEGFPITAIR----EIKILRQLVHQSVVNMKEIVTDKQdaldfkkdkg 803
Cdd:cd14082     10 VLGSGQFGIVYGGKHRKTGRDVAIKVI----DKLRFPTKQESqlrnEVAILQQLSHPGVVNLECMFETPE---------- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  804 AFYLVFEYMDHDLMGL-LESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTN---------KV 873
Cdd:cd14082     76 RVFVVMEKLHGDMLEMiLSSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPFPQvklcdfgfaRI 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1907082950  874 I-----------TLWYRPPELLLgEERYTPAIDVWSCGCIL 903
Cdd:cd14082    156 IgeksfrrsvvgTPAYLAPEVLR-NKGYNRSLDMWSVGVII 195
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
728-916 3.95e-13

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: 71.19  E-value: 3.95e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKD-KDTGELVALKKVRLDNEKEGfPITAIREIKILRQLVHQSVVNMkeivtdkqdaLDFKKDKGAFY 806
Cdd:cd14201     13 LVGHGAFAVVFKGRHrKKTDWEVAIKSINKKNLSKS-QILLGKEIKILKELQHENIVAL----------YDVQEMPNSVF 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVFEYMDH-DLMGLLESGLVhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN--NSRPYTNKVITL------- 876
Cdd:cd14201     82 LVMEYCNGgDLADYLQAKGT-LSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSyaSRKKSSVSGIRIkiadfgf 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  877 -----------------WYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQAN 916
Cdd:cd14201    161 arylqsnmmaatlcgspMYMAPEVIM-SQHYDAKADLWSIGTVIYQCLVGKPPFQAN 216
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
729-1007 4.04e-13

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: 71.68  E-value: 4.04e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPItaIREIKILRQLVHQSVVNMkeivtdkqdaLDFKKDKGAFYLV 808
Cdd:cd06656     27 IGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELI--INEILVMRENKNPNIVNY----------LDSYLVGDELWVV 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDHdlmGLLESGLVH--FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN------------------NSRP 868
Cdd:cd06656     95 MEYLAG---GSLTDVVTEtcMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGmdgsvkltdfgfcaqitpEQSK 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  869 YTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISrlcgspcpavwpdviklpyfNT 948
Cdd:cd06656    172 RSTMVGTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIA--------------------TN 230
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  949 MKPKKQYRRRLREEFSfipsaalDLLDHMLTLDPSKRCTAEQTLQSDFLKDVE-LSKMAP 1007
Cdd:cd06656    231 GTPELQNPERLSAVFR-------DFLNRCLEMDVDRRGSAKELLQHPFLKLAKpLSSLTP 283
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
722-997 4.64e-13

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


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 71.03  E-value: 4.64e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFpitAIREIKILRQLVHQSVVNMKEiVTDKQDALdfkkd 801
Cdd:cd14087      2 KYDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGREV---CESELNVLRRVRHTNIIQLIE-VFETKERV----- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 kgafYLVFEYMDHdlmGLLESGLV---HFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTNKVITLW- 877
Cdd:cd14087     73 ----YMVMELATG---GELFDRIIakgSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPDSKIMITDFg 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  878 ---------------------YRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAV 936
Cdd:cd14087    146 lastrkkgpnclmkttcgtpeYIAPEILL-RKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSGEP 224
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  937 WPDVIKLpyfntmkpkkqyrrrlreefsfipsaALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14087    225 WPSVSNL--------------------------AKDFIDRLLTVNPGERLSATQALKHPWI 259
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
721-997 5.95e-13

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: 71.20  E-value: 5.95e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKV----RLDNEKEGfpitairEIKILRQLV-HQSVVNMKEIVtdkqda 795
Cdd:cd06638     18 DTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILdpihDIDEEIEA-------EYNILKALSdHPNVVKFYGMY------ 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  796 ldFKKDK---GAFYLVFEYMD----HDLM-GLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNIL----- 862
Cdd:cd06638     85 --YKKDVkngDQLWLVLELCNggsvTDLVkGFLKRG-ERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILltteg 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  863 ------------LNNSRPYTN-KVITLWYRPPELLLGEER----YTPAIDVWSCGCILGELFTKKPifqanlELAQLEli 925
Cdd:cd06638    162 gvklvdfgvsaqLTSTRLRRNtSVGTPFWMAPEVIACEQQldstYDARCDVWSLGITAIELGDGDP------PLADLH-- 233
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  926 srlcgsPCPAVWpdviKLPyfNTMKPKKQYRRRLREEFSfipsaalDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd06638    234 ------PMRALF----KIP--RNPPPTLHQPELWSNEFN-------DFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
721-993 6.07e-13

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: 70.82  E-value: 6.07e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVA---LKKVRLDNEKEGFPITAI-REIKILRQLVHQSVVNMKEIVTDKQDAL 796
Cdd:cd14194      5 DYYDTGEELGSGQFAVVKKCREKSTGLQYAakfIKKRRTKSSRRGVSREDIeREVSILKEIQHPNVITLHEVYENKTDVI 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  797 dfkkdkgafyLVFEYMD----HDLMGLLESglvhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNI-LLNNSRPYTN 871
Cdd:cd14194     85 ----------LILELVAggelFDFLAEKES----LTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENImLLDRNVPKPR 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  872 -KVITLW--------------YRPPELLLGE-ERYTP---AIDVWSCGCILGELFTKKPIFQANLELAQLELISrlcgsp 932
Cdd:cd14194    151 iKIIDFGlahkidfgnefkniFGTPEFVAPEiVNYEPlglEADMWSIGVITYILLSGASPFLGDTKQETLANVS------ 224
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  933 cpAVWPDviklpyFNtmkpkkqyrrrlREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd14194    225 --AVNYE------FE------------DEYFSNTSALAKDFIRRLLVKDPKKRMTIQDSLQ 265
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
729-863 6.50e-13

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: 67.47  E-value: 6.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKkvRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQDaldfkkdkGAFYLV 808
Cdd:cd13968      1 MGEGASAKVFWAEGECTTIGVAVK--IGDDVNNEEGEDLESEMDILRRLKGLELNIPKVLVTEDVD--------GPNILL 70
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  809 FEYMDHDLMGLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL 863
Cdd:cd13968     71 MELVKGGTLIAYTQE-EELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILL 124
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
725-966 7.58e-13

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: 70.40  E-value: 7.58e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  725 IIGIIGEGTYGQVYKAKDKdtGELVALKKVRLDNEKEGFpitaIREIKILRQLVHQSVVNMKEIVTDkqdaldfkkDKGA 804
Cdd:cd05082     10 LLQTIGKGEFGDVMLGDYR--GNKVAVKCIKNDATAQAF----LAEASVMTQLRHSNLVQLLGVIVE---------EKGG 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  805 FYLVFEYMDH-DLMGLLES-GLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN----------------NS 866
Cdd:cd05082     75 LYIVTEYMAKgSLVDYLRSrGRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSednvakvsdfgltkeaSS 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 RPYTNKVITLWYRPPELLlgEERYTPAIDVWSCGCILGELFTKKPIFQANLELAqlELISRL-------CGSPCPAVWPD 939
Cdd:cd05082    155 TQDTGKLPVKWTAPEALR--EKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLK--DVVPRVekgykmdAPDGCPPAVYD 230
                          250       260
                   ....*....|....*....|....*...
gi 1907082950  940 VIKLPYfnTMKPKKQYR-RRLREEFSFI 966
Cdd:cd05082    231 VMKNCW--HLDAAMRPSfLQLREQLEHI 256
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
729-997 7.81e-13

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


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 70.35  E-value: 7.81e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLD-----NEKEGFPItairEIKILRQLVHQSVVNMKeivtdkqdalDFKKDKG 803
Cdd:cd14187     15 LGKGGFAKCYEITDADTKEVFAGKIVPKSlllkpHQKEKMSM----EIAIHRSLAHQHVVGFH----------GFFEDND 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  804 AFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN------------------N 865
Cdd:cd14187     81 FVYVVLELCRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNddmevkigdfglatkveyD 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 SRPYTNKVITLWYRPPELLlGEERYTPAIDVWSCGCILGELFTKKPIFQanlelaqlelisrlcgspcpavwpdviklpy 945
Cdd:cd14187    161 GERKKTLCGTPNYIAPEVL-SKKGHSFEVDIWSIGCIMYTLLVGKPPFE------------------------------- 208
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  946 fnTMKPKKQYRRRLREEFSF---IPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14187    209 --TSCLKETYLRIKKNEYSIpkhINPVAASLIQKMLQTDPTARPTINELLNDEFF 261
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
725-914 9.08e-13

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 72.91  E-value: 9.08e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  725 IIGIIGEGTYGQVYKAKDKDTGELVALKKVRLD-NEKEGFpiTA--IREIKILRQLVHQSVVNMkeivtdkqdaLDFKKD 801
Cdd:NF033483    11 IGERIGRGGMAEVYLAKDTRLDRDVAVKVLRPDlARDPEF--VArfRREAQSAASLSHPNIVSV----------YDVGED 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 KGAFYLVFEYMD-HDLMGLL-ESGLVHFSEdhIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL---------------- 863
Cdd:NF033483    79 GGIPYIVMEYVDgRTLKDYIrEHGPLSPEE--AVEIMIQILSALEHAHRNGIVHRDIKPQNILItkdgrvkvtdfgiara 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  864 --NNSRPYTNKVI-TLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQ 914
Cdd:NF033483   157 lsSTTMTQTNSVLgTVHYLSPEQARG-GTVDARSDIYSLGIVLYEMLTGRPPFD 209
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
729-998 9.64e-13

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: 70.45  E-value: 9.64e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKvrLDNEKEGFPITAIREIKILRQLVHQSVVNMKE--IVTDKqdaldfkkdkgaFY 806
Cdd:cd06658     30 IGEGSTGIVCIATEKHTGKQVAVKK--MDLRKQQRRELLFNEVVIMRDYHHENVVDMYNsyLVGDE------------LW 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVFEYMDHdlmGLLESGLVH--FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN---------------SRPY 869
Cdd:cd06658     96 VVMEFLEG---GALTDIVTHtrMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSdgriklsdfgfcaqvSKEV 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  870 TNK---VITLWYRPPELLlGEERYTPAIDVWSCGCILGELFTKKPifqanlelaqlelisrlcgspcpavwpdviklPYF 946
Cdd:cd06658    173 PKRkslVGTPYWMAPEVI-SRLPYGTEVDIWSLGIMVIEMIDGEP--------------------------------PYF 219
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  947 NtmKPKKQYRRRLRE-------EFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLK 998
Cdd:cd06658    220 N--EPPLQAMRRIRDnlpprvkDSHKVSSVLRGFLDLMLVREPSQRATAQELLQHPFLK 276
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
714-932 1.08e-12

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 73.23  E-value: 1.08e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  714 DWGKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQ 793
Cdd:PTZ00266     6 DDGESRLNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKEREKSQLVIEVNVMRELKHKNIVRYIDRFLNKA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  794 DAldfkkdkgAFYLVFEYMDH-DLMGLLESGLVHFS--EDH-IKSFMKQLMEGLDYCHK-------KNFLHRDIKCSNIL 862
Cdd:PTZ00266    86 NQ--------KLYILMEFCDAgDLSRNIQKCYKMFGkiEEHaIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIF 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  863 LN----------------NSRPYT------------------NKVITLWYRPPELLLGEER-YTPAIDVWSCGCILGELF 907
Cdd:PTZ00266   158 LStgirhigkitaqannlNGRPIAkigdfglsknigiesmahSCVGTPYYWSPELLLHETKsYDDKSDMWALGCIIYELC 237
                          250       260
                   ....*....|....*....|....*
gi 1907082950  908 TKKPIFQANLELAQleLISRLCGSP 932
Cdd:PTZ00266   238 SGKTPFHKANNFSQ--LISELKRGP 260
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
729-993 1.12e-12

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


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 70.30  E-value: 1.12e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRlDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVtdkqdaldfkKDKGAFYLV 808
Cdd:cd14169     11 LGEGAFSEVVLAQERGSQRLVALKCIP-KKALRGKEAMVENEIAVLRRINHENIVSLEDIY----------ESPTHLYLA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDHD--LMGLLESGlvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLnnSRPYTNKVI------------ 874
Cdd:cd14169     80 MELVTGGelFDRIIERG--SYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLY--ATPFEDSKImisdfglskiea 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  875 ---------TLWYRPPELLlGEERYTPAIDVWSCGCILGELftkkpifqanlelaqlelisrLCGSPcpavwpdviklPY 945
Cdd:cd14169    156 qgmlstacgTPGYVAPELL-EQKPYGKAVDVWAIGVISYIL---------------------LCGYP-----------PF 202
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  946 FNTMKPKkQYRRRLREEFSF-------IPSAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd14169    203 YDENDSE-LFNQILKAEYEFdspywddISESAKDFIRHLLERDPEKRFTCEQALQ 256
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
728-902 1.17e-12

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


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 69.94  E-value: 1.17e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITaiREIKILRQLVHQSVVNMkeivtdkQDALDFKKDkgaFYL 807
Cdd:cd14193     11 ILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEEVK--NEIEVMNQLNHANLIQL-------YDAFESRND---IVL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYMDH-DLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTNKVITLW----YRP-- 880
Cdd:cd14193     79 VMEYVDGgELFDRIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSREANQVKIIDFGlarrYKPre 158
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1907082950  881 --------PELLLGE----ERYTPAIDVWSCGCI 902
Cdd:cd14193    159 klrvnfgtPEFLAPEvvnyEFVSFPTDMWSLGVI 192
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
728-911 1.20e-12

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: 70.11  E-value: 1.20e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVRLDNE--KEGFPITAIR-EIKILRQLVHQSVVNMKEIVTDKQDAldfkkdkgA 804
Cdd:cd06651     14 LLGQGAFGRVYLCYDVDTGRELAAKQVQFDPEspETSKEVSALEcEIQLLKNLQHERIVQYYGCLRDRAEK--------T 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  805 FYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS------------------ 866
Cdd:cd06651     86 LTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAgnvklgdfgaskrlqtic 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  867 ------RPYTNkviTLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKP 911
Cdd:cd06651    166 msgtgiRSVTG---TPYWMSPEVISGEG-YGRKADVWSLGCTVVEMLTEKP 212
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
729-903 1.28e-12

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


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 69.50  E-value: 1.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKV-RLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIvtdkqdaldFKKDKGAFYL 807
Cdd:cd14164      8 IGEGSFSKVKLATSQKYCCKVAIKIVdRRRASPDFVQKFLPRELSILRRVNHPNIVQMFEC---------IEVANGRLYI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYMDHDLMGLLESgLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN-----------------NSRP-- 868
Cdd:cd14164     79 VMEAAATDLLQKIQE-VHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSaddrkikiadfgfarfvEDYPel 157
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1907082950  869 YTNKVITLWYRPPELLLGEERYTPAIDVWSCGCIL 903
Cdd:cd14164    158 STTFCGSRAYTPPEVILGTPYDPKKYDVWSLGVVL 192
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
729-1007 1.39e-12

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: 70.14  E-value: 1.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPItaIREIKILRQLVHQSVVNMkeivtdkqdaLDFKKDKGAFYLV 808
Cdd:cd06654     28 IGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKELI--INEILVMRENKNPNIVNY----------LDSYLVGDELWVV 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDHdlmGLLESGLVH--FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN------------------NSRP 868
Cdd:cd06654     96 MEYLAG---GSLTDVVTEtcMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGmdgsvkltdfgfcaqitpEQSK 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  869 YTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISrlcgspcpavwpdviklpyfNT 948
Cdd:cd06654    173 RSTMVGTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIA--------------------TN 231
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  949 MKPKKQYRRRLREEFSfipsaalDLLDHMLTLDPSKRCTAEQTLQSDFLKDVE-LSKMAP 1007
Cdd:cd06654    232 GTPELQNPEKLSAIFR-------DFLNRCLEMDVEKRGSAKELLQHQFLKIAKpLSSLTP 284
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
717-929 1.47e-12

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: 69.84  E-value: 1.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  717 KRCVDKFDIIGII------GEGTYGQVYKAKDKDTgeLVALKK------VRLDNEKEGFPitaiREIKILRQLVHQSVVN 784
Cdd:cd14158      5 KNMTNNFDERPISvggnklGEGGFGVVFKGYINDK--NVAVKKlaamvdISTEDLTKQFE----QEIQVMAKCQHENLVE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  785 MkeivtdkqdaLDFKKDKGAFYLVFEYMDHdlmGLLESGLVhfSEDHIKSFMKQL--------MEGLDYCHKKNFLHRDI 856
Cdd:cd14158     79 L----------LGYSCDGPQLCLVYTYMPN---GSLLDRLA--CLNDTPPLSWHMrckiaqgtANGINYLHENNHIHRDI 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  857 KCSNILLNN-----------SRP--------YTNKVI-TLWYRPPELLLGEerYTPAIDVWSCGCILGELFTKKPIFQAN 916
Cdd:cd14158    144 KSANILLDEtfvpkisdfglARAsekfsqtiMTERIVgTTAYMAPEALRGE--ITPKSDIFSFGVVLLEIITGLPPVDEN 221
                          250
                   ....*....|....
gi 1907082950  917 LELAQL-ELISRLC 929
Cdd:cd14158    222 RDPQLLlDIKEEIE 235
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
721-902 1.70e-12

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: 69.10  E-value: 1.70e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDK--DTGELVALKKVRLDNEKEgfpiTAIREIKILRQLVHQSVVNMkeivtdkqdaLDF 798
Cdd:cd14112      3 GRFSFGSEIFRGRFSVIVKAVDSttETDAHCAVKIFEVSDEAS----EAVREFESLRTLQHENVQRL----------IAA 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  799 KKDKGAFYLVFEYMDHDLMGLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTNKVI---- 874
Cdd:cd14112     69 FKPSNFAYLVMEKLQEDVFTRFSSN-DYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSWQVKLVdfgr 147
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1907082950  875 --------------TLWYRPPELLLGEERYTPAIDVWSCGCI 902
Cdd:cd14112    148 aqkvsklgkvpvdgDTDWASPEFHNPETPITVQSDIWGLGVL 189
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
721-863 1.84e-12

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


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 69.21  E-value: 1.84e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVA---LKKVRLDNEKEGFPITAI-REIKILRQLVHQSVVNMKEIVTDKQDAL 796
Cdd:cd14196      5 DFYDIGEELGSGQFAIVKKCREKSTGLEYAakfIKKRQSRASRRGVSREEIeREVSILRQVLHPNIITLHDVYENRTDVV 84
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  797 dfkkdkgafyLVFEYMD----HDLMGLLESglvhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL 863
Cdd:cd14196     85 ----------LILELVSggelFDFLAQKES----LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIML 141
pknD PRK13184
serine/threonine-protein kinase PknD;
722-863 1.95e-12

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 72.11  E-value: 1.95e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVR---LDNE--KEGFpitaIREIKILRQLVHQSVVNMKEIVTDKQdal 796
Cdd:PRK13184     3 RYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIRedlSENPllKKRF----LREAKIAADLIHPGIVPVYSICSDGD--- 75
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  797 dfkkdkgAFYLVFEYMD-HDLMGLLESGLVH--FSEDH-----IKSFMK---QLMEGLDYCHKKNFLHRDIKCSNILL 863
Cdd:PRK13184    76 -------PVYYTMPYIEgYTLKSLLKSVWQKesLSKELaektsVGAFLSifhKICATIEYVHSKGVLHRDLKPDNILL 146
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
721-911 2.15e-12

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


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 69.64  E-value: 2.15e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKV----RLDNEKEGfpitairEIKILRQLV-HQSVVnmkeivtdKQDA 795
Cdd:cd06639     22 DTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILdpisDVDEEIEA-------EYNILRSLPnHPNVV--------KFYG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  796 LDFKKDK---GAFYLVFEYMD----HDLM-GLLESGLvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNIL----- 862
Cdd:cd06639     87 MFYKADQyvgGQLWLVLELCNggsvTELVkGLLKCGQ-RLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILltteg 165
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  863 ------------LNNSRPYTN-KVITLWYRPPELLLGEERYTPA----IDVWSCGCILGELFTKKP 911
Cdd:cd06639    166 gvklvdfgvsaqLTSARLRRNtSVGTPFWMAPEVIACEQQYDYSydarCDVWSLGITAIELADGDP 231
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
728-902 2.58e-12

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 68.84  E-value: 2.58e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITaiREIKILRQLVHqsvVNMKEIVtdkqDALDFKKDkgaFYL 807
Cdd:cd14192     11 VLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEVK--NEINIMNQLNH---VNLIQLY----DAFESKTN---LTL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYMDH-DLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTNKVITLW----YRP-- 880
Cdd:cd14192     79 IMEYVDGgELFDRITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNSTGNQIKIIDFGlarrYKPre 158
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1907082950  881 --------PELLLGE----ERYTPAIDVWSCGCI 902
Cdd:cd14192    159 klkvnfgtPEFLAPEvvnyDFVSFPTDMWSVGVI 192
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
721-985 3.59e-12

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


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 68.97  E-value: 3.59e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKvrLDNEKegfpitaireIKILRQLVHqsVVNMKEIVtdkqDALDFK- 799
Cdd:cd14209      1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKI--LDKQK----------VVKLKQVEH--TLNEKRIL----QAINFPf 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 --------KDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLnNSRPYTn 871
Cdd:cd14209     63 lvkleysfKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLI-DQQGYI- 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  872 KVI-----------------TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELIsrlcgspcp 934
Cdd:cd14209    141 KVTdfgfakrvkgrtwtlcgTPEYLAPEIILSKG-YNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKI--------- 210
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  935 aVWPDViKLPyfntmkpkkqyrrrlreefSFIPSAALDLLDHMLTLDPSKR 985
Cdd:cd14209    211 -VSGKV-RFP-------------------SHFSSDLKDLLRNLLQVDLTKR 240
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
723-1069 4.37e-12

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: 69.18  E-value: 4.37e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVY---KAKDKDTGELVALKKVR----LDNEKEgfpITAIREIKILRQLVHQSVVnmkeIVTDKqda 795
Cdd:cd05614      2 FELLKVLGTGAYGKVFlvrKVSGHDANKLYAMKVLRkaalVQKAKT---VEHTRTERNVLEHVRQSPF----LVTLH--- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  796 LDFKKDkGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN---------- 865
Cdd:cd05614     72 YAFQTD-AKLHLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSeghvvltdfg 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 -SRPYTNK--------VITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLEL-AQLELISRL--CGSPC 933
Cdd:cd05614    151 lSKEFLTEekertysfCGTIEYMAPEIIRGKSGHGKAVDWWSLGILMFELLTGASPFTLEGEKnTQSEVSRRIlkCDPPF 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  934 PavwpdviklpyfntmkpkkqyrrrlreefSFIPSAALDLLDHMLTLDPSKRC-----TAEQTLQSDFLKDVELSKMAPP 1008
Cdd:cd05614    231 P-----------------------------SFIGPVARDLLQKLLCKDPKKRLgagpqGAQEIKEHPFFKGLDWEALALR 281
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950 1009 DLPhwqdchelwskkrrrqrqsgiviedPPPSKASRKETTSG------TTAEPVKNNSPAPPQPAPV 1069
Cdd:cd05614    282 KVN-------------------------PPFRPSIRSELDVGnfaeefTNLEPVYSPAGTPPSGARV 323
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
721-913 5.81e-12

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: 68.23  E-value: 5.81e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKkvrldnekegfpITAIREIKILRQLVHqsVVNMKEIVTDKQDALDFK- 799
Cdd:cd05612      1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALK------------VMAIPEVIRLKQEQH--VHNEKRVLKEVSHPFIIRl 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 ----KDKGAFYLVFEYM-DHDLMGLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN--------- 865
Cdd:cd05612     67 fwteHDQRFLYMLMEYVpGGELFSYLRNS-GRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKeghikltdf 145
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  866 --SRPYTNKVITLW----YRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIF 913
Cdd:cd05612    146 gfAKKLRDRTWTLCgtpeYLAPE-VIQSKGHNKAVDWWALGILIYEMLVGYPPF 198
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
728-997 5.86e-12

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 67.64  E-value: 5.86e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEgfPITAIREIKILRQLVHQSVVNMKEIVTDKQDALdfkkdkgafyL 807
Cdd:cd14190     11 VLGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKD--KEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIV----------L 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYMDH-DLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTNKVITLW----YRP-- 880
Cdd:cd14190     79 FMEYVEGgELFERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTGHQVKIIDFGlarrYNPre 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  881 --------PELLLGE----ERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELIsrLCGSpcpavWpdviklpYFNt 948
Cdd:cd14190    159 klkvnfgtPEFLSPEvvnyDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNV--LMGN-----W-------YFD- 223
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1907082950  949 mkpkkqyrrrlREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14190    224 -----------EETFEHVSDEAKDFVSNLIIKERSARMSATQCLKHPWL 261
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
728-997 6.30e-12

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


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 67.34  E-value: 6.30e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALK-----KVRLDNEKEGFPitaiREIKILRQLVHQSVVNMKEIVTDKQDaldfkkdk 802
Cdd:cd14188      8 VLGKGGFAKCYEMTDLTTNKVYAAKiiphsRVSKPHQREKID----KEIELHRILHHKHVVQFYHYFEDKEN-------- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 gaFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS--------------RP 868
Cdd:cd14188     76 --IYILLEYCSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENmelkvgdfglaarlEP 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  869 YTNKVITLW----YRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQanlelaqlelisrlcgspcpavwpdviklp 944
Cdd:cd14188    154 LEHRRRTICgtpnYLSPE-VLNKQGHGCESDIWALGCVMYTMLLGRPPFE------------------------------ 202
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  945 yfnTMKPKKQYrRRLREEFSFIPSA----ALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14188    203 ---TTNLKETY-RCIREARYSLPSSllapAKHLIASMLSKNPEDRPSLDEIIRHDFF 255
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
729-904 7.51e-12

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: 68.02  E-value: 7.51e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLD---NEKEGFpitaIREIKILRQLVHQSVVNMKEIVTDKQDALDfkkdkGAF 805
Cdd:cd14039      1 LGTGGFGNVCLYQNQETGEKIAIKSCRLElsvKNKDRW----CHEIQIMKKLNHPNVVKACDVPEEMNFLVN-----DVP 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  806 YLVFEYMDH-DLMGLLES-----GLvhfSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYT-NKVI---- 874
Cdd:cd14039     72 LLAMEYCSGgDLRKLLNKpenccGL---KESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKIvHKIIdlgy 148
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907082950  875 ---------------TLWYRPPELLLGEErYTPAIDVWSCG-----CILG 904
Cdd:cd14039    149 akdldqgslctsfvgTLQYLAPELFENKS-YTVTVDYWSFGtmvfeCIAG 197
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
729-950 8.27e-12

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: 66.92  E-value: 8.27e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGElVALKKVrldneKEG--FPITAIREIKILRQLVHQSVVNMKEIVTDKQdaldfkkdkgAFY 806
Cdd:cd05034      3 LGAGQFGEVWMGVWNGTTK-VAVKTL-----KPGtmSPEAFLQEAQIMKKLRHDKLVQLYAVCSDEE----------PIY 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVFEYMDH-DLMGLLESG---LVHFsEDHIKsFMKQLMEGLDYCHKKNFLHRDIKCSNILL--NNS-------------- 866
Cdd:cd05034     67 IVTELMSKgSLLDYLRTGegrALRL-PQLID-MAAQIASGMAYLESRNYIHRDLAARNILVgeNNVckvadfglarlied 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 RPYTNKVITL----WYRPPELLLGeeRYTPAIDVWSCGCILGELFTKKPI---FQANLE-LAQLELISRLcgsPCPAVWP 938
Cdd:cd05034    145 DEYTAREGAKfpikWTAPEAALYG--RFTIKSDVWSFGILLYEIVTYGRVpypGMTNREvLEQVERGYRM---PKPPGCP 219
                          250
                   ....*....|..
gi 1907082950  939 DviklPYFNTMK 950
Cdd:cd05034    220 D----ELYDIML 227
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
729-1007 9.48e-12

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: 67.83  E-value: 9.48e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPItaIREIKILRQLVHQSVVNMkeivtdkqdaLDFKKDKGAFYLV 808
Cdd:cd06655     27 IGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKELI--INEILVMKELKNPNIVNF----------LDSFLVGDELFVV 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDHdlmGLLESGLVH--FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN------------------NSRP 868
Cdd:cd06655     95 MEYLAG---GSLTDVVTEtcMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGmdgsvkltdfgfcaqitpEQSK 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  869 YTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISrlcgspcpavwpdviklpyfNT 948
Cdd:cd06655    172 RSTMVGTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIA--------------------TN 230
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  949 MKPKKQYRRRLREEFSfipsaalDLLDHMLTLDPSKRCTAEQTLQSDFLKDVE-LSKMAP 1007
Cdd:cd06655    231 GTPELQNPEKLSPIFR-------DFLNRCLEMDVEKRGSAKELLQHPFLKLAKpLSSLTP 283
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
729-908 9.62e-12

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


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 67.68  E-value: 9.62e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRldneKEGFPITAIR---EIKILRQLVHQSVVNMKEIvtdkQDALDFKKDKGAF 805
Cdd:cd14038      2 LGTGGFGNVLRWINQETGEQVAIKQCR----QELSPKNRERwclEIQIMKRLNHPNVVAARDV----PEGLQKLAPNDLP 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  806 YLVFEYMDH-DL---MGLLES--GLvhfSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNIL----------------- 862
Cdd:cd14038     74 LLAMEYCQGgDLrkyLNQFENccGL---REGAILTLLSDISSALRYLHENRIIHRDLKPENIVlqqgeqrlihkiidlgy 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1907082950  863 ---LNNSRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFT 908
Cdd:cd14038    151 akeLDQGSLCTSFVGTLQYLAPE-LLEQQKYTVTVDYWSFGTLAFECIT 198
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
729-966 1.21e-11

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: 66.49  E-value: 1.21e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRlDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQdaldfkkdkgAFYLV 808
Cdd:cd05084      4 IGRGNFGEVFSGRLRADNTPVAVKSCR-ETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQ----------PIYIV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDH-DLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-----------SRPYTNKVITL 876
Cdd:cd05084     73 MELVQGgDFLTFLRTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEknvlkisdfgmSREEEDGVYAA 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  877 ----------WYRPPELLLGeeRYTPAIDVWSCGCILGELFTKKPIFQANLELAQL-ELISRLCGSPCPAVWPDVIklpy 945
Cdd:cd05084    153 tggmkqipvkWTAPEALNYG--RYSSESDVWSFGILLWETFSLGAVPYANLSNQQTrEAVEQGVRLPCPENCPDEV---- 226
                          250       260
                   ....*....|....*....|.
gi 1907082950  946 FNTMKPKKQYRRRLREEFSFI 966
Cdd:cd05084    227 YRLMEQCWEYDPRKRPSFSTV 247
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
728-998 1.25e-11

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


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 66.80  E-value: 1.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPI----TAIREIKILRQLV----HQSVVNMkeivtdkqdaLDFK 799
Cdd:cd14101      7 LLGKGGFGTVYAGHRISDGLQVAIKQISRNRVQQWSKLpgvnPVPNEVALLQSVGggpgHRGVIRL----------LDWF 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 KDKGAFYLVFEYMDH--DLMGLL-ESGLVhfSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSR--------- 867
Cdd:cd14101     77 EIPEGFLLVLERPQHcqDLFDYItERGAL--DESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLRTgdiklidfg 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  868 --------PYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLElisrlcgspcpavwpd 939
Cdd:cd14101    155 sgatlkdsMYTDFDGTRVYSPPEWILYHQYHALPATVWSLGILLYDMVCGDIPFERDTDILKAK---------------- 218
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  940 viklPYFNTMkpkkqyrrrlreefsfIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLK 998
Cdd:cd14101    219 ----PSFNKR----------------VSNDCRSLIRSCLAYNPSDRPSLEQILLHPWMM 257
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
728-985 1.26e-11

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


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 67.60  E-value: 1.26e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPIT-AIREIKILRQLVHQSVVNMKeivtdkqdaLDFKKdKGAFY 806
Cdd:cd05585      1 VIGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEVThTLAERTVLAQVDCPFIVPLK---------FSFQS-PEKLY 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVFEYMDHDLM--GLLESGlvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNnsrpYTNKVI---------- 874
Cdd:cd05585     71 LVLAFINGGELfhHLQREG--RFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLD----YTGHIAlcdfglckln 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  875 ------------TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPifqanlelaqlelisrlcgspcpavwpdvik 942
Cdd:cd05585    145 mkdddktntfcgTPEYLAPELLLGHG-YTKAVDWWTLGVLLYEMLTGLP------------------------------- 192
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1907082950  943 lPYFNTMKPkKQYRRRLREEFSF---IPSAALDLLDHMLTLDPSKR 985
Cdd:cd05585    193 -PFYDENTN-EMYRKILQEPLRFpdgFDRDAKDLLIGLLNRDPTKR 236
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
723-985 1.55e-11

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 67.54  E-value: 1.55e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVA---LKKVRLDNEKEGFPITAirEIKILRQLVHQSVVNMkeivtdkqdaLDFK 799
Cdd:PTZ00263    20 FEMGETLGTGSFGRVRIAKHKGTGEYYAikcLKKREILKMKQVQHVAQ--EKSILMELSHPFIVNM----------MCSF 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 KDKGAFYLVFEY-MDHDLMGLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-----------SR 867
Cdd:PTZ00263    88 QDENRVYFLLEFvVGGELFTHLRKA-GRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNkghvkvtdfgfAK 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  868 PYTNKVITLW----YRPPElLLGEERYTPAIDVWSCGCILGELftkkpifqanlelaqlelisrLCGSPcpavwpdvikl 943
Cdd:PTZ00263   167 KVPDRTFTLCgtpeYLAPE-VIQSKGHGKAVDWWTMGVLLYEF---------------------IAGYP----------- 213
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1907082950  944 PYFNTmKPKKQYRRRLREEFSF---IPSAALDLLDHMLTLDPSKR 985
Cdd:PTZ00263   214 PFFDD-TPFRIYEKILAGRLKFpnwFDGRARDLVKGLLQTDHTKR 257
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
729-999 1.59e-11

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: 66.09  E-value: 1.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKakdkdtGELVALKKVRLDNEKEGF--PITAIREIKILRQLVHQSVVNMKEIVTDKqdaldfkkdkgAFY 806
Cdd:cd14203      3 LGQGCFGEVWM------GTWNGTTKVAIKTLKPGTmsPEAFLEEAQIMKKLRHDKLVQLYAVVSEE-----------PIY 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVFEYMDH-DLMGLLESGLVHFSE-DHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS----------------RP 868
Cdd:cd14203     66 IVTEFMSKgSLLDFLKDGEGKYLKlPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNlvckiadfglarliedNE 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  869 YT----NKVITLWYRPPELLLGeeRYTPAIDVWSCGCILGELFTKKPI---FQANLELaqLELISRLCGSPCPavwPDVi 941
Cdd:cd14203    146 YTarqgAKFPIKWTAPEAALYG--RFTIKSDVWSFGILLTELVTKGRVpypGMNNREV--LEQVERGYRMPCP---PGC- 217
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  942 klpyfntmkpkkqyrrrlreefsfiPSAALDLLDHMLTLDPSKRCTAEQtLQSdFLKD 999
Cdd:cd14203    218 -------------------------PESLHELMCQCWRKDPEERPTFEY-LQS-FLED 248
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
729-908 2.01e-11

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: 65.59  E-value: 2.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKdtGELVALKKVRldNEKEgfpitaiREIKILRQLVHQSVVNMKEIVTDKQdaldfkkdkgAFYLV 808
Cdd:cd14059      1 LGSGAQGAVFLGKFR--GEEVAVKKVR--DEKE-------TDIKHLRKLNHPNIIKFKGVCTQAP----------CYCIL 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDH-DLMGLLESGLVhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-----------SRPYTNKVI-- 874
Cdd:cd14059     60 MEYCPYgQLYEVLRAGRE-ITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYndvlkisdfgtSKELSEKSTkm 138
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1907082950  875 ----TLWYRPPELLLGEErYTPAIDVWSCGCILGELFT 908
Cdd:cd14059    139 sfagTVAWMAPEVIRNEP-CSEKVDIWSFGVVLWELLT 175
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
728-993 2.07e-11

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 66.59  E-value: 2.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVRldnEKEGFPITAI-REIKILRQLvhQSVVNMKEIVtdkqdalDFKKDKGAFY 806
Cdd:cd14173      9 VLGEGAYARVQTCINLITNKEYAVKIIE---KRPGHSRSRVfREVEMLYQC--QGHRNVLELI-------EFFEEEDKFY 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNIL----------------------LN 864
Cdd:cd14173     77 LVFEKMRGGSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILcehpnqvspvkicdfdlgsgikLN 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 -NSRPY-TNKVIT----LWYRPPELL--LGEER--YTPAIDVWSCGCILGELFTKKPIFQANlelaqlelisrlCGSPCP 934
Cdd:cd14173    157 sDCSPIsTPELLTpcgsAEYMAPEVVeaFNEEAsiYDKRCDLWSLGVILYIMLSGYPPFVGR------------CGSDCG 224
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  935 AVW----PDVIKLPYFNTMKPKKQYRRRlreEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd14173    225 WDRgeacPACQNMLFESIQEGKYEFPEK---DWAHISCAAKDLISKLLVRDAKQRLSAAQVLQ 284
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
721-997 2.22e-11

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


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 66.22  E-value: 2.22e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDnEKEGFPITAiREIKILRQLVHQSVVNMKeivtdkqdALDFKK 800
Cdd:cd06645     11 EDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLE-PGEDFAVVQ-QEIIMMKDCKHSNIVAYF--------GSYLRR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DKgaFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS-------------- 866
Cdd:cd06645     81 DK--LWICMEFCGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNghvkladfgvsaqi 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 ----RPYTNKVITLWYRPPELLLGEER--YTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPcpavwpdv 940
Cdd:cd06645    159 tatiAKRKSFIGTPYWMAPEVAAVERKggYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMTKSNFQP-------- 230
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  941 iklpyfntmkPKKQYRRRLREEFSFIPSAAldlldhmLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd06645    231 ----------PKLKDKMKWSNSFHHFVKMA-------LTKNPKKRPTAEKLLQHPFV 270
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
729-910 2.73e-11

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: 65.55  E-value: 2.73e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMkeivtdkqdaLDFKKDKGAFYLV 808
Cdd:cd13978      1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLPL----------LGVCVERRSLGLV 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDH-DLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCH--KKNFLHRDIKCSNILLNN-------------------- 865
Cdd:cd13978     71 MEYMENgSLKSLLEREIQDVPWSLRFRIIHEIALGMNFLHnmDPPLLHHDLKPENILLDNhfhvkisdfglsklgmksis 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1907082950  866 ---SRPYTNKVITLWYRPPELL-LGEERYTPAIDVWSCGCILGELFTKK 910
Cdd:cd13978    151 anrRRGTENLGGTPIYMAPEAFdDFNKKPTSKSDVYSFAIVIWAVLTRK 199
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
723-1004 3.13e-11

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: 66.22  E-value: 3.13e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKeGFPITAIREIKILRQLVHQSVVNMKEIVtdkqdaldfkKDK 802
Cdd:cd14168     12 FEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALK-GKESSIENEIAVLRKIKHENIVALEDIY----------ESP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 GAFYLVFEYMDHDLM--GLLESGLvhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTNKVI------ 874
Cdd:cd14168     81 NHLYLVMQLVSGGELfdRIVEKGF--YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQDEESKIMIsdfgls 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  875 --------------TLWYRPPElLLGEERYTPAIDVWSCGCILGELftkkpifqanlelaqlelisrLCGSPcpavwpdv 940
Cdd:cd14168    159 kmegkgdvmstacgTPGYVAPE-VLAQKPYSKAVDCWSIGVIAYIL---------------------LCGYP-------- 208
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  941 iklPYFNTmKPKKQYRRRLREEFSF-------IPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLK-DVELSK 1004
Cdd:cd14168    209 ---PFYDE-NDSKLFEQILKADYEFdspywddISDSAKDFIRNLMEKDPNKRYTCEQALRHPWIAgDTALCK 276
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
729-999 3.47e-11

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


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 66.05  E-value: 3.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKV--RLDNEKEgfpitaiREIKILRQL-VHQSVVNMKEIVTDKQDAldfkkdkgaf 805
Cdd:cd14180     14 LGEGSFSVCRKCRHRQSGQEYAVKIIsrRMEANTQ-------REVAALRLCqSHPNIVALHEVLHDQYHT---------- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  806 YLVFEYMDHDlmGLLE--SGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL-------------------- 863
Cdd:cd14180     77 YLVMELLRGG--ELLDriKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYadesdgavlkvidfgfarlr 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  864 -NNSRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANlelaqleliSRLCGSPCPAvwpdvik 942
Cdd:cd14180    155 pQGSRPLQTPCFTLQYAAPE-LFSNQGYDESCDLWSLGVILYTMLSGQVPFQSK---------RGKMFHNHAA------- 217
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  943 lpyfNTMKPKKQYRRRLR-EEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLKD 999
Cdd:cd14180    218 ----DIMHKIKEGDFSLEgEAWKGVSEEAKDLVRGLLTVDPAKRLKLSELRESDWLQG 271
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
728-996 3.89e-11

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


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 65.37  E-value: 3.89e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQ-VYKAKDKdtGELVALKKVRLDnekegFPITAIREIKILRQL-VHQSVVNMkeivtdkqdaLDFKKDKGAF 805
Cdd:cd13982      8 VLGYGSEGTiVFRGTFD--GRPVAVKRLLPE-----FFDFADREVQLLRESdEHPNVIRY----------FCTEKDRQFL 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  806 YLVFEYMDHDLMGLLESGLVHFSEDHI----KSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN-NSRPYTNKVI------ 874
Cdd:cd13982     71 YIALELCAASLQDLVESPRESKLFLRPglepVRLLRQIASGLAHLHSLNIVHRDLKPQNILIStPNAHGNVRAMisdfgl 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  875 -------------------TLWYRPPELLLGE--ERYTPAIDVWSCGCIL------GE-LFTKKPIFQANlelaqlelis 926
Cdd:cd13982    151 ckkldvgrssfsrrsgvagTSGWIAPEMLSGStkRRQTRAVDIFSLGCVFyyvlsgGShPFGDKLEREAN---------- 220
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  927 rlcgspcpavwpdvIKLPYFNTMKpkkqyrrrLREEFSFIPSAAlDLLDHMLTLDPSKRCTAEQTLQSDF 996
Cdd:cd13982    221 --------------ILKGKYSLDK--------LLSLGEHGPEAQ-DLIERMIDFDPEKRPSAEEVLNHPF 267
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
730-902 3.91e-11

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


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 65.23  E-value: 3.91e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  730 GEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGfpiTAIREIKILRQLVHQSVVNMKEI-VTDKqdaldfkkdkgafYLV 808
Cdd:cd14111     12 ARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQ---GVLQEYEILKSLHHERIMALHEAyITPR-------------YLV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 F--EYMDHD--LMGLLESglVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS------------------ 866
Cdd:cd14111     76 LiaEFCSGKelLHSLIDR--FRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLnaikivdfgsaqsfnpls 153
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1907082950  867 -RPYTNKVITLWYRPPELLLGEErYTPAIDVWSCGCI 902
Cdd:cd14111    154 lRQLGRRTGTLEYMAPEMVKGEP-VGPPADIWSIGVL 189
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
737-1010 4.44e-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: 4.44e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  737 VYKAKDKDTGELVALKKVRLDNE-KEGFpiTAI-REIKILRQLVHQSVVNMKEIVTDKQDaldfkkdkgaFYLVFEYMDH 814
Cdd:cd08216     16 VHLAKHKPTNTLVAVKKINLESDsKEDL--KFLqQEILTSRQLQHPNILPYVTSFVVDND----------LYVVTPLMAY 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  815 ----DLM-GLLESGlvhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSR---------------------- 867
Cdd:cd08216     84 gscrDLLkTHFPEG---LPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGkvvlsglryaysmvkhgkrqrv 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  868 ---PYTNKVITLWYRPPELL----LGeerYTPAIDVWSCGCILGELFTKKPIFqANLELAQLeLISRLCGSP-------- 932
Cdd:cd08216    161 vhdFPKSSEKNLPWLSPEVLqqnlLG---YNEKSDIYSVGITACELANGVVPF-SDMPATQM-LLEKVRGTTpqlldcst 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  933 CPAVWPDVIKLPYFNTMKPKKQ------YRRRLREEFSfipsaalDLLDHMLTLDPSKRCTAEQTLQSDFLKDVELSKMA 1006
Cdd:cd08216    236 YPLEEDSMSQSEDSSTEHPNNRdtrdipYQRTFSEAFH-------QFVELCLQRDPELRPSASQLLAHSFFKQCRRSNTS 308

                   ....
gi 1907082950 1007 PPDL 1010
Cdd:cd08216    309 LLDL 312
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
721-1003 4.60e-11

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: 65.26  E-value: 4.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPiTAIREIKILRQLVHQSVVNMKEIVTdkqdaldfkk 800
Cdd:cd06622      1 DEIEVLDELGKGNYGSVYKVLHRPTGVTMAMKEIRLELDESKFN-QIIMELDILHKAVSPYIVDFYGAFF---------- 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DKGAFYLVFEYMDHDLMGLLESGLVHFS---EDHIKSFMKQLMEGLDYCHKK-NFLHRDIKCSNILLNN----------- 865
Cdd:cd06622     70 IEGAVYMCMEYMDAGSLDKLYAGGVATEgipEDVLRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGngqvklcdfgv 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 ------SRPYTNkVITLWYRPPELLLGEE-----RYTPAIDVWSCGCILGEL----FTKKPIFQANLeLAQLELIsrlCG 930
Cdd:cd06622    150 sgnlvaSLAKTN-IGCQSYMAPERIKSGGpnqnpTYTVQSDVWSLGLSILEMalgrYPYPPETYANI-FAQLSAI---VD 224
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  931 SPCPavwpdviklpyfntmkpkkqyrrRLREEFSfipSAALDLLDHMLTLDPSKRCTAEQTLQSDFLK-----DVELS 1003
Cdd:cd06622    225 GDPP-----------------------TLPSGYS---DDAQDFVAKCLNKIPNRRPTYAQLLEHPWLVkyknaDVDMA 276
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
721-992 4.94e-11

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 65.05  E-value: 4.94e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVrlDNEK-EGFPITAIREIKILRQLVHQSVVNMKEIVTDKQDaldfk 799
Cdd:cd14184      1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKII--DKAKcCGKEHLIENEVSILRRVKHPNIIMLIEEMDTPAE----- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 kdkgaFYLVFEYMDH-DLMGLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL----NNSR------- 867
Cdd:cd14184     74 -----LYLVMELVKGgDLFDAITSS-TKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKslklgdf 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  868 --------PYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGS-PCPAvwp 938
Cdd:cd14184    148 glatvvegPLYTVCGTPTYVAPE-IIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNLQEDLFDQILLGKlEFPS--- 223
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  939 dviklPYFNTmkpkkqyrrrlreefsfIPSAALDLLDHMLTLDPSKRCTAEQTL 992
Cdd:cd14184    224 -----PYWDN-----------------ITDSAKELISHMLQVNVEARYTAEQIL 255
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
729-997 6.06e-11

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


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 64.96  E-value: 6.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILrQLVHQS--VVNMKEIVTDKQDALdfkkdkgafy 806
Cdd:cd14197     17 LGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRMEIIHEIAVL-ELAQANpwVINLHEVYETASEMI---------- 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVFEY------MDHDLMGLLESglvhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTN-KVI----- 874
Cdd:cd14197     86 LVLEYaaggeiFNQCVADREEA----FKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLGDiKIVdfgls 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  875 --------------TLWYRPPELLlgeeRYTP---AIDVWSCGCILGELFTKKPIFQANLELAQLELISRlcgspcpavw 937
Cdd:cd14197    162 rilknseelreimgTPEYVAPEIL----SYEPistATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQ---------- 227
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  938 pdvIKLPYFNtmkpkkqyrrrlrEEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14197    228 ---MNVSYSE-------------EEFEHLSESAIDFIKTLLIKKPENRATAEDCLKHPWL 271
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
726-908 6.11e-11

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: 64.91  E-value: 6.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  726 IGIIGEGTYGQV----YKAKDKDTGELVALKKVRLDNEKEGFPITaiREIKILRQLVHQSVVNMKEIVtdkqdaldFKKD 801
Cdd:cd05081      9 ISQLGKGNFGSVelcrYDPLGDNTGALVAVKQLQHSGPDQQRDFQ--REIQILKALHSDFIVKYRGVS--------YGPG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 KGAFYLVFEYM-DHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLnNSRPYTN-------KV 873
Cdd:cd05081     79 RRSLRLVMEYLpSGCLRDFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILV-ESEAHVKiadfglaKL 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  874 ITL----------------WYRPPEllLGEERYTPAIDVWSCGCILGELFT 908
Cdd:cd05081    158 LPLdkdyyvvrepgqspifWYAPES--LSDNIFSRQSDVWSFGVVLYELFT 206
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
723-902 6.39e-11

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


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 64.53  E-value: 6.39e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGfpiTAIREIKILRQLVHQSVVNMkeivtdkqdaLDFKKDK 802
Cdd:cd14107      4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRSSTRA---RAFQERDILARLSHRRLTCL----------LDQFETR 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 GAFYLVFEY------MDHdlmgLLESGLVhfSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL------------- 863
Cdd:cd14107     71 KTLILILELcsseelLDR----LFLKGVV--TEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMvsptredikicdf 144
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907082950  864 ------NNSRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCI 902
Cdd:cd14107    145 gfaqeiTPSEHQFSKYGSPEFVAPE-IVHQEPVSAATDIWALGVI 188
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
706-1013 6.49e-11

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: 65.09  E-value: 6.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  706 GERRQTEsdwgkrcVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEgfpitairEIK-ILRQLvhqsvvn 784
Cdd:cd06618      7 GKKYKAD-------LNDLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRSGNKE--------ENKrILMDL------- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  785 mkEIVTDKQDALDFKKDKGAF------YLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKK-NFLHRDIK 857
Cdd:cd06618     65 --DVVLKSHDCPYIVKCYGYFitdsdvFICMELMSTCLDKLLKRIQGPIPEDILGKMTVSIVKALHYLKEKhGVIHRDVK 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  858 CSNILLN-----------------NSRPYTNKVITLWYRPPELLLGEE--RYTPAIDVWSCGCILGELFTKK-PIFQANL 917
Cdd:cd06618    143 PSNILLDesgnvklcdfgisgrlvDSKAKTRSAGCAAYMAPERIDPPDnpKYDIRADVWSLGISLVELATGQfPYRNCKT 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  918 ElaqLELISRLCGSPCPavwpdviKLPYfntmkpkkqyrrrlREEFS--FIpsaalDLLDHMLTLDPSKRCTAEQTLQSD 995
Cdd:cd06618    223 E---FEVLTKILNEEPP-------SLPP--------------NEGFSpdFC-----SFVDLCLTKDHRYRPKYRELLQHP 273
                          330
                   ....*....|....*...
gi 1907082950  996 FLKDVELSKMappDLPHW 1013
Cdd:cd06618    274 FIRRYETAEV---DVASW 288
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
744-1000 6.63e-11

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 66.58  E-value: 6.63e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  744 DTGELVALKKVRLDNEKEGfpITAIREIKILRQLVHQSVVNMKEivtdkqdalDFKKDKgAFYLVFEY-MDHDLMGLLES 822
Cdd:PTZ00267    91 DPKEKVVAKFVMLNDERQA--AYARSELHCLAACDHFGIVKHFD---------DFKSDD-KLLLIMEYgSGGDLNKQIKQ 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  823 GL---VHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL-----------NNSRPYTNKVI---------TLWYR 879
Cdd:PTZ00267   159 RLkehLPFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLmptgiiklgdfGFSKQYSDSVSldvassfcgTPYYL 238
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  880 PPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQ--ANLELAQLELISRLCGSPCPAVwpdviklpyfNTMKPkkqyrr 957
Cdd:PTZ00267   239 APE-LWERKRYSKKADMWSLGVILYELLTLHRPFKgpSQREIMQQVLYGKYDPFPCPVS----------SGMKA------ 301
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1907082950  958 rlreefsfipsaaldLLDHMLTLDPSKRCTAEQTLQSDFLKDV 1000
Cdd:PTZ00267   302 ---------------LLDPLLSKNPALRPTTQQLLHTEFLKYV 329
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
725-908 6.66e-11

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: 64.70  E-value: 6.66e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  725 IIGIIGEGTYGQVYKAKDKDTGE---LVALKKVRL---DNEKEGFpitaIREIKILRQLVHQSVVNMKEIVTDKQDALdf 798
Cdd:cd05033      8 IEKVIGGGEFGEVCSGSLKLPGKkeiDVAIKTLKSgysDKQRLDF----LTEASIMGQFDHPNVIRLEGVVTKSRPVM-- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  799 kkdkgafyLVFEYMDHdlmGLLESGLVH----FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN--------- 865
Cdd:cd05033     82 --------IVTEYMEN---GSLDKFLREndgkFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSdlvckvsdf 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  866 --SR-------PYTNK--VITLWYRPPElLLGEERYTPAIDVWSCGCILGELFT 908
Cdd:cd05033    151 glSRrledseaTYTTKggKIPIRWTAPE-AIAYRKFTSASDVWSFGIVMWEVMS 203
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
725-906 7.91e-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: 64.61  E-value: 7.91e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  725 IIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEgfPITAIREIKILRQLV-HQSVVNMkeivtdkqdaLDFK--KD 801
Cdd:cd14037      7 IEKYLAEGGFAHVYLVKTSNGGNRAALKRVYVNDEHD--LNVCKREIEIMKRLSgHKNIVGY----------IDSSanRS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 KGAFYLVFEYMDH-------DLMGL-LESGlvhFSEDHIKSFMKQLMEGLDYCH--KKNFLHRDIKCSNILLNNSRPY-- 869
Cdd:cd14037     75 GNGVYEVLLLMEYckgggviDLMNQrLQTG---LTESEILKIFCDVCEAVAAMHylKPPLIHRDLKVENVLISDSGNYkl 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  870 ------TNKVI-------------------TLWYRPPEL--LLGEERYTPAIDVWSCGCILGEL 906
Cdd:cd14037    152 cdfgsaTTKILppqtkqgvtyveedikkytTLQYRAPEMidLYRGKPITEKSDIWALGCLLYKL 215
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
729-927 8.71e-11

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: 64.11  E-value: 8.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGElVALKKVRLDN-EKEGFpitaIREIKILRQLVHQSVVNMKEIVTDKQdaldfkkdkgAFYL 807
Cdd:cd05114     12 LGSGLFGVVRLGKWRAQYK-VAIKAIREGAmSEEDF----IEEAKVMMKLTHPKLVQLYGVCTQQK----------PIYI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYMDHD-LMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS----------------RPYT 870
Cdd:cd05114     77 VTEFMENGcLLNYLRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTgvvkvsdfgmtryvldDQYT 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  871 N----KVITLWyRPPELLLgEERYTPAIDVWSCGCILGELFTK-KPIFQANLELAQLELISR 927
Cdd:cd05114    157 SssgaKFPVKW-SPPEVFN-YSKFSSKSDVWSFGVLMWEVFTEgKMPFESKSNYEVVEMVSR 216
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
729-1008 9.15e-11

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: 64.66  E-value: 9.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKvrLDNEKEGFPITAIREIKILRQLVHQSVVNMKE--IVTDKqdaldfkkdkgaFY 806
Cdd:cd06657     28 IGEGSTGIVCIATVKSSGKLVAVKK--MDLRKQQRRELLFNEVVIMRDYQHENVVEMYNsyLVGDE------------LW 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVFEYMDHdlmGLLESGLVH--FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL-----------------NNSR 867
Cdd:cd06657     94 VVMEFLEG---GALTDIVTHtrMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLthdgrvklsdfgfcaqvSKEV 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  868 PYTNKVI-TLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPifqanlelaqlelisrlcgspcpavwpdviklPYF 946
Cdd:cd06657    171 PRRKSLVgTPYWMAPE-LISRLPYGPEVDIWSLGIMVIEMVDGEP--------------------------------PYF 217
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  947 NT--MKPKKQYRRRLREEFSFIPSAALDL---LDHMLTLDPSKRCTAEQTLQSDFlkdveLSKMAPP 1008
Cdd:cd06657    218 NEppLKAMKMIRDNLPPKLKNLHKVSPSLkgfLDRLLVRDPAQRATAAELLKHPF-----LAKAGPP 279
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
729-994 1.01e-10

Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein 15; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Vps15 is a large protein consisting of an N-terminal kinase domain, a C-terminal WD-repeat containing domain, and an intermediate bridge domain that contain HEAT repeats. The kinase domain is necessary for the signaling functions of Vps15. Human Vps15 was previously called p150. It associates and regulates Vps34, also called Class III phosphoinositide 3-kinase (PI3K), which catalyzes the phosphorylation of D-myo-phosphatidylinositol (PtdIns). Vps34 is the only PI3K present in yeast. It plays an important role in the regulation of protein and vesicular trafficking and sorting, autophagy, trimeric G-protein signaling, and phagocytosis. The Vps15 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 64.20  E-value: 1.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTgelVALKKVrLDNEKEGFPITAI-REIKILRQLVHQsVVNM----KEIVTDKqdaldfkkdkg 803
Cdd:cd13980      8 LGSTRFLKVARARHDEG---LVVVKV-FVKPDPALPLRSYkQRLEEIRDRLLE-LPNVlpfqKVIETDK----------- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  804 AFYLVFEYMDHDL---------MGLLESGLVHFsedhiksfmkQLMEGLDYCHKKNFLHRDIKCSNILL----------- 863
Cdd:cd13980     72 AAYLIRQYVKYNLydristrpfLNLIEKKWIAF----------QLLHALNQCHKRGVCHGDIKTENVLVtswnwvyltdf 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  864 ----------NN----------SR------------PYTNKVITLWYRPPELllgeeryTPAIDVWSCGCILGELFTK-K 910
Cdd:cd13980    142 asfkptylpeDNpadfsyffdtSRrrtcyiaperfvDALTLDAESERRDGEL-------TPAMDIFSLGCVIAELFTEgR 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  911 PIFqanlELAQLelisrlcgspcpavwpdvikLPYfntmkpkKQYRRRLREEFSFIPSAAL-DLLDHMLTLDPSKRCTAE 989
Cdd:cd13980    215 PLF----DLSQL--------------------LAY-------RKGEFSPEQVLEKIEDPNIrELILHMIQRDPSKRLSAE 263

                   ....*
gi 1907082950  990 QTLQS 994
Cdd:cd13980    264 DYLKK 268
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
723-964 1.02e-10

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: 64.28  E-value: 1.02e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVR----LDNEKEGfpiTAIREIKILRQLVHQSVVNMkeivtdkqdaLDF 798
Cdd:cd08228      4 FQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQifemMDAKARQ---DCVKEIDLLKQLNHPNVIKY----------LDS 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  799 KKDKGAFYLVFEYMDhdlMGLLESGLVHFS-------EDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS----- 866
Cdd:cd08228     71 FIEDNELNIVLELAD---AGDLSQMIKYFKkqkrlipERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATgvvkl 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 ------RPYTNK-------VITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANlelaQLELISrLCGSPC 933
Cdd:cd08228    148 gdlglgRFFSSKttaahslVGTPYYMSPE-RIHENGYNFKSDIWSLGCLLYEMAALQSPFYGD----KMNLFS-LCQKIE 221
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1907082950  934 PAVWPDViklpyfntmkPKKQYRRRLREEFS 964
Cdd:cd08228    222 QCDYPPL----------PTEHYSEKLRELVS 242
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
723-997 1.12e-10

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


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 63.89  E-value: 1.12e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDnEKEGFPITAiREIKILRQLVHQSVVNMKEIVTDKQDaldfkkdk 802
Cdd:cd06646     11 YELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLE-PGDDFSLIQ-QEIFMVKECKHCNIVAYFGSYLSREK-------- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 gaFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS---------------- 866
Cdd:cd06646     81 --LWICMEYCGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNgdvkladfgvaakita 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 --RPYTNKVITLWYRPPELLLGEER--YTPAIDVWSCGCI---LGELftKKPIFQANlELAQLELISRLCGSPcpavwpd 939
Cdd:cd06646    159 tiAKRKSFIGTPYWMAPEVAAVEKNggYNQLCDIWAVGITaieLAEL--QPPMFDLH-PMRALFLMSKSNFQP------- 228
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  940 viklpyfntmkPKKQYRRRLREEF-SFIPSAaldlldhmLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd06646    229 -----------PKLKDKTKWSSTFhNFVKIS--------LTKNPKKRPTAERLLTHLFV 268
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
769-992 1.13e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 65.25  E-value: 1.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  769 REIKILRQLVHQSVVNmkeivtdkqdALDFKKDKGAFYLVFEYMDHDLMGLLEsGLVHFSEDHIKSFMKQLMEGLDYCHK 848
Cdd:PHA03207   135 REIDILKTISHRAIIN----------LIHAYRWKSTVCMVMPKYKCDLFTYVD-RSGPLPLEQAITIQRRLLEALAYLHG 203
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  849 KNFLHRDIKCSNILLNN----------------SRPYTNK----VITLWYRPPElLLGEERYTPAIDVWSCGCILGELFT 908
Cdd:PHA03207   204 RGIIHRDVKTENIFLDEpenavlgdfgaackldAHPDTPQcygwSGTLETNSPE-LLALDPYCAKTDIWSAGLVLFEMSV 282
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  909 KK-PIF--QANLELAQLELISRlCGSPCPAVWPdviKLPYFNTMKPKKQYRRRLREEFS-------FIPSAALD-LLDHM 977
Cdd:PHA03207   283 KNvTLFgkQVKSSSSQLRSIIR-CMQVHPLEFP---QNGSTNLCKHFKQYAIVLRPPYTippvirkYGMHMDVEyLIAKM 358
                          250
                   ....*....|....*
gi 1907082950  978 LTLDPSKRCTAEQTL 992
Cdd:PHA03207   359 LTFDQEFRPSAQDIL 373
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
721-1011 1.15e-10

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 64.61  E-value: 1.15e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDN-EKEGFPITAIREIKILRQLVHQSVVNMKEIVtdkqdaldfk 799
Cdd:cd05632      2 NTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRiKKRKGESMALNEKQILEKVNSQFVVNLAYAY---------- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 KDKGAFYLVFEYMDH-DL-MGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN------------ 865
Cdd:cd05632     72 ETKDALCLVLTIMNGgDLkFHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDyghirisdlgla 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 -----SRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRlcgspcpavwpdv 940
Cdd:cd05632    152 vkipeGESIRGRVGTVGYMAPE-VLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDR------------- 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  941 iklpyfNTMKPKKQYRRRLREEfsfipsaALDLLDHMLTLDPSKR--CT---AEQTLQSDFLKDVELSK-----MAPPDL 1010
Cdd:cd05632    218 ------RVLETEEVYSAKFSEE-------AKSICKMLLTKDPKQRlgCQeegAGEVKRHPFFRNMNFKRleagmLDPPFV 284

                   .
gi 1907082950 1011 P 1011
Cdd:cd05632    285 P 285
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
728-1012 1.18e-10

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


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 64.64  E-value: 1.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVRldnekegfpitaiREIKILRQLVHQSVVNMKEIVTDKQDALDFKK------D 801
Cdd:cd05595      2 LLGKGTFGKVILVREKATGRYYAMKILR-------------KEVIIAKDEVAHTVTESRVLQNTRHPFLTALKyafqthD 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 KGAFylVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN---------------- 865
Cdd:cd05595     69 RLCF--VMEYANGGELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKdghikitdfglckegi 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 SRPYTNKVI--TLWYRPPElLLGEERYTPAIDVWSCGCILGELftkkpifqanlelaqlelisrLCGspcpavwpdviKL 943
Cdd:cd05595    147 TDGATMKTFcgTPEYLAPE-VLEDNDYGRAVDWWGLGVVMYEM---------------------MCG-----------RL 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  944 PYFNtMKPKKQYRRRLREEFSF---IPSAALDLLDHMLTLDPSKRC-----TAEQTLQSDFL-----KDVELSKMAPPDL 1010
Cdd:cd05595    194 PFYN-QDHERLFELILMEEIRFprtLSPEAKSLLAGLLKKDPKQRLgggpsDAKEVMEHRFFlsinwQDVVQKKLLPPFK 272

                   ..
gi 1907082950 1011 PH 1012
Cdd:cd05595    273 PQ 274
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
729-999 1.21e-10

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


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 64.68  E-value: 1.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKV--RLDNEKEgfpitaiREIKILRQLV-HQSVVNMKEIVTDKQDAldfkkdkgaf 805
Cdd:cd14179     15 LGEGSFSICRKCLHKKTNQEYAVKIVskRMEANTQ-------REIAALKLCEgHPNIVKLHEVYHDQLHT---------- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  806 YLVFEymdhdlmgLLESGLV--------HFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN------------- 864
Cdd:cd14179     78 FLVME--------LLKGGELlerikkkqHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTdesdnseikiidf 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 --------NSRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLElaqleliSRLCGSPcpav 936
Cdd:cd14179    150 gfarlkppDNQPLKTPCFTLHYAAPE-LLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDK-------SLTCTSA---- 217
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  937 wpdviklpyFNTMKPKKQyrrrlrEEFSF-------IPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLKD 999
Cdd:cd14179    218 ---------EEIMKKIKQ------GDFSFegeawknVSQEAKDLIQGLLTVDPNKRIKMSGLRYNEWLQD 272
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
728-927 1.24e-10

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: 63.91  E-value: 1.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKV---RLDNEKEGFpiTAIREIKILRQLVHQSVVNMkeivtdkqdALDFKKdKGA 804
Cdd:cd05605      7 VLGKGGFGEVCACQVRATGKMYACKKLekkRIKKRKGEA--MALNEKQILEKVNSRFVVSL---------AYAYET-KDA 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  805 FYLVFEYMDH-DL------MGllESGlvhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN------------- 864
Cdd:cd05605     75 LCLVLTIMNGgDLkfhiynMG--NPG---FEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDdhghvrisdlgla 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  865 ----NSRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISR 927
Cdd:cd05605    150 veipEGETIRGRVGTVGYMAPE-VVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEKVKREEVDR 215
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
722-995 1.24e-10

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: 63.98  E-value: 1.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELV-ALKKVRLDNEKEGFPITAIREIKILRQLV---HQSVVNMkeivtdkqdaLD 797
Cdd:cd14052      1 RFANVELIGSGEFSQVYKVSERVPTGKVyAVKKLKPNYAGAKDRLRRLEEVSILRELTldgHDNIVQL----------ID 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 FKKDKGAFYLVFEYMDH-DLMGLL-ESGLVHFSED-HIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNnsRPYTNKV- 873
Cdd:cd14052     71 SWEYHGHLYIQTELCENgSLDVFLsELGLLGRLDEfRVWKILVELSLGLRFIHDHHFVHLDLKPANVLIT--FEGTLKIg 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  874 ----ITLW-------------YRPPELLLGEERYTPAiDVWSCGCILGELftkkpifQANLELAQ------------LEL 924
Cdd:cd14052    149 dfgmATVWplirgieregdreYIAPEILSEHMYDKPA-DIFSLGLILLEA-------AANVVLPDngdawqklrsgdLSD 220
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  925 ISRLcgspcpaVWPDVIKLPYFNTMKPKKQyrrrlreEFSFIPSAALD-LLDHMLTLDPSKRCTAEQTLQSD 995
Cdd:cd14052    221 APRL-------SSTDLHSASSPSSNPPPDP-------PNMPILSGSLDrVVRWMLSPEPDRRPTADDVLATP 278
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
723-911 1.36e-10

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 63.87  E-value: 1.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRL-DNEKEGFPItairEIKILRQLVHQsvvnmKEIVTdKQDALDFKKD 801
Cdd:cd06636     18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVtEDEEEEIKL----EINMLKKYSHH-----RNIAT-YYGAFIKKSP 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 KG---AFYLVFEYMDH----DLMGLLESGLvhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYT---- 870
Cdd:cd06636     88 PGhddQLWLVMEFCGAgsvtDLVKNTKGNA--LKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKlvdf 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  871 -------------NKVI-TLWYRPPELLLGEER----YTPAIDVWSCGCILGELFTKKP 911
Cdd:cd06636    166 gvsaqldrtvgrrNTFIgTPYWMAPEVIACDENpdatYDYRSDIWSLGITAIEMAEGAP 224
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
728-978 1.40e-10

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: 63.84  E-value: 1.40e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGE---LVALKKVR---LDNEKEGFpitaIREIKILRQLVHQSVVNMKEIVTDKQDALdfkkd 801
Cdd:cd05063     12 VIGAGEFGEVFRGILKMPGRkevAVAIKTLKpgyTEKQRQDF----LSEASIMGQFSHHNIIRLEGVVTKFKPAM----- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 kgafyLVFEYMDHdlmGLLESGLV----HFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-----------S 866
Cdd:cd05063     83 -----IITEYMEN---GALDKYLRdhdgEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSnleckvsdfglS 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 R--------PYTN---KVITLWYRPPEllLGEERYTPAIDVWSCGCILGEL--FTKKPIFQ-ANLELaqLELISRLCGSP 932
Cdd:cd05063    155 RvleddpegTYTTsggKIPIRWTAPEA--IAYRKFTSASDVWSFGIVMWEVmsFGERPYWDmSNHEV--MKAINDGFRLP 230
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1907082950  933 CPAVWPDVIklpyFNTMKPKKQYRRRLREEFSFIpsaaLDLLDHML 978
Cdd:cd05063    231 APMDCPSAV----YQLMLQCWQQDRARRPRFVDI----VNLLDKLL 268
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
729-934 1.80e-10

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: 63.55  E-value: 1.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAK-----DKDTGELVALKKVRLDNE---KEGFPitaiREIKILRQLVHQSVVNMKEIVTDKQdaldfkk 800
Cdd:cd05048     13 LGEGAFGKVYKGEllgpsSEESAISVAIKTLKENASpktQQDFR----REAELMSDLQHPNIVCLLGVCTKEQ------- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 dkgAFYLVFEYMDH-DLMGLL------ESGLVHFSEDHIKSFMK---------QLMEGLDYCHKKNFLHRDIKCSNILLN 864
Cdd:cd05048     82 ---PQCMLFEYMAHgDLHEFLvrhsphSDVGVSSDDDGTASSLDqsdflhiaiQIAAGMEYLSSHHYVHRDLAARNCLVG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 NSRpyTNKVITL----------WYR------------PPE-LLLGeeRYTPAIDVWSCGCILGELFT--KKPIFQ-ANLE 918
Cdd:cd05048    159 DGL--TVKISDFglsrdiyssdYYRvqsksllpvrwmPPEaILYG--KFTTESDVWSFGVVLWEIFSygLQPYYGySNQE 234
                          250
                   ....*....|....*.
gi 1907082950  919 LaqLELISRLCGSPCP 934
Cdd:cd05048    235 V--IEMIRSRQLLPCP 248
PTZ00284 PTZ00284
protein kinase; Provisional
722-937 1.85e-10

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 64.99  E-value: 1.85e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRldnEKEGFPITAIREIKILRQlVHQSVVNMKEIVTDKQDAldFKKD 801
Cdd:PTZ00284   130 RFKILSLLGEGTFGKVVEAWDRKRKEYCAVKIVR---NVPKYTRDAKIEIQFMEK-VRQADPADRFPLMKIQRY--FQNE 203
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 KGAFYLVfeyMDHDLMGLLESGLVH--FSEDHIKSFMKQLMEGLDYCHKK-NFLHRDIKCSNILLNNSR----PYTNK-- 872
Cdd:PTZ00284   204 TGHMCIV---MPKYGPCLLDWIMKHgpFSHRHLAQIIFQTGVALDYFHTElHLMHTDLKPENILMETSDtvvdPVTNRal 280
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  873 -------------------------VITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISR 927
Cdd:PTZ00284   281 ppdpcrvricdlggccderhsrtaiVSTRHYRSPEVVLGLG-WMYSTDMWSMGCIIYELYTGKLLYDTHDNLEHLHLMEK 359
                          250
                   ....*....|
gi 1907082950  928 LCGSpCPAVW 937
Cdd:PTZ00284   360 TLGR-LPSEW 368
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
728-985 1.95e-10

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


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 63.50  E-value: 1.95e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVRLDN-EKEGFPITAIREIKILRQLVHQSVVNMkeivtdkqdALDFKKdKGAFY 806
Cdd:cd05630      7 VLGKGGFGEVCACQVRATGKMYACKKLEKKRiKKRKGEAMALNEKQILEKVNSRFVVSL---------AYAYET-KDALC 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVFEYMDH-DL-MGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-----------------SR 867
Cdd:cd05630     77 LVLTLMNGgDLkFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDhghirisdlglavhvpeGQ 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  868 PYTNKVITLWYRPPELLlGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCgspcpavwpdviklpyfn 947
Cdd:cd05630    157 TIKGRVGTVGYMAPEVV-KNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLV------------------ 217
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1907082950  948 tmkpkkqyrRRLREEFS--FIPSAAlDLLDHMLTLDPSKR 985
Cdd:cd05630    218 ---------KEVPEEYSekFSPQAR-SLCSMLLCKDPAER 247
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
717-1012 2.00e-10

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 64.33  E-value: 2.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  717 KRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALK----KVRLDNEKEGFPITairEIKILRQLVHQSVVNMKEIVTDK 792
Cdd:cd05593     11 RKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKilkkEVIIAKDEVAHTLT---ESRVLKNTRHPFLTSLKYSFQTK 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  793 qDALDFkkdkgafylVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN------- 865
Cdd:cd05593     88 -DRLCF---------VMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKdghikit 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 ---------SRPYTNKVI--TLWYRPPElLLGEERYTPAIDVWSCGCILGELftkkpifqanlelaqlelisrLCGspcp 934
Cdd:cd05593    158 dfglckegiTDAATMKTFcgTPEYLAPE-VLEDNDYGRAVDWWGLGVVMYEM---------------------MCG---- 211
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  935 avwpdviKLPYFNtMKPKKQYRRRLREEFSF---IPSAALDLLDHMLTLDPSKRC-----TAEQTLQSDFL-----KDVE 1001
Cdd:cd05593    212 -------RLPFYN-QDHEKLFELILMEDIKFprtLSADAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFtgvnwQDVY 283
                          330
                   ....*....|.
gi 1907082950 1002 LSKMAPPDLPH 1012
Cdd:cd05593    284 DKKLVPPFKPQ 294
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
806-996 2.00e-10

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 63.15  E-value: 2.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  806 YLVFEYMDHDLMG-LLESGLvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL--------------------- 863
Cdd:cd14012     80 YLLTEYAPGGSLSeLLDSVG-SVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLdrdagtgivkltdyslgktll 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  864 -NNSRPYTNKVITLWYRPPELLLGEERYTPAIDVWScgciLGELFtkkpifqanlelaqlelISRLCGSPCPAVWPDVIK 942
Cdd:cd14012    159 dMCSRGSLDEFKQTYWLPPELAQGSKSPTRKTDVWD----LGLLF-----------------LQMLFGLDVLEKYTSPNP 217
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  943 LPYFNTMKPKKQyrrrlreefsfipsaalDLLDHMLTLDPSKRCTAEQTLQSDF 996
Cdd:cd14012    218 VLVSLDLSASLQ-----------------DFLSKCLSLDPKKRPTALELLPHEF 254
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
722-909 2.02e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 65.10  E-value: 2.02e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYK-AKDKDTGELVALKKVRLDNEKEG---------------FPITAIREIKILRQLVHQSVVNM 785
Cdd:PHA03210   149 HFRVIDDLPAGAFGKIFIcALRASTEEAEARRGVNSTNQGKPkcerliakrvkagsrAAIQLENEILALGRLNHENILKI 228
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  786 KEIVTDKQDAldfkkdkgafYLVFEYMDHDLMGLLESGLVHFSED----HIKSFMKQLMEGLDYCHKKNFLHRDIKCSNI 861
Cdd:PHA03210   229 EEILRSEANT----------YMITQKYDFDLYSFMYDEAFDWKDRpllkQTRAIMKQLLCAVEYIHDKKLIHRDIKLENI 298
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  862 LLN-----------NSRPYTNK--------VITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTK 909
Cdd:PHA03210   299 FLNcdgkivlgdfgTAMPFEKEreafdygwVGTVATNSPEILAGDG-YCEITDIWSCGLILLDMLSH 364
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
729-918 2.03e-10

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: 63.45  E-value: 2.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAK------DKDTgELVALKKVRLDNE--KEGFPitaiREIKILRQLVHQSVVNMKEIVTDKQDALdfkk 800
Cdd:cd05092     13 LGEGAFGKVFLAEchnllpEQDK-MLVAVKALKEATEsaRQDFQ----REAELLTVLQHQHIVRFYGVCTEGEPLI---- 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 dkgafyLVFEYMDH-DLMGLLES-----GLVHFSED---------HIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN 865
Cdd:cd05092     84 ------MVFEYMRHgDLNRFLRShgpdaKILDGGEGqapgqltlgQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQ 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  866 -----------SRPYTNkviTLWYR------------PPELLLgEERYTPAIDVWSCGCILGELFT--KKPIFQ-ANLE 918
Cdd:cd05092    158 glvvkigdfgmSRDIYS---TDYYRvggrtmlpirwmPPESIL-YRKFTTESDIWSFGVVLWEIFTygKQPWYQlSNTE 232
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
729-867 2.09e-10

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: 63.30  E-value: 2.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKK-VRLDNE-KEGFpitaIREIKILRQLVHQSVVNMKEIVTdkqdaldfkKDKgAFY 806
Cdd:cd14154      1 LGKGFFGQAIKVTHRETGEVMVMKElIRFDEEaQRNF----LKEVKVMRSLDHPNVLKFIGVLY---------KDK-KLN 66
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  807 LVFEYMDHD-LMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSR 867
Cdd:cd14154     67 LITEYIPGGtLKDVLKDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDK 128
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
729-997 2.83e-10

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


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 63.25  E-value: 2.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKkVRLDNEKegfpitAIREIKILRQLV-HQSVVNMKEIVTDKqdaLDFKKD---KGA 804
Cdd:cd14171     14 LGTGISGPVRVCVKKSTGERFALK-ILLDRPK------ARTEVRLHMMCSgHPNIVQIYDVYANS---VQFPGEsspRAR 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  805 FYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL-NNSRPYTNKV---------- 873
Cdd:cd14171     84 LLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLkDNSEDAPIKLcdfgfakvdq 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  874 -------ITLWYRPPELLLGEER----------------YTPAIDVWSCGCILGELftkkpifqanlelaqlelisrLCG 930
Cdd:cd14171    164 gdlmtpqFTPYYVAPQVLEAQRRhrkersgiptsptpytYDKSCDMWSLGVIIYIM---------------------LCG 222
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  931 SPcpavwpdviklPYFNTMkPKKQYRRRLR------------EEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14171    223 YP-----------PFYSEH-PSRTITKDMKrkimtgsyefpeEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
721-864 2.98e-10

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


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 64.10  E-value: 2.98e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRldnEKEGFPITAIREIKILRQLVHQS----VVNMkeiVTDKQDAL 796
Cdd:cd05629      1 EDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLL---KSEMFKKDQLAHVKAERDVLAESdspwVVSL---YYSFQDAQ 74
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  797 dfkkdkgAFYLVFEYM-DHDLMGLLESGLVhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN 864
Cdd:cd05629     75 -------YLYLIMEFLpGGDLMTMLIKYDT-FSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILID 135
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
729-909 3.29e-10

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: 62.27  E-value: 3.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKA----KDKdtgelVALKKVRldnekEGFPITA--IREIKILRQLVHQSVVNMKEIVTDKqdaldfkkdk 802
Cdd:cd05112     12 IGSGQFGLVHLGywlnKDK-----VAIKTIR-----EGAMSEEdfIEEAEVMMKLSHPKLVQLYGVCLEQ---------- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 GAFYLVFEYMDHD-LMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSR-------------- 867
Cdd:cd05112     72 APICLVFEFMEHGcLSDYLRTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQvvkvsdfgmtrfvl 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1907082950  868 --PYTN----KVITLWYRPPELLLGeeRYTPAIDVWSCGCILGELFTK 909
Cdd:cd05112    152 ddQYTSstgtKFPVKWSSPEVFSFS--RYSSKSDVWSFGVLMWEVFSE 197
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
729-985 3.80e-10

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: 62.28  E-value: 3.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKK-VRLDNEKEGfpiTAIREIKILRQLVHQSVvnMKEI-VTDKQDALDFkkdkgafy 806
Cdd:cd14221      1 LGKGCFGQAIKVTHRETGEVMVMKElIRFDEETQR---TFLKEVKVMRCLEHPNV--LKFIgVLYKDKRLNF-------- 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 lVFEYMDH-DLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL---------------------- 863
Cdd:cd14221     68 -ITEYIKGgTLRGIIKSMDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVrenksvvvadfglarlmvdekt 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  864 ------NNSRPYTNKVITL----WYRPPELLLGEErYTPAIDVWSCGCILGELFTK---KPIF---QANLELAQLELISR 927
Cdd:cd14221    147 qpeglrSLKKPDRKKRYTVvgnpYWMAPEMINGRS-YDEKVDVFSFGIVLCEIIGRvnaDPDYlprTMDFGLNVRGFLDR 225
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  928 LCGSPCPAvwpdviklpyfntmkpkkqyrrrlreefSFIPSAALdlldhMLTLDPSKR 985
Cdd:cd14221    226 YCPPNCPP----------------------------SFFPIAVL-----CCDLDPEKR 250
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
729-997 3.92e-10

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 62.25  E-value: 3.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILrQLVHQS--VVNMKEIV-TDKQDALDFKKDKGAf 805
Cdd:cd14198     16 LGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAEILHEIAVL-ELAKSNprVVNLHEVYeTTSEIILILEYAAGG- 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  806 yLVFEYMDHDLMGLLesglvhfSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTN-KVI---------- 874
Cdd:cd14198     94 -EIFNLCVPDLAEMV-------SENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPLGDiKIVdfgmsrkigh 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  875 ---------TLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQAnlelaqlelisrlcgspcpavwpDVIKLPY 945
Cdd:cd14198    166 acelreimgTPEYLAPE-ILNYDPITTATDMWNIGVIAYMLLTHESPFVG-----------------------EDNQETF 221
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  946 FNTMKPKKQYRrrlREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14198    222 LNISQVNVDYS---EETFSSVSQLATDFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
721-911 4.16e-10

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: 62.77  E-value: 4.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRL-----DNEKEGFPITAIREIKILRQLVHQSVVNMKEIvtdkqda 795
Cdd:cd14041      6 DRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLnknwrDEKKENYHKHACREYRIHKELDHPRIVKLYDY------- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  796 ldFKKDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCH--KKNFLHRDIKCSNILLNNSRPYTNKV 873
Cdd:cd14041     79 --FSLDTDSFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNeiKPPIIHYDLKPGNILLVNGTACGEIK 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  874 I----------------------------TLWYRPPE-LLLGEE--RYTPAIDVWSCGCILGE-LFTKKP 911
Cdd:cd14041    157 ItdfglskimdddsynsvdgmeltsqgagTYWYLPPEcFVVGKEppKISNKVDVWSVGVIFYQcLYGRKP 226
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
726-908 4.52e-10

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: 62.10  E-value: 4.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  726 IGIIGEGTYGQVYKAKDKDT----GELVALKKVrLDNEKEGFPITAI-REIKILRQLVHQSVVNMkeivtdkqdaLDFKK 800
Cdd:cd05046     10 ITTLGRGEFGEVFLAKAKGIeeegGETLVLVKA-LQKTKDENLQSEFrRELDMFRKLSHKNVVRL----------LGLCR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DKGAFYLVFEYMD-HDLMGLL--------ESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSR---- 867
Cdd:cd05046     79 EAEPHYMILEYTDlGDLKQFLratkskdeKLKPPPLSTKQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQRevkv 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  868 ---------------PYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFT 908
Cdd:cd05046    159 sllslskdvynseyyKLRNALIPLRWLAPEAVQ-EDDFSTKSDVWSFGVLMWEVFT 213
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
729-908 5.83e-10

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: 61.60  E-value: 5.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKdtGELVALKKVRLD-NEKEGFpitaIREIKILRQLVHQSVVNMKEIVTDKQdaldfkkdkgAFYL 807
Cdd:cd05039     14 IGKGEFGDVMLGDYR--GQKVAVKCLKDDsTAAQAF----LAEASVMTTLRHPNLVQLLGVVLEGN----------GLYI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYMDH-DLMGLLES-GLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN----------------NSRPY 869
Cdd:cd05039     78 VTEYMAKgSLVDYLRSrGRAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSednvakvsdfglakeaSSNQD 157
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1907082950  870 TNKVITLWYRPPELLLGeeRYTPAIDVWSCGCILGELFT 908
Cdd:cd05039    158 GGKLPIKWTAPEALREK--KFSTKSDVWSFGILLWEIYS 194
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
720-998 6.69e-10

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 61.41  E-value: 6.69e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  720 VDKFDIIgiigEGTYGQVYKAKDKDTGELVALKKVRLDNekegfpITAIrEIKIlRQLV--HQSVVNMKEIVTDKQDALd 797
Cdd:PHA03390    19 VKKLKLI----DGKFGKVSVLKHKPTQKLFVQKIIKAKN------FNAI-EPMV-HQLMkdNPNFIKLYYSVTTLKGHV- 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 fkkdkgafyLVFEYM-DHDLMGLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRP------Y- 869
Cdd:PHA03390    86 ---------LIMDYIkDGDLFDLLKKE-GKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAKDriylcdYg 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  870 TNKVI--------TLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQAN----LELAQLelisrlcgspcpavw 937
Cdd:PHA03390   156 LCKIIgtpscydgTLDYFSPEKIKG-HNYDVSFDWWAVGVLTYELLTGKHPFKEDedeeLDLESL--------------- 219
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  938 pdviklpyfntmkpKKQYRRRLrEEFSFIPSAALDLLDHMLTLDPSKR-CTAEQTLQSDFLK 998
Cdd:PHA03390   220 --------------LKRQQKKL-PFIKNVSKNANDFVQSMLKYNINYRlTNYNEIIKHPFLK 266
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
729-903 7.64e-10

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: 61.91  E-value: 7.64e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALK---KVRLdNEKEGFP---------------------ITAI-REIKILRQLVHQSVV 783
Cdd:cd14199     10 IGKGSYGVVKLAYNEDDNTYYAMKvlsKKKL-MRQAGFPrrppprgaraapegctqprgpIERVyQEIAILKKLDHPNVV 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  784 NMKEIVTD-KQDALdfkkdkgafYLVFEymdhdlmgLLESGLVH-------FSEDHIKSFMKQLMEGLDYCHKKNFLHRD 855
Cdd:cd14199     89 KLVEVLDDpSEDHL---------YMVFE--------LVKQGPVMevptlkpLSEDQARFYFQDLIKGIEYLHYQKIIHRD 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  856 IKCSNILL------------------NNSRPYTNKVITLWYRPPElLLGEERYT---PAIDVWSCGCIL 903
Cdd:cd14199    152 VKPSNLLVgedghikiadfgvsnefeGSDALLTNTVGTPAFMAPE-TLSETRKIfsgKALDVWAMGVTL 219
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
728-964 9.44e-10

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: 60.79  E-value: 9.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGElVALKKVRLDNEKEgFPITAIREIKILRQLVHQSVVNMKEIVTDKQdaldfkkdkgAFYL 807
Cdd:cd05085      3 LLGKGNFGEVYKGTLKDKTP-VAVKTCKEDLPQE-LKIKFLSEARILKQYDHPNIVKLIGVCTQRQ----------PIYI 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYMDH-DLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRP----------------YT 870
Cdd:cd05085     71 VMELVPGgDFLSFLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNAlkisdfgmsrqeddgvYS 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  871 N---KVITLWYRPPELLlGEERYTPAIDVWSCGCILGELFT----KKPIFQANLELAQLELISRLCgspCPAVWPDVIkl 943
Cdd:cd05085    151 SsglKQIPIKWTAPEAL-NYGRYSSESDVWSFGILLWETFSlgvcPYPGMTNQQAREQVEKGYRMS---APQRCPEDI-- 224
                          250       260
                   ....*....|....*....|.
gi 1907082950  944 pyFNTMKPKKQYRRRLREEFS 964
Cdd:cd05085    225 --YKIMQRCWDYNPENRPKFS 243
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
721-917 9.90e-10

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 62.33  E-value: 9.90e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVrldNEKEgfpITAIREIKILRQLVHQSVVNMKEIVTDKQDALdfkK 800
Cdd:cd05624     72 DDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKIL---NKWE---MLKRAETACFREERNVLVNGDCQWITTLHYAF---Q 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DKGAFYLVFEY-MDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL---------------- 863
Cdd:cd05624    143 DENYLYLVMDYyVGGDLLTLLSKFEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLdmnghirladfgsclk 222
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  864 ---NNSRPYTNKVITLWYRPPELLLGEE----RYTPAIDVWSCG-CILGELFTKKPIFQANL 917
Cdd:cd05624    223 mndDGTVQSSVAVGTPDYISPEILQAMEdgmgKYGPECDWWSLGvCMYEMLYGETPFYAESL 284
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
729-939 1.00e-09

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: 61.24  E-value: 1.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYkakdkdTGELVALKKVRLDNEKEG--FPITAIREIKILRQLVHQSVVNMKEIVTDKqdaldfkkdkgAFY 806
Cdd:cd05069     20 LGQGCFGEVW------MGTWNGTTKVAIKTLKPGtmMPEAFLQEAQIMKKLRHDKLVPLYAVVSEE-----------PIY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVFEYMDH-DLMGLLESGL-VHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS----------------RP 868
Cdd:cd05069     83 IVTEFMGKgSLLDFLKEGDgKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNlvckiadfglarliedNE 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  869 YT----NKVITLWYRPPELLLGeeRYTPAIDVWSCGCILGELFTKKPI-FQANLELAQLELISRLCGSPCPAVWPD 939
Cdd:cd05069    163 YTarqgAKFPIKWTAPEAALYG--RFTIKSDVWSFGILLTELVTKGRVpYPGMVNREVLEQVERGYRMPCPQGCPE 236
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
729-997 1.44e-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: 60.84  E-value: 1.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEgfpitairEIKILRQLVhqsvvnmkeIVTDKQDALDFKKDKGAF--- 805
Cdd:cd06640     12 IGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAED--------EIEDIQQEI---------TVLSQCDSPYVTKYYGSYlkg 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  806 ---YLVFEYMDH-DLMGLLESGlvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-----------SRPYT 870
Cdd:cd06640     75 tklWIIMEYLGGgSALDLLRAG--PFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEqgdvkladfgvAGQLT 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  871 NKVI-------TLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPifqANLELAQLELIsrlcgspcpavwpdvIKL 943
Cdd:cd06640    153 DTQIkrntfvgTPFWMAPE-VIQQSAYDSKADIWSLGITAIELAKGEP---PNSDMHPMRVL---------------FLI 213
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  944 PYFNTMKPKKQYRRRLREefsfipsaaldLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd06640    214 PKNNPPTLVGDFSKPFKE-----------FIDACLNKDPSFRPTAKELLKHKFI 256
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
703-922 1.47e-09

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: 60.82  E-value: 1.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  703 PRYGERRQTESDWGKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRL-DNEKEGFPITAIREIKILRQLVHQS 781
Cdd:cd08229      6 PQFQPQKALRPDMGYNTLANFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIfDLMDAKARADCIKEIDLLKQLNHPN 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  782 VVNMKEIVTDKQDaldfkkdkgaFYLVFEYMDhdlMGLLESGLVHFS-------EDHIKSFMKQLMEGLDYCHKKNFLHR 854
Cdd:cd08229     86 VIKYYASFIEDNE----------LNIVLELAD---AGDLSRMIKHFKkqkrlipEKTVWKYFVQLCSALEHMHSRRVMHR 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  855 DIKCSNILLNNS-----------RPYTNK-------VITLWYRPPElLLGEERYTPAIDVWSCGCILGELFT-KKPIFQA 915
Cdd:cd08229    153 DIKPANVFITATgvvklgdlglgRFFSSKttaahslVGTPYYMSPE-RIHENGYNFKSDIWSLGCLLYEMAAlQSPFYGD 231

                   ....*..
gi 1907082950  916 NLELAQL 922
Cdd:cd08229    232 KMNLYSL 238
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
729-908 1.49e-09

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: 60.88  E-value: 1.49e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELV----ALKKVRLDNEKEGFPITAIR---EIKILRQLVHQSVVNMKeivtdkqdALDFKKD 801
Cdd:cd14001      7 LGYGTGVNVYLMKRSPRGGSSrspwAVKKINSKCDKGQRSLYQERlkeEAKILKSLNHPNIVGFR--------AFTKSED 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 kGAFYLVFEYMDHDLMGLLE----SGLVHFSEDHIKSFMKQLMEGLDYCH-KKNFLHRDIKCSNILLNN----------- 865
Cdd:cd14001     79 -GSLCLAMEYGGKSLNDLIEeryeAGLGPFPAATILKVALSIARALEYLHnEKKILHGDIKSGNVLIKGdfesvklcdfg 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  866 ------------SRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFT 908
Cdd:cd14001    158 vslpltenlevdSDPKAQYVGTEPWKAKEALEEGGVITDKADIFAYGLVLWEMMT 212
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
721-997 1.69e-09

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: 60.37  E-value: 1.69e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDI----IGIIGEGTYGQVYKAKDKDTGELVALKKVrldNEKEGFPITAIREIKILRQLVHQSVVNMkeivtdkqdaL 796
Cdd:cd14113      3 DNFDSfyseVAELGRGRFSVVKKCDQRGTKRAVATKFV---NKKLMKRDQVTHELGVLQSLQHPQLVGL----------L 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  797 DFKKDKGAFYLVFEYMDHdlmGLLESGLV---HFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN--------- 864
Cdd:cd14113     70 DTFETPTSYILVLEMADQ---GRLLDYVVrwgNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDqslskptik 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 ----------NSRPYTNKVI-TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTK-KPIFQANLELAQLElISRLCGSp 932
Cdd:cd14113    147 ladfgdavqlNTTYYIHQLLgSPEFAAPEIILGNP-VSLTSDLWSIGVLTYVLLSGvSPFLDESVEETCLN-ICRLDFS- 223
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  933 cpavWPDviklpyfntmkpkkqyrrrlrEEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14113    224 ----FPD---------------------DYFKGVSQKAKDFVCFLLQMDPAKRPSAALCLQEQWL 263
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
727-903 1.89e-09

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 60.22  E-value: 1.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  727 GIIGEGTYGQVYKAKDKDTGELVALKKVRLdnekEGFpitAIREIKILRQLVHQSVVNMKEIVTDkqdaldfkkdkGAFY 806
Cdd:cd13991     12 LRIGRGSFGEVHRMEDKQTGFQCAVKKVRL----EVF---RAEELMACAGLTSPRVVPLYGAVRE-----------GPWV 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVF-EYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYT--------------- 870
Cdd:cd13991     74 NIFmDLKEGGSLGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSDAflcdfghaecldpdg 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1907082950  871 --NKVITLWYRP-------PELLLGEERYTPAiDVWSCGCIL 903
Cdd:cd13991    154 lgKSLFTGDYIPgtethmaPEVVLGKPCDAKV-DVWSSCCMM 194
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
723-1011 1.95e-09

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


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 60.40  E-value: 1.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVY---KAKDKDTGELVALKKVRldnekegfPITAIREIKIL------RQLVHQsvVNMKEIVTDKQ 793
Cdd:cd05613      2 FELLKVLGTGAYGKVFlvrKVSGHDAGKLYAMKVLK--------KATIVQKAKTAehtrteRQVLEH--IRQSPFLVTLH 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  794 DAldFKKDKgAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN--------- 864
Cdd:cd05613     72 YA--FQTDT-KLHLILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDssghvvltd 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 -----------NSRPYTnKVITLWYRPPELLL-GEERYTPAIDVWSCGCILGELFTKKPIFQANLEL-AQLELISRLCGS 931
Cdd:cd05613    149 fglskeflldeNERAYS-FCGTIEYMAPEIVRgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKnSQAEISRRILKS 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  932 pcpavwpdviKLPYFNTMKPkkqyrrrlreefsfipsAALDLLDHMLTLDPSKRC-----TAEQTLQSDFLKDVELSKMA 1006
Cdd:cd05613    228 ----------EPPYPQEMSA-----------------LAKDIIQRLLMKDPKKRLgcgpnGADEIKKHPFFQKINWDDLA 280

                   ....*
gi 1907082950 1007 PPDLP 1011
Cdd:cd05613    281 AKKVP 285
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
729-939 1.97e-09

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: 60.47  E-value: 1.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGElVALKKVRLDNEKegfPITAIREIKILRQLVHQSVVNMKEIVTDKqdaldfkkdkgAFYLV 808
Cdd:cd05071     17 LGQGCFGEVWMGTWNGTTR-VAIKTLKPGTMS---PEAFLQEAQVMKKLRHEKLVQLYAVVSEE-----------PIYIV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDH-DLMGLLESGL-VHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS----------------RPYT 870
Cdd:cd05071     82 TEYMSKgSLLDFLKGEMgKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENlvckvadfglarliedNEYT 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  871 ----NKVITLWYRPPELLLGeeRYTPAIDVWSCGCILGELFTKKPI-FQANLELAQLELISRLCGSPCPAVWPD 939
Cdd:cd05071    162 arqgAKFPIKWTAPEAALYG--RFTIKSDVWSFGILLTELTTKGRVpYPGMVNREVLDQVERGYRMPCPPECPE 233
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
729-997 2.03e-09

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


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 60.22  E-value: 2.03e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITA--IREIKILRQLVHQSVVNMKEIVtdkqdaldfkKDKGAFY 806
Cdd:cd14070     10 LGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDSYVTKnlRREGRIQQMIRHPNITQLLDIL----------ETENSYY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVFEY-MDHDLMGLLESGLvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-------------------- 865
Cdd:cd14070     80 LVMELcPGGNLMHRIYDKK-RLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDEndniklidfglsncagilgy 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 SRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGcilgelftkkpifqanlelaqLELISRLCGSpcpavwpdvikLPY 945
Cdd:cd14070    159 SDPFSTQCGSPAYAAPE-LLARKKYGPKVDVWSIG---------------------VNMYAMLTGT-----------LPF 205
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  946 fnTMKP---KKQYRRRLREEFSFIPS----AALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14070    206 --TVEPfslRALHQKMVDKEMNPLPTdlspGAISFLRSLLEPDPLKRPNIKQALANRWL 262
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
729-987 2.18e-09

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: 60.09  E-value: 2.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDnEKEGFPITAIREIKILRQLVHQSVVNMKEivtdkqdalDFKKDKgAFYLV 808
Cdd:cd06641     12 IGKGSFGEVFKGIDNRTQKVVAIKIIDLE-EAEDEIEDIQQEITVLSQCDSPYVTKYYG---------SYLKDT-KLWII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDH-DLMGLLESGlvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN-----------------NSRPYT 870
Cdd:cd06641     81 MEYLGGgSALDLLEPG--PLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSehgevkladfgvagqltDTQIKR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  871 NKVI-TLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELIsrlcgspcPAVWPDVIKLPYFNTM 949
Cdd:cd06641    159 N*FVgTPFWMAPE-VIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLI--------PKNNPPTLEGNYSKPL 229
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1907082950  950 kpKKQYRRRLREEFSFIPSAAlDLLDHMLTLDPSKRCT 987
Cdd:cd06641    230 --KEFVEACLNKEPSFRPTAK-ELLKHKFILRNAKKTS 264
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
728-911 2.21e-09

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: 59.71  E-value: 2.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKdtGELVALKKVRLDNEKEgFPITA---IREIKILRQLVHQSVVNMKEIVTDKQDaldfkkdkga 804
Cdd:cd14061      1 VIGVGGFGKVYRGIWR--GEEVAVKAARQDPDED-ISVTLenvRQEARLFWMLRHPNIIALRGVCLQPPN---------- 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  805 FYLVFEYMDhdlMGLLESglvHFSEDHIK-----SFMKQLMEGLDYCHKKN---FLHRDIKCSNILLN---NSRPYTNKV 873
Cdd:cd14061     68 LCLVMEYAR---GGALNR---VLAGRKIPphvlvDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILeaiENEDLENKT 141
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  874 ITL--------WYR-------------PPElLLGEERYTPAIDVWSCGCILGELFTKKP 911
Cdd:cd14061    142 LKItdfglareWHKttrmsaagtyawmAPE-VIKSSTFSKASDVWSYGVLLWELLTGEV 199
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
721-997 2.44e-09

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 59.63  E-value: 2.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITaiREIKILRQLVHQSVVNMKEIVTDKQDALDFKK 800
Cdd:cd14191      2 DFYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKENIR--QEISIMNCLHHPKLVQCVDAFEEKANIVMVLE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DKGAFYLVFEYMDHDLmgllesglvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTNKVI------ 874
Cdd:cd14191     80 MVSGGELFERIIDEDF---------ELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTKIKLIdfglar 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  875 --------TLWYRPPELLLGE----ERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRlcgspcpAVWPdvik 942
Cdd:cd14191    151 rlenagslKVLFGTPEFVAPEvinyEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTS-------ATWD---- 219
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  943 lpyFNTmkpkkqyrrrlrEEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14191    220 ---FDD------------EAFDEISDDAKDFISNLLKKDMKARLTCTQCLQHPWL 259
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
721-938 3.05e-09

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: 59.70  E-value: 3.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKakdkdtGELVALKKVRLDNEKEGF--PITAIREIKILRQLVHQSVVNMKEIVTDKqdaldf 798
Cdd:cd05070      9 ESLQLIKRLGNGQFGEVWM------GTWNGNTKVAIKTLKPGTmsPESFLEEAQIMKKLKHDKLVQLYAVVSEE------ 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  799 kkdkgAFYLVFEYMDH-DLMGLLESGLVH-FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN----------- 865
Cdd:cd05070     77 -----PIYIVTEYMSKgSLLDFLKDGEGRaLKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNglickiadfgl 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 -----SRPYT----NKVITLWYRPPELLLGeeRYTPAIDVWSCGCILGELFTKKPIFQANLELAQ-LELISRLCGSPCPA 935
Cdd:cd05070    152 arlieDNEYTarqgAKFPIKWTAPEAALYG--RFTIKSDVWSFGILLTELVTKGRVPYPGMNNREvLEQVERGYRMPCPQ 229

                   ...
gi 1907082950  936 VWP 938
Cdd:cd05070    230 DCP 232
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
729-963 3.10e-09

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: 59.52  E-value: 3.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTgelvalKKVRLDNEKEGF--PITAIREIKILRQLVHQSVVNMKEIVTdkqdaldfkkdKGAFY 806
Cdd:cd05067     15 LGAGQFGEVWMGYYNGH------TKVAIKSLKQGSmsPDAFLAEANLMKQLQHQRLVRLYAVVT-----------QEPIY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVFEYMDH-DLMGLLESGLVH-FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS----------------RP 868
Cdd:cd05067     78 IITEYMENgSLVDFLKTPSGIkLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTlsckiadfglarliedNE 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  869 YT----NKVITLWYRPPELLLGEerYTPAIDVWSCGCILGELFTKKPI---FQANLELAQ-LELISRL-CGSPCPAVWPD 939
Cdd:cd05067    158 YTaregAKFPIKWTAPEAINYGT--FTIKSDVWSFGILLTEIVTHGRIpypGMTNPEVIQnLERGYRMpRPDNCPEELYQ 235
                          250       260
                   ....*....|....*....|....*.
gi 1907082950  940 VIKLPYFNT--MKPKKQYRRRLREEF 963
Cdd:cd05067    236 LMRLCWKERpeDRPTFEYLRSVLEDF 261
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
721-866 3.35e-09

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


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 59.15  E-value: 3.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGfpiTAIREIKILRQLVHQSVVNMKEIvtdkqdaldFKK 800
Cdd:cd14108      2 DYYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKT---SARRELALLAELDHKSIVRFHDA---------FEK 69
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  801 dKGAFYLVFEYMDHDLMgLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS 866
Cdd:cd14108     70 -RRVVIIVTELCHEELL-ERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQ 133
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
728-1011 3.40e-09

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


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 59.62  E-value: 3.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVRLDN-EKEGFPITAIREIKILRQLVHQSVVNMKeIVTDKQDALdfkkdkgafY 806
Cdd:cd05631      7 VLGKGGFGEVCACQVRATGKMYACKKLEKKRiKKRKGEAMALNEKRILEKVNSRFVVSLA-YAYETKDAL---------C 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVFEYMDH-DL-MGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-----------------SR 867
Cdd:cd05631     77 LVLTIMNGgDLkFHIYNMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDrghirisdlglavqipeGE 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  868 PYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRlcgspcpavwpdviklpyfN 947
Cdd:cd05631    157 TVRGRVGTVGYMAPE-VINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKREEVDR-------------------R 216
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  948 TMKPKKQYRRRLREEfsfipsaALDLLDHMLTLDPSKR--CT---AEQTLQSDFLKDV-----ELSKMAPPDLP 1011
Cdd:cd05631    217 VKEDQEEYSEKFSED-------AKSICRMLLTKNPKERlgCRgngAAGVKQHPIFKNInfkrlEANMLEPPFCP 283
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
728-927 3.87e-09

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 59.21  E-value: 3.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKE-GFPITAIR---EIKILRQLVH--QSVVNMkeivtdkqdaLDFKKD 801
Cdd:cd14100      7 LLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVSEwGELPNGTRvpmEIVLLKKVGSgfRGVIRL----------LDWFER 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 KGAFYLVFEYMD--HDLMGLL-ESGLVhfSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRP---------- 868
Cdd:cd14100     77 PDSFVLVLERPEpvQDLFDFItERGAL--PEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDLNTGelklidfgsg 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  869 -------YTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISR 927
Cdd:cd14100    155 allkdtvYTDFDGTRVYSPPEWIRFHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIRGQVFFR 220
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
728-990 3.93e-09

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


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 59.23  E-value: 3.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKkVRLDNEKegfpitAIREIKIlrqlvHQSVVNMKEIVTDKQDALDFKKDKGAFYL 807
Cdd:cd14172     11 VLGLGVNGKVLECFHRRTGQKCALK-LLYDSPK------ARREVEH-----HWRASGGPHIVHILDVYENMHHGKRCLLI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYMDH-DLMG-LLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSR------------------ 867
Cdd:cd14172     79 IMECMEGgELFSrIQERGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEkdavlkltdfgfakettv 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  868 --PYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELftkkpifqanlelaqlelisrLCGSPcpavwpdviklPY 945
Cdd:cd14172    159 qnALQTPCYTPYYVAPE-VLGPEKYDKSCDMWSLGVIMYIL---------------------LCGFP-----------PF 205
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  946 F-NT---MKPKKQYRRRLRE------EFSFIPSAALDLLDHMLTLDPSKRCTAEQ 990
Cdd:cd14172    206 YsNTgqaISPGMKRRIRMGQygfpnpEWAEVSEEAKQLIRHLLKTDPTERMTITQ 260
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
722-997 4.07e-09

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK3 is highly expressed in the heart and skeletal muscles, and is controlled by a muscle-specific enhancer that is regulated by MEF2. It may play an important role in muscle development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271120 [Multi-domain]  Cd Length: 365  Bit Score: 60.42  E-value: 4.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRldnEKEGFPITAIREIKILRQLVHQSVVNMK-EIVTDKQDALDFKK 800
Cdd:cd14218     11 RYHVVRKLGWGHFSTVWLCWDIQRKRFVALKVVK---SAVHYTETAVDEIKLLKCVRDSDPSDPKrETIVQLIDDFKISG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DKGAFY-LVFEYMDHDLMG-LLESGLVHFSEDHIKSFMKQLMEGLDYCHKK-NFLHRDIKCSNILLNNSRPYTNKV---I 874
Cdd:cd14218     88 VNGVHVcMVLEVLGHQLLKwIIKSNYQGLPLPCVKSILRQVLQGLDYLHTKcKIIHTDIKPENILMCVDEGYVRRLaaeA 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  875 TLW----------------------------------------------------------YRPPELLLGEERYTPAiDV 896
Cdd:cd14218    168 TIWqqagapppsgssvsfgasdflvnplepqnadkirvkiadlgnacwvhkhftediqtrqYRALEVLIGAEYGTPA-DI 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  897 WSCGCILGELFTKKPIFQAN------LELAQLELISRLCGSPCPA-VWPDVIKLPYFN---------TMKPKKQYRRRLR 960
Cdd:cd14218    247 WSTACMAFELATGDYLFEPHsgedytRDEDHIAHIVELLGDIPPHfALSGRYSREYFNrrgelrhikNLKHWGLYEVLVE 326
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1907082950  961 E-EFSFIPSAAL-DLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14218    327 KyEWPLEQAAQFtDFLLPMMEFLPEKRATAAQCLQHPWL 365
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
723-927 4.25e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 60.68  E-value: 4.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKvrldnekeGFPITAIREIKILRQLVHQSVVNMkeivtdkqdaLDFKKDK 802
Cdd:PHA03211   171 FAIHRALTPGSEGCVFESSHPDYPQRVVVKA--------GWYASSVHEARLLRRLSHPAVLAL----------LDVRVVG 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 GAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN----------------- 865
Cdd:PHA03211   233 GLTCLVLPKYRSDLYTYLGARLRPLGLAQVTAVARQLLSAIDYIHGEGIIHRDIKTENVLVNGpediclgdfgaacfarg 312
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  866 --SRPYTNKVI-TLWYRPPELLLGEErYTPAIDVWSCGCIlgelftkkpIFQANLELAQLELISR 927
Cdd:PHA03211   313 swSTPFHYGIAgTVDTNAPEVLAGDP-YTPSVDIWSAGLV---------IFEAAVHTASLFSASR 367
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
721-917 4.33e-09

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 60.41  E-value: 4.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVrldNEKEgfpITAIREIKILRQLVHQSVVNMKEIVTDKQDALdfkK 800
Cdd:cd05623     72 EDFEILKVIGRGAFGEVAVVKLKNADKVFAMKIL---NKWE---MLKRAETACFREERDVLVNGDSQWITTLHYAF---Q 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DKGAFYLVFEY-MDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN--------------- 864
Cdd:cd05623    143 DDNNLYLVMDYyVGGDLLTLLSKFEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDmnghirladfgsclk 222
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  865 ----NSRPYTNKVITLWYRPPELLL----GEERYTPAIDVWSCG-CILGELFTKKPIFQANL 917
Cdd:cd05623    223 lmedGTVQSSVAVGTPDYISPEILQamedGKGKYGPECDWWSLGvCMYEMLYGETPFYAESL 284
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
723-992 5.43e-09

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 58.81  E-value: 5.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIR---EIKILRQL--VHQSVVNMkeivtdkqdaLD 797
Cdd:cd14102      2 YQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGTLNGVMvplEIVLLKKVgsGFRGVIKL----------LD 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 FKKDKGAFYLVFEYMD--HDLMGLL-ESGLVhfSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN---------- 864
Cdd:cd14102     72 WYERPDGFLIVMERPEpvKDLFDFItEKGAL--DEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDlrtgelklid 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 -------NSRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQleliSRLCgspcpavw 937
Cdd:cd14102    150 fgsgallKDTVYTDFDGTRVYSPPEWIRYHRYHGRSATVWSLGVLLYDMVCGDIPFEQDEEILR----GRLY-------- 217
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  938 pdviklpyfntmkpkkqYRRRLREEFSfipsaalDLLDHMLTLDPSKRCTAEQTL 992
Cdd:cd14102    218 -----------------FRRRVSPECQ-------QLIKWCLSLRPSDRPTLEQIF 248
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
722-911 6.16e-09

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


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 59.06  E-value: 6.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPItaIREIKILRQLV-HQSVVNMKEIVTDKQDALDFKK 800
Cdd:cd14036      1 KLRIKRVIAEGGFAFVYEAQDVGTGKEYALKRLLSNEEEKNKAI--IQEINFMKKLSgHPNIVQFCSAASIGKEESDQGQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DKgaFYLVFEYMDHDLMGLLES--GLVHFSEDHIKSFMKQLMEGLDYCHKKN--FLHRDIKCSNILLNN----------- 865
Cdd:cd14036     79 AE--YLLLTELCKGQLVDFVKKveAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNqgqiklcdfgs 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  866 --SRPYT-----------------NKVITLWYRPPELLLGEERY--TPAIDVWSCGCILGEL-FTKKP 911
Cdd:cd14036    157 atTEAHYpdyswsaqkrslvedeiTRNTTPMYRTPEMIDLYSNYpiGEKQDIWALGCILYLLcFRKHP 224
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
725-997 6.29e-09

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


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 58.50  E-value: 6.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  725 IIGIIGEGTYGQVYKAKDKDTGELVALK---KVRLDNEKEGFpitAIREIKILRQLVHQSVVNMKEIVtdkqdaldfkKD 801
Cdd:cd14075      6 IRGELGSGNFSQVKLGIHQLTKEKVAIKildKTKLDQKTQRL---LSREISSMEKLHHPNIIRLYEVV----------ET 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 KGAFYLVFEYMDH-DLMGLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSR----------PYT 870
Cdd:cd14075     73 LSKLHLVMEYASGgELYTKISTE-GKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNcvkvgdfgfsTHA 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  871 NKVITL-------WYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQAnlelaqlelisrlcgspcpavwPDVIKL 943
Cdd:cd14075    152 KRGETLntfcgspPYAAPELFKDEHYIGIYVDIWALGVLLYFMVTGVMPFRA----------------------ETVAKL 209
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  944 pyfntmkpKKqyrRRLREEF---SFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14075    210 --------KK---CILEGTYtipSYVSEPCQELIRGILQPVPSDRYSIDEIKNSEWL 255
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
728-920 6.33e-09

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


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 59.28  E-value: 6.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVRlDNEKegfpitAIREIKIlrqlvHQSVVNMKEIVTDKQDALDFKKDKGAFYL 807
Cdd:cd14170      9 VLGLGINGKVLQIFNKRTQEKFALKMLQ-DCPK------ARREVEL-----HWRASQCPHIVRIVDVYENLYAGRKCLLI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYMDH-DLMGLLES-GLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYT--------------- 870
Cdd:cd14170     77 VMECLDGgELFSRIQDrGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAilkltdfgfaketts 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  871 -NKVITLWYRP----PElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELA 920
Cdd:cd14170    157 hNSLTTPCYTPyyvaPE-VLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLA 210
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
723-992 6.95e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 59.50  E-value: 6.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKvrldnekeGFPITAIREIKILRQLVHQSVVNMKEIVTDKqdaldfkkdk 802
Cdd:PHA03209    68 YTVIKTLTPGSEGRVFVATKPGQPDPVVLKI--------GQKGTTLIEAMLLQNVNHPSVIRMKDTLVSG---------- 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 GAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN-----------------N 865
Cdd:PHA03209   130 AITCMVLPHYSSDLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINdvdqvcigdlgaaqfpvV 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 SRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFT-KKPIFQA----------NLELAQLELISRL------ 928
Cdd:PHA03209   210 APAFLGLAGTVETNAPE-VLARDKYNSKADIWSAGIVLFEMLAyPSTIFEDppstpeeyvkSCHSHLLKIISTLkvhpee 288
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  929 -CGSPCPAVWPDVIKlpYFNTM-KPKKQYRRRLREEfsfIPSAALDLLDHMLTLDPSKRCTAEQTL 992
Cdd:PHA03209   289 fPRDPGSRLVRGFIE--YASLErQPYTRYPCFQRVN---LPIDGEFLVHKMLTFDAAMRPSAEEIL 349
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
720-864 7.94e-09

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 59.30  E-value: 7.94e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  720 VDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIR-EIKILRQLVHQSVVNMKEIVTDKQDaldf 798
Cdd:cd05627      1 LDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRaERDILVEADGAWVVKMFYSFQDKRN---- 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  799 kkdkgaFYLVFEYM-DHDLMGLLESGLVhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN 864
Cdd:cd05627     77 ------LYLIMEFLpGGDMMTLLMKKDT-LSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLD 136
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
722-868 9.50e-09

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


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 58.72  E-value: 9.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLdNEKEGFPItAIREIKILR--QLVHQSVVNMKEIVTdKQDALDFK 799
Cdd:cd13977      1 KYSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRC-NAPENVEL-ALREFWALSsiQRQHPNVIQLEECVL-QRDGLAQR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 KDKG-------------------------AFYLVFeYMDHDLMGLLESGLVHFSEDHI--KSFMKQLMEGLDYCHKKNFL 852
Cdd:cd13977     78 MSHGssksdlylllvetslkgercfdprsACYLWF-VMEFCDGGDMNEYLLSRRPDRQtnTSFMLQLSSALAFLHRNQIV 156
                          170
                   ....*....|....*.
gi 1907082950  853 HRDIKCSNILLNNSRP 868
Cdd:cd13977    157 HRDLKPDNILISHKRG 172
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
728-1011 1.06e-08

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 58.22  E-value: 1.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALK---KVRLdNEKEGfPITAIREiKILRQLVHQS-----VVNMkeivtdkqdALDFK 799
Cdd:cd05606      1 IIGRGGFGEVYGCRKADTGKMYAMKcldKKRI-KMKQG-ETLALNE-RIMLSLVSTGgdcpfIVCM---------TYAFQ 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 K-DKGAFYLvfeymdhDLM--GLLESGLVH---FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS------- 866
Cdd:cd05606     69 TpDKLCFIL-------DLMngGDLHYHLSQhgvFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHghvrisd 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 ----------RPYTNkVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELisrlcgspcpav 936
Cdd:cd05606    142 lglacdfskkKPHAS-VGTHGYMAPEVLQKGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKDKHEI------------ 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  937 wpDVIKLpyfnTMKPKkqyrrrLREEFSfipSAALDLLDHMLTLDPSKR--C---TAEQTLQSDFLKDVE-----LSKMA 1006
Cdd:cd05606    209 --DRMTL----TMNVE------LPDSFS---PELKSLLEGLLQRDVSKRlgClgrGATEVKEHPFFKGVDwqqvyLQKYP 273

                   ....*
gi 1907082950 1007 PPDLP 1011
Cdd:cd05606    274 PPLIP 278
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
727-943 1.19e-08

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: 57.67  E-value: 1.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  727 GIIGEGTYGQVYKA--KDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVtdkqdaldfkkDKGA 804
Cdd:cd05116      1 GELGSGNFGTVKKGyyQMKKVVKTVAVKILKNEANDPALKDELLREANVMQQLDNPYIVRMIGIC-----------EAES 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  805 FYLVFEYMDhdlMGLLESGLV---HFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL------------------ 863
Cdd:cd05116     70 WMLVMEMAE---LGPLNKFLQknrHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLvtqhyakisdfglskalr 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  864 NNSRPY----TNKVITLWYRPPelLLGEERYTPAIDVWSCGCILGELFT--KKPI--FQANLELAQLELISRL-CGSPCP 934
Cdd:cd05116    147 ADENYYkaqtHGKWPVKWYAPE--CMNYYKFSSKSDVWSFGVLMWEAFSygQKPYkgMKGNEVTQMIEKGERMeCPAGCP 224

                   ....*....
gi 1907082950  935 AVWPDVIKL 943
Cdd:cd05116    225 PEMYDLMKL 233
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
728-909 1.26e-08

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: 57.93  E-value: 1.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKA--KDKDTGEL-VALKKVRLDN----EKEGFpitaIREIKILRQLVHQSVVNMKEIVTDKQDALDFKK 800
Cdd:cd05035      6 ILGEGEFGSVMEAqlKQDDGSQLkVAVKTMKVDIhtysEIEEF----LSEAACMKDFDHPNVMRLIGVCFTASDLNKPPS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DkgafYLVFEYMDH-DLMGLL-----ESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSrpYTNKVI 874
Cdd:cd05035     82 P----MVILPFMKHgDLHSYLlysrlGGLPEKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDEN--MTVCVA 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  875 TL----------WYR-------PPELL----LGEERYTPAIDVWSCGCILGELFTK 909
Cdd:cd05035    156 DFglsrkiysgdYYRqgriskmPVKWIalesLADNVYTSKSDVWSFGVTMWEIATR 211
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
722-863 1.40e-08

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


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 57.65  E-value: 1.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPItairEIKILRQLvhQSVVNMKEIVtdkqdalDFKKD 801
Cdd:cd14017      1 RWKVVKKIGGGGFGEIYKVRDVVDGEEVAMKVESKSQPKQVLKM----EVAVLKKL--QGKPHFCRLI-------GCGRT 67
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  802 KGAFYLVFEYMDHDLMGLLES-GLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL 863
Cdd:cd14017     68 ERYNYIVMTLLGPNLAELRRSqPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAI 130
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
721-911 1.44e-08

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


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 58.14  E-value: 1.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRL-----DNEKEGFPITAIREIKILRQLVHQSVVNMKEIvtdkqda 795
Cdd:cd14040      6 ERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLnkswrDEKKENYHKHACREYRIHKELDHPRIVKLYDY------- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  796 ldFKKDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCH--KKNFLHRDIKCSNILLNNSRPYTNKV 873
Cdd:cd14040     79 --FSLDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGTACGEIK 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  874 I---------------------------TLWYRPPE-LLLGEE--RYTPAIDVWSCGCILGE-LFTKKP 911
Cdd:cd14040    157 ItdfglskimdddsygvdgmdltsqgagTYWYLPPEcFVVGKEppKISNKVDVWSVGVIFFQcLYGRKP 225
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
729-908 1.47e-08

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: 57.58  E-value: 1.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGElVALKKVRLDNEKEGfpiTAIREIKILRQLVHQSVVNMKEIVTDKQdaldfkkdkgAFYLV 808
Cdd:cd05113     12 LGTGQFGVVKYGKWRGQYD-VAIKMIKEGSMSED---EFIEEAKVMMNLSHEKLVQLYGVCTKQR----------PIFII 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDHD-LMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-----------SR-----PYTN 871
Cdd:cd05113     78 TEYMANGcLLNYLREMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDqgvvkvsdfglSRyvlddEYTS 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1907082950  872 KVITLW---YRPPELLLgEERYTPAIDVWSCGCILGELFT 908
Cdd:cd05113    158 SVGSKFpvrWSPPEVLM-YSKFSSKSDVWAFGVLMWEVYS 196
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
722-903 1.80e-08

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: 57.32  E-value: 1.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIgiIGEGTYGQVYKAKDKDTGELVA---LKKVRLDN-EKEGFPitaiREIKILRQLVHQSVVNM----KEIVtdkq 793
Cdd:cd14033      4 KFNIE--IGRGSFKTVYRGLDTETTVEVAwceLQTRKLSKgERQRFS----EEVEMLKGLQHPNIVRFydswKSTV---- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  794 daldfkKDKGAFYLVFEYMDHdlmGLLESGLVHFSEDHIKSFMK---QLMEGLDYCHKKN--FLHRDIKCSNILLN---- 864
Cdd:cd14033     74 ------RGHKCIILVTELMTS---GTLKTYLKRFREMKLKLLQRwsrQILKGLHFLHSRCppILHRDLKCDNIFITgptg 144
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  865 ------------NSRPYTNKVI-TLWYRPPELLlgEERYTPAIDVWSCG-CIL 903
Cdd:cd14033    145 svkigdlglatlKRASFAKSVIgTPEFMAPEMY--EEKYDEAVDVYAFGmCIL 195
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
721-908 1.89e-08

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: 57.36  E-value: 1.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGElVALKKVRLDNEK-EGFpitaIREIKILRQLVHQSVVNMKEIVTDKQdaldfk 799
Cdd:cd05072      7 ESIKLVKKLGAGQFGEVWMGYYNNSTK-VAVKTLKPGTMSvQAF----LEEANLMKTLQHDKLVRLYAVVTKEE------ 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 kdkgAFYLVFEYMDH----DLMGLLESGLVHFSEdhIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS--------- 866
Cdd:cd05072     76 ----PIYIITEYMAKgsllDFLKSDEGGKVLLPK--LIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESlmckiadfg 149
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  867 -------RPYT----NKVITLWYRPPELLLGEerYTPAIDVWSCGCILGELFT 908
Cdd:cd05072    150 larviedNEYTaregAKFPIKWTAPEAINFGS--FTIKSDVWSFGILLYEIVT 200
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
729-908 2.06e-08

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: 57.07  E-value: 2.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGElVALKKVRLDN-EKEGFpitaIREIKILRQLVHQSVVNMKEIVTDKqdaldfkkdkGAFYL 807
Cdd:cd05059     12 LGSGQFGVVHLGKWRGKID-VAIKMIKEGSmSEDDF----IEEAKVMMKLSHPKLVQLYGVCTKQ----------RPIFI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYMDHD-LMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-----------SR-----PYT 870
Cdd:cd05059     77 VTEYMANGcLLNYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEqnvvkvsdfglARyvlddEYT 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1907082950  871 NKVITLW---YRPPELLLgEERYTPAIDVWSCGCILGELFT 908
Cdd:cd05059    157 SSVGTKFpvkWSPPEVFM-YSKFSSKSDVWSFGVLMWEVFS 196
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
720-915 2.56e-08

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


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 57.77  E-value: 2.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  720 VDKFDIIGIIGEGTYGQVYKAKDKDTGELVALK---KVRLDNEKEgfpiTAI----REIkilrqLVHqsvVNMKEIVtdk 792
Cdd:cd05596     25 AEDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKllsKFEMIKRSD----SAFfweeRDI-----MAH---ANSEWIV--- 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  793 QDALDFKKDKgAFYLVFEYM-DHDLMGLLESglVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS----- 866
Cdd:cd05596     90 QLHYAFQDDK-YLYMVMDYMpGGDLVNLMSN--YDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASghlkl 166
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  867 ---------------RPYTnKVITLWYRPPELLLGEER---YTPAIDVWSCGCILGELFTKKPIFQA 915
Cdd:cd05596    167 adfgtcmkmdkdglvRSDT-AVGTPDYISPEVLKSQGGdgvYGRECDWWSVGVFLYEMLVGDTPFYA 232
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
729-903 2.88e-08

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


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 56.88  E-value: 2.88e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALK---KVRL--------------------DNEKEGFPITAI-REIKILRQLVHQSVVN 784
Cdd:cd14200      8 IGKGSYGVVKLAYNESDDKYYAMKvlsKKKLlkqygfprrppprgskaaqgEQAKPLAPLERVyQEIAILKKLDHVNIVK 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  785 MKEIVTD-KQDALdfkkdkgafYLVFEymdhdlmgLLESGLVH-------FSEDHIKSFMKQLMEGLDYCHKKNFLHRDI 856
Cdd:cd14200     88 LIEVLDDpAEDNL---------YMVFD--------LLRKGPVMevpsdkpFSEDQARLYFRDIVLGIEYLHYQKIVHRDI 150
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  857 KCSNILL------------------NNSRPYTNKVITLWYRPPELLL--GEERYTPAIDVWSCGCIL 903
Cdd:cd14200    151 KPSNLLLgddghvkiadfgvsnqfeGNDALLSSTAGTPAFMAPETLSdsGQSFSGKALDVWAMGVTL 217
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
729-934 2.91e-08

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: 56.97  E-value: 2.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAK------DKDTgELVALKKVR--LDNEKEGFPitaiREIKILRQLVHQSVVNMKEIVTDKQDALdfkk 800
Cdd:cd05093     13 LGEGAFGKVFLAEcynlcpEQDK-ILVAVKTLKdaSDNARKDFH----REAELLTNLQHEHIVKFYGVCVEGDPLI---- 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 dkgafyLVFEYMDH-DLMGLLES------------GLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS- 866
Cdd:cd05093     84 ------MVFEYMKHgDLNKFLRAhgpdavlmaegnRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENl 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 -------------------RPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFT--KKPIFQ-ANLELAQLEL 924
Cdd:cd05093    158 lvkigdfgmsrdvystdyyRVGGHTMLPIRWMPPESIM-YRKFTTESDVWSLGVVLWEIFTygKQPWYQlSNNEVIECIT 236
                          250
                   ....*....|..
gi 1907082950  925 ISRLCGSP--CP 934
Cdd:cd05093    237 QGRVLQRPrtCP 248
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
729-911 4.07e-08

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: 56.22  E-value: 4.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEgfpitairEIKILRQLVhqsvvnmkeIVTDKQDALDFKKDKGAF--- 805
Cdd:cd06642     12 IGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAED--------EIEDIQQEI---------TVLSQCDSPYITRYYGSYlkg 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  806 ---YLVFEYMDH-DLMGLLESGlvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN----------------- 864
Cdd:cd06642     75 tklWIIMEYLGGgSALDLLKPG--PLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSeqgdvkladfgvagqlt 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1907082950  865 NSRPYTNKVI-TLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKP 911
Cdd:cd06642    153 DTQIKRNTFVgTPFWMAPE-VIKQSAYDFKADIWSLGITAIELAKGEP 199
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
721-992 5.02e-08

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


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 55.60  E-value: 5.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDII-GIIGEGTYGQVYKAKDKDTGELVALKKVRLDNekegfpiTAIREIKILRQLVHQSVVNMKEIVTDKQDALdfk 799
Cdd:cd14109      3 ELYEIGeEDEKRAAQGAPFHVTERSTGRNFLAQLRYGDP-------FLMREVDIHNSLDHPNIVQMHDAYDDEKLAV--- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 kdkgafyLVFEYMDHDLMGLLESGLV---HFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS---------- 866
Cdd:cd14109     73 -------TVIDNLASTIELVRDNLLPgkdYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDDklkladfgqs 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 -RPYTNKVITLWYRPPELLLGE----ERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLElisrlcgspcpavwpdvi 941
Cdd:cd14109    146 rRLLRGKLTTLIYGSPEFVSPEivnsYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLT------------------ 207
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  942 klpyfNTMKPKKQYRrrlREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTL 992
Cdd:cd14109    208 -----NVRSGKWSFD---SSPLGNISDDARDFIKKLLVYIPESRLTVDEAL 250
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
729-941 5.59e-08

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: 55.90  E-value: 5.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGElVALKKVRLDNEKEGFPITaiREIKILRQLVHQSVVNMKEIVTDKQdaldfkkdkgAFYLV 808
Cdd:cd05148     14 LGSGYFGEVWEGLWKNRVR-VAIKILKSDDLLKQQDFQ--KEVQALKRLRHKHLISLFAVCSVGE----------PVYII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDH-DLMGLLES--GLVHFSEdHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSrpYTNKV------------ 873
Cdd:cd05148     81 TELMEKgSLLAFLRSpeGQVLPVA-SLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGED--LVCKVadfglarliked 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  874 --------ITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPI-FQANLELAQLELISRLCGSPCPAVWPDVI 941
Cdd:cd05148    158 vylssdkkIPYKWTAPE-AASHGTFSTKSDVWSFGILLYEMFTYGQVpYPGMNNHEVYDQITAGYRMPCPAKCPQEI 233
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
723-999 5.89e-08

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 56.27  E-value: 5.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGfpiTAIREIKILRQLVHQSVVNMKEIVTDKQDALDFKKDk 802
Cdd:cd06637      8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEE---EIKQEINMLKKYSHHRNIATYYGAFIKKNPPGMDDQ- 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 gaFYLVFEYMDH----DLMGLLESGLVhfSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYT-------- 870
Cdd:cd06637     84 --LWLVMEFCGAgsvtDLIKNTKGNTL--KEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKlvdfgvsa 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  871 ---------NKVI-TLWYRPPELLLGEER----YTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRlcgSPCPAV 936
Cdd:cd06637    160 qldrtvgrrNTFIgTPYWMAPEVIACDENpdatYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRALFLIPR---NPAPRL 236
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  937 wpdviklpyfntmkPKKQYRRRLReefSFIPSAaldlldhmLTLDPSKRCTAEQTLQSDFLKD 999
Cdd:cd06637    237 --------------KSKKWSKKFQ---SFIESC--------LVKNHSQRPSTEQLMKHPFIRD 274
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
728-908 6.41e-08

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: 55.26  E-value: 6.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDkdTGELVALKKVRLDNEKEGFpitaIREIKILRQLVHQSVVNMKEIVTdkqdaldfkkdKGAFYL 807
Cdd:cd05083     13 IIGEGEFGAVLQGEY--MGQKVAVKNIKCDVTAQAF----LEETAVMTKLQHKNLVRLLGVIL-----------HNGLYI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYMDH-DLMGLLES-GLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN---------------NSRPYT 870
Cdd:cd05083     76 VMELMSKgNLVNFLRSrGRALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSedgvakisdfglakvGSMGVD 155
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1907082950  871 NKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFT 908
Cdd:cd05083    156 NSRLPVKWTAPE-ALKNKKFSSKSDVWSYGVLLWEVFS 192
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
732-865 6.93e-08

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: 55.58  E-value: 6.93e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  732 GTYGQVYKAKDKDTGeLVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKqdaldfkkdkGAFYLVFEY 811
Cdd:cd14027      4 GGFGKVSLCFHRTQG-LVVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEE----------GKYSLVMEY 72
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  812 MDH-DLMGLLESGLVHFSedhIKS-FMKQLMEGLDYCHKKNFLHRDIKCSNILLNN 865
Cdd:cd14027     73 MEKgNLMHVLKKVSVPLS---VKGrIILEIIEGMAYLHGKGVIHKDLKPENILVDN 125
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
723-1000 8.04e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 56.16  E-value: 8.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKvrldNEKEGfpitAIREIKILRQLVHQSVVNMKEIVT-DKQDALDFKKD 801
Cdd:PHA03212    94 FSILETFTPGAEGFAFACIDNKTCEHVVIKA----GQRGG----TATEAHILRAINHPSIIQLKGTFTyNKFTCLILPRY 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 KGAFYLVFEymDHDLMGLLEsglvhfsedhIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN----------------- 864
Cdd:PHA03212   166 KTDLYCYLA--AKRNIAICD----------ILAIERSVLRAIQYLHENRIIHRDIKAENIFINhpgdvclgdfgaacfpv 233
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 --NSRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFT-KKPIFQAN------LELAQLELISRLCGSPcPA 935
Cdd:PHA03212   234 diNANKYYGWAGTIATNAPE-LLARDPYGPAVDIWSAGIVLFEMATcHDSLFEKDgldgdcDSDRQIKLIIRRSGTH-PN 311
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  936 VWP----DVIKLPYFNTMK--PKKQYRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLKDV 1000
Cdd:PHA03212   312 EFPidaqANLDEIYIGLAKksSRKPGSRPLWTNLYELPIDLEYLICKMLAFDAHHRPSAEALLDFAAFQDI 382
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
728-985 9.21e-08

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


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 55.09  E-value: 9.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVY---KAKDKDTGELVA---LKKVRLDNEKEGFPIT--------AIREIKILRQLvHQSvvnmkeivtdkq 793
Cdd:cd05583      1 VLGTGAYGKVFlvrKVGGHDAGKLYAmkvLKKATIVQKAKTAEHTmterqvleAVRQSPFLVTL-HYA------------ 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  794 daldFKKDkGAFYLVFEYMDHdlmGLLESGLV---HFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN----- 865
Cdd:cd05583     68 ----FQTD-AKLHLILDYVNG---GELFTHLYqreHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSeghvv 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 ------SRPYTNKVI--------TLWYRPPELLLGEER-YTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRlcg 930
Cdd:cd05583    140 ltdfglSKEFLPGENdraysfcgTIEYMAPEVVRGGSDgHDKAVDWWSLGVLTYELLTGASPFTVDGERNSQSEISK--- 216
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  931 spcpavwpdviKLPYFNTMKPKkqyrrrlreEFSfipSAALDLLDHMLTLDPSKR 985
Cdd:cd05583    217 -----------RILKSHPPIPK---------TFS---AEAKDFILKLLEKDPKKR 248
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
729-908 1.01e-07

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: 54.71  E-value: 1.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTgelVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQDALDFKKDKGA-FYL 807
Cdd:cd14062      1 IGSGSFGTVYKGRWHGD---VAVKKLNVTDPTPSQLQAFKNEVAVLRKTRHVNILLFMGYMTKPQLAIVTQWCEGSsLYK 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYMDhdlmgllesglVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSrpYTNK--------VITLW-- 877
Cdd:cd14062     78 HLHVLE-----------TKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHED--LTVKigdfglatVKTRWsg 144
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907082950  878 ------------YRPPEL--LLGEERYTPAIDVWSCGCILGELFT 908
Cdd:cd14062    145 sqqfeqptgsilWMAPEVirMQDENPYSFQSDVYAFGIVLYELLT 189
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
720-1011 1.02e-07

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


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 55.66  E-value: 1.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  720 VDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRldnekegfpitaiREIKILRQLVHQsvvnmkeiVTDKQDALDFK 799
Cdd:cd05610      3 IEEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVK-------------KADMINKNMVHQ--------VQAERDALALS 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 KDK------------GAFYLVFEYM-DHDLMGLLESgLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS 866
Cdd:cd05610     62 KSPfivhlyyslqsaNNVYLVMEYLiGGDVKSLLHI-YGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNE 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 --------------------------------------------------------RPY-TNKVI--------------T 875
Cdd:cd05610    141 ghikltdfglskvtlnrelnmmdilttpsmakpkndysrtpgqvlslisslgfntpTPYrTPKSVrrgaarvegerilgT 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  876 LWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFqaNLELAQlELISRLCGSPCPavWPDViklpyfntmkpkkqy 955
Cdd:cd05610    221 PDYLAPELLLGKP-HGPAVDWWALGVCLFEFLTGIPPF--NDETPQ-QVFQNILNRDIP--WPEG--------------- 279
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  956 rrrlREEFSFIPSAALDLLdhmLTLDPSKRCTAEQTLQSDFLKDVE---LSKMAPPDLP 1011
Cdd:cd05610    280 ----EEELSVNAQNAIEIL---LTMDPTKRAGLKELKQHPLFHGVDwenLQNQTMPFIP 331
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
728-976 1.50e-07

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 54.50  E-value: 1.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVRLDnekegfpITAIREIKILRQLvhqsvvnmkEIVTdKQDALDFKKDKGAFY- 806
Cdd:cd06619      8 ILGHGNGGTVYKAYHLLTRRILAVKVIPLD-------ITVELQKQIMSEL---------EILY-KCDSPYIIGFYGAFFv 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 -----LVFEYMDHDLMGLLESglvhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-----------SRPYT 870
Cdd:cd06619     71 enrisICTEFMDGGSLDVYRK----IPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTrgqvklcdfgvSTQLV 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  871 NKVITLW-----YRPPELLLGEErYTPAIDVWSCGCILGEL----FTKKPIFQANLELAQLELISRLCGSPCPaVWPDVI 941
Cdd:cd06619    147 NSIAKTYvgtnaYMAPERISGEQ-YGIHSDVWSLGISFMELalgrFPYPQIQKNQGSLMPLQLLQCIVDEDPP-VLPVGQ 224
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1907082950  942 ---KLPYFNTMKPKKQYRRRLREEfsfipsaalDLLDH 976
Cdd:cd06619    225 fseKFVHFITQCMRKQPKERPAPE---------NLMDH 253
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
728-915 1.66e-07

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


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 55.10  E-value: 1.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAK---DKDTGELVALKKVR----LDNEKEGFPITAIReiKILRQLVHQSVVNMKeivtdkqdaLDFKK 800
Cdd:cd05584      3 VLGKGGYGKVFQVRkttGSDKGKIFAMKVLKkasiVRNQKDTAHTKAER--NILEAVKHPFIVDLH---------YAFQT 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DkGAFYLVFEYMDH-DLMGLLE-SGLvhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS------------ 866
Cdd:cd05584     72 G-GKLYLILEYLSGgELFMHLErEGI--FMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQghvkltdfglck 148
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  867 -RPYTNKVI-----TLWYRPPELLL--GEERytpAIDVWSCGCILGELFTKKPIFQA 915
Cdd:cd05584    149 eSIHDGTVThtfcgTIEYMAPEILTrsGHGK---AVDWWSLGALMYDMLTGAPPFTA 202
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
721-908 1.86e-07

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: 54.35  E-value: 1.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGEL------VALKKVRLD-NEKEgfPITAIREIKILRQL-VHQSVVNMKEIVTDK 792
Cdd:cd05053     12 DRLTLGKPLGEGAFGQVVKAEAVGLDNKpnevvtVAVKMLKDDaTEKD--LSDLVSEMEMMKMIgKHKNIINLLGACTQD 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  793 qdaldfkkdkGAFYLVFEYMDH-DLMGLLES----------GLVHFSED-----HIKSFMKQLMEGLDYCHKKNFLHRDI 856
Cdd:cd05053     90 ----------GPLYVVVEYASKgNLREFLRArrppgeeaspDDPRVPEEqltqkDLVSFAYQVARGMEYLASKKCIHRDL 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  857 KCSNILLNNS--------------------RPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFT 908
Cdd:cd05053    160 AARNVLVTEDnvmkiadfglardihhidyyRKTTNGRLPVKWMAPEALF-DRVYTHQSDVWSFGVLLWEIFT 230
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
728-1019 1.86e-07

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


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 54.63  E-value: 1.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALK---KVRLDNEKEGFPITAIREIkILRQLVHQSVVNMKeivtdkqdaLDFK-KDKg 803
Cdd:cd05575      2 VIGKGSFGKVLLARHKAEGKLYAVKvlqKKAILKRNEVKHIMAERNV-LLKNVKHPFLVGLH---------YSFQtKDK- 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  804 aFYLVFEYMDHdlmGLLESGLV---HFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN---------------- 864
Cdd:cd05575     71 -LYFVLDYVNG---GELFFHLQrerHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDsqghvvltdfglckeg 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 -NSRPYTNKVI-TLWYRPPELLLGEErYTPAIDVWSCGCILGELftkkpifqanlelaqlelisrLCGspcpavwpdvik 942
Cdd:cd05575    147 iEPSDTTSTFCgTPEYLAPEVLRKQP-YDRTVDWWCLGAVLYEM---------------------LYG------------ 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  943 LPYFNTMKPKKQYRRRLREEFSF---IPSAALDLLDHMLTLDPSKRCTAeqtlQSDFL-------------KDVELSKMA 1006
Cdd:cd05575    193 LPPFYSRDTAEMYDNILHKPLRLrtnVSPSARDLLEGLLQKDRTKRLGS----GNDFLeiknhsffrpinwDDLEAKKIP 268
                          330
                   ....*....|...
gi 1907082950 1007 PPDLPHWQDCHEL 1019
Cdd:cd05575    269 PPFNPNVSGPLDL 281
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
727-910 1.95e-07

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: 54.29  E-value: 1.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  727 GIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKegfpitaiREIKILRQLVHqsvVNMK-----EIVtdKQDALDFKKd 801
Cdd:cd06616     12 GEIGRGAFGTVNKMLHKPSGTIMAVKRIRSTVDE--------KEQKRLLMDLD---VVMRssdcpYIV--KFYGALFRE- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 kGAFYLVFEYMDHDL----MGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKK-NFLHRDIKCSNILLN------------ 864
Cdd:cd06616     78 -GDCWICMELMDISLdkfyKYVYEVLDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDrngniklcdfgi 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  865 -----NSRPYTNKVITLWYRPPELLLGE---ERYTPAIDVWSCGCILGELFTKK 910
Cdd:cd06616    157 sgqlvDSIAKTRDAGCRPYMAPERIDPSasrDGYDVRSDVWSLGITLYEVATGK 210
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
721-865 1.95e-07

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 55.05  E-value: 1.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIR-EIKILRQLVHQSVVNMKEIVTDKQDaldfk 799
Cdd:cd05628      1 EDFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRaERDILVEADSLWVVKMFYSFQDKLN----- 75
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  800 kdkgaFYLVFEYM-DHDLMGLLESGLVhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN 865
Cdd:cd05628     76 -----LYLIMEFLpGGDMMTLLMKKDT-LTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDS 136
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
721-1004 1.98e-07

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


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 54.25  E-value: 1.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVrlDNEKEgfpiTAIREIKIL-RQLVHQSVVNMKEIVtdkqdaldfk 799
Cdd:cd14178      3 DGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKII--DKSKR----DPSEEIEILlRYGQHPNIITLKDVY---------- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 kDKGAF-YLVFEYMdhdlMG--LLESGLVH--FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS-------- 866
Cdd:cd14178     67 -DDGKFvYLVMELM----RGgeLLDRILRQkcFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDEsgnpesir 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 ----------RPYTNKVITLWYR----PPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLcGSP 932
Cdd:cd14178    142 icdfgfakqlRAENGLLMTPCYTanfvAPE-VLKRQGYDAACDIWSLGILLYTMLAGFTPFANGPDDTPEEILARI-GSG 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  933 CPAV----WPDviklpyfntmkpkkqyrrrlreefsfIPSAALDLLDHMLTLDPSKRCTAEQTLQ------SDFLKDVEL 1002
Cdd:cd14178    220 KYALsggnWDS--------------------------ISDAAKDIVSKMLHVDPHQRLTAPQVLRhpwivnREYLSQNQL 273

                   ..
gi 1907082950 1003 SK 1004
Cdd:cd14178    274 SR 275
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
717-1049 2.36e-07

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 54.65  E-value: 2.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  717 KRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRldnekegfpitaiREIKILRQLVHQSVVNMKEIVTDKQDAL 796
Cdd:cd05594     21 KVTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILK-------------KEVIVAKDEVAHTLTENRVLQNSRHPFL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  797 DFKK------DKGAFylVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCH-KKNFLHRDIKCSNILLNN---- 865
Cdd:cd05594     88 TALKysfqthDRLCF--VMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKdghi 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 ------------SRPYTNKVI--TLWYRPPElLLGEERYTPAIDVWSCGCILGELftkkpifqanlelaqlelisrLCGs 931
Cdd:cd05594    166 kitdfglckegiKDGATMKTFcgTPEYLAPE-VLEDNDYGRAVDWWGLGVVMYEM---------------------MCG- 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  932 pcpavwpdviKLPYFNtMKPKKQYRRRLREEFSF---IPSAALDLLDHMLTLDPSKRC-----TAEQTLQSDFL-----K 998
Cdd:cd05594    223 ----------RLPFYN-QDHEKLFELILMEEIRFprtLSPEAKSLLSGLLKKDPKQRLgggpdDAKEIMQHKFFagivwQ 291
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  999 DVELSKMAPPDLPhwQDCHELWSKKRRRQRQSGIVIEDPPPSKASRKETTS 1049
Cdd:cd05594    292 DVYEKKLVPPFKP--QVTSETDTRYFDEEFTAQMITITPPDQDDSMETVDN 340
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
728-913 2.72e-07

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


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 54.20  E-value: 2.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALK---KVRLDNEKEGFPITAIREIkILRQLVHQSVVNMKeivtdkqdaLDFKKDKgA 804
Cdd:cd05603      2 VIGKGSFGKVLLAKRKCDGKFYAVKvlqKKTILKKKEQNHIMAERNV-LLKNLKHPFLVGLH---------YSFQTSE-K 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  805 FYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNnsrpYTNKVI---------- 874
Cdd:cd05603     71 LYFVLDYVNGGELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLD----CQGHVVltdfglckeg 146
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  875 ------------TLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIF 913
Cdd:cd05603    147 mepeettstfcgTPEYLAPE-VLRKEPYDRTVDWWCLGAVLYEMLYGLPPF 196
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
728-911 2.75e-07

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: 53.72  E-value: 2.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGE---LVALKKVR---LDNEKEGFpitaIREIKILRQLVHQSVVNMKEIVTDKQDALdfkkd 801
Cdd:cd05065     11 VIGAGEFGEVCRGRLKLPGKreiFVAIKTLKsgyTEKQRRDF----LSEASIMGQFDHPNIIHLEGVVTKSRPVM----- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 kgafyLVFEYMDHdlmGLLESGLV----HFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN------------ 865
Cdd:cd05065     82 -----IITEFMEN---GALDSFLRqndgQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSnlvckvsdfgls 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 -------SRP-YTN----KVITLWYRPPELLLgeERYTPAIDVWSCGCILGEL--FTKKP 911
Cdd:cd05065    154 rfleddtSDPtYTSslggKIPIRWTAPEAIAY--RKFTSASDVWSYGIVMWEVmsYGERP 211
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
728-1012 3.08e-07

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 54.20  E-value: 3.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALK----KVRLdNEKEGFPITAIREIkILRQLVHQSVVNMKEI--VTDKqdaldfkkd 801
Cdd:cd05604      3 VIGKGSFGKVLLAKRKRDGKYYAVKvlqkKVIL-NRKEQKHIMAERNV-LLKNVKHPFLVGLHYSfqTTDK--------- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 kgaFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN----------------- 864
Cdd:cd05604     72 ---LYFVLDFVNGGELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDsqghivltdfglckegi 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 -NSRPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQaNLELAQLelisrlcgspcpavWPDVIKL 943
Cdd:cd05604    149 sNSDTTTTFCGTPEYLAPEVIR-KQPYDNTVDWWCLGSVLYEMLYGLPPFY-CRDTAEM--------------YENILHK 212
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  944 PYfnTMKPKkqyrrrlreefsfIPSAALDLLDHMLTLDPSKRCTAEQTLQS----DFLK-----DVELSKMAPPDLPH 1012
Cdd:cd05604    213 PL--VLRPG-------------ISLTAWSILEELLEKDRQLRLGAKEDFLEiknhPFFEsinwtDLVQKKIPPPFNPN 275
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
729-941 3.08e-07

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: 53.86  E-value: 3.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKA--------KDKDTGELVALKKVRLDNEKEgfpitAIREIKILRQLVHQSVVNMKEIVTDKQDALdfkk 800
Cdd:cd05094     13 LGEGAFGKVFLAecynlsptKDKMLVAVKTLKDPTLAARKD-----FQREAELLTNLQHDHIVKFYGVCGDGDPLI---- 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 dkgafyLVFEYMDH------------DLMGLLE------SGLVHFSED-HIKSfmkQLMEGLDYCHKKNFLHRDIKCSNI 861
Cdd:cd05094     84 ------MVFEYMKHgdlnkflrahgpDAMILVDgqprqaKGELGLSQMlHIAT---QIASGMVYLASQHFVHRDLATRNC 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  862 LLNNS--------------------RPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFT--KKPIFQ-ANLE 918
Cdd:cd05094    155 LVGANllvkigdfgmsrdvystdyyRVGGHTMLPIRWMPPESIM-YRKFTTESDVWSFGVILWEIFTygKQPWFQlSNTE 233
                          250       260
                   ....*....|....*....|....*
gi 1907082950  919 LAQLELISRLCGSP--CPAVWPDVI 941
Cdd:cd05094    234 VIECITQGRVLERPrvCPKEVYDIM 258
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
721-866 3.13e-07

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


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 54.17  E-value: 3.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALK---KVRLDNEKEGFPITAirEIKILRQLVHQSVVNM-KEIVTDKQdal 796
Cdd:cd05574      1 DHFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKvldKEEMIKRNKVKRVLT--EREILATLDHPFLPTLyASFQTSTH--- 75
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  797 dfkkdkgaFYLVFEY-MDHDLMGLLESGLVH-FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS 866
Cdd:cd05574     76 --------LCFVMDYcPGGELFRLLQKQPGKrLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHES 139
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
729-906 3.39e-07

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: 53.41  E-value: 3.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKK-VRLDNEKEGfpiTAIREIKILRQLVHQSVVNMKEIVTdkqdaldfkKDKgAFYL 807
Cdd:cd14222      1 LGKGFFGQAIKVTHKATGKVMVMKElIRCDEETQK---TFLTEVKVMRSLDHPNVLKFIGVLY---------KDK-RLNL 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNIL--LNNS------------------- 866
Cdd:cd14222     68 LTEFIEGGTLKDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLikLDKTvvvadfglsrliveekkkp 147
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  867 ---RPYTNK--------------VITLWYRPPELLLGeERYTPAIDVWSCGCILGEL 906
Cdd:cd14222    148 ppdKPTTKKrtlrkndrkkrytvVGNPYWMAPEMLNG-KSYDEKVDIFSFGIVLCEI 203
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
721-1010 3.42e-07

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


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 54.26  E-value: 3.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVrlDNEKEgfpiTAIREIKIL-RQLVHQSVVNMKEIVTDKQdaldfk 799
Cdd:cd14176     19 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKII--DKSKR----DPTEEIEILlRYGQHPNIITLKDVYDDGK------ 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 kdkgAFYLVFEYMDHDlmGLLESGLVH--FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL--NNSRPYTNKVI- 874
Cdd:cd14176     87 ----YVYVVTELMKGG--ELLDKILRQkfFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdESGNPESIRICd 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  875 -------------------TLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPa 935
Cdd:cd14176    161 fgfakqlraengllmtpcyTANFVAPE-VLERQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFS- 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  936 vwpdvIKLPYFNTmkpkkqyrrrlreefsfIPSAALDLLDHMLTLDPSKRCTAEQTLQ------SDFLKDVELSKMAPPD 1009
Cdd:cd14176    239 -----LSGGYWNS-----------------VSDTAKDLVSKMLHVDPHQRLTAALVLRhpwivhWDQLPQYQLNRQDAPH 296

                   .
gi 1907082950 1010 L 1010
Cdd:cd14176    297 L 297
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
729-941 3.61e-07

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: 53.12  E-value: 3.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKA--KDKDTGEL-VA---LKKVRLDNEKEGFpitaIREIKILRQLVHQSVVNMKEIVTDKQdaldfkkdk 802
Cdd:cd05060      3 LGHGNFGSVRKGvyLMKSGKEVeVAvktLKQEHEKAGKKEF----LREASVMAQLDHPCIVRLIGVCKGEP--------- 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 gaFYLVFEYMDhdlMGLLESGLV---HFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-----------SRP 868
Cdd:cd05060     70 --LMLVMELAP---LGPLLKYLKkrrEIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNrhqakisdfgmSRA 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  869 -------YT----NKVITLWYRPPELLLGeeRYTPAIDVWSCGCILGELFT--KKPI--FQANLELAQLELISRLcgsPC 933
Cdd:cd05060    145 lgagsdyYRattaGRWPLKWYAPECINYG--KFSSKSDVWSYGVTLWEAFSygAKPYgeMKGPEVIAMLESGERL---PR 219

                   ....*...
gi 1907082950  934 PAVWPDVI 941
Cdd:cd05060    220 PEECPQEI 227
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
729-908 3.86e-07

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: 53.44  E-value: 3.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGE--------------LVALKKVRLD---NEKEGFpitaIREIKILRQLVHQSVVNMKEIVTd 791
Cdd:cd05097     13 LGEGQFGEVHLCEAEGLAEflgegapefdgqpvLVAVKMLRADvtkTARNDF----LKEIKIMSRLKNPNIIRLLGVCV- 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  792 KQDALdfkkdkgafYLVFEYMDH-DLMGLL-----ESGLVH------FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCS 859
Cdd:cd05097     88 SDDPL---------CMITEYMENgDLNQFLsqreiESTFTHannipsVSIANLLYMAVQIASGMKYLASLNFVHRDLATR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  860 NILLNNSrpYTNKVITL-----------------------WYRPPELLLGeeRYTPAIDVWSCGCILGELFT 908
Cdd:cd05097    159 NCLVGNH--YTIKIADFgmsrnlysgdyyriqgravlpirWMAWESILLG--KFTTASDVWAFGVTLWEMFT 226
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
724-908 3.96e-07

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: 53.12  E-value: 3.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  724 DIIGIIGEGTYGQVYKAKDKdtGElVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVV-----NMKE----IVTDkqd 794
Cdd:cd14063      3 EIKEVIGKGRFGRVHRGRWH--GD-VAIKLLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVlfmgaCMDPphlaIVTS--- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  795 aldFKKDKGAFYLVFEYMDHdlmgllesglvhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRpytnKVI 874
Cdd:cd14063     77 ---LCKGRTLYSLIHERKEK------------FDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLENGR----VVI 137
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  875 T--------------------------LWYRPPELL---------LGEERYTPAIDVWSCGCILGELFT 908
Cdd:cd14063    138 TdfglfslsgllqpgrredtlvipngwLCYLAPEIIralspdldfEESLPFTKASDVYAFGTVWYELLA 206
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
729-939 6.05e-07

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: 52.79  E-value: 6.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGElVALKKVRLDN-EKEGFpitaIREIKILRQLVHQSVVNMKEIVTDKQdaldfkkdkgAFYL 807
Cdd:cd05068     16 LGSGQFGEVWEGLWNNTTP-VAVKTLKPGTmDPEDF----LREAQIMKKLRHPKLIQLYAVCTLEE----------PIYI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYMDHdlmgllESGLVHFSEDHIKSFMKQLME-------GLDYCHKKNFLHRDIKCSNILLNNSR------------- 867
Cdd:cd05068     81 ITELMKH------GSLLEYLQGKGRSLQLPQLIDmaaqvasGMAYLESQNYIHRDLAARNVLVGENNickvadfglarvi 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  868 ----PYTNKVITL----WYRPPELLLgeERYTPAIDVWSCGCILGELFTKKPIFQANLELAQ-LELISRLCGSPCPAVWP 938
Cdd:cd05068    155 kvedEYEAREGAKfpikWTAPEAANY--NRFSIKSDVWSFGILLTEIVTYGRIPYPGMTNAEvLQQVERGYRMPCPPNCP 232

                   .
gi 1907082950  939 D 939
Cdd:cd05068    233 P 233
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
729-911 6.89e-07

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: 52.52  E-value: 6.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFpitaIREIKILRQLVHQSVVNMKEIVTdkqdaldfkKDkGAFYLV 808
Cdd:cd14156      1 IGSGFFSKVYKVTHGATGKVMVVKIYKNDVDQHKI----VREISLLQKLSHPNIVRYLGICV---------KD-EKLHPI 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDHD-LMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNIL------------------------- 862
Cdd:cd14156     67 LEYVSGGcLEELLAREELPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLirvtprgreavvtdfglarevgemp 146
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1907082950  863 LNNSRPYTNKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKP 911
Cdd:cd14156    147 ANDPERKLSLVGSAFWMAPEMLRGEP-YDRKVDVFSFGIVLCEILARIP 194
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
728-908 6.93e-07

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: 52.87  E-value: 6.93e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAK-----DKDTGELVALK----KVRLDnEKEGFpitaIREIKILRQL-VHQSVVNMKEIVTDKqdald 797
Cdd:cd05055     42 TLGAGAFGKVVEATayglsKSDAVMKVAVKmlkpTAHSS-EREAL----MSELKIMSHLgNHENIVNLLGACTIG----- 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 fkkdkGAFYLVFEYMDH-DLMGLLESGLVHFSE-DHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSR-------- 867
Cdd:cd05055    112 -----GPILVITEYCCYgDLLNFLRRKRESFLTlEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKivkicdfg 186
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  868 ---------PYTNKVITL----WYRPPELLlgEERYTPAIDVWSCGCILGELFT 908
Cdd:cd05055    187 lardimndsNYVVKGNARlpvkWMAPESIF--NCVYTFESDVWSYGILLWEIFS 238
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
728-908 7.78e-07

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: 52.35  E-value: 7.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTG-----ELVALKKVRLDNEKEGFPitaiREIKILRQL-VHQSVVNMkeivtdkqdaLDFKKD 801
Cdd:cd05047      2 VIGEGNFGQVLKARIKKDGlrmdaAIKRMKEYASKDDHRDFA----GELEVLCKLgHHPNIINL----------LGACEH 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 KGAFYLVFEYMDH-DLMGLLESGLV---------------HFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN 865
Cdd:cd05047     68 RGYLYLAIEYAPHgNLLDFLRKSRVletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGE 147
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  866 -----------SRPYTNKVITLWYRPPELLLGEER-----YTPAIDVWSCGCILGELFT 908
Cdd:cd05047    148 nyvakiadfglSRGQEVYVKKTMGRLPVRWMAIESlnysvYTTNSDVWSYGVLLWEIVS 206
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
729-908 8.90e-07

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: 52.30  E-value: 8.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVY--------KAKDKD--------TGELVALKKVRLD---NEKEGFpitaIREIKILRQLVHQSVVNMKEI- 788
Cdd:cd05095     13 LGEGQFGEVHlceaegmeKFMDKDfalevsenQPVLVAVKMLRADankNARNDF----LKEIKIMSRLKDPNIIRLLAVc 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  789 VTDkqDALdfkkdkgafYLVFEYMDH-DLMGLL-----ESGLVHFSEDHIKSFMK------QLMEGLDYCHKKNFLHRDI 856
Cdd:cd05095     89 ITD--DPL---------CMITEYMENgDLNQFLsrqqpEGQLALPSNALTVSYSDlrfmaaQIASGMKYLSSLNFVHRDL 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  857 KCSNILLnnSRPYTNKVITL-----------------------WYRPPELLLGeeRYTPAIDVWSCGCILGELFT 908
Cdd:cd05095    158 ATRNCLV--GKNYTIKIADFgmsrnlysgdyyriqgravlpirWMSWESILLG--KFTTASDVWAFGVTLWETLT 228
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
720-914 1.12e-06

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


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 52.37  E-value: 1.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  720 VDKFDIIGIIGEGTYGQVYKAKDKDTGELVALK---KVRLdNEKEGfpitairEIKILRQLVHQSVVNMKEIvtdkqdal 796
Cdd:cd05633      4 MNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldKKRI-KMKQG-------ETLALNERIMLSLVSTGDC-------- 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  797 dfkkdkgAFYLVFEYMDHD------LMGLLESGLVH--------FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNIL 862
Cdd:cd05633     68 -------PFIVCMTYAFHTpdklcfILDLMNGGDLHyhlsqhgvFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANIL 140
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  863 LN-----------------NSRPYTNkVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQ 914
Cdd:cd05633    141 LDehghvrisdlglacdfsKKKPHAS-VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFR 208
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
721-999 1.18e-06

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


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 51.92  E-value: 1.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRlDNEKEGFPITAIREIKILRQLVHQSVVnmkeIVTDKQDALDfkk 800
Cdd:cd14183      6 ERYKVGRTIGDGNFAVVKECVERSTGREYALKIIN-KSKCRGKEHMIQNEVSILRRVKHPNIV----LLIEEMDMPT--- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 dkgAFYLVFEYMDH-DLMGLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSR------------ 867
Cdd:cd14183     78 ---ELYLVMELVKGgDLFDAITST-NKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQdgskslklgdfg 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  868 -------PYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSpcpAVWPdv 940
Cdd:cd14183    154 latvvdgPLYTVCGTPTYVAPE-IIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQEVLFDQILMGQ---VDFP-- 227
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  941 ikLPYFNTmkpkkqyrrrlreefsfIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLKD 999
Cdd:cd14183    228 --SPYWDN-----------------VSDSAKELITMMLQVDVDQRYSALQVLEHPWVND 267
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
728-915 1.25e-06

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


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 52.02  E-value: 1.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVY---KAKDKDTGELVALK-------KVRlDNEKEGFpitairEIKILRQLVHQSVVNMKeivtdkqdaLD 797
Cdd:cd05582      2 VLGQGSFGKVFlvrKITGPDAGTLYAMKvlkkatlKVR-DRVRTKM------ERDILADVNHPFIVKLH---------YA 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 FKKDkGAFYLVFEYM-DHDLMGLLeSGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN----------- 865
Cdd:cd05582     66 FQTE-GKLYLILDFLrGGDLFTRL-SKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEdghikltdfgl 143
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  866 SRPYTNKVI-------TLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQA 915
Cdd:cd05582    144 SKESIDHEKkaysfcgTVEYMAPE-VVNRRGHTQSADWWSFGVLMFEMLTGSLPFQG 199
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
721-908 1.30e-06

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: 51.57  E-value: 1.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYK--AKDKDTGEL---VALKKVRlDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQDA 795
Cdd:cd05032      6 EKITLIRELGQGSFGMVYEglAKGVVKGEPetrVAIKTVN-ENASMRERIEFLNEASVMKEFNCHHVVRLLGVVSTGQPT 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  796 LdfkkdkgafyLVFEYMDH-DLMGLLESglvHFSEDHIKSFMK------------QLMEGLDYCHKKNFLHRDIKCSNIL 862
Cdd:cd05032     85 L----------VVMELMAKgDLKSYLRS---RRPEAENNPGLGpptlqkfiqmaaEIADGMAYLAAKKFVHRDLAARNCM 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  863 LNNSRpyTNKV----------ITLWYRP------------PELLLgEERYTPAIDVWSCGCILGELFT 908
Cdd:cd05032    152 VAEDL--TVKIgdfgmtrdiyETDYYRKggkgllpvrwmaPESLK-DGVFTTKSDVWSFGVVLWEMAT 216
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
730-961 1.58e-06

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: 51.11  E-value: 1.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  730 GEGTYGQVYKAKDKDTGELVALKKVrLDNEKEGfpitaireiKILRQLVHQSVVNMKEIVTDKQDaldfkkdkgaFYLVF 809
Cdd:cd14060      2 GGGSFGSVYRAIWVSQDKEVAVKKL-LKIEKEA---------EILSVLSHRNIIQFYGAILEAPN----------YGIVT 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  810 EYMD----HDLMGLLESGLVHFseDHIKSFMKQLMEGLDYCHKK---NFLHRDIKCSNILLNN-----------SRPYTN 871
Cdd:cd14060     62 EYASygslFDYLNSNESEEMDM--DQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAAdgvlkicdfgaSRFHSH 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  872 KVI-----TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQA--NLELAQL--ELISRLC-GSPCPAVWPDVI 941
Cdd:cd14060    140 TTHmslvgTFPWMAPEVIQSLP-VSETCDTYSYGVVLWEMLTREVPFKGleGLQVAWLvvEKNERPTiPSSCPRSFAELM 218
                          250       260
                   ....*....|....*....|
gi 1907082950  942 KLPYFNTMKPKKQYRRRLRE 961
Cdd:cd14060    219 RRCWEADVKERPSFKQIIGI 238
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
728-927 2.00e-06

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 51.44  E-value: 2.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKV---RLdnEKEGFPITAIREIKILRQLVHQSVVNMkeivtdkqdALDFKKdKGA 804
Cdd:cd05607      9 VLGKGGFGEVCAVQVKNTGQMYACKKLdkkRL--KKKSGEKMALLEKEILEKVNSPFIVSL---------AYAFET-KTH 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  805 FYLVFEYMDH-DL-MGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS---------------- 866
Cdd:cd05607     77 LCLVMSLMNGgDLkYHIYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNgncrlsdlglavevke 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  867 -RPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISR 927
Cdd:cd05607    157 gKPITQRAGTNGYMAPEILK-EESYSYPVDWFAMGCSIYEMVAGRTPFRDHKEKVSKEELKR 217
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
729-938 2.28e-06

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: 51.17  E-value: 2.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAK----DKDTGELVALKKVRLDNEKEGFPiTAIREIKILRQLVHQSVVNMKEIVTDKQDALdfkkdkga 804
Cdd:cd05090     13 LGECAFGKIYKGHlylpGMDHAQLVAIKTLKDYNNPQQWN-EFQQEASLMTELHHPNIVCLLGVVTQEQPVC-------- 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  805 fyLVFEYMDH-DLMGLL--------------ESGLVHFSEDHiKSFMK---QLMEGLDYCHKKNFLHRDIKCSNILLNNS 866
Cdd:cd05090     84 --MLFEFMNQgDLHEFLimrsphsdvgcssdEDGTVKSSLDH-GDFLHiaiQIAAGMEYLSSHFFVHKDLAARNILVGEQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 --------------------RPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTK--KPIFQ-ANLELaqLE 923
Cdd:cd05090    161 lhvkisdlglsreiyssdyyRVQNKSLLPIRWMPPEAIM-YGKFSSDSDIWSFGVVLWEIFSFglQPYYGfSNQEV--IE 237
                          250
                   ....*....|....*
gi 1907082950  924 LISRLCGSPCPAVWP 938
Cdd:cd05090    238 MVRKRQLLPCSEDCP 252
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
721-984 2.42e-06

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: 51.21  E-value: 2.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDnEKEGFPITAIREIKILRQLVHQSVVNMKeivtdkqdaldfkk 800
Cdd:cd06650      5 DDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLE-IKPAIRNQIIRELQVLHECNSPYIVGFY-------------- 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 dkGAFY------LVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKN-FLHRDIKCSNILLNNS------- 866
Cdd:cd06650     70 --GAFYsdgeisICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKHkIMHRDVKPSNILVNSRgeiklcd 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 --------RPYTNKVI-TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKK-PIFQANLElaQLELISRLCGSPCPAV 936
Cdd:cd06650    148 fgvsgqliDSMANSFVgTRSYMSPERLQGTH-YSVQSDIWSMGLSLVEMAVGRyPIPPPDAK--ELELMFGCQVEGDAAE 224
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1907082950  937 WPDVIKLPyfntMKPKKQYRRRLREefsfiPSAALDLLDHMLTLDPSK 984
Cdd:cd06650    225 TPPRPRTP----GRPLSSYGMDSRP-----PMAIFELLDYIVNEPPPK 263
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
728-939 2.45e-06

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: 50.81  E-value: 2.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDkdTGELVALKKVRLD-NEKEGFPITAIR-EIKILRQLVHQSVVNMKEIVTDKQDaldfkkdkgaF 805
Cdd:cd14145     13 IIGIGGFGKVYRAIW--IGDEVAVKAARHDpDEDISQTIENVRqEAKLFAMLKHPNIIALRGVCLKEPN----------L 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  806 YLVFEYMDHDLMGLLESGlVHFSEDHIKSFMKQLMEGLDYCHKKNF---LHRDIKCSNILL---NNSRPYTNKVITL--- 876
Cdd:cd14145     81 CLVMEFARGGPLNRVLSG-KRIPPDILVNWAVQIARGMNYLHCEAIvpvIHRDLKSSNILIlekVENGDLSNKILKItdf 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  877 -----WYR-------------PPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQA--NLELAQLELISRLcGSPCPAV 936
Cdd:cd14145    160 glareWHRttkmsaagtyawmAPEVIRS-SMFSKGSDVWSYGVLLWELLTGEVPFRGidGLAVAYGVAMNKL-SLPIPST 237

                   ...
gi 1907082950  937 WPD 939
Cdd:cd14145    238 CPE 240
STKc_SRPK2 cd14217
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs ...
722-914 2.59e-06

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK2 mediates neuronal cell cycle and cell death through regulation of nuclear cyclin D1. It has also been found to promote leukemia cell proliferation by regulating cyclin A1. SRPK2 also plays a role in regulating pre-mRNA splicing and is required for spliceosomal B complex formation. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271119 [Multi-domain]  Cd Length: 366  Bit Score: 51.57  E-value: 2.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRldnEKEGFPITAIREIKILRQLVHQSVVN-MKEIVTDKQDALDFKK 800
Cdd:cd14217     13 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVK---SAQHYTETALDEIKLLRCVRESDPEDpNKDMVVQLIDDFKISG 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DKGAFY-LVFEYMDHDLMG-LLESGLVHFSEDHIKSFMKQLMEGLDYCHKK-NFLHRDIKCSNIL--------------- 862
Cdd:cd14217     90 MNGIHVcMVFEVLGHHLLKwIIKSNYQGLPIRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILmcvddayvrrmaaea 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  863 -----------------------------------------LNNS----RPYTNKVITLWYRPPELLLGEERYTPAiDVW 897
Cdd:cd14217    170 tewqkagapppsgsavstapdllvnpldprnadkirvkiadLGNAcwvhKHFTEDIQTRQYRSIEVLIGAGYSTPA-DIW 248
                          250
                   ....*....|....*..
gi 1907082950  898 SCGCILGELFTKKPIFQ 914
Cdd:cd14217    249 STACMAFELATGDYLFE 265
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
721-1003 2.62e-06

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: 50.90  E-value: 2.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDnEKEGFPITAIREIKILRQlvhqsvVNMKEIVtdkqdalDFKk 800
Cdd:cd06615      1 DDFEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHLE-IKPAIRNQIIRELKVLHE------CNSPYIV-------GFY- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 dkGAFY------LVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKK-NFLHRDIKCSNILLNnSR------ 867
Cdd:cd06615     66 --GAFYsdgeisICMEHMDGGSLDQVLKKAGRIPENILGKISIAVLRGLTYLREKhKIMHRDVKPSNILVN-SRgeiklc 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  868 ----------PYTNK-VITLWYRPPELLLGEeRYTPAIDVWSCGCILGELFTKK-PIFQAN-LELAQL------ELISRL 928
Cdd:cd06615    143 dfgvsgqlidSMANSfVGTRSYMSPERLQGT-HYTVQSDIWSLGLSLVEMAIGRyPIPPPDaKELEAMfgrpvsEGEAKE 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  929 CGSPCPAVWPDVIK-------LPYFNTMKPKKQYRRRLREEFsfipsaaLDLLDHMLTLDPSKRCTAEQTLQSDFLKDVE 1001
Cdd:cd06615    222 SHRPVSGHPPDSPRpmaifelLDYIVNEPPPKLPSGAFSDEF-------QDFVDKCLKKNPKERADLKELTKHPFIKRAE 294

                   ..
gi 1907082950 1002 LS 1003
Cdd:cd06615    295 LE 296
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
729-908 2.65e-06

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: 50.79  E-value: 2.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAK-DKDTgelvalkKVRLDNEKEG-FPITA-IREIKILRQLVHQSVVNMKEIVTdkqdaldfkkdKGAF 805
Cdd:cd05073     19 LGAGQFGEVWMATyNKHT-------KVAVKTMKPGsMSVEAfLAEANVMKTLQHDKLVKLHAVVT-----------KEPI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  806 YLVFEYMDH----DLMGLLESGLVHFSEdhIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN----------------N 865
Cdd:cd05073     81 YIITEFMAKgsllDFLKSDEGSKQPLPK--LIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSaslvckiadfglarviE 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1907082950  866 SRPYT----NKVITLWYRPPELLLGEerYTPAIDVWSCGCILGELFT 908
Cdd:cd05073    159 DNEYTaregAKFPIKWTAPEAINFGS--FTIKSDVWSFGILLMEIVT 203
COG2112 COG2112
Predicted Ser/Thr protein kinase [Signal transduction mechanisms];
726-869 2.83e-06

Predicted Ser/Thr protein kinase [Signal transduction mechanisms];


Pssm-ID: 441715 [Multi-domain]  Cd Length: 225  Bit Score: 50.02  E-value: 2.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  726 IGIIGEGTYGQVYKAKDKdtGELVALKKVRLDNEKEgfpiTAIREIKILRQLvhqsvvNMKEI---VtdkqdaLDFKKDk 802
Cdd:COG2112     45 LRLLGKGYRGVVFLGKLG--GKKVALKIRRTDSPRP----SLKKEAEILKKA------NGAGVgpkL------YDYGRD- 105
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 gafYLVFEYMDhdlmGL-LESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCS--NILLNNSRPY 869
Cdd:COG2112    106 ---FLVMEYIE----GEpLKDWLENLDKEELRKVIRELLEAAYLLDRIGIDHGELSRPgkHVIVDKGRPY 168
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
729-997 2.83e-06

Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNT7 is a plant thylakoid-associated kinase that is essential in short- and long-term acclimation responses to cope with various light conditions in order to maintain photosynthetic redox poise for optimal photosynthetic performance. Short-term response involves state transitions over periods of minutes while the long-term response (LTR) occurs over hours to days and involves changing the relative amounts of photosystems I and II. SNT7 acts as a redox sensor and a signal transducer for both responses, which are triggered by the redox state of the plastoquinone (PQ) pool. It is positioned at the top of a phosphorylation cascade that induces state transitions by phosphorylating light-harvesting complex II (LHCII), and triggers the LTR through the phosphorylation of chloroplast proteins. The SNT7 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 50.90  E-value: 2.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKA--KDKDTGEL---VALKKVRLDNEKEgfpitaIREIKILRQLVHQSVVnmkEIVTDKQDALDFKKDKG 803
Cdd:cd14013      3 LGEGGFGTVYKGslLQKDPGGEkrrVVLKKAKEYGEVE------IWMNERVRRACPSSCA---EFVGAFLDTTSKKFTKP 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  804 AFYLVFEYM-DHDLMGLLESGLVHFSEDH-------------------IKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL 863
Cdd:cd14013     74 SLWLVWKYEgDATLADLMQGKEFPYNLEPiifgrvlipprgpkrenviIKSIMRQILVALRKLHSTGIVHRDVKPQNIIV 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  864 NNsRPYTNKVITLW----------YRPPELLLgEERYTPA---------------------------------IDVWSCG 900
Cdd:cd14013    154 SE-GDGQFKIIDLGaaadlriginYIPKEFLL-DPRYAPPeqyimstqtpsappapvaaalspvlwqmnlpdrFDMYSAG 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  901 CIL-----GELFTKKPIFQANLELAQLELisrlcgspcpavwpdviKLPYFNTMKPKKQyRRRLREEFSFI---PSAALD 972
Cdd:cd14013    232 VILlqmafPNLRSDSNLIAFNRQLKQCDY-----------------DLNAWRMLVEPRA-SADLREGFEILdldDGAGWD 293
                          330       340
                   ....*....|....*....|....*
gi 1907082950  973 LLDHMLTLDPSKRCTAEQTLQSDFL 997
Cdd:cd14013    294 LVTKLIRYKPRGRLSASAALAHPYF 318
STKc_CK1_alpha cd14128
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze ...
722-873 3.16e-06

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. CK1alpha plays a role in cell cycle progression, spindle dynamics, and chromosome segregation. It is also involved in regulating apoptosis mediated by Fas or the retinoid X receptor (RXR), and is a positive regulator of Wnt signaling. CK1alpha phosphorylates the NS5A protein of flaviviruses such as the Hepatitis C virus (HCV) and yellow fever virus (YFV), and influences flaviviral replication. The CK1 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: 271030 [Multi-domain]  Cd Length: 266  Bit Score: 50.58  E-value: 3.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVAlkkVRLDNEKEGFPiTAIREIKILRQLvhQSVVNMKEIVTdkqdaldFKKD 801
Cdd:cd14128      1 KYRLVRKIGSGSFGDIYLGINITNGEEVA---VKLESQKARHP-QLLYESKLYKIL--QGGVGIPHIRW-------YGQE 67
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  802 KGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRpYTNKV 873
Cdd:cd14128     68 KDYNVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMIGRIEYVHNKNFIHRDIKPDNFLMGIGR-HCNKL 138
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
729-993 3.38e-06

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


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 50.34  E-value: 3.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGfpiTAIREIKILRQLVHQSVVNMkeivtdkqdaLDFKKDKGAFYLV 808
Cdd:cd14115      1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKKKE---QAAHEAALLQHLQHPQYITL----------HDTYESPTSYILV 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDHDLmgLLESGLVH--FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTN-KVITL-------WY 878
Cdd:cd14115     68 LELMDDGR--LLDYLMNHdeLMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRvKLIDLedavqisGH 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  879 RPPELLLGEERY--------TP---AIDVWSCGCILGELFTKKPIFqanLELAQLELISRLCgsPCPAVWPDviklpyfn 947
Cdd:cd14115    146 RHVHHLLGNPEFaapeviqgTPvslATDIWSIGVLTYVMLSGVSPF---LDESKEETCINVC--RVDFSFPD-------- 212
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1907082950  948 tmkpkkqyrrrlrEEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd14115    213 -------------EYFGDVSQAARDFINVILQEDPRRRPTAATCLQ 245
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
728-909 3.52e-06

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: 50.40  E-value: 3.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDtgELVALKKVRLdNEKEGFpiTAIREIKILRQLVHQSVVNMkeIVTDKQDaldfKKDKGAFYL 807
Cdd:cd14053      2 IKARGRFGAVWKAQYLN--RLVAVKIFPL-QEKQSW--LTEREIYSLPGMKHENILQF--IGAEKHG----ESLEAEYWL 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYMDH-DLMGLLESGLVHFSE-DHIKSFMKQlmeGLDYCH----------KKNFLHRDIKCSNILLNN---------- 865
Cdd:cd14053     71 ITEFHERgSLCDYLKGNVISWNElCKIAESMAR---GLAYLHedipatngghKPSIAHRDFKSKNVLLKSdltaciadfg 147
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  866 -------SRPYTN---KVITLWYRPPELLLGEERYTP----AIDVWSCGCILGELFTK 909
Cdd:cd14053    148 lalkfepGKSCGDthgQVGTRRYMAPEVLEGAINFTRdaflRIDMYAMGLVLWELLSR 205
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
729-977 4.21e-06

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: 50.11  E-value: 4.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDN-EKEGFpitaIREIKILRQLVHQSVVNMKEIVTDKQdaldfkkdkgAFYL 807
Cdd:cd05052     14 LGGGQYGEVYEGVWKKYNLTVAVKTLKEDTmEVEEF----LKEAAVMKEIKHPNLVQLLGVCTREP----------PFYI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYMDHdlmGLLESGLVHFSEDHIKS----FMK-QLMEGLDYCHKKNFLHRDIKCSNILL--NN---------SRPYTN 871
Cdd:cd05052     80 ITEFMPY---GNLLDYLRECNREELNAvvllYMAtQIASAMEYLEKKNFIHRDLAARNCLVgeNHlvkvadfglSRLMTG 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  872 KVITL---------WYRPPEllLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQ----LELISRL-CGSPCPavw 937
Cdd:cd05052    157 DTYTAhagakfpikWTAPES--LAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQvyelLEKGYRMeRPEGCP--- 231
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1907082950  938 PDVIKLpyfntMKPKKQYRRRLREEFSFIPSAaldlLDHM 977
Cdd:cd05052    232 PKVYEL-----MRACWQWNPSDRPSFAEIHQA----LETM 262
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
728-908 4.78e-06

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: 49.86  E-value: 4.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGE---LVALKKVRL---DNEKEGFpitaIREIKILRQLVHQSVVNMKEIVTDKQDALdfkkd 801
Cdd:cd05066     11 VIGAGEFGEVCSGRLKLPGKreiPVAIKTLKAgytEKQRRDF----LSEASIMGQFDHPNIIHLEGVVTRSKPVM----- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 kgafyLVFEYMDHdlmGLLESGLV----HFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN-----------S 866
Cdd:cd05066     82 -----IVTEYMEN---GSLDAFLRkhdgQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSnlvckvsdfglS 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  867 R--------PYTN---KVITLWYRPPELLLgeERYTPAIDVWSCGCILGELFT 908
Cdd:cd05066    154 RvleddpeaAYTTrggKIPIRWTAPEAIAY--RKFTSASDVWSYGIVMWEVMS 204
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
729-908 5.13e-06

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: 50.03  E-value: 5.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAK----------------DKDTGELVALKKVRLD---NEKEGFpitaIREIKILRQLVHQSVVNMKEIV 789
Cdd:cd05051     13 LGEGQFGEVHLCEanglsdltsddfigndNKDEPVLVAVKMLRPDaskNAREDF----LKEVKIMSQLKDPNIVRLLGVC 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  790 TdkqdaldfkKDKGAFyLVFEYMDH-DLMGLLESglvHFSEDHIKSFMKQLM--------------EGLDYCHKKNFLHR 854
Cdd:cd05051     89 T---------RDEPLC-MIVEYMENgDLNQFLQK---HEAETQGASATNSKTlsygtllymatqiaSGMKYLESLNFVHR 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  855 DIKCSNILLNNSrpYTNKVITL----------WYR-------P------PELLLGeeRYTPAIDVWSCGCILGELFT 908
Cdd:cd05051    156 DLATRNCLVGPN--YTIKIADFgmsrnlysgdYYRiegravlPirwmawESILLG--KFTTKSDVWAFGVTLWEILT 228
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
729-918 5.44e-06

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: 49.80  E-value: 5.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKdKDTGELVALKKV---RLDNEKEGFPitaiREIKILRQLVHQSVVNMKEIVTDKQDALdfkkdkgaf 805
Cdd:cd14664      1 IGRGGAGTVYKGV-MPNGTLVAVKRLkgeGTQGGDHGFQ----AEIQTLGMIRHRNIVRLRGYCSNPTTNL--------- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  806 yLVFEYMDHDLMGllesGLVHFSEDHIKSF--------MKQLMEGLDYCHKK---NFLHRDIKCSNILLNN--------- 865
Cdd:cd14664     67 -LVYEYMPNGSLG----ELLHSRPESQPPLdwetrqriALGSARGLAYLHHDcspLIIHRDVKSNNILLDEefeahvadf 141
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082950  866 ----------SRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFT-KKPIFQANLE 918
Cdd:cd14664    142 glaklmddkdSHVMSSVAGSYGYIAPE-YAYTGKVSEKSDVYSYGVVLLELITgKRPFDEAFLD 204
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
728-911 6.03e-06

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: 49.54  E-value: 6.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGE---LVALKKVRL---DNEKEGFpitaIREIKILRQLVHQSVVNMKEIVTDKQDALdfkkd 801
Cdd:cd05064     12 ILGTGRFGELCRGCLKLPSKrelPVAIHTLRAgcsDKQRRGF----LAEALTLGQFDHSNIVRLEGVITRGNTMM----- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 kgafyLVFEYMDHD-LMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS--------RP---- 868
Cdd:cd05064     83 -----IVTEYMSNGaLDSFLRKHEGQLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLVNSDlvckisgfRRlqed 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  869 -----YTN---KVITLWYRPPELLLGeeRYTPAIDVWSCGCILGEL--FTKKP 911
Cdd:cd05064    158 kseaiYTTmsgKSPVLWAAPEAIQYH--HFSSASDVWSFGIVMWEVmsYGERP 208
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
728-909 6.22e-06

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: 49.39  E-value: 6.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAK--DKDTGEL-VALKKV-RLDN--EKEGFpitaIREIKILRQLVHQSVVNMKEIVTDKQdaldfkkd 801
Cdd:cd05058      2 VIGKGHFGCVYHGTliDSDGQKIhCAVKSLnRITDieEVEQF----LKEGIIMKDFSHPNVLSLLGICLPSE-------- 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 kGAFYLVFEYMDH-DLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSrpYTNKVITL---- 876
Cdd:cd05058     70 -GSPLVVLPYMKHgDLRNFIRSETHNPTVKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDES--FTVKVADFglar 146
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  877 ------WYRPPELL-------------LGEERYTPAIDVWSCGCILGELFTK 909
Cdd:cd05058    147 diydkeYYSVHNHTgaklpvkwmalesLQTQKFTTKSDVWSFGVLLWELMTR 198
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
723-864 6.31e-06

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


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 50.40  E-value: 6.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVR---LDNEKEGFPITAIREIkiLRQLVHQSVVNMKEIVTDKQDaldfk 799
Cdd:cd05626      3 FVKIKTLGIGAFGEVCLACKVDTHALYAMKTLRkkdVLNRNQVAHVKAERDI--LAEADNEWVVKLYYSFQDKDN----- 75
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  800 kdkgaFYLVFEYM-DHDLMGLLESGLVhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN 864
Cdd:cd05626     76 -----LYFVMDYIpGGDMMSLLIRMEV-FPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILID 135
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
729-908 7.09e-06

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: 49.26  E-value: 7.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAK-DKDTGEL--VALKKVRLDN-EKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQ----------- 793
Cdd:cd05040      3 LGDGSFGVVRRGEwTTPSGKViqVAVKCLKSDVlSQPNAMDDFLKEVNAMHSLDHPNLIRLYGVVLSSPlmmvtelaplg 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  794 DALDFKKDKGAFYLVfeymdhdlmglleSGLVHFSEdhiksfmkQLMEGLDYCHKKNFLHRDIKCSNILL---------- 863
Cdd:cd05040     83 SLLDRLRKDQGHFLI-------------STLCDYAV--------QIANGMAYLESKRFIHRDLAARNILLaskdkvkigd 141
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  864 --------NNSRPYT---NKVITLWYRPPELLlGEERYTPAIDVWSCGCILGELFT 908
Cdd:cd05040    142 fglmralpQNEDHYVmqeHRKVPFAWCAPESL-KTRKFSHASDVWMFGVTLWEMFT 196
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
723-914 8.62e-06

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


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 49.66  E-value: 8.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALK---KVRLdNEKEGfpitairEIKILRQLVHQSVVNMKEIvtdkqdaldfk 799
Cdd:cd14223      2 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldKKRI-KMKQG-------ETLALNERIMLSLVSTGDC----------- 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 kdkgAFYLVFEYMDHD------LMGLLESGLVH--------FSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN- 864
Cdd:cd14223     63 ----PFIVCMSYAFHTpdklsfILDLMNGGDLHyhlsqhgvFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDe 138
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  865 ----------------NSRPYTNkVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQ 914
Cdd:cd14223    139 fghvrisdlglacdfsKKKPHAS-VGTHGYMAPEVLQKGVAYDSSADWFSLGCMLFKLLRGHSPFR 203
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
728-909 9.38e-06

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: 49.36  E-value: 9.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKdtGELVALKKVRLDNEKEGFpitaiREIKILR--QLVHQSVVNMkeIVTDKQDALDFKKdkgaF 805
Cdd:cd13998      2 VIGKGRFGEVWKASLK--NEPVAVKIFSSRDKQSWF-----REKEIYRtpMLKHENILQF--IAADERDTALRTE----L 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  806 YLVFEYMDH------------------DLMGLLESGLVHFSEDHIKSFMkqlmegldycHKKNFLHRDIKCSNILLNNS- 866
Cdd:cd13998     69 WLVTAFHPNgsl*dylslhtidwvslcRLALSVARGLAHLHSEIPGCTQ----------GKPAIAHRDLKSKNILVKNDg 138
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 -------------RPYTNK--------VITLWYRPPELLLG------EERYTpAIDVWSCGCILGELFTK 909
Cdd:cd13998    139 tcciadfglavrlSPSTGEednanngqVGTKRYMAPEVLEGainlrdFESFK-RVDIYAMGLVLWEMASR 207
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
721-908 1.07e-05

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: 49.20  E-value: 1.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYK--AKDKDTGEL---VALKKVrldNEKEGFP--ITAIREIKILRQLVHQSVVNMKEIVTDKQ 793
Cdd:cd05061      6 EKITLLRELGQGSFGMVYEgnARDIIKGEAetrVAVKTV---NESASLRerIEFLNEASVMKGFTCHHVVRLLGVVSKGQ 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  794 DALdfkkdkgafyLVFEYMDH-DLMGLLESgLVHFSED-------HIKSFMK---QLMEGLDYCHKKNFLHRDIKCSNIL 862
Cdd:cd05061     83 PTL----------VVMELMAHgDLKSYLRS-LRPEAENnpgrpppTLQEMIQmaaEIADGMAYLNAKKFVHRDLAARNCM 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  863 LnnSRPYTNKV----------ITLWYR------------PPElLLGEERYTPAIDVWSCGCILGELFT 908
Cdd:cd05061    152 V--AHDFTVKIgdfgmtrdiyETDYYRkggkgllpvrwmAPE-SLKDGVFTTSSDMWSFGVVLWEITS 216
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
723-918 1.15e-05

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: 49.23  E-value: 1.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDnekegfpiTAIREIKILRQLVHQSVVNMKE---IVTDKQDALdfk 799
Cdd:cd05615     12 FNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKD--------VVIQDDDVECTMVEKRVLALQDkppFLTQLHSCF--- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  800 KDKGAFYLVFEYMDH-DLMGLLESgLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN-------------- 864
Cdd:cd05615     81 QTVDRLYFVMEYVNGgDLMYHIQQ-VGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDseghikiadfgmck 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  865 -------NSRPYTNkviTLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLE 918
Cdd:cd05615    160 ehmvegvTTRTFCG---TPDYIAPE-IIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDE 216
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
729-912 1.17e-05

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: 49.05  E-value: 1.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTgeLVALKKVRLDNE------KEGFpitaIREIKILRQLVHQSVVnmkeivtdkqDALDFKKDK 802
Cdd:cd14159      1 IGEGGFGCVYQAVMRNT--EYAVKRLKEDSEldwsvvKNSF----LTEVEKLSRFRHPNIV----------DLAGYSAQQ 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 GAFYLVFEYMDHdlmGLLESGLvHFSEDHIKSFMKQLME-------GLDYCH--KKNFLHRDIKCSNILLNN-------- 865
Cdd:cd14159     65 GNYCLIYVYLPN---GSLEDRL-HCQVSCPCLSWSQRLHvllgtarAIQYLHsdSPSLIHGDVKSSNILLDAalnpklgd 140
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  866 ----------SRPYTNKVI--------TLWYRPPElLLGEERYTPAIDVWSCGCILGELFT-KKPI 912
Cdd:cd14159    141 fglarfsrrpKQPGMSSTLartqtvrgTLAYLPEE-YVKTGTLSVEIDVYSFGVVLLELLTgRRAM 205
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
729-909 1.47e-05

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: 48.47  E-value: 1.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGEL--VALKKVRL----DNEKEGFpitaIREIKILRQLVHQSVVNMKEIVTDKQDALDFKkdk 802
Cdd:cd05075      8 LGEGEFGSVMEGQLNQDDSVlkVAVKTMKIaictRSEMEDF----LSEAVCMKEFDHPNVMRLIGVCLQNTESEGYP--- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 gAFYLVFEYMDH-DLMG-LLESGL----VHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTNKVITL 876
Cdd:cd05075     81 -SPVVILPFMKHgDLHSfLLYSRLgdcpVYLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGL 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  877 --------WYR-------PPELL----LGEERYTPAIDVWSCGCILGELFTK 909
Cdd:cd05075    160 skkiyngdYYRqgriskmPVKWIaiesLADRVYTTKSDVWSFGVTMWEIATR 211
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
729-900 1.51e-05

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: 48.38  E-value: 1.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGfpiTAIREIKILRQLVHQSVVNMK-EIVTDKQDALDFKKDKGAfyl 807
Cdd:cd14110     11 INRGRFSVVRQCEEKRSGQMLAAKIIPYKPEDKQ---LVLREYQVLRRLSHPRIAQLHsAYLSPRHLVLIEELCSGP--- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 vfeymdHDLMGLLESGLvhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNIL-----------LNNSRPYT------ 870
Cdd:cd14110     85 ------ELLYNLAERNS--YSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIiteknllkivdLGNAQPFNqgkvlm 156
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1907082950  871 --NKVITLWYRPPELLLGEErYTPAIDVWSCG 900
Cdd:cd14110    157 tdKKGDYVETMAPELLEGQG-AGPQTDIWAIG 187
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
729-906 1.59e-05

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: 48.24  E-value: 1.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFpitaIREIKILRQLVHQSVVNMKEIVTDKqdaldfkkdkGAFYLV 808
Cdd:cd14155      1 IGSGFFSEVYKVRHRTSGQVMALKMNTLSSNRANM----LREVQLMNRLSHPNILRFMGVCVHQ----------GQLHAL 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 FEYMDH-DLMGLLESGLVHFSEDHIKsFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS-RPYTNKVITL---------- 876
Cdd:cd14155     67 TEYINGgNLEQLLDSNEPLSWTVRVK-LALDIARGLSYLHSKGIFHRDLTSKNCLIKRDeNGYTAVVGDFglaekipdys 145
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1907082950  877 ------------WYRPPELLLGEErYTPAIDVWSCGCILGEL 906
Cdd:cd14155    146 dgkeklavvgspYWMAPEVLRGEP-YNEKADVFSYGIILCEI 186
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
728-908 1.59e-05

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: 48.46  E-value: 1.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGE-----LVALKKVRLDNEKEGFPitaiREIKILRQLVHQ-SVVNMkeivtdkqdaLDFKKD 801
Cdd:cd05089      9 VIGEGNFGQVIKAMIKKDGLkmnaaIKMLKEFASENDHRDFA----GELEVLCKLGHHpNIINL----------LGACEN 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  802 KGAFYLVFEYMDH-DLMGLLESGLV-----HFSEDH----------IKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN 865
Cdd:cd05089     75 RGYLYIAIEYAPYgNLLDFLRKSRVletdpAFAKEHgtastltsqqLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGE 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  866 -----------SRPYTNKVITLWYRPPELLLGEER-----YTPAIDVWSCGCILGELFT 908
Cdd:cd05089    155 nlvskiadfglSRGEEVYVKKTMGRLPVRWMAIESlnysvYTTKSDVWSFGVLLWEIVS 213
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
727-911 1.63e-05

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


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 48.08  E-value: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  727 GIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGfpitairEIKILRQLVHQSVVNMKeivtdkqdaldfkkdkGAfy 806
Cdd:cd13995     10 DFIPRGAFGKVYLAQDTKTKKRMACKLIPVEQFKPS-------DVEIQACFRHENIAELY----------------GA-- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  807 LVFEYMDHDLMGLLESGLV--------HFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRP---------- 868
Cdd:cd13995     65 LLWEETVHLFMEAGEGGSVleklescgPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAvlvdfglsvq 144
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907082950  869 -----YTNKVI--TLWYRPPELLLGEERYTPAiDVWSCGCILGELFTKKP 911
Cdd:cd13995    145 mtedvYVPKDLrgTEIYMSPEVILCRGHNTKA-DIYSLGATIIHMQTGSP 193
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
721-908 2.07e-05

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: 48.29  E-value: 2.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAK-------DKDTgeLVALKKVR----LDNEKEGFpitaiREIKILRQLVHQSVVNMKEIV 789
Cdd:cd05050      5 NNIEYVRDIGQGAFGRVFQARapgllpyEPFT--MVAVKMLKeeasADMQADFQ-----REAALMAEFDHPNIVKLLGVC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  790 TDKQdaldfkkdkgAFYLVFEYMDH-DLMGLL-------ESGLVH--------------FSEDHIKSFMKQLMEGLDYCH 847
Cdd:cd05050     78 AVGK----------PMCLLFEYMAYgDLNEFLrhrspraQCSLSHstssarkcglnplpLSCTEQLCIAKQVAAGMAYLS 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  848 KKNFLHRDIKCSNILLNNS--------------------RPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELF 907
Cdd:cd05050    148 ERKFVHRDLATRNCLVGENmvvkiadfglsrniysadyyKASENDAIPIRWMPPESIF-YNRYTTESDVWAYGVVLWEIF 226

                   .
gi 1907082950  908 T 908
Cdd:cd05050    227 S 227
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
723-1001 2.56e-05

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


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 47.79  E-value: 2.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNekegfpitaireiKILRQLVHQSVVnmkeivtdKQDALDFKKDK 802
Cdd:cd05609      2 FETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQN-------------LILRNQIQQVFV--------ERDILTFAENP 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 G--AFYLVFEYMDH--DLMGLLESG--------LVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN----- 865
Cdd:cd05609     61 FvvSMYCSFETKRHlcMVMEYVEGGdcatllknIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSmghik 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  866 --------------------------SRPYTNKVI--TLWYRPPELLLgEERYTPAIDVWSCGCILGE-LFTKKPIFQAN 916
Cdd:cd05609    141 ltdfglskiglmslttnlyeghiekdTREFLDKQVcgTPEYIAPEVIL-RQGYGKPVDWWAMGIILYEfLVGCVPFFGDT 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  917 LElaqlELISRLCGSpcPAVWPdviklpyfntmkpkkqyrrrlrEEFSFIPSAALDLLDHMLTLDPSKR---CTAEQTLQ 993
Cdd:cd05609    220 PE----ELFGQVISD--EIEWP----------------------EGDDALPDDAQDLITRLLQQNPLERlgtGGAEEVKQ 271

                   ....*...
gi 1907082950  994 SDFLKDVE 1001
Cdd:cd05609    272 HPFFQDLD 279
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
729-935 3.12e-05

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: 47.25  E-value: 3.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYG----QVYKAKDKDTGelVALKKVRLDNEKeGFPITAIREIKILRQLVHQSVVNMKEIVtdkqdaldfkkDKGA 804
Cdd:cd05115     12 LGSGNFGcvkkGVYKMRKKQID--VAIKVLKQGNEK-AVRDEMMREAQIMHQLDNPYIVRMIGVC-----------EAEA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  805 FYLVFEYMDHD-LMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSR---------------- 867
Cdd:cd05115     78 LMLVMEMASGGpLNKFLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHyakisdfglskalgad 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  868 --PYTNKVITLW---YRPPELLLgEERYTPAIDVWSCGCILGELFT--KKPI--FQANLELAQLELISRL-CGSPCPA 935
Cdd:cd05115    158 dsYYKARSAGKWplkWYAPECIN-FRKFSSRSDVWSYGVTMWEAFSygQKPYkkMKGPEVMSFIEQGKRMdCPAECPP 234
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
729-908 3.16e-05

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: 47.32  E-value: 3.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTgelVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQDALDFKKDKGAfylv 808
Cdd:cd14150      8 IGTGSFGTVFRGKWHGD---VAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGFMTRPNFAIITQWCEGS---- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 feymdhDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN--------------------SRP 868
Cdd:cd14150     81 ------SLYRHLHVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEgltvkigdfglatvktrwsgSQQ 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1907082950  869 YTNKVITLWYRPPELLLGEER--YTPAIDVWSCGCILGELFT 908
Cdd:cd14150    155 VEQPSGSILWMAPEVIRMQDTnpYSFQSDVYAYGVVLYELMS 196
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
723-913 3.34e-05

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 47.71  E-value: 3.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRldnekegfpitaireikilRQLVHQSV----VNMKEIVTDKQDALDF 798
Cdd:cd05617     17 FDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVK-------------------KELVHDDEdidwVQTEKHVFEQASSNPF 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  799 K-------KDKGAFYLVFEYMDH-DLMGLLESGLvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS---- 866
Cdd:cd05617     78 LvglhscfQTTSRLFLVIEYVNGgDLMFHMQRQR-KLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADghik 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  867 -----------RPYTNKVI---TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIF 913
Cdd:cd05617    157 ltdygmckeglGPGDTTSTfcgTPNYIAPEILRGEE-YGFSVDWWALGVLMFEMMAGRSPF 216
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
729-862 3.73e-05

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


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 47.49  E-value: 3.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKvrLDNEKEGFPITA-IREIKILRQLVHQSVVNM---KEIVTDKQDALDFKK-DKG 803
Cdd:cd13988      1 LGQGATANVFRGRHKKTGDLYAVKV--FNNLSFMRPLDVqMREFEVLKKLNHKNIVKLfaiEEELTTRHKVLVMELcPCG 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  804 AFYLVFEYMDhDLMGLLESGLVHFSEDhiksfmkqLMEGLDYCHKKNFLHRDIKCSNIL 862
Cdd:cd13988     79 SLYTVLEEPS-NAYGLPESEFLIVLRD--------VVAGMNHLRENGIVHRDIKPGNIM 128
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
729-908 4.11e-05

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: 46.75  E-value: 4.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKdtGELVALKKVRLD-----NEKEGFpitaIREIKILRQLVHQSVVNMKEIVTDkqdaldfkkDKG 803
Cdd:cd14064      1 IGSGSFGKVYKGRCR--NKIVAIKRYRANtycskSDVDMF----CREVSILCRLNHPCVIQFVGACLD---------DPS 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  804 AFYLVFEYMdhdlmglleSGLVHFSEDHIKsfmKQLME-------------GLDYCHK--KNFLHRDIKCSNILLN---- 864
Cdd:cd14064     66 QFAIVTQYV---------SGGSLFSLLHEQ---KRVIDlqskliiavdvakGMEYLHNltQPIIHRDLNSHNILLYedgh 133
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082950  865 -------NSR--------PYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFT 908
Cdd:cd14064    134 avvadfgESRflqsldedNMTKQPGNLRWMAPEVFTQCTRYSIKADVFSYALCLWELLT 192
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
722-922 4.16e-05

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: 47.02  E-value: 4.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIgiIGEGTYGQVYKAKDKDTGELVA---LKKVRLDN-EKEGFPitaiREIKILRQLVHQSVVNMkeivTDKQDALd 797
Cdd:cd14031     13 KFDIE--LGRGAFKTVYKGLDTETWVEVAwceLQDRKLTKaEQQRFK----EEAEMLKGLQHPNIVRF----YDSWESV- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 fKKDKGAFYLVFEYMDHdlmGLLESGLVHFS---EDHIKSFMKQLMEGLDYCHKKN--FLHRDIKCSNILLNN------- 865
Cdd:cd14031     82 -LKGKKCIVLVTELMTS---GTLKTYLKRFKvmkPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGptgsvki 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  866 ---------SRPYTNKVI-TLWYRPPELLlgEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQL 922
Cdd:cd14031    158 gdlglatlmRTSFAKSVIgTPEFMAPEMY--EEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQI 222
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
723-864 4.22e-05

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


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 47.73  E-value: 4.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLdnekegfpitaiREIKILRQLVHqsVVNMKEIVTDKQDALDFK--- 799
Cdd:cd05625      3 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRK------------KDVLLRNQVAH--VKAERDILAEADNEWVVRlyy 68
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  800 --KDKGAFYLVFEYM-DHDLMGLLESGLVhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN 864
Cdd:cd05625     69 sfQDKDNLYFVMDYIpGGDMMSLLIRMGV-FPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILID 135
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
723-913 4.28e-05

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 47.72  E-value: 4.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVR--LDNEKEGFPITAIREIKILRQLVHQSVVNMKEIvtdkqdaldFKK 800
Cdd:cd05618     22 FDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKkeLVNDDEDIDWVQTEKHVFEQASNHPFLVGLHSC---------FQT 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DKGAFYlVFEYMDH-DLMGLLESGLvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNS------------- 866
Cdd:cd05618     93 ESRLFF-VIEYVNGgDLMFHMQRQR-KLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEghikltdygmcke 170
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  867 --RPYTNKVI---TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIF 913
Cdd:cd05618    171 glRPGDTTSTfcgTPNYIAPEILRGED-YGFSVDWWALGVLMFEMMAGRSPF 221
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
722-922 5.33e-05

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: 46.61  E-value: 5.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIgiIGEGTYGQVYKAKDKDTGELVA---LKKVRLDN-EKEGFPitaiREIKILRQLVHQSVVNMKEIVTDKqdald 797
Cdd:cd14032      4 KFDIE--LGRGSFKTVYKGLDTETWVEVAwceLQDRKLTKvERQRFK----EEAEMLKGLQHPNIVRFYDFWESC----- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 fKKDKGAFYLVFEYMDHdlmGLLESGLVHFS---EDHIKSFMKQLMEGLDYCHKKN--FLHRDIKCSNILLNNSR----- 867
Cdd:cd14032     73 -AKGKRCIVLVTELMTS---GTLKTYLKRFKvmkPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGPTgsvki 148
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  868 -----------PYTNKVI-TLWYRPPELLlgEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQL 922
Cdd:cd14032    149 gdlglatlkraSFAKSVIgTPEFMAPEMY--EEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQI 213
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
728-925 7.40e-05

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: 46.48  E-value: 7.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVR-----LDNEKEgfpiTAIREIKILRQLVHQSVVNMKEIVTDKQDALdfkkdk 802
Cdd:cd05620      2 VLGKGSFGKVLLAELKGKGEYFAVKALKkdvvlIDDDVE----CTMVEKRVLALAWENPFLTHLYCTFQTKEHL------ 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  803 gafYLVFEYMDH-DLM-GLLESGlvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYT---------- 870
Cdd:cd05620     72 ---FFVMEFLNGgDLMfHIQDKG--RFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKiadfgmcken 146
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  871 ----NKVITLWYRP----PELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELI 925
Cdd:cd05620    147 vfgdNRASTFCGTPdyiaPEILQG-LKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESI 208
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
729-978 7.43e-05

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: 46.56  E-value: 7.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKegfpITAIR-EIKILRQLVHQSVVNMKEIVTdkqdaldfkkdKGAFYL 807
Cdd:cd14149     20 IGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQ----FQAFRnEVAVLRKTRHVNILLFMGYMT-----------KDNLAI 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYMD-HDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN--------------------S 866
Cdd:cd14149     85 VTQWCEgSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEgltvkigdfglatvksrwsgS 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  867 RPYTNKVITLWYRPPELLLGEER--YTPAIDVWSCGCILGELFTKK-PIFQANLELAQLELISRlcgspcPAVWPDVIKL 943
Cdd:cd14149    165 QQVEQPTGSILWMAPEVIRMQDNnpFSFQSDVYSYGIVLYELMTGElPYSHINNRDQIIFMVGR------GYASPDLSKL 238
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1907082950  944 pYFNTMKPKKQYR----RRLREEFSFIPS--AALDLLDHML 978
Cdd:cd14149    239 -YKNCPKAMKRLVadciKKVKEERPLFPQilSSIELLQHSL 278
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
722-866 8.22e-05

Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 46.20  E-value: 8.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKD---TGELVALKKVRldnekegfPiTAIREIKILRQLvHQSVVNMKeIVTDKQDALDF 798
Cdd:cd13981      1 TYVISKELGEGGYASVYLAKDDDeqsDGSLVALKVEK--------P-PSIWEFYICDQL-HSRLKNSR-LRESISGAHSA 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  799 KKDKGAFYLVFEYMDH----DL---------MGLLESGLVHFSedhiksfmKQLMEGLDYCHKKNFLHRDIKCSNILLNN 865
Cdd:cd13981     70 HLFQDESILVMDYSSQgtllDVvnkmknktgGGMDEPLAMFFT--------IELLKVVEALHEVGIIHGDIKPDNFLLRL 141

                   .
gi 1907082950  866 S 866
Cdd:cd13981    142 E 142
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
728-908 1.00e-04

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: 46.14  E-value: 1.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELV--ALKKVRLDNEKEGFPITAiREIKILRQL-VHQSVVNMkeivtdkqdaLDFKKDKGA 804
Cdd:cd05088     14 VIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFA-GELEVLCKLgHHPNIINL----------LGACEHRGY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  805 FYLVFEYMDH-DLMGLLESGLV---------------HFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN--- 865
Cdd:cd05088     83 LYLAIEYAPHgNLLDFLRKSRVletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGEnyv 162
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  866 --------SRPYTNKVITLWYRPPELLLGEER-----YTPAIDVWSCGCILGELFT 908
Cdd:cd05088    163 akiadfglSRGQEVYVKKTMGRLPVRWMAIESlnysvYTTNSDVWSYGVLLWEIVS 218
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
707-918 1.11e-04

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 46.40  E-value: 1.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  707 ERRQTESDWGKRcvdkfdiigIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEG-----------------FPITAIR 769
Cdd:PTZ00283    27 AKEQAKKYWISR---------VLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMSEAdknraqaevccllncdfFSIVKCH 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  770 EIKILRQLVHQSVVNMKEIVTDKQDALDFKKD-KGAFYLVFEYMDHdlmgllESGLVHFsedhiksfmkQLMEGLDYCHK 848
Cdd:PTZ00283    98 EDFAKKDPRNPENVLMIALVLDYANAGDLRQEiKSRAKTNRTFREH------EAGLLFI----------QVLLAVHHVHS 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  849 KNFLHRDIKCSNILLNN-----------SRPYTNKVI---------TLWYRPPELLLgEERYTPAIDVWSCGCILGELFT 908
Cdd:PTZ00283   162 KHMIHRDIKSANILLCSnglvklgdfgfSKMYAATVSddvgrtfcgTPYYVAPEIWR-RKPYSKKADMFSLGVLLYELLT 240
                          250
                   ....*....|.
gi 1907082950  909 -KKPIFQANLE 918
Cdd:PTZ00283   241 lKRPFDGENME 251
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
728-908 1.16e-04

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: 45.79  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKdtGELVALKKVRLDNEkEGFPITA---IREIKILRQLVHQSVVNMKEIVTDKQDaldfkkdkga 804
Cdd:cd14147     10 VIGIGGFGKVYRGSWR--GELVAVKAARQDPD-EDISVTAesvRQEARLFAMLAHPNIIALKAVCLEEPN---------- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  805 FYLVFEYMDHdlmGLLESGLV--HFSEDHIKSFMKQLMEGLDYCHKKNF---LHRDIKCSNILL------NNSRPYTNKV 873
Cdd:cd14147     77 LCLVMEYAAG---GPLSRALAgrRVPPHVLVNWAVQIARGMHYLHCEALvpvIHRDLKSNNILLlqpienDDMEHKTLKI 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  874 ITL-----WYRPPEL------------LLGEERYTPAIDVWSCGCILGELFT 908
Cdd:cd14147    154 TDFglareWHKTTQMsaagtyawmapeVIKASTFSKGSDVWSFGVLLWELLT 205
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
722-867 1.19e-04

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: 45.77  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKdtGElVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVV-NMKEIVTDKQDALDFKK 800
Cdd:cd14153      1 QLEIGELIGKGRFGQVYHGRWH--GE-VAIRLIDIERDNEEQLKAFKREVMAYRQTRHENVVlFMGACMSPPHLAIITSL 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  801 DKGafylvfeymdHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSR 867
Cdd:cd14153     78 CKG----------RTLYSVVRDAKVVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGK 134
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
799-993 1.79e-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: 45.67  E-value: 1.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  799 KKDKGAFYLVFEYMDHDLMG--LLESGLVHFSEDHIkSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPY------- 869
Cdd:cd05104    182 KADKRRGVRSGSYVDQDVTSeiLEEDELALDTEDLL-SFSYQVAKGMEFLASKNCIHRDLAARNILLTHGRITkicdfgl 260
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  870 -------TNKVITLWYRPPELLLGEER-----YTPAIDVWSCGCILGELFTkkpifqanlelaqlelisrLCGSPCPAVW 937
Cdd:cd05104    261 ardirndSNYVVKGNARLPVKWMAPESifecvYTFESDVWSYGILLWEIFS-------------------LGSSPYPGMP 321
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  938 PDViklpyfNTMKPKKQYRRRLREEFSfiPSAALDLLDHMLTLDPSKRCTAEQTLQ 993
Cdd:cd05104    322 VDS------KFYKMIKEGYRMDSPEFA--PSEMYDIMRSCWDADPLKRPTFKQIVQ 369
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
723-868 2.26e-04

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 44.70  E-value: 2.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREI---KILRQlvHQSVVNMKEIVTDKqdaldfk 799
Cdd:cd14051      2 FHEVEKIGSGEFGSVYKCINRLDGCVYAIKKSKKPVAGSVDEQNALNEVyahAVLGK--HPHVVRYYSAWAED------- 72
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  800 kdkGAFYLVFEYMD----HDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRP 868
Cdd:cd14051     73 ---DHMIIQNEYCNggslADAISENEKAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISRTPN 142
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
722-910 2.30e-04

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: 45.04  E-value: 2.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIgiIGEGTYGQVYKAKDKDTGELVA---LKKVRLD-NEKEGFPitaiREIKILRQLVHQSVVNMKEIVTDKQdald 797
Cdd:cd14030     28 KFDIE--IGRGSFKTVYKGLDTETTVEVAwceLQDRKLSkSERQRFK----EEAGMLKGLQHPNIVRFYDSWESTV---- 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 fkKDKGAFYLVFEYMDHdlmGLLESGLVHFSEDHIK---SFMKQLMEGLDYCHKKN--FLHRDIKCSNILLN-------- 864
Cdd:cd14030     98 --KGKKCIVLVTELMTS---GTLKTYLKRFKVMKIKvlrSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgptgsvki 172
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  865 --------NSRPYTNKVI-TLWYRPPELLlgEERYTPAIDVWSCGCILGELFTKK 910
Cdd:cd14030    173 gdlglatlKRASFAKSVIgTPEFMAPEMY--EEKYDESVDVYAFGMCMLEMATSE 225
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
728-922 3.63e-04

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: 44.14  E-value: 3.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAK---DKDTGELVALKKVRLD----NEKEGFpitaIREIKILRQLVHQSVVNMKEIVTDKqdaldfkK 800
Cdd:cd05074     16 MLGKGEFGSVREAQlksEDGSFQKVAVKMLKADifssSDIEEF----LREAACMKEFDHPNVIKLIGVSLRS-------R 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 DKGAF---YLVFEYMDHD------LMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTN 871
Cdd:cd05074     85 AKGRLpipMVILPFMKHGdlhtflLMSRIGEEPFTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCV 164
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  872 KVITL--------WYR-------PPELL----LGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQL 922
Cdd:cd05074    165 ADFGLskkiysgdYYRqgcasklPVKWLalesLADNVYTTHSDVWAFGVTMWEIMTRGQTPYAGVENSEI 234
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
723-913 3.79e-04

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 44.62  E-value: 3.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  723 FDIIGIIGEGTYGQVYKAKDKDTGELVALK---KVRLDNEKEGFPITAIREIkILRQLVHQSVVNMKEI--VTDKqdald 797
Cdd:cd05602      9 FHFLKVIGKGSFGKVLLARHKSDEKFYAVKvlqKKAILKKKEEKHIMSERNV-LLKNVKHPFLVGLHFSfqTTDK----- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  798 fkkdkgaFYLVFEYMDH-DLMGLLESGLVhFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN------------ 864
Cdd:cd05602     83 -------LYFVLDYINGgELFYHLQRERC-FLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDsqghivltdfgl 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  865 ---NSRPytNKVITLWYRPPELL----LGEERYTPAIDVWSCGCILGELFTKKPIF 913
Cdd:cd05602    155 ckeNIEP--NGTTSTFCGTPEYLapevLHKQPYDRTVDWWCLGAVLYEMLYGLPPF 208
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
729-863 3.99e-04

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. The delta and epsilon isoforms of CK1 play important roles in circadian rhythm and cell growth. They phosphorylate PERIOD proteins (PER1-3), which are circadian clock proteins that fulfill negative regulatory functions. PER phosphorylation leads to its degradation. However, CRY proteins form a complex with PER and CK1delta/epsilon that protects PER from degradation and leads to nuclear accummulation of the complex, which inhibits BMAL1-CLOCK dependent transcription activation. CK1delta/epsilon also phosphorylate the tumor suppressor p53 and the cellular oncogene Mdm2, which are key regulators of cell growth, genome integrity, and the development of cancer. This subfamily also includes the CK1 fungal proteins Saccharomyces cerevisiae HRR25 and Schizosaccharomyces pombe HHP1. These fungal proteins are involved in DNA repair. The CK1 delta/epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271027 [Multi-domain]  Cd Length: 275  Bit Score: 43.90  E-value: 3.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKkvrLDNEKEGFPITAIrEIKILRQLvhQSVVNMKEIVTDKQDAlDFKkdkgafYLV 808
Cdd:cd14125      8 IGSGSFGDIYLGTNIQTGEEVAIK---LESVKTKHPQLLY-ESKLYKIL--QGGVGIPNVRWYGVEG-DYN------VMV 74
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907082950  809 FEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL 863
Cdd:cd14125     75 MDLLGPSLEDLFNFCSRKFSLKTVLMLADQMISRIEYVHSKNFIHRDIKPDNFLM 129
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
728-918 4.54e-04

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


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 44.02  E-value: 4.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKDTGELVALKKVRLDN--EKEGFPITAIrEIKILrqlvhqSVVNMKEIVTDKQDALDfKKDKgaF 805
Cdd:cd05591      2 VLGKGSFGKVMLAERKGTDEVYAIKVLKKDVilQDDDVDCTMT-EKRIL------ALAAKHPFLTALHSCFQ-TKDR--L 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  806 YLVFEYMDH-DLMGLLESGLvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN------------------NS 866
Cdd:cd05591     72 FFVMEYVNGgDLMFQIQRAR-KFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDaeghckladfgmckegilNG 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907082950  867 RPYTNKVITLWYRPPELLlGEERYTPAIDVWSCGCILGELFTKKPIFQANLE 918
Cdd:cd05591    151 KTTTTFCGTPDYIAPEIL-QELEYGPSVDWWALGVLMYEMMAGQPPFEADNE 201
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
767-869 1.32e-03

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


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 41.10  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  767 AIREIKILRQLvHQSVVNMKEIvtdkqdaLDFkkDKGAFYLVFEYMDH-DLMGLLESGlvhfseDHIKSFMKQLMEGLDY 845
Cdd:COG3642      3 TRREARLLREL-REAGVPVPKV-------LDV--DPDDADLVMEYIEGeTLADLLEEG------ELPPELLRELGRLLAR 66
                           90       100
                   ....*....|....*....|....
gi 1907082950  846 CHKKNFLHRDIKCSNILLNNSRPY 869
Cdd:COG3642     67 LHRAGIVHGDLTTSNILVDDGGVY 90
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
729-903 1.60e-03

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 42.09  E-value: 1.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEgFPITAIrEIKILRQLV-HQSVVNMKEIVTDKQDALDFKKdkgAFYL 807
Cdd:cd13975      8 LGRGQYGVVYACDSWGGHFPCALKSVVPPDDKH-WNDLAL-EFHYTRSLPkHERIVSLHGSVIDYSYGGGSSI---AVLL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  808 VFEYMDHDLMGLLESGLVHFSEDHIKSfmkQLMEGLDYCHKKNFLHRDIKCSNILLNNS-----------RPYT----NK 872
Cdd:cd13975     83 IMERLHRDLYTGIKAGLSLEERLQIAL---DVVEGIRFLHSQGLVHRDIKLKNVLLDKKnrakitdlgfcKPEAmmsgSI 159
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1907082950  873 VITLWYRPPELLLGeeRYTPAIDVWSCGCIL 903
Cdd:cd13975    160 VGTPIHMAPELFSG--KYDNSVDVYAFGILF 188
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
834-908 1.85e-03

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: 42.32  E-value: 1.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  834 SFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSR-----------------PYTNKVITL----WYRPPELLlgEERYTP 892
Cdd:cd05105    241 SFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKivkicdfglardimhdsNYVSKGSTFlpvkWMAPESIF--DNLYTT 318
                           90
                   ....*....|....*.
gi 1907082950  893 AIDVWSCGCILGELFT 908
Cdd:cd05105    319 LSDVWSYGILLWEIFS 334
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
728-906 1.95e-03

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 42.04  E-value: 1.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  728 IIGEGTYGQVYKAKDKdtGELVALKKVRLDNEKEGFPITAIREIKILRqlvHQSVVNMkeIVTDkqdaldfKKDKGAF-- 805
Cdd:cd14143      2 SIGKGRFGEVWRGRWR--GEDVAVKIFSSREERSWFREAEIYQTVMLR---HENILGF--IAAD-------NKDNGTWtq 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  806 -YLVFEYMDHdlmGLLESGLVHFSEDhIKSFMKQLME---GLDYCH--------KKNFLHRDIKCSNILLNNSR------ 867
Cdd:cd14143     68 lWLVSDYHEH---GSLFDYLNRYTVT-VEGMIKLALSiasGLAHLHmeivgtqgKPAIAHRDLKSKNILVKKNGtcciad 143
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082950  868 ----------------PYTNKVITLWYRPPELL------LGEERYTPAiDVWSCGCILGEL 906
Cdd:cd14143    144 lglavrhdsatdtidiAPNHRVGTKRYMAPEVLddtinmKHFESFKRA-DIYALGLVFWEI 203
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
721-906 2.19e-03

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 41.96  E-value: 2.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  721 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDnEKEGFPITAIREIKILRQLVHQSVVNMKeivtdkqdaldfkk 800
Cdd:cd06649      5 DDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLE-IKPAIRNQIIRELQVLHECNSPYIVGFY-------------- 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  801 dkGAFY------LVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKN-FLHRDIKCSNILLNN-------- 865
Cdd:cd06649     70 --GAFYsdgeisICMEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKHqIMHRDVKPSNILVNSrgeiklcd 147
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1907082950  866 --------SRPYTNKVITLWYRPPELLLGEErYTPAIDVWSCGCILGEL 906
Cdd:cd06649    148 fgvsgqliDSMANSFVGTRSYMSPERLQGTH-YSVQSDIWSMGLSLVEL 195
STKc_VRK cd14015
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs ...
797-864 2.75e-03

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins (VRK1, VRK2, and VRK3) while invertebrates, specifically fruit flies and nematodes, seem to carry only a single ortholog. Mutations of VRK in Drosophila and Caenorhabditis elegans showed varying phenotypes ranging from embryonic lethality to mitotic and meiotic defects resulting in sterility. In vertebrates, VRK1 is implicated in cell cycle progression and proliferation, nuclear envelope assembly, and chromatin condensation. VRK2 is involved in modulating JNK signaling. VRK3 is an inactive pseudokinase that inhibits ERK signaling. The VRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270917 [Multi-domain]  Cd Length: 300  Bit Score: 41.50  E-value: 2.75e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  797 DFKKDKGAFyLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLN 864
Cdd:cd14015     95 EYKGEKYRF-LVMPRFGRDLQKIFEKNGKRFPEKTVLQLALRILDVLEYIHENGYVHADIKASNLLLG 161
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
722-863 3.12e-03

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


Pssm-ID: 271032 [Multi-domain]  Cd Length: 262  Bit Score: 41.17  E-value: 3.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPItairEIKILRQLVHQSVVnMKEIVTDKQDALDfkkd 801
Cdd:cd14130      1 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKM----EVAVLKKLQGKDHV-CRFIGCGRNEKFN---- 71
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  802 kgafYLVFEYMDHDLMGLLESG-LVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL 863
Cdd:cd14130     72 ----YVVMQLQGRNLADLRRSQpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAM 130
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
806-863 3.40e-03

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 41.33  E-value: 3.40e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082950  806 YLVFEYMDHDLMGLLESGlvHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL 863
Cdd:cd14018    116 FLVMKNYPCTLRQYLWVN--TPSYRLARVMILQLLEGVDHLVRHGIAHRDLKSDNILL 171
THRAP3_BCLAF1 pfam15440
THRAP3/BCLAF1 family; This family includes thyroid hormone receptor-associated protein 3 ...
214-359 4.81e-03

THRAP3/BCLAF1 family; This family includes thyroid hormone receptor-associated protein 3 (THRAP3), which is a spliceosome component and a subunit of the TRAP complex which plays a role in pre-mRNA splicing and in mRNA decay. It also includes the transcriptional repressor Bcl-2-associated transcription factor 1 (BCLAF1).


Pssm-ID: 464718  Cd Length: 641  Bit Score: 41.30  E-value: 4.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  214 SPKRRSRSPhRKWSDSSKQDDSPSGASygqdydlsppRSHTSSNYDSYKKSPGSTSRRQSisppyKEPSAYQSSTRSPsp 293
Cdd:pfam15440    7 SPKRRSLSP-RSRSRSHYSDRSSSGRS----------RSSSSRSSSNHSKDPKRSKRWRM-----DDKKHGQKDPRIS-- 68
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082950  294 ysrrQRSVSPYSRRRSSSYERSGSYSGRSPSPygRRRSSSPFLSKRSLSRSPLPSRKSMKSRSRSP 359
Cdd:pfam15440   69 ----PHGNDHNRSYEHRSPDAKSSEASKSWSP--KRRSPLESVYVYKPSPRPSPERGDSSRRDQYM 128
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
722-863 5.09e-03

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


Pssm-ID: 271031 [Multi-domain]  Cd Length: 262  Bit Score: 40.42  E-value: 5.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  722 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPItairEIKILRQLVHQSVVnMKEIVTDKQDALDfkkd 801
Cdd:cd14129      1 RWKVLRKIGGGGFGEIYDALDLLTRENVALKVESAQQPKQVLKM----EVAVLKKLQGKDHV-CRFIGCGRNDRFN---- 71
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082950  802 kgafYLVFEYMDHDLMGLLES-GLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILL 863
Cdd:cd14129     72 ----YVVMQLQGRNLADLRRSqSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAM 130
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
729-932 5.89e-03

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: 40.43  E-value: 5.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKDTgelVALKKVRLDNEKEGFPITAIREIKILRQLVHQSVVNMKEIVTDKQDALDFKKDKGAfylv 808
Cdd:cd14151     16 IGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGS---- 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  809 feymdhDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNN--------------------SRP 868
Cdd:cd14151     89 ------SLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEdltvkigdfglatvksrwsgSHQ 162
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082950  869 YTNKVITLWYRPPELLLGEER--YTPAIDVWSCGCILGELFTKK-PIFQANLELAQLELISRLCGSP 932
Cdd:cd14151    163 FEQLSGSILWMAPEVIRMQDKnpYSFQSDVYAFGIVLYELMTGQlPYSNINNRDQIIFMVGRGYLSP 229
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
829-914 6.37e-03

Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3. RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. The RPK118-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 40.22  E-value: 6.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  829 EDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSRPYTNKVITLW---------------YRPPEL-LLGEEryTP 892
Cdd:cd05576    112 EECIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWsevedscdsdaienmYCAPEVgGISEE--TE 189
                           90       100
                   ....*....|....*....|..
gi 1907082950  893 AIDVWSCGCILGELFTKKPIFQ 914
Cdd:cd05576    190 ACDWWSLGALLFELLTGKALVE 211
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
729-948 8.07e-03

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 40.15  E-value: 8.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  729 IGEGTYGQVYKAKDKdtGELVALKKVRLDNEKEGFPITAIREIKILRqlvHQSVVNMkeIVTDKqdaldfkKDKGAF--- 805
Cdd:cd14144      3 VGKGRYGEVWKGKWR--GEKVAVKIFFTTEEASWFRETEIYQTVLMR---HENILGF--IAADI-------KGTGSWtql 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  806 YLVFEY--------------MDHDLMGLL----ESGLVHFsedHIKSFMKQlmegldycHKKNFLHRDIKCSNILLN--- 864
Cdd:cd14144     69 YLITDYhengslydflrgntLDTQSMLKLaysaACGLAHL---HTEIFGTQ--------GKPAIAHRDIKSKNILVKkng 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082950  865 -------------NSR------PYTNKVITLWYRPPELL---LGEERYTPAI--DVWSCGCILGElftkkpifqanlela 920
Cdd:cd14144    138 tcciadlglavkfISEtnevdlPPNTRVGTKRYMAPEVLdesLNRNHFDAYKmaDMYSFGLVLWE--------------- 202
                          250       260
                   ....*....|....*....|....*...
gi 1907082950  921 qlelISRLCGSPCPAvwpDVIKLPYFNT 948
Cdd:cd14144    203 ----IARRCISGGIV---EEYQLPYYDA 223
 
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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