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Conserved domains on  [gi|30694992|ref|NP_191500|]
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protein kinase family protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
418-729 8.54e-147

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: 443.73  E-value: 8.54e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  418 SSRYLNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEiPVNSRIVREVATLSRLQHQHVVRYYQAWFETGvv 497
Cdd:cd14046    1 FSRYLTDFEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIKLRSES-KNNSRILREVMLLSRLNHQHVVRYYQAWIERA-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  498 dpfaganwgsktagssmfsysgavsteipeqdnnlestYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAH 576
Cdd:cd14046   78 --------------------------------------NLYIQMEYCEKsTLRDLIDSGLFQDTDRLWRLFRQILEGLAY 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  577 IHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKL--EQLDQDGGFSTDVA-GSGVDSTGQAGTYFYTAPEIEQD-WP 652
Cdd:cd14046  120 IHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATSNKLnvELATQDINKSTSAAlGSSGDLTGNVGTALYVAPEVQSGtKS 199
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30694992  653 KIDEKADMYSLGVVFFELWHPFGTAMERHVILTNLKL-KGELPLKWV-NEFPEQASLLRRLMSPSPSDRPSATELLKHA 729
Cdd:cd14046  200 TYNEKVDMYSLGIIFFEMCYPFSTGMERVQILTALRSvSIEFPPDFDdNKHSKQAKLIRWLLNHDPAKRPSAQELLKSE 278
PLN02972 super family cl33611
Histidyl-tRNA synthetase
796-1226 1.46e-38

Histidyl-tRNA synthetase


The actual alignment was detected with superfamily member PLN02972:

Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 155.43  E-value: 1.46e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   796 LRDYVVEITKEVFRQHCAKHLE--VIPMR--LLSDCPQFSRKTVKLLTNGGDMLELCYELRLPFVHWISVNQKSSFKRYE 871
Cdd:PLN02972  343 IREKAFSIITSVFKRHGATALDtpVFELRetLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKRYQ 422
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   872 ISHVYRRaighspPNPC-------LQADFDIVGGTLSL-TEAEVLKVIVDITTHIfHRGSCDIHLNHGDLLDAIWSWAGI 943
Cdd:PLN02972  423 IAKVYRR------DNPSkgryrefYQCDFDIAGVYEPMgPDFEIIKVLTELLDEL-DIGTYEVKLNHRKLLDGMLEICGV 495
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   944 KAEHRRKVAellSMMGSLRPQSSERklkwvfIRRQLLQELKLPEAVVNRLQT-VASRfcGDADQALPRLR--GALRADRP 1020
Cdd:PLN02972  496 PPEKFRTIC---SSIDKLDKQSFEQ------VKKEMVEEKGLSNETADKIGNfVKER--GPPLELLSKLRqeGSEFLGNA 564
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  1021 -TRKALDELSNLLTYLRVWRIEEHVHIDVLMPPTESYHRNLFFQ-VFLTKENSSgtsndgvlLAVGGRYDWLVQEVCDRE 1098
Cdd:PLN02972  565 sSRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEaVFKGAQVGS--------IAAGGRYDNLVGMFSGKQ 636
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  1099 hkmnLPgAVGVSLALETIFQHLPMD-------LRPIRNEVSTSVLvcsrgGGGLLVQRMELVAELWEKSIKAEFVPTpdP 1171
Cdd:PLN02972  637 ----VP-AVGVSLGIERVFAIMEQQeeeksqvIRPTETEVLVSII-----GDDKLALAAELVSELWNAGIKAEYKVS--T 704
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 30694992  1172 SLTEQYEYANEHEIKCLVIITESGVAQNqieFVKVRHLELKKEKVVGREELVKFL 1226
Cdd:PLN02972  705 RKAKHLKRAKESGIPWMVLVGEKELSKG---FVKLKNLEAGVEEEVDRTCFVQEL 756
RWD_RNF25 cd23818
RWD domain of RING finger protein 25 (RNF25) and related proteins; RNF25 (EC 2.3.2.27), also ...
35-146 3.74e-34

RWD domain of RING finger protein 25 (RNF25) and related proteins; RNF25 (EC 2.3.2.27), also known as AO7, is a putative E3 ubiquitin-protein ligase that was initially identified as an interacting protein of the E2 ubiquitin-conjugating enzyme, Ubc5B. It is ubiquitously expressed in various tissues and is predominantly localized in the nucleus. RNF25 activates nuclear factor (NF)-kappaB-dependent gene expression upon stimulation with interleukin-1 beta (IL-1beta), or tumor necrosis factor (TNF), or overexpression of NF-kappaB-inducing kinase. It interacts with the p65 transactivation domain (TAD) and modulates its transcriptional activity.


:

Pssm-ID: 467654  Cd Length: 109  Bit Score: 126.89  E-value: 3.74e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   35 LSEEITALSAIFQEDCKVVSDSRSPPQIAIKLRPYSKDMGyEDTDISAMLIVRCLPGYPYKCPKLQITPEQGLTTADAEK 114
Cdd:cd23818    1 LEEELEALEAIYPDELKVVSEDGAPTELSITLHPATADDE-SEQYVRLTLVITLPPGYPEEPPKISLRNPRGLSDARLAR 79
                         90       100       110
                 ....*....|....*....|....*....|..
gi 30694992  115 LLSLLEDQANSNAreGRVMIFNLVEAAQEFLS 146
Cdd:cd23818   80 LLSLLKELAEERA--GEPMLFELIELAKEFLT 109
 
Name Accession Description Interval E-value
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
418-729 8.54e-147

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: 443.73  E-value: 8.54e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  418 SSRYLNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEiPVNSRIVREVATLSRLQHQHVVRYYQAWFETGvv 497
Cdd:cd14046    1 FSRYLTDFEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIKLRSES-KNNSRILREVMLLSRLNHQHVVRYYQAWIERA-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  498 dpfaganwgsktagssmfsysgavsteipeqdnnlestYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAH 576
Cdd:cd14046   78 --------------------------------------NLYIQMEYCEKsTLRDLIDSGLFQDTDRLWRLFRQILEGLAY 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  577 IHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKL--EQLDQDGGFSTDVA-GSGVDSTGQAGTYFYTAPEIEQD-WP 652
Cdd:cd14046  120 IHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATSNKLnvELATQDINKSTSAAlGSSGDLTGNVGTALYVAPEVQSGtKS 199
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30694992  653 KIDEKADMYSLGVVFFELWHPFGTAMERHVILTNLKL-KGELPLKWV-NEFPEQASLLRRLMSPSPSDRPSATELLKHA 729
Cdd:cd14046  200 TYNEKVDMYSLGIIFFEMCYPFSTGMERVQILTALRSvSIEFPPDFDdNKHSKQAKLIRWLLNHDPAKRPSAQELLKSE 278
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
425-730 3.45e-66

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 223.95  E-value: 3.45e-66
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992     425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRlKDKEIPVNSRIVREVATLSRLQHQHVVRYYqAWFETgvvdpfagan 504
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIK-KKKIKKDRERILREIKILKKLKHPNIVRLY-DVFED---------- 68
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992     505 wgsktagssmfsysgavsteipeqdnnleSTYLYIQMEYCP-RTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGII 583
Cdd:smart00220   69 -----------------------------EDKLYLVMEYCEgGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIV 119
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992     584 HRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqdggfstdvagSGVDSTGQAGTYFYTAPEIeQDWPKIDEKADMYSL 663
Cdd:smart00220  120 HRDLKPENILLDEDGHVKLADFGLARQLD----------------PGEKLTTFVGTPEYMAPEV-LLGKGYGKAVDIWSL 182
                           250       260       270       280       290       300       310
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30694992     664 GVVFFEL---WHPFGTAMERHVILTNLKLKGELPLKWVNEFPEQA-SLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:smart00220  183 GVILYELltgKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAkDLIRKLLVKDPEKRLTAEEALQHPF 253
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
422-727 2.83e-50

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 185.99  E-value: 2.83e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIR---LKDKEipVNSRIVREVATLSRLQHQHVVRYYqAWFEtgvvd 498
Cdd:COG0515    6 LGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRpelAADPE--ARERFRREARALARLNHPNIVRVY-DVGE----- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  499 pfaganwgsktagssmfsysgavsteipeqdnnlESTYLYIQMEYCP-RTLRQVFESYNHFDKDFAWHLIRQIVEGLAHI 577
Cdd:COG0515   78 ----------------------------------EDGRPYLVMEYVEgESLADLLRRRGPLPPAEALRILAQLAEALAAA 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  578 HGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQDGGFstdvagsgvdstgqAGTYFYTAPEIEQDwPKIDEK 657
Cdd:COG0515  124 HAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTQTGTV--------------VGTPGYMAPEQARG-EPVDPR 188
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30694992  658 ADMYSLGVVFFELW---HPFGTAMERHVILTNLKLKGELPLKWVNEFPEQ-ASLLRRLMSPSPSDRP-SATELLK 727
Cdd:COG0515  189 SDVYSLGVTLYELLtgrPPFDGDSPAELLRAHLREPPPPPSELRPDLPPAlDAIVLRALAKDPEERYqSAAELAA 263
PLN02972 PLN02972
Histidyl-tRNA synthetase
796-1226 1.46e-38

Histidyl-tRNA synthetase


Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 155.43  E-value: 1.46e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   796 LRDYVVEITKEVFRQHCAKHLE--VIPMR--LLSDCPQFSRKTVKLLTNGGDMLELCYELRLPFVHWISVNQKSSFKRYE 871
Cdd:PLN02972  343 IREKAFSIITSVFKRHGATALDtpVFELRetLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKRYQ 422
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   872 ISHVYRRaighspPNPC-------LQADFDIVGGTLSL-TEAEVLKVIVDITTHIfHRGSCDIHLNHGDLLDAIWSWAGI 943
Cdd:PLN02972  423 IAKVYRR------DNPSkgryrefYQCDFDIAGVYEPMgPDFEIIKVLTELLDEL-DIGTYEVKLNHRKLLDGMLEICGV 495
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   944 KAEHRRKVAellSMMGSLRPQSSERklkwvfIRRQLLQELKLPEAVVNRLQT-VASRfcGDADQALPRLR--GALRADRP 1020
Cdd:PLN02972  496 PPEKFRTIC---SSIDKLDKQSFEQ------VKKEMVEEKGLSNETADKIGNfVKER--GPPLELLSKLRqeGSEFLGNA 564
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  1021 -TRKALDELSNLLTYLRVWRIEEHVHIDVLMPPTESYHRNLFFQ-VFLTKENSSgtsndgvlLAVGGRYDWLVQEVCDRE 1098
Cdd:PLN02972  565 sSRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEaVFKGAQVGS--------IAAGGRYDNLVGMFSGKQ 636
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  1099 hkmnLPgAVGVSLALETIFQHLPMD-------LRPIRNEVSTSVLvcsrgGGGLLVQRMELVAELWEKSIKAEFVPTpdP 1171
Cdd:PLN02972  637 ----VP-AVGVSLGIERVFAIMEQQeeeksqvIRPTETEVLVSII-----GDDKLALAAELVSELWNAGIKAEYKVS--T 704
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 30694992  1172 SLTEQYEYANEHEIKCLVIITESGVAQNqieFVKVRHLELKKEKVVGREELVKFL 1226
Cdd:PLN02972  705 RKAKHLKRAKESGIPWMVLVGEKELSKG---FVKLKNLEAGVEEEVDRTCFVQEL 756
RWD_RNF25 cd23818
RWD domain of RING finger protein 25 (RNF25) and related proteins; RNF25 (EC 2.3.2.27), also ...
35-146 3.74e-34

RWD domain of RING finger protein 25 (RNF25) and related proteins; RNF25 (EC 2.3.2.27), also known as AO7, is a putative E3 ubiquitin-protein ligase that was initially identified as an interacting protein of the E2 ubiquitin-conjugating enzyme, Ubc5B. It is ubiquitously expressed in various tissues and is predominantly localized in the nucleus. RNF25 activates nuclear factor (NF)-kappaB-dependent gene expression upon stimulation with interleukin-1 beta (IL-1beta), or tumor necrosis factor (TNF), or overexpression of NF-kappaB-inducing kinase. It interacts with the p65 transactivation domain (TAD) and modulates its transcriptional activity.


Pssm-ID: 467654  Cd Length: 109  Bit Score: 126.89  E-value: 3.74e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   35 LSEEITALSAIFQEDCKVVSDSRSPPQIAIKLRPYSKDMGyEDTDISAMLIVRCLPGYPYKCPKLQITPEQGLTTADAEK 114
Cdd:cd23818    1 LEEELEALEAIYPDELKVVSEDGAPTELSITLHPATADDE-SEQYVRLTLVITLPPGYPEEPPKISLRNPRGLSDARLAR 79
                         90       100       110
                 ....*....|....*....|....*....|..
gi 30694992  115 LLSLLEDQANSNAreGRVMIFNLVEAAQEFLS 146
Cdd:cd23818   80 LLSLLKELAEERA--GEPMLFELIELAKEFLT 109
Pkinase pfam00069
Protein kinase domain;
425-730 1.93e-30

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 120.04  E-value: 1.93e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992    425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAWfetgvvdpfagan 504
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAF------------- 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992    505 wgsktagssmfsysgavsteipeqdnnLESTYLYIQMEYCP-RTLRQVFESYNHFDKDFAWHLIRQIVEGLAhihgqgii 583
Cdd:pfam00069   68 ---------------------------EDKDNLYLVLEYVEgGSLFDLLSEKGAFSEREAKFIMKQILEGLE-------- 112
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992    584 hrdftpnniffdarndikigdfglakflkleqldqdggfstdvagSGVDSTGQAGTYFYTAPEIEQDwPKIDEKADMYSL 663
Cdd:pfam00069  113 ---------------------------------------------SGSSLTTFVGTPWYMAPEVLGG-NPYGPKVDVWSL 146
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992    664 GVVFFELW---HPFGTAMERHVILTNLKLKGELPLKWVNEFPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:pfam00069  147 GCILYELLtgkPPFPGINGNEIYELIIDQPYAFPELPSNLSEEAKDLLKKLLKKDPSKRLTATQALQHPW 216
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
422-732 2.86e-25

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 113.68  E-value: 2.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   422 LNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIR---LKDKEipvNSRIVREVATLSRLQHQHVVRYyqawfetgvVD 498
Cdd:PTZ00266   12 LNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISyrgLKERE---KSQLVIEVNVMRELKHKNIVRY---------ID 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   499 PFAganwgsktagssmfsysgavsteipeqdnNLESTYLYIQMEYC-----PRTLRQVFESYNHFDKDFAWHLIRQIVEG 573
Cdd:PTZ00266   80 RFL-----------------------------NKANQKLYILMEFCdagdlSRNIQKCYKMFGKIEEHAIVDITRQLLHA 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   574 LAHIH-------GQGIIHRDFTPNNIFF-----------------DARNDIKIGDFGLAKFLKLEQLdqdggfstdvAGS 629
Cdd:PTZ00266  131 LAYCHnlkdgpnGERVLHRDLKPQNIFLstgirhigkitaqannlNGRPIAKIGDFGLSKNIGIESM----------AHS 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   630 GVdstgqaGTYFYTAPEIE-QDWPKIDEKADMYSLGVVFFELWH---PFGTAMERHVILTNLKLKGELPLKwvNEFPEQA 705
Cdd:PTZ00266  201 CV------GTPYYWSPELLlHETKSYDDKSDMWALGCIIYELCSgktPFHKANNFSQLISELKRGPDLPIK--GKSKELN 272
                         330       340       350
                  ....*....|....*....|....*....|..
gi 30694992   706 SLLRRLMSPSPSDRPSAT-----ELLKHAFPP 732
Cdd:PTZ00266  273 ILIKNLLNLSAKERPSALqclgyQIIKNVGPP 304
RWD smart00591
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily ...
38-148 3.11e-23

domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily related to the UBCc domain;


Pssm-ID: 214735  Cd Length: 107  Bit Score: 95.50  E-value: 3.11e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992      38 EITALSAIFQEDCKVVSDSRSPPQIAIKLRPYSKDmgYEDTDISAMLIVRCLPGYPYKCPKLQITPEQGLTTADAEKLLS 117
Cdd:smart00591    1 ELEALESIYPEDFEVIDEDARIPEITIKLSPSSDE--GEDQYVSLTLQVKLPENYPDEAPPISLLNSEGLSDEQLAELLK 78
                            90       100       110
                    ....*....|....*....|....*....|.
gi 30694992     118 LLEDQANSNarEGRVMIFNLVEAAQEFLSEI 148
Cdd:smart00591   79 KLEEIAEEN--LGEVMIFELVEKLQEFLSEF 107
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
33-145 2.78e-20

RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. The function of this domain is unknown. GCN2 is the alpha-subunit of the only translation initiation factor (eIF2 alpha) kinase that appears in all eukaryotes. Its function requires an interaction with GCN1 via the domain at its N-terminus, which is termed the RWD domain after three major RWD-containing proteins: RING finger-containing proteins, WD-repeat-containing proteins, and yeast DEAD (DEXD)-like helicases. The structure forms an alpha + beta sandwich fold consisting of two layers: a four-stranded antiparallel beta-sheet, and three side-by-side alpha-helices.


Pssm-ID: 399058  Cd Length: 111  Bit Score: 87.38  E-value: 2.78e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992     33 ELLSEEITALSAIFQEDCKVVSDSR-SPPQIAIKLRPYSKDMGyEDTDISAMLIVRCLPGYPYKCPKLQITPEQGLTTAD 111
Cdd:pfam05773    1 EEQEEELEALESIYPDEFEVISDSPyESLEIEIKLSLDSDESD-SSHLPPLVLKFTLPEDYPDEPPKISLSSPWNLSDEQ 79
                           90       100       110
                   ....*....|....*....|....*....|....
gi 30694992    112 AEKLLSLLEDQANSNarEGRVMIFNLVEAAQEFL 145
Cdd:pfam05773   80 VLSLLEELEELAEEN--LGEVMIFELIEWLQENL 111
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
538-726 9.72e-17

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 85.23  E-value: 9.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   538 YIQMEYCP-RTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFlkleql 616
Cdd:NF033483   83 YIVMEYVDgRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARA------ 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   617 dqdggfstdVAGSGVDSTGQA-GTYFYTAPE-IEQDwpKIDEKADMYSLGVVFFELwhpfgtamerhviLTnlklkGELP 694
Cdd:NF033483  157 ---------LSSTTMTQTNSVlGTVHYLSPEqARGG--TVDARSDIYSLGIVLYEM-------------LT-----GRPP 207
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 30694992   695 ----------LKWVNEFPEQASLLR------------RLMSPSPSDRP-SATELL 726
Cdd:NF033483  208 fdgdspvsvaYKHVQEDPPPPSELNpgipqsldavvlKATAKDPDDRYqSAAEMR 262
HisS COG0124
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ...
794-1231 2.53e-15

Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439894 [Multi-domain]  Cd Length: 422  Bit Score: 79.78  E-value: 2.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  794 TELRDYVVEITKEVFRQHCAKHLEvipMRLLSDCPQFSRK-----TVKLL----TNGGDMLELCYELRLPFVHwiSVNQK 864
Cdd:COG0124   18 SAKWQYVEDTIREVFERYGFQEIR---TPIFEYTELFARKigediVEKEMytfeDRGGRSLTLRPEGTAPVAR--AVAEH 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  865 SS-----FKRYEISHVYRraigHSPPNPC-----LQADFDIVGGTLSLTEAEVLKVIVDItthiFHR---GSCDIHLNH- 930
Cdd:COG0124   93 GNelpfpFKLYYIGPVFR----YERPQKGryrqfHQFGVEVIGSDSPLADAEVIALAADL----LKAlglKDFTLEINSr 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  931 -------GDLLDAIwswagiKAEHRRKVAELLSmmgslrpQSSERKLKWVFIRRQLlqELKLPEavvnrlqtvasrfCGD 1003
Cdd:COG0124  165 glpeeraEALLRYL------DKLDKIGHEDVLD-------EDSQRRLETNPLRAIL--DSKGPD-------------CQE 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992 1004 ADQALPRLrgalrADRPTRKALDELSNLLTYLRVWRIEehVHIDvlmpPTE----SYHRNLFFQVFLTKENSSGTsndgv 1079
Cdd:COG0124  217 VLADAPKL-----LDYLGEEGLAHFEEVLELLDALGIP--YVID----PRLvrglDYYTGTVFEIVTDGLGAQGS----- 280
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992 1080 lLAVGGRYDWLVQEVCDREhkmnLPgAVGVSLALETIFQHLPMDLRPIRNEVSTSVLVCSRGGGGLLvQRMELVAELWEK 1159
Cdd:COG0124  281 -VCGGGRYDGLVEQLGGPP----TP-AVGFAIGLERLLLLLEELGLLPAAEPPPDVYVVPLGEEARA-EALKLAQELRAA 353
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30694992 1160 SIKAEFVPTPDpSLTEQYEYANEHEIKCLVIITESGVAQNQiefVKVRHLELKKEKVVGREELVKFLLDAMA 1231
Cdd:COG0124  354 GIRVELDLGGR-KLKKQLKYADKSGAPFVLILGEDELANGT---VTLKDLATGEQETVPLDELVEYLKELLA 421
HisRS-like_core cd00773
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ...
794-1121 2.77e-14

Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain.


Pssm-ID: 238396 [Multi-domain]  Cd Length: 261  Bit Score: 74.18  E-value: 2.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  794 TELRDYVVEITKEVFRQHCAKhlEVI-PMRLLSDCpqFSRK--------TVKLLTNGGDMLELCYELRLPFVHWISVNQK 864
Cdd:cd00773    2 AALRRYIEDTLREVFERYGYE--EIDtPVFEYTEL--FLRKsgdevskeMYRFKDKGGRDLALRPDLTAPVARAVAENLL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  865 S---SFKRYEISHVYRRaighspPNPCL-------QADFDIVGGTLSLTEAEVLKVIVDITTHIFHRGSCdIHLNHGDLL 934
Cdd:cd00773   78 SlplPLKLYYIGPVFRY------ERPQKgryrefyQVGVEIIGSDSPLADAEVIALAVEILEALGLKDFQ-IKINHRGIL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  935 DAIWSWAGIKAEHRRKVAELLsmmgslrpqsserklkwvfirrqllqelklpeavvnrlqtvasrfcgdadqalprlrga 1014
Cdd:cd00773  151 DGIAGLLEDREEYIERLIDKL----------------------------------------------------------- 171
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992 1015 lradrpTRKALDELSNLLTYLRVWRIEEHVHIDVLMPPTESYHRNLFFQVFLTKENSSGTsndgvlLAVGGRYDWLVQEV 1094
Cdd:cd00773  172 ------DKEALAHLEKLLDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQGS------IAGGGRYDGLLEEF 239
                        330       340
                 ....*....|....*....|....*..
gi 30694992 1095 CDREhkmnLPgAVGVSLALETIFQHLP 1121
Cdd:cd00773  240 GGED----VP-AVGFAIGLERLLLALE 261
tRNA-synt_His pfam13393
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ...
889-1116 1.94e-10

Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP phosphoribosyltransferase regulatory subunits.


Pssm-ID: 433170 [Multi-domain]  Cd Length: 309  Bit Score: 63.37  E-value: 1.94e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992    889 LQADFDIVGGTLSLTEAEVLKVIVDITTHIfhrGSCDIH--LNHGDLLDAIWSWAGIKAEHRRKVAELLsmmgslrpqss 966
Cdd:pfam13393  112 LQVGAELIGHAGIEADAEIISLLLEALAAA---GVPGVTldLGHVGLVRALLEAAGLSEALEEALRAAL----------- 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992    967 ERKlKWVFIRrQLLQELKLPEAVVNRLQTVASrFCGDADqALPRLRGALRADRPTRKALDELSNLLTYLRVWRIEEHVHI 1046
Cdd:pfam13393  178 QRK-DAAELA-ELAAEAGLPPALRRALLALPD-LYGGPE-VLDEARAALPGLPALQEALDELEALAALLEALGDGVRLTF 253
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30694992   1047 DvlmpPTE----SYHRNLFFQVFltkenssgTSNDGVLLAVGGRYDWLVQEVcdrehKMNLPgAVGVSLALETI 1116
Cdd:pfam13393  254 D----LAElrgyEYYTGIVFAAY--------APGVGEPLARGGRYDDLGAAF-----GRARP-ATGFSLDLEAL 309
lanthi_synth_IV NF038150
class IV lanthionine synthetase LanL; Several classes of lanthionine bridge-producing ...
537-751 1.94e-08

class IV lanthionine synthetase LanL; Several classes of lanthionine bridge-producing peptide-modifying enzymes (lanthionine synthases) have been defined. LanC enzymes are class I, LanM are class II, LanKC are class III, and LanL are class IV. Members of this family are the class IV enzyme, active in the maturation of class IV lanthipeptides, a large fraction of which act as lantibiotics.


Pssm-ID: 468386 [Multi-domain]  Cd Length: 853  Bit Score: 58.74  E-value: 1.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   537 LYIQMEYCP-RTLRQ------VFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAK 609
Cdd:NF038150  269 LFLAQEEVPgVTLRRwvaerlRYRGDGGPPRADALALARRLVDLVAAVHARGLVLRDLTPNNVMVTPDGELRLIDLELAA 348
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   610 flkleqldqdggfstdVAGSGVdstGQAGTYFYTAPE-IEQDWPKIDEKADMYSLG-VVFFELW---------HPFGTAM 678
Cdd:NF038150  349 ----------------RPGDLV---TRVGTPGYSAPEqLAGAPPAAPPTADLYSLGaTLFFLATgldpvllddEPAARPV 409
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   679 ERHV--ILTNLKLKGELPlkwvnefPEQASLLRRLMSPSPSDRPSATELLKH--------------AFPPRMESELLDNI 742
Cdd:NF038150  410 NERLalWLLAAALPGPAP-------RALAPLILGLMADDPARRWDLARARAAlagpappaaarlppAAPDRLLVDGLDHL 482

                  ....*....
gi 30694992   743 LRIMQTSED 751
Cdd:NF038150  483 VATMTPDDD 491
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
539-610 1.54e-06

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 50.29  E-value: 1.54e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30694992    539 IQMEYCP-RTLRQVFESYNHfdkdfawHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARnDIKIGDFGLAKF 610
Cdd:TIGR03724   74 IVMEYIEgKPLKDVIEENGD-------ELAREIGRLVGKLHKAGIVHGDLTTSNIIVRDD-KVYLIDFGLGKY 138
 
Name Accession Description Interval E-value
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
418-729 8.54e-147

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: 443.73  E-value: 8.54e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  418 SSRYLNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEiPVNSRIVREVATLSRLQHQHVVRYYQAWFETGvv 497
Cdd:cd14046    1 FSRYLTDFEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIKLRSES-KNNSRILREVMLLSRLNHQHVVRYYQAWIERA-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  498 dpfaganwgsktagssmfsysgavsteipeqdnnlestYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAH 576
Cdd:cd14046   78 --------------------------------------NLYIQMEYCEKsTLRDLIDSGLFQDTDRLWRLFRQILEGLAY 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  577 IHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKL--EQLDQDGGFSTDVA-GSGVDSTGQAGTYFYTAPEIEQD-WP 652
Cdd:cd14046  120 IHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATSNKLnvELATQDINKSTSAAlGSSGDLTGNVGTALYVAPEVQSGtKS 199
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30694992  653 KIDEKADMYSLGVVFFELWHPFGTAMERHVILTNLKL-KGELPLKWV-NEFPEQASLLRRLMSPSPSDRPSATELLKHA 729
Cdd:cd14046  200 TYNEKVDMYSLGIIFFEMCYPFSTGMERVQILTALRSvSIEFPPDFDdNKHSKQAKLIRWLLNHDPAKRPSAQELLKSE 278
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
418-726 4.21e-97

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: 311.15  E-value: 4.21e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  418 SSRYLNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIpVNSRIVREVATLSRLQHQHVVRYYQAWfetgvv 497
Cdd:cd13996    1 NSRYLNDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSS-ASEKVLREVKALAKLNHPNIVRYYTAW------ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  498 dpfaganwgsktagssmfsysgavsteipeqdnnLESTYLYIQMEYCP-RTLRQVFESYNHF---DKDFAWHLIRQIVEG 573
Cdd:cd13996   74 ----------------------------------VEEPPLYIQMELCEgGTLRDWIDRRNSSsknDRKLALELFKQILKG 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  574 LAHIHGQGIIHRDFTPNNIFFDARND-IKIGDFGLAKFLKlEQLDQDGGFSTDVAGSGVDSTGQAGTYFYTAPEIEQDWP 652
Cdd:cd13996  120 VSYIHSKGIVHRDLKPSNIFLDNDDLqVKIGDFGLATSIG-NQKRELNNLNNNNNGNTSNNSVGIGTPLYASPEQLDGEN 198
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30694992  653 kIDEKADMYSLGVVFFELWHPFGTAMERHVILTNLKlKGELPLKWVNEFPEQASLLRRLMSPSPSDRPSATELL 726
Cdd:cd13996  199 -YNEKADIYSLGIILFEMLHPFKTAMERSTILTDLR-NGILPESFKAKHPKEADLIQSLLSKNPEERPSAEQLL 270
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
425-730 3.45e-66

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 223.95  E-value: 3.45e-66
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992     425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRlKDKEIPVNSRIVREVATLSRLQHQHVVRYYqAWFETgvvdpfagan 504
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIK-KKKIKKDRERILREIKILKKLKHPNIVRLY-DVFED---------- 68
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992     505 wgsktagssmfsysgavsteipeqdnnleSTYLYIQMEYCP-RTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGII 583
Cdd:smart00220   69 -----------------------------EDKLYLVMEYCEgGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIV 119
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992     584 HRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqdggfstdvagSGVDSTGQAGTYFYTAPEIeQDWPKIDEKADMYSL 663
Cdd:smart00220  120 HRDLKPENILLDEDGHVKLADFGLARQLD----------------PGEKLTTFVGTPEYMAPEV-LLGKGYGKAVDIWSL 182
                           250       260       270       280       290       300       310
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30694992     664 GVVFFEL---WHPFGTAMERHVILTNLKLKGELPLKWVNEFPEQA-SLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:smart00220  183 GVILYELltgKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAkDLIRKLLVKDPEKRLTAEEALQHPF 253
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
419-729 3.97e-66

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 225.14  E-value: 3.97e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  419 SRYLNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNsRIVREVATLSRLQHQHVVRYYQAWFETgvvd 498
Cdd:cd14048    2 SRFLTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLPNNELARE-KVLREVRALAKLDHPGIVRYFNAWLER---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  499 PFAGanWGSKtagssmfsysgavsteipeqdnnLESTYLYIQMEYCPR-TLRQ------VFESYNHFdkdFAWHLIRQIV 571
Cdd:cd14048   77 PPEG--WQEK-----------------------MDEVYLYIQMQLCRKeNLKDwmnrrcTMESRELF---VCLNIFKQIA 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  572 EGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleQLDQDGGFSTDVAGSGVDS--TGQAGTYFYTAPEiEQ 649
Cdd:cd14048  129 SAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFGLVT-----AMDQGEPEQTVLTPMPAYAkhTGQVGTRLYMSPE-QI 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  650 DWPKIDEKADMYSLGVVFFELWHPFGTAMERHVILTNLKlKGELPLKWVNEFPEQASLLRRLMSPSPSDRPSATELLKHA 729
Cdd:cd14048  203 HGNQYSEKVDIFALGLILFELIYSFSTQMERIRTLTDVR-KLKFPALFTNKYPEERDMVQQMLSPSPSERPEAHEVIEHA 281
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
418-726 1.57e-60

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: 209.29  E-value: 1.57e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  418 SSRYLNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAWFEtgvv 497
Cdd:cd14049    1 TSRYLNEFEEIARLGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMKVLREVKVLAGLQHPNIVGYHTAWME---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  498 dpfaganwgsktagssmfsysgavsteipeqdnNLESTyLYIQMEYCPRTLR------------QVFESYNH--FDKDFA 563
Cdd:cd14049   77 ---------------------------------HVQLM-LYIQMQLCELSLWdwivernkrpceEEFKSAPYtpVDVDVT 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  564 WHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARN-DIKIGDFGLAKFLkleQLDQDGGFSTDVAGSGVDSTGQAGTYFY 642
Cdd:cd14049  123 TKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDiHVRIGDFGLACPD---ILQDGNDSTTMSRLNGLTHTSGVGTCLY 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  643 TAPEiEQDWPKIDEKADMYSLGVVFFELWHPFGTAMERHVILTNLKlKGELPLKWVNEFPEQASLLRRLMSPSPSDRPSA 722
Cdd:cd14049  200 AAPE-QLEGSHYDFKSDMYSIGVILLELFQPFGTEMERAEVLTQLR-NGQIPKSLCKRWPVQAKYIKLLTSTEPSERPSA 277

                 ....
gi 30694992  723 TELL 726
Cdd:cd14049  278 SQLL 281
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
419-728 1.08e-54

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: 191.94  E-value: 1.08e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  419 SRYLNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLkdkeipVNSRIVREVATLSRLQHQHVVRYYQAWFET-GVV 497
Cdd:cd14047    2 ERFRQDFKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVKL------NNEKAEREVKALAKLDHPNIVRYNGCWDGFdYDP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  498 DPFAGANWGSKTagssmfsysgavsteipeqdnnlesTYLYIQMEYCPR-TLRQVFE--SYNHFDKDFAWHLIRQIVEGL 574
Cdd:cd14047   76 ETSSSNSSRSKT-------------------------KCLFIQMEFCEKgTLESWIEkrNGEKLDKVLALEIFEQITKGV 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  575 AHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAkflkleqldqdggfsTDVAGSGVDSTGQaGTYFYTAPEiEQDWPKI 654
Cdd:cd14047  131 EYIHSKKLIHRDLKPSNIFLVDTGKVKIGDFGLV---------------TSLKNDGKRTKSK-GTLSYMSPE-QISSQDY 193
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30694992  655 DEKADMYSLGVVFFELWHPFGTAMERHVILTNLKlKGELPLKWVNEFPEQASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14047  194 GKEVDIYALGLILFELLHVCDSAFEKSKFWTDLR-NGILPDIFDKRYKIEKTIIKKMLSKKPEDRPNASEILRT 266
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
431-728 5.44e-54

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: 187.86  E-value: 5.44e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNsRIVREVATLSRLQHQHVVRYYqAWFETGvvdpfaganwgskta 510
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLLE-ELLREIEILKKLNHPNIVKLY-DVFETE--------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  511 gssmfsysgavsteipeqdnnlesTYLYIQMEYCPR-TLRQVFESYNH-FDKDFAWHLIRQIVEGLAHIHGQGIIHRDFT 588
Cdd:cd00180   64 ------------------------NFLYLVMEYCEGgSLKDLLKENKGpLSEEEALSILRQLLSALEYLHSNGIIHRDLK 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  589 PNNIFFDARNDIKIGDFGLAKFLKLEQLDQDGgfstdvagsgvdsTGQAGTYFYTAPEIEQDwPKIDEKADMYSLGVVFF 668
Cdd:cd00180  120 PENILLDSDGTVKLADFGLAKDLDSDDSLLKT-------------TGGTTPPYYAPPELLGG-RYYGPKVDIWSLGVILY 185
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  669 ELwhpfgtamerhviltnlklkgelplkwvnefPEQASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd00180  186 EL-------------------------------EELKDLIRRMLQYDPKKRPSAKELLEH 214
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
428-726 2.15e-52

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: 184.71  E-value: 2.15e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  428 LKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVN-SRIVREVATLSRLQHQHVVRYYQAWFETGVvdpfaganwg 506
Cdd:cd14014    5 VRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFrERFLREARALARLSHPNIVRVYDVGEDDGR---------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  507 sktagssmfsysgavsteipeqdnnlestyLYIQMEYCP-RTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHR 585
Cdd:cd14014   75 ------------------------------PYIVMEYVEgGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHR 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  586 DFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQDGGFstdvagsgvdstgqAGTYFYTAPEIEQDWPkIDEKADMYSLGV 665
Cdd:cd14014  125 DIKPANILLTEDGRVKLTDFGIARALGDSGLTQTGSV--------------LGTPAYMAPEQARGGP-VDPRSDIYSLGV 189
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30694992  666 VFFELW---HPFGTAMERHVILTNLKLKGELPLKWVNEFPEQ-ASLLRRLMSPSPSDRP-SATELL 726
Cdd:cd14014  190 VLYELLtgrPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPAlDAIILRALAKDPEERPqSAAELL 255
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
424-731 2.19e-52

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: 184.59  E-value: 2.19e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRL-----KDKEipvnsRIVREVATLSRLQHQHVVRYYQAWFETGvvd 498
Cdd:cd08215    1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLsnmseKERE-----EALNEVKLLSKLKHPNIVKYYESFEENG--- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  499 pfaganwgsktagssmfsysgavsteipeqdnnlestYLYIQMEYCP-RTLRQVFESYN----HFDKDFAWHLIRQIVEG 573
Cdd:cd08215   73 -------------------------------------KLCIVMEYADgGDLAQKIKKQKkkgqPFPEEQILDWFVQICLA 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  574 LAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleQLDQdggfSTDVAGSGVdstgqaGTYFYTAPEIEQDWPk 653
Cdd:cd08215  116 LKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISK-----VLES----TTDLAKTVV------GTPYYLSPELCENKP- 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  654 IDEKADMYSLGVVFFE---LWHPFgTAMERHVILTNLkLKGELPlkwvnEFPEQAS-----LLRRLMSPSPSDRPSATEL 725
Cdd:cd08215  180 YNYKSDIWALGCVLYElctLKHPF-EANNLPALVYKI-VKGQYP-----PIPSQYSselrdLVNSMLQKDPEKRPSANEI 252

                 ....*.
gi 30694992  726 LKHAFP 731
Cdd:cd08215  253 LSSPFI 258
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
422-727 2.83e-50

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 185.99  E-value: 2.83e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIR---LKDKEipVNSRIVREVATLSRLQHQHVVRYYqAWFEtgvvd 498
Cdd:COG0515    6 LGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRpelAADPE--ARERFRREARALARLNHPNIVRVY-DVGE----- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  499 pfaganwgsktagssmfsysgavsteipeqdnnlESTYLYIQMEYCP-RTLRQVFESYNHFDKDFAWHLIRQIVEGLAHI 577
Cdd:COG0515   78 ----------------------------------EDGRPYLVMEYVEgESLADLLRRRGPLPPAEALRILAQLAEALAAA 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  578 HGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQDGGFstdvagsgvdstgqAGTYFYTAPEIEQDwPKIDEK 657
Cdd:COG0515  124 HAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTQTGTV--------------VGTPGYMAPEQARG-EPVDPR 188
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30694992  658 ADMYSLGVVFFELW---HPFGTAMERHVILTNLKLKGELPLKWVNEFPEQ-ASLLRRLMSPSPSDRP-SATELLK 727
Cdd:COG0515  189 SDVYSLGVTLYELLtgrPPFDGDSPAELLRAHLREPPPPPSELRPDLPPAlDAIVLRALAKDPEERYqSAAELAA 263
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
429-730 7.69e-47

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: 168.85  E-value: 7.69e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYqawfetgvvdpfaganwgsk 508
Cdd:cd06606    6 ELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYL-------------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  509 taGSsmfsysgavsteipEQDNNlestYLYIQMEYCP-RTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDF 587
Cdd:cd06606   66 --GT--------------ERTEN----TLNIFLEYVPgGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDI 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  588 TPNNIFFDARNDIKIGDFGLAKflKLEQLDQDGGFSTdvagsgvdstgQAGTYFYTAPE-IEQDwpKIDEKADMYSLGVV 666
Cdd:cd06606  126 KGANILVDSDGVVKLADFGCAK--RLAEIATGEGTKS-----------LRGTPYWMAPEvIRGE--GYGRAADIWSLGCT 190
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30694992  667 FFEL------WHPFGTAMErhvILTNLKLKGELPlkwvnEFPEQAS-----LLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd06606  191 VIEMatgkppWSELGNPVA---ALFKIGSSGEPP-----PIPEHLSeeakdFLRKCLQRDPKKRPTADELLQHPF 257
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
424-728 2.11e-45

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: 164.57  E-value: 2.11e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYqAWFETGvvdpfaga 503
Cdd:cd05117    1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLY-EVFEDD-------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssmfsysgavsteipeqdnnlesTYLYIQMEYCP-RTLrqvFE---SYNHFDKDFAWHLIRQIVEGLAHIHG 579
Cdd:cd05117   72 -------------------------------KNLYLVMELCTgGEL---FDrivKKGSFSEREAAKIMKQILSAVAYLHS 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  580 QGIIHRDFTPNNIFFDARND---IKIGDFGLAKFLkleqldQDGGFSTDVagsgvdstgqAGTYFYTAPEIEQDwPKIDE 656
Cdd:cd05117  118 QGIVHRDLKPENILLASKDPdspIKIIDFGLAKIF------EEGEKLKTV----------CGTPYYVAPEVLKG-KGYGK 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  657 KADMYSLGVVFFEL---WHPFG--TAMErhvILTNLKlKGEL--PLKWVNEFPEQA-SLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd05117  181 KCDIWSLGVILYILlcgYPPFYgeTEQE---LFEKIL-KGKYsfDSPEWKNVSEEAkDLIKRLLVVDPKKRLTAAEALNH 256
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
424-728 2.87e-45

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: 163.84  E-value: 2.87e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAwFETgvvdpfaga 503
Cdd:cd14003    1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEV-IET--------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssmfsysgavsteipeqdnnleSTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGI 582
Cdd:cd14003   71 ------------------------------ENKIYLVMEYASGgELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGI 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  583 IHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLdqdggFSTdvagsgvdstgQAGTYFYTAPEIEQDWPKIDEKADMYS 662
Cdd:cd14003  121 VHRDLKLENILLDKNGNLKIIDFGLSNEFRGGSL-----LKT-----------FCGTPAYAAPEVLLGRKYDGPKADVWS 184
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30694992  663 LGVVFF-----ELwhPFGtamERHVILTNLK-LKGELPL-KWVNefPEQASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14003  185 LGVILYamltgYL--PFD---DDNDSKLFRKiLKGKYPIpSHLS--PDARDLIRRMLVVDPSKRITIEEILNH 250
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
424-728 1.88e-42

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: 156.00  E-value: 1.88e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRL-QHQHVVRYYQAWFETGvvdpfag 502
Cdd:cd13997    1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKKPFRGPKERARALREVEAHAALgQHPNIVRYYSSWEEGG------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgsktagssmfsysgavsteipeqdnnlestYLYIQMEYCPR-TLRQVFESY---NHFDKDFAWHLIRQIVEGLAHIH 578
Cdd:cd13997   74 ---------------------------------HLYIQMELCENgSLQDALEELspiSKLSEAEVWDLLLQVALGLAFIH 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  579 GQGIIHRDFTPNNIFFDARNDIKIGDFGLAkflkleqldqdggfsTDVAGSGVDSTGQAGtyfYTAPEIEQDWPKIDEKA 658
Cdd:cd13997  121 SKGIVHLDIKPDNIFISNKGTCKIGDFGLA---------------TRLETSGDVEEGDSR---YLAPELLNENYTHLPKA 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  659 DMYSLGVVFFELwhpfgtamerhviLTNLKL--KGELplkWVN------EFPEQASL---LRRL----MSPSPSDRPSAT 723
Cdd:cd13997  183 DIFSLGVTVYEA-------------ATGEPLprNGQQ---WQQlrqgklPLPPGLVLsqeLTRLlkvmLDPDPTRRPTAD 246

                 ....*
gi 30694992  724 ELLKH 728
Cdd:cd13997  247 QLLAH 251
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
424-730 4.74e-42

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: 154.67  E-value: 4.74e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIpvNSRIVREVATLSRLQHQHVVRYYQAWfetgvvdpfaga 503
Cdd:cd05122    1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEK--KESILNEIAILKKCKHPNIVKYYGSY------------ 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssmfsysgavsteipeqdnnLESTYLYIQMEYCPR-TLRQVFESYNH-FDKDFAWHLIRQIVEGLAHIHGQG 581
Cdd:cd05122   67 ----------------------------LKKDELWIVMEFCSGgSLKDLLKNTNKtLTEQQIAYVCKEVLKGLEYLHSHG 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqdggfstdvagSGVDSTGQAGTYFYTAPEIEQDWPkIDEKADMY 661
Cdd:cd05122  119 IIHRDIKAANILLTSDGEVKLIDFGLSAQLS----------------DGKTRNTFVGTPYWMAPEVIQGKP-YGFKADIW 181
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30694992  662 SLGVVFFEL------WHPFGT--AMERhvILTNL--KLKGelPLKWVNEFpeqASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd05122  182 SLGITAIEMaegkppYSELPPmkALFL--IATNGppGLRN--PKKWSKEF---KDFLKKCLQKDPEKRPTAEQLLKHPF 253
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
431-730 1.13e-41

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: 154.25  E-value: 1.13e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVK---KIRLKDKEIPVNSR---------IVREVATLSRLQHQHVVRYYQawfetgVVD 498
Cdd:cd14008    1 LGRGSFGKVKLALDTETGQLYAIKifnKSRLRKRREGKNDRgkiknalddVRREIAIMKKLDHPNIVRLYE------VID 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  499 pfaganwgsktagssmfsysgavsteIPEQDnnlestYLYIQMEYCPR-TL--RQVFESYNHFDKDFAWHLIRQIVEGLA 575
Cdd:cd14008   75 --------------------------DPESD------KLYLVLEYCEGgPVmeLDSGDRVPPLPEETARKYFRDLVLGLE 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  576 HIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLkleqldqdGGFSTDVAGSgvdstgqAGTYFYTAPEI--EQDWPK 653
Cdd:cd14008  123 YLHENGIVHRDIKPENLLLTADGTVKISDFGVSEMF--------EDGNDTLQKT-------AGTPAFLAPELcdGDSKTY 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  654 IDEKADMYSLGVVFFELWH---PFGTAMErhVILTNLKLKGELPLKWVNEF-PEQASLLRRLMSPSPSDRPSATELLKHA 729
Cdd:cd14008  188 SGKAADIWALGVTLYCLVFgrlPFNGDNI--LELYEAIQNQNDEFPIPPELsPELKDLLRRMLEKDPEKRITLKEIKEHP 265

                 .
gi 30694992  730 F 730
Cdd:cd14008  266 W 266
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
424-727 1.16e-41

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: 153.72  E-value: 1.16e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAWFETGVvdpfaga 503
Cdd:cd08529    1 DFEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGK------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssmfsysgavsteipeqdnnlestyLYIQMEYCPR-TLRQVFESY--NHFDKDFAWHLIRQIVEGLAHIHGQ 580
Cdd:cd08529   74 ---------------------------------LNIVMEYAENgDLHSLIKSQrgRPLPEDQIWKFFIQTLLGLSHLHSK 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFDARNDIKIGDFGLAKFLkleqldqdgGFSTDVAGSGVdstgqaGTYFYTAPEIEQDWPkIDEKADM 660
Cdd:cd08529  121 KILHRDIKSMNIFLDKGDNVKIGDLGVAKIL---------SDTTNFAQTIV------GTPYYLSPELCEDKP-YNEKSDV 184
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30694992  661 YSLGVVFFELW---HPFGTAMERHVILTNLKLKGE-LPLKWVnefPEQASLLRRLMSPSPSDRPSATELLK 727
Cdd:cd08529  185 WALGCVLYELCtgkHPFEAQNQGALILKIVRGKYPpISASYS---QDLSQLIDSCLTKDYRQRPDTTELLR 252
PLN02972 PLN02972
Histidyl-tRNA synthetase
796-1226 1.46e-38

Histidyl-tRNA synthetase


Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 155.43  E-value: 1.46e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   796 LRDYVVEITKEVFRQHCAKHLE--VIPMR--LLSDCPQFSRKTVKLLTNGGDMLELCYELRLPFVHWISVNQKSSFKRYE 871
Cdd:PLN02972  343 IREKAFSIITSVFKRHGATALDtpVFELRetLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKRYQ 422
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   872 ISHVYRRaighspPNPC-------LQADFDIVGGTLSL-TEAEVLKVIVDITTHIfHRGSCDIHLNHGDLLDAIWSWAGI 943
Cdd:PLN02972  423 IAKVYRR------DNPSkgryrefYQCDFDIAGVYEPMgPDFEIIKVLTELLDEL-DIGTYEVKLNHRKLLDGMLEICGV 495
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   944 KAEHRRKVAellSMMGSLRPQSSERklkwvfIRRQLLQELKLPEAVVNRLQT-VASRfcGDADQALPRLR--GALRADRP 1020
Cdd:PLN02972  496 PPEKFRTIC---SSIDKLDKQSFEQ------VKKEMVEEKGLSNETADKIGNfVKER--GPPLELLSKLRqeGSEFLGNA 564
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  1021 -TRKALDELSNLLTYLRVWRIEEHVHIDVLMPPTESYHRNLFFQ-VFLTKENSSgtsndgvlLAVGGRYDWLVQEVCDRE 1098
Cdd:PLN02972  565 sSRAALDELEIMFKALEKSKAIGKIVFDLSLARGLDYYTGVIYEaVFKGAQVGS--------IAAGGRYDNLVGMFSGKQ 636
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  1099 hkmnLPgAVGVSLALETIFQHLPMD-------LRPIRNEVSTSVLvcsrgGGGLLVQRMELVAELWEKSIKAEFVPTpdP 1171
Cdd:PLN02972  637 ----VP-AVGVSLGIERVFAIMEQQeeeksqvIRPTETEVLVSII-----GDDKLALAAELVSELWNAGIKAEYKVS--T 704
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 30694992  1172 SLTEQYEYANEHEIKCLVIITESGVAQNqieFVKVRHLELKKEKVVGREELVKFL 1226
Cdd:PLN02972  705 RKAKHLKRAKESGIPWMVLVGEKELSKG---FVKLKNLEAGVEEEVDRTCFVQEL 756
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
424-730 1.77e-38

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: 144.99  E-value: 1.77e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKI---RLKDKEipvNSRIVREVATLSRLQHQHVVRYYQAwfetgVVDPf 500
Cdd:cd08217    1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIdygKMSEKE---KQQLVSEVNILRELKHPNIVRYYDR-----IVDR- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  501 aganwgsktagssmfsysgavsteipeqdnnlESTYLYIQMEYCPR-TLRQVFESY----NHFDKDFAWHLIRQIVEGLA 575
Cdd:cd08217   72 --------------------------------ANTTLYIVMEYCEGgDLAQLIKKCkkenQYIPEEFIWKIFTQLLLALY 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  576 HIH-----GQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLkleqldqdgGFSTDVAGSGVdstgqaGTYFYTAPEIEQD 650
Cdd:cd08217  120 ECHnrsvgGGKILHRDLKPANIFLDSDNNVKLGDFGLARVL---------SHDSSFAKTYV------GTPYYMSPELLNE 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  651 WPkIDEKADMYSLGVVFFE---LWHPFgTAMErHVILTNLKLKGELPlkwvnEFPEQAS-----LLRRLMSPSPSDRPSA 722
Cdd:cd08217  185 QS-YDEKSDIWSLGCLIYElcaLHPPF-QAAN-QLELAKKIKEGKFP-----RIPSRYSselneVIKSMLNVDPDKRPSV 256

                 ....*...
gi 30694992  723 TELLKHAF 730
Cdd:cd08217  257 EELLQLPL 264
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
424-729 2.90e-38

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: 144.07  E-value: 2.90e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRL-----KDKEIPVNsrivrEVATLSRLQHQHVVRYYQAWFetgvvd 498
Cdd:cd08530    1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLgslsqKEREDSVN-----EIRLLASVNHPNIIRYKEAFL------ 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  499 pfaganwgsktagssmfsysgavsteipeqDNNLestyLYIQMEYCP-----RTLRQVFESYNHFDKDFAWHLIRQIVEG 573
Cdd:cd08530   70 ------------------------------DGNR----LCIVMEYAPfgdlsKLISKRKKKRRLFPEDDIWRIFIQMLRG 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  574 LAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqdggfstdvagSGVDSTgQAGTYFYTAPEIEQDWPk 653
Cdd:cd08530  116 LKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLK----------------KNLAKT-QIGTPLYAAPEVWKGRP- 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  654 IDEKADMYSLGVVFFELW---HPF-GTAMERhviLTNLKLKGELPLKWVNEFPEQASLLRRLMSPSPSDRPSATELLKHA 729
Cdd:cd08530  178 YDYKSDIWSLGCLLYEMAtfrPPFeARTMQE---LRYKVCRGKFPPIPPVYSQDLQQIIRSLLQVNPKKRPSCDKLLQSP 254
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
424-730 3.73e-38

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: 143.38  E-value: 3.73e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKD-KEIPVNSRIVREVATLSRLQHQHVVRYYqAWFEtgvvdpfag 502
Cdd:cd14007    1 DFEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQlQKSGLEHQLRREIEIQSHLRHPNILRLY-GYFE--------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgsktagssmfsysgavsteipeqdnnlESTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQG 581
Cdd:cd14007   71 ------------------------------DKKRIYLILEYAPNgELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKN 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGLAKFlkleqldqdggfstdvAGSGVDSTgQAGTYFYTAPEI--EQDWpkiDEKAD 659
Cdd:cd14007  121 IIHRDIKPENILLGSNGELKLADFGWSVH----------------APSNRRKT-FCGTLDYLPPEMveGKEY---DYKVD 180
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30694992  660 MYSLGVVFFELWH---PFgTAMERHVILTNLKlkgELPLKWVNEFPEQA-SLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14007  181 IWSLGVLCYELLVgkpPF-ESKSHQETYKRIQ---NVDIKFPSSVSPEAkDLISKLLQKDPSKRLSLEQVLNHPW 251
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
431-727 1.02e-36

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: 139.21  E-value: 1.02e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVvlCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYqawfetgvvdpfaganwgskta 510
Cdd:cd13999    1 IGSGSFGEV--YKGKWRGTDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFI---------------------- 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  511 gssmfsysGAVsteipeqdnnLESTYLYIQMEYCPR-TLRQVF-ESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFT 588
Cdd:cd13999   57 --------GAC----------LSPPPLCIVTEYMPGgSLYDLLhKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLK 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  589 PNNIFFDARNDIKIGDFGLAKFLkleqldqdggfstdvAGSGVDSTGQAGTYFYTAPE-IEQDwpKIDEKADMYSLGVVF 667
Cdd:cd13999  119 SLNILLDENFTVKIADFGLSRIK---------------NSTTEKMTGVVGTPRWMAPEvLRGE--PYTEKADVYSFGIVL 181
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30694992  668 FEL---WHPFGTAMERHVILTNLkLKGELPLKWVNEFPEQASLLRRLMSPSPSDRPSATELLK 727
Cdd:cd13999  182 WELltgEVPFKELSPIQIAAAVV-QKGLRPPIPPDCPPELSKLIKRCWNEDPEKRPSFSEIVK 243
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
425-730 1.98e-34

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: 132.74  E-value: 1.98e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDkeiPVNSRIVREVATLSRL----QHQHVVRYYqAWFETGvvdpf 500
Cdd:cd05118    1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDF---RHPKAALREIKLLKHLndveGHPNIVKLL-DVFEHR----- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  501 aganwgsktagssmfsysgavsteipeqdnnlESTYLYIQMEYCPRTLRQVFESYN-HFDKDFAWHLIRQIVEGLAHIHG 579
Cdd:cd05118   72 --------------------------------GGNHLCLVFELMGMNLYELIKDYPrGLPLDLIKSYLYQLLQALDFLHS 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  580 QGIIHRDFTPNNIFFDARN-DIKIGDFGLAKFlkleqLDQDggfstdvagsgvDSTGQAGTYFYTAPEIEQDWPKIDEKA 658
Cdd:cd05118  120 NGIIHRDLKPENILINLELgQLKLADFGLARS-----FTSP------------PYTPYVATRWYRAPEVLLGAKPYGSSI 182
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30694992  659 DMYSLGVVFFELW---HPFGTAMERHVILTNLKLKGElplkwvnefPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd05118  183 DIWSLGCILAELLtgrPLFPGDSEVDQLAKIVRLLGT---------PEALDLLSKMLKYDPAKRITASQALAHPY 248
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
432-730 2.15e-34

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: 133.20  E-value: 2.15e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  432 GQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYqawfetGVvdpfaganwgsktag 511
Cdd:cd06626    9 GEGTFGKVYTAVNLDTGELMAMKEIRFQDNDPKTIKEIADEMKVLEGLDHPNLVRYY------GV--------------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  512 ssmfsysgavstEIPEQDnnlestyLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPN 590
Cdd:cd06626   68 ------------EVHREE-------VYIFMEYCQEgTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPA 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  591 NIFFDARNDIKIGDFGLAKFLKleqldqdggfSTDVAGSGVDSTGQAGTYFYTAPEI--EQDWPKIDEKADMYSLGVVFF 668
Cdd:cd06626  129 NIFLDSNGLIKLGDFGSAVKLK----------NNTTTMAPGEVNSLVGTPAYMAPEVitGNKGEGHGRAADIWSLGCVVL 198
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30694992  669 EL------WHPFGT---------AMERHVILTNLKLKgelplkwvnefPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd06626  199 EMatgkrpWSELDNewaimyhvgMGHKPPIPDSLQLS-----------PEGKDFLSRCLESDPKKRPTASELLDHPF 264
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
425-730 3.48e-34

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: 132.99  E-value: 3.48e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKE--IPVNSriVREVATLSRLQHQHVVRYYqawfetgvvdpfag 502
Cdd:cd07829    1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDNEEegIPSTA--LREISLLKELKHPNIVKLL-------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgsktagssmfsysgavstEIPEQDNNLestylYIQMEYCPRTLRQVFESYN-HFDKDFAWHLIRQIVEGLAHIHGQG 581
Cdd:cd07829   65 ---------------------DVIHTENKL-----YLVFEYCDQDLKKYLDKRPgPLPPNLIKSIMYQLLRGLAYCHSHR 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDqdggFSTDVAgsgvdstgqagTYFYTAPEIEQDWPKIDEKADMY 661
Cdd:cd07829  119 ILHRDLKPQNLLINRDGVLKLADFGLARAFGIPLRT----YTHEVV-----------TLWYRAPEILLGSKHYSTAVDIW 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  662 SLGVVFFELW--HP-----------------FGTAMERHVI-LTNLKLKGELPLKWV---------NEFPEQASLLRRLM 712
Cdd:cd07829  184 SVGCIFAELItgKPlfpgdseidqlfkifqiLGTPTEESWPgVTKLPDYKPTFPKWPkndlekvlpRLDPEGIDLLSKML 263
                        330
                 ....*....|....*...
gi 30694992  713 SPSPSDRPSATELLKHAF 730
Cdd:cd07829  264 QYNPAKRISAKEALKHPY 281
RWD_RNF25 cd23818
RWD domain of RING finger protein 25 (RNF25) and related proteins; RNF25 (EC 2.3.2.27), also ...
35-146 3.74e-34

RWD domain of RING finger protein 25 (RNF25) and related proteins; RNF25 (EC 2.3.2.27), also known as AO7, is a putative E3 ubiquitin-protein ligase that was initially identified as an interacting protein of the E2 ubiquitin-conjugating enzyme, Ubc5B. It is ubiquitously expressed in various tissues and is predominantly localized in the nucleus. RNF25 activates nuclear factor (NF)-kappaB-dependent gene expression upon stimulation with interleukin-1 beta (IL-1beta), or tumor necrosis factor (TNF), or overexpression of NF-kappaB-inducing kinase. It interacts with the p65 transactivation domain (TAD) and modulates its transcriptional activity.


Pssm-ID: 467654  Cd Length: 109  Bit Score: 126.89  E-value: 3.74e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   35 LSEEITALSAIFQEDCKVVSDSRSPPQIAIKLRPYSKDMGyEDTDISAMLIVRCLPGYPYKCPKLQITPEQGLTTADAEK 114
Cdd:cd23818    1 LEEELEALEAIYPDELKVVSEDGAPTELSITLHPATADDE-SEQYVRLTLVITLPPGYPEEPPKISLRNPRGLSDARLAR 79
                         90       100       110
                 ....*....|....*....|....*....|..
gi 30694992  115 LLSLLEDQANSNAreGRVMIFNLVEAAQEFLS 146
Cdd:cd23818   80 LLSLLKELAEERA--GEPMLFELIELAKEFLT 109
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
425-728 3.72e-33

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: 128.97  E-value: 3.72e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRL-QHQHVVRYYQAWFETGVvdpfaga 503
Cdd:cd14050    3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDRKRKLEEVERHEKLgEHPNCVRFIKAWEEKGI------- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssmfsysgavsteipeqdnnlestyLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGII 583
Cdd:cd14050   76 ---------------------------------LYIQTELCDTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLI 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  584 HRDFTPNNIFFDARNDIKIGDFGLAkflkleqLDQDGGFSTDVagsgvdstgQAGTYFYTAPEIEQDWPKIdeKADMYSL 663
Cdd:cd14050  123 HLDIKPANIFLSKDGVCKLGDFGLV-------VELDKEDIHDA---------QEGDPRYMAPELLQGSFTK--AADIFSL 184
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30694992  664 GVVFFEL------------WHPFgtameRhviltnlklKGELPLKWVNEFP-EQASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14050  185 GITILELacnlelpsggdgWHQL-----R---------QGYLPEEFTAGLSpELRSIIKLMMDPDPERRPTAEDLLAL 248
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
429-730 3.84e-33

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: 129.70  E-value: 3.84e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLcKNKLDGRQYAVKKI-----RLKDKEIpvnsRIVREVAtlsrlQHQHVVRYYQAwfetgvvdpfaga 503
Cdd:cd13982    7 KVLGYGSEGTIVF-RGTFDGRPVAVKRLlpeffDFADREV----QLLRESD-----EHPNVIRYFCT------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssmfsysgavsteipEQDNNlestYLYIQMEYCPRTLRQVFESYNHFDKDF-----AWHLIRQIVEGLAHIH 578
Cdd:cd13982   64 -----------------------EKDRQ----FLYIALELCAASLQDLVESPRESKLFLrpglePVRLLRQIASGLAHLH 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  579 GQGIIHRDFTPNNIFFDARND-----IKIGDFGLAKflKLeqldqDGGFSTDVAGSGVdstgqAGTYFYTAPEI--EQDW 651
Cdd:cd13982  117 SLNIVHRDLKPQNILISTPNAhgnvrAMISDFGLCK--KL-----DVGRSSFSRRSGV-----AGTSGWIAPEMlsGSTK 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  652 PKIDEKADMYSLGVVFFELW----HPFGTAMER--HVILTNLKLKGELPLKwvNEFPEQASLLRRLMSPSPSDRPSATEL 725
Cdd:cd13982  185 RRQTRAVDIFSLGCVFYYVLsggsHPFGDKLEReaNILKGKYSLDKLLSLG--EHGPEAQDLIERMIDFDPEKRPSAEEV 262

                 ....*
gi 30694992  726 LKHAF 730
Cdd:cd13982  263 LNHPF 267
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
433-730 1.63e-32

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: 127.72  E-value: 1.63e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  433 QGGFGHVVLCKNKLDGRQYAVKKIRlKDKEIPVN--SRIVREVATLSRLQHQHVVRYYQAwfetgvvdpFAGANwgskta 510
Cdd:cd05579    3 RGAYGRVYLAKKKSTGDLYAIKVIK-KRDMIRKNqvDSVLAERNILSQAQNPFVVKLYYS---------FQGKK------ 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  511 gssmfsysgavsteipeqdnnlestYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTP 589
Cdd:cd05579   67 -------------------------NLYLVMEYLPGgDLYSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKP 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  590 NNIFFDARNDIKIGDFGLAKF-LKLEQLDQDGGFSTDVAGSgVDSTGQAGTYFYTAPEI--------EQDWpkidekadm 660
Cdd:cd05579  122 DNILIDANGHLKLTDFGLSKVgLVRRQIKLSIQKKSNGAPE-KEDRRIVGTPDYLAPEIllgqghgkTVDW--------- 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  661 YSLGVVFFEL---WHPFG--TAMErhvILTNLkLKGELPlkWVNEF---PEQASLLRRLMSPSPSDRP---SATELLKHA 729
Cdd:cd05579  192 WSLGVILYEFlvgIPPFHaeTPEE---IFQNI-LNGKIE--WPEDPevsDEAKDLISKLLTPDPEKRLgakGIEEIKNHP 265

                 .
gi 30694992  730 F 730
Cdd:cd05579  266 F 266
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
423-730 1.72e-32

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: 128.10  E-value: 1.72e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVK---KIRLKdKEIPVNSrIVREVATLSRLQHQHVVRYYQawfetgvvdp 499
Cdd:cd05581    1 NDFKFGKPLGEGSYSTVVLAKEKETGKEYAIKvldKRHII-KEKKVKY-VTIEKEVLSRLAHPGIVKLYY---------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  500 faganwgskTAgssmfsysgavsteipeQDnnleSTYLYIQMEYCP-RTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIH 578
Cdd:cd05581   69 ---------TF-----------------QD----ESKLYFVLEYAPnGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLH 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  579 GQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQdgGFSTDVAGSGVDSTGQA----GTYFYTAPEI--EQDWP 652
Cdd:cd05581  119 SKGIIHRDLKPENILLDEDMHIKITDFGTAKVLGPDSSPE--STKGDADSQIAYNQARAasfvGTAEYVSPELlnEKPAG 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  653 KideKADMYSLGVVFFELW---HPFGTAMERHVILTNLKLKGELPlkwvNEFPEQAS-LLRRLMSPSPSDRP------SA 722
Cdd:cd05581  197 K---SSDLWALGCIIYQMLtgkPPFRGSNEYLTFQKIVKLEYEFP----ENFPPDAKdLIQKLLVLDPSKRLgvnengGY 269

                 ....*...
gi 30694992  723 TELLKHAF 730
Cdd:cd05581  270 DELKAHPF 277
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
425-730 1.21e-31

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: 126.87  E-value: 1.21e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVryyqawfetGVVDPFagan 504
Cdd:cd07834    2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISNVFDDLIDAKRILREIKILRHLKHENII---------GLLDIL---- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysgavsteIPEQDNNLEStyLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIH 584
Cdd:cd07834   69 --------------------RPPSPEEFND--VYIVTELMETDLHKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIH 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  585 RDFTPNNIFFDARNDIKIGDFGLAKFLkleQLDQDGGFSTD-VAgsgvdstgqagTYFYTAPEIEQDWPKIDEKADMYSL 663
Cdd:cd07834  127 RDLKPSNILVNSNCDLKICDFGLARGV---DPDEDKGFLTEyVV-----------TRWYRAPELLLSSKKYTKAIDIWSV 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  664 GVVFFELW-------------------HPFGT-AMERHVILTNLKLKGEL-------PLKWVNEFP---EQA-SLLRRLM 712
Cdd:cd07834  193 GCIFAELLtrkplfpgrdyidqlnlivEVLGTpSEEDLKFISSEKARNYLkslpkkpKKPLSEVFPgasPEAiDLLEKML 272
                        330
                 ....*....|....*...
gi 30694992  713 SPSPSDRPSATELLKHAF 730
Cdd:cd07834  273 VFNPKKRITADEALAHPY 290
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
423-730 5.43e-31

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: 123.09  E-value: 5.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIpVNSRIVREVATLSRLQHQHVVRYYQAWFETGVVdpfag 502
Cdd:cd06623    1 SDLERVKVLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEE-FRKQLLRELKTLRSCESPYVVKCYGAFYKEGEI----- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgsktagssmfsysgavsteipeqdnnlestylYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQ- 580
Cdd:cd06623   75 -----------------------------------SIVLEYMDGgSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTKr 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFDARNDIKIGDFGLAKFlkLEQldqdggfSTDVAGSGVdstgqaGTYFYTAPEieqdwpKIDEK--- 657
Cdd:cd06623  120 HIIHRDIKPSNLLINSKGEVKIADFGISKV--LEN-------TLDQCNTFV------GTVTYMSPE------RIQGEsys 178
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  658 --ADMYSLGVVFFELW---HPF---GT----AMERHViltnlkLKGELPLKWVNEF-PEQASLLRRLMSPSPSDRPSATE 724
Cdd:cd06623  179 yaADIWSLGLTLLECAlgkFPFlppGQpsffELMQAI------CDGPPPSLPAEEFsPEFRDFISACLQKDPKKRPSAAE 252

                 ....*.
gi 30694992  725 LLKHAF 730
Cdd:cd06623  253 LLQHPF 258
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
429-730 5.75e-31

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: 123.05  E-value: 5.75e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVN-SRIVREVATLSRLQHQHVVRYYQAwFEtgvvdpfaganwgs 507
Cdd:cd14099    7 KFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKPKQrEKLKSEIKIHRSLKHPNIVKFHDC-FE-------------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 ktagssmfsysgavsteipeqDNNlestYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRD 586
Cdd:cd14099   72 ---------------------DEE----NVYILLELCSNgSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRD 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  587 FTPNNIFFDARNDIKIGDFGLAKflkleQLDQDGGFSTDVagsgvdstgqAGTYFYTAPEIEQDWPKIDEKADMYSLGVV 666
Cdd:cd14099  127 LKLGNLFLDENMNVKIGDFGLAA-----RLEYDGERKKTL----------CGTPNYIAPEVLEKKKGHSFEVDIWSLGVI 191
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30694992  667 FFELW---HPFGTAmERHVILTNLKlKGELplkwvnEFPEQA-------SLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14099  192 LYTLLvgkPPFETS-DVKETYKRIK-KNEY------SFPSHLsisdeakDLIRSMLQPDPTKRPSLDEILSHPF 257
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
431-730 6.20e-31

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: 123.03  E-value: 6.20e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRL-------KDKEIPVNSRIVREVATLSRLQHQHVVRYYqawfetgvvdpfaga 503
Cdd:cd06628    8 IGSGSFGSVYLGMNASSGELMAVKQVELpsvsaenKDRKKSMLDALQREIALLRELQHENIVQYL--------------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssmfsysgavsteipeqDNNLESTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGI 582
Cdd:cd06628   73 -------------------------GSSSDANHLNIFLEYVPGgSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGI 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  583 IHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLdqdggfstdVAGSGVDSTGQAGTYFYTAPEIEQDwPKIDEKADMYS 662
Cdd:cd06628  128 IHRDIKGANILVDNKGGIKISDFGISKKLEANSL---------STKNNGARPSLQGSVFWMAPEVVKQ-TSYTRKADIWS 197
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30694992  663 LGVVFFELW---HPFGTAMERHVIltnLKLkGELPLKwvnEFPEQAS-----LLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd06628  198 LGCLVVEMLtgtHPFPDCTQMQAI---FKI-GENASP---TIPSNISseardFLEKTFEIDHNKRPTADELLKHPF 266
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
425-730 9.94e-31

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: 122.32  E-value: 9.94e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIpvnSRIVREVATLSRLQHQHVVRYYQawfetgvvdpfagan 504
Cdd:cd06614    2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQNK---ELIINEILIMKECKHPNIVDYYD--------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfSYsgavsteipeqdnnLESTYLYIQMEYCPR-TLRQVFEsynHFDKDFAWHLI----RQIVEGLAHIHG 579
Cdd:cd06614   64 -----------SY--------------LVGDELWVVMEYMDGgSLTDIIT---QNPVRMNESQIayvcREVLQGLEYLHS 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  580 QGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQdggfstdvagsgvdsTGQAGTYFYTAPEI--EQDWpkiDEK 657
Cdd:cd06614  116 QNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKSKR---------------NSVVGTPYWMAPEVikRKDY---GPK 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  658 ADMYSLGVVFFEL------WHPFGTAMERHVILTNL--KLKGelPLKWVNEFPEqasLLRRLMSPSPSDRPSATELLKHA 729
Cdd:cd06614  178 VDIWSLGIMCIEMaegeppYLEEPPLRALFLITTKGipPLKN--PEKWSPEFKD---FLNKCLVKDPEKRPSAEELLQHP 252

                 .
gi 30694992  730 F 730
Cdd:cd06614  253 F 253
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
423-730 1.44e-30

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: 122.81  E-value: 1.44e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAwfetgvvdpfag 502
Cdd:cd07833    1 NKYEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKESEDDEDVKKTALREVKVLRQLRHENIVNLKEA------------ 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgsktagssmFSYSGAvsteipeqdnnlestyLYIQMEYCPRTLRQVFESY-NHFDKDFAWHLIRQIVEGLAHIHGQG 581
Cdd:cd07833   69 ------------FRRKGR----------------LYLVFEYVERTLLELLEASpGGLPPDAVRSYIWQLLQAIAYCHSHN 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqdggfstdvAGSGVDSTGQAGTYFYTAPEIEQDWPKIDEKADMY 661
Cdd:cd07833  121 IIHRDIKPENILVSESGVLKLCDFGFARALT--------------ARPASPLTDYVATRWYRAPELLVGDTNYGKPVDVW 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  662 SLGVVFFE----------------LWH---PFGTAMERHVIL--TNLKLKGE----------LPLKWVNEFPEQA-SLLR 709
Cdd:cd07833  187 AIGCIMAElldgeplfpgdsdidqLYLiqkCLGPLPPSHQELfsSNPRFAGVafpepsqpesLERRYPGKVSSPAlDFLK 266
                        330       340
                 ....*....|....*....|.
gi 30694992  710 RLMSPSPSDRPSATELLKHAF 730
Cdd:cd07833  267 ACLRMDPKERLTCDELLQHPY 287
Pkinase pfam00069
Protein kinase domain;
425-730 1.93e-30

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 120.04  E-value: 1.93e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992    425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAWfetgvvdpfagan 504
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAF------------- 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992    505 wgsktagssmfsysgavsteipeqdnnLESTYLYIQMEYCP-RTLRQVFESYNHFDKDFAWHLIRQIVEGLAhihgqgii 583
Cdd:pfam00069   68 ---------------------------EDKDNLYLVLEYVEgGSLFDLLSEKGAFSEREAKFIMKQILEGLE-------- 112
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992    584 hrdftpnniffdarndikigdfglakflkleqldqdggfstdvagSGVDSTGQAGTYFYTAPEIEQDwPKIDEKADMYSL 663
Cdd:pfam00069  113 ---------------------------------------------SGSSLTTFVGTPWYMAPEVLGG-NPYGPKVDVWSL 146
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992    664 GVVFFELW---HPFGTAMERHVILTNLKLKGELPLKWVNEFPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:pfam00069  147 GCILYELLtgkPPFPGINGNEIYELIIDQPYAFPELPSNLSEEAKDLLKKLLKKDPSKRLTATQALQHPW 216
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
425-730 2.02e-30

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: 121.22  E-value: 2.02e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAWFETGvvdpfagan 504
Cdd:cd08225    2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENG--------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysgavsteipeqdnnlestYLYIQMEYC------PRTLRQ---VFESynhfDKDFAWHLirQIVEGLA 575
Cdd:cd08225   73 -------------------------------RLFIVMEYCdggdlmKRINRQrgvLFSE----DQILSWFV--QISLGLK 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  576 HIHGQGIIHRDFTPNNIFFDARNDI-KIGDFGLAKflkleQLDQdggfSTDVAGSGVdstgqaGTYFYTAPEIEQDWPkI 654
Cdd:cd08225  116 HIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIAR-----QLND----SMELAYTCV------GTPYYLSPEICQNRP-Y 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  655 DEKADMYSLGVVFFELW---HPFGTAMERHVIltnLKL-KGELPLKWVNEFPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd08225  180 NNKTDIWSLGCVLYELCtlkHPFEGNNLHQLV---LKIcQGYFAPISPNFSRDLRSLISQLFKVSPRDRPSITSILKRPF 256
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
431-730 2.83e-30

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: 121.33  E-value: 2.83e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRL--------KDKEIPVNSRIVREVATLSRLQHQHVVRYYQawFETGvvdpfag 502
Cdd:cd06629    9 IGKGTYGRVYLAMNATTGEMLAVKQVELpktssdraDSRQKTVVDALKSEIDTLKDLDHPNIVQYLG--FEET------- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgsktagssmfsysgavsteipeqdnnleSTYLYIQMEYCP-----RTLRQvfesYNHFDKDFAWHLIRQIVEGLAHI 577
Cdd:cd06629   80 -------------------------------EDYFSIFLEYVPggsigSCLRK----YGKFEEDLVRFFTRQILDGLAYL 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  578 HGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleqldqdggFSTDVAGSGVDSTGQaGTYFYTAPE-IEQDWPKIDE 656
Cdd:cd06629  125 HSKGILHRDLKADNILVDLEGICKISDFGISK------------KSDDIYGNNGATSMQ-GSVFWMAPEvIHSQGQGYSA 191
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30694992  657 KADMYSLGVVFFELW---HPFGTAMERHVILTNLKLKGELPLKW-VNEFPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd06629  192 KVDIWSLGCVVLEMLagrRPWSDDEAIAAMFKLGNKRSAPPVPEdVNLSPEALDFLNACFAIDPRDRPTAAELLSHPF 269
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
425-730 1.21e-29

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: 119.15  E-value: 1.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKI---RLKDKEIPvNSRivREVATLSRLQHQHVVRYYQAwFEtgvvdpfa 501
Cdd:cd08218    2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEInisKMSPKERE-ESR--KEVAVLSKMKHPNIVQYQES-FE-------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 ganwgsktagssmfsysgavsteipeqdnnlESTYLYIQMEYCPRTlrQVFESYNH-----FDKDFAWHLIRQIVEGLAH 576
Cdd:cd08218   70 -------------------------------ENGNLYIVMDYCDGG--DLYKRINAqrgvlFPEDQILDWFVQLCLALKH 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  577 IHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqdggfstdvagsgvdSTGQ-----AGTYFYTAPEIEQDW 651
Cdd:cd08218  117 VHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLN--------------------STVElartcIGTPYYLSPEICENK 176
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  652 PkIDEKADMYSLGVVFFE---LWHPFGTAMERHVILTnlKLKGELPLKWVNEFPEQASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd08218  177 P-YNNKSDIWALGCVLYEmctLKHAFEAGNMKNLVLK--IIRGSYPPVPSRYSYDLRSLVSQLFKRNPRDRPSINSILEK 253

                 ..
gi 30694992  729 AF 730
Cdd:cd08218  254 PF 255
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
431-730 1.77e-29

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: 118.39  E-value: 1.77e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIR----LKDKEIPvnsRIVREVATLSRLQHQHVVRYYQAWfetgvvdpfaganwg 506
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKVLRkkeiIKRKEVE---HTLNERNILERVNHPFIVKLHYAF--------------- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  507 sktagssmfsysgavsteipeQDNNlestYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHR 585
Cdd:cd05123   63 ---------------------QTEE----KLYLVLDYVPGgELFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYR 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  586 DFTPNNIFFDARNDIKIGDFGLAKflkleqldqdggfstdVAGSGVDSTGQ-AGTYFYTAPEIEQ--------DWpkide 656
Cdd:cd05123  118 DLKPENILLDSDGHIKLTDFGLAK----------------ELSSDGDRTYTfCGTPEYLAPEVLLgkgygkavDW----- 176
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  657 kadmYSLGVVFFEL---WHPFgTAMERHVILTNLKlkgELPLKWVNEFPEQA-SLLRRLMSPSPSDR---PSATELLKHA 729
Cdd:cd05123  177 ----WSLGVLLYEMltgKPPF-YAENRKEIYEKIL---KSPLKFPEYVSPEAkSLISGLLQKDPTKRlgsGGAEEIKAHP 248

                 .
gi 30694992  730 F 730
Cdd:cd05123  249 F 249
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
431-730 2.95e-29

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: 118.18  E-value: 2.95e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLC--KNKLDGRQYAVKKIRLKDKEIPVN---SRIVREVATLSRLQHQHVVRyyqawfetgVVDPfaganw 505
Cdd:cd13994    1 IGKGATSVVRIVtkKNPRSGVLYAVKEYRRRDDESKRKdyvKRLTSEYIISSKLHHPNIVK---------VLDL------ 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  506 gsktagssmfsysgavsteipeqDNNLESTYLYIqMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIH 584
Cdd:cd13994   66 -----------------------CQDLHGKWCLV-MEYCPGgDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAH 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  585 RDFTPNNIFFDARNDIKIGDFGLAkflkleqldqdggfstDVAGSGVDST-----GQAGTYFYTAPEIEQDWPKIDEKAD 659
Cdd:cd13994  122 RDLKPENILLDEDGVLKLTDFGTA----------------EVFGMPAEKEspmsaGLCGSEPYMAPEVFTSGSYDGRAVD 185
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30694992  660 MYSLGVVFFELW---HPFGTAMERHVI----LTNLKLKGELPLKWVNEFPEQA-SLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd13994  186 VWSCGIVLFALFtgrFPWRSAKKSDSAykayEKSGDFTNGPYEPIENLLPSECrRLIYRMLHPDPEKRITIDEALNDPW 264
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
431-730 3.47e-29

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: 117.89  E-value: 3.47e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRLKD---KEIPVNSRIVREVATLSRLQHQHVVRYYqawfetgvvdpfaganwGS 507
Cdd:cd06632    8 LGSGSFGSVYEGFNGDTGDFFAVKEVSLVDddkKSRESVKQLEQEIALLSKLRHPNIVQYY-----------------GT 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 KTAGSSmfsysgavsteipeqdnnlestyLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRD 586
Cdd:cd06632   71 EREEDN-----------------------LYIFLEYVPGgSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRD 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  587 FTPNNIFFDARNDIKIGDFGLAKFLKleqldqdgGFSTdvAGSGVdstgqaGTYFYTAPE-IEQDWPKIDEKADMYSLGV 665
Cdd:cd06632  128 IKGANILVDTNGVVKLADFGMAKHVE--------AFSF--AKSFK------GSPYWMAPEvIMQKNSGYGLAVDIWSLGC 191
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30694992  666 VFFEL------WHPFgtamERHVILTNLKLKGELPlkwvnEFPEQASL-----LRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd06632  192 TVLEMatgkppWSQY----EGVAAIFKIGNSGELP-----PIPDHLSPdakdfIRLCLQRDPEDRPTASQLLEHPF 258
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
425-730 5.77e-29

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: 118.37  E-value: 5.77e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIrLKDKEIpvnsrIVREVATLSRLQHQHVVRYYqawfetgvvdpfagan 504
Cdd:cd14137    6 YTIEKVIGSGSFGVVYQAKLLETGEVVAIKKV-LQDKRY-----KNRELQIMRRLKHPNIVKLK---------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssMFSYSgavsteipeQDNNLESTYLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIR----QIVEGLAHIHGQ 580
Cdd:cd14137   64 ---------YFFYS---------SGEKKDEVYLNLVMEYMPETLYRVIRHYSKNKQTIPIIYVKlysyQLFRGLAYLHSL 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFDARN-DIKIGDFGLAKFLKleqldqdggfstdvagSGVDSTGQAGTYFYTAPEIEQDWPKIDEKAD 659
Cdd:cd14137  126 GICHRDIKPQNLLVDPETgVLKLCDFGSAKRLV----------------PGEPNVSYICSRYYRAPELIFGATDYTTAID 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  660 MYSLGVVFFELW--HP-----------------FGT-------AMERHVILTNL-KLKGeLPLKWV---NEFPEQASLLR 709
Cdd:cd14137  190 IWSAGCVLAELLlgQPlfpgessvdqlveiikvLGTptreqikAMNPNYTEFKFpQIKP-HPWEKVfpkRTPPDAIDLLS 268
                        330       340
                 ....*....|....*....|.
gi 30694992  710 RLMSPSPSDRPSATELLKHAF 730
Cdd:cd14137  269 KILVYNPSKRLTALEALAHPF 289
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
424-726 2.78e-28

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: 115.07  E-value: 2.78e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPV-NSRivREVATLSRLQHQHVVRYYQAWFETGvvdpfag 502
Cdd:cd08219    1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSSAVeDSR--KEAVLLAKMKHPNIVAFKESFEADG------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgsktagssmfsysgavsteipeqdnnlestYLYIQMEYCP--RTLRQVFESYNH-FDKDFAWHLIRQIVEGLAHIHG 579
Cdd:cd08219   72 ---------------------------------HLYIVMEYCDggDLMQKIKLQRGKlFPEDTILQWFVQMCLGVQHIHE 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  580 QGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLkleqldqdggfstdvAGSGVDSTGQAGTYFYTAPEIEQDWPkIDEKAD 659
Cdd:cd08219  119 KRVLHRDIKSKNIFLTQNGKVKLGDFGSARLL---------------TSPGAYACTYVGTPYYVPPEIWENMP-YNNKSD 182
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30694992  660 MYSLGVVFFELW---HPFGTAMERHVILTNLK-LKGELPLKWVNEFpeqASLLRRLMSPSPSDRPSATELL 726
Cdd:cd08219  183 IWSLGCILYELCtlkHPFQANSWKNLILKVCQgSYKPLPSHYSYEL---RSLIKQMFKRNPRSRPSATTIL 250
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
431-730 5.03e-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: 114.24  E-value: 5.03e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYqawfetgvvdpfaganwgskta 510
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKLQENLESEIAILKSIKHPNIVRLY---------------------- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  511 gssmfsysgavstEIPEqdnnlESTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTP 589
Cdd:cd14009   59 -------------DVQK-----TEDFIYLVLEYCAGgDLSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKP 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  590 NNIFFDARND---IKIGDFGLAKFLkleqldQDGGFSTDVAGSGvdstgqagtyFYTAPEIEQdWPKIDEKADMYSLGVV 666
Cdd:cd14009  121 QNLLLSTSGDdpvLKIADFGFARSL------QPASMAETLCGSP----------LYMAPEILQ-FQKYDAKADLWSVGAI 183
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30694992  667 FFELWH---PFGTAmeRHV-ILTNLKlKGELPLKW---VNEFPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14009  184 LFEMLVgkpPFRGS--NHVqLLRNIE-RSDAVIPFpiaAQLSPDCKDLLRRLLRRDPAERISFEEFFAHPF 251
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
431-728 5.45e-28

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: 114.24  E-value: 5.45e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYqawfetgvvdpfaganwgskta 510
Cdd:cd06627    8 IGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYI---------------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  511 gssmfsysGAVSTEipeqdnnlesTYLYIQMEYCP-RTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTP 589
Cdd:cd06627   66 --------GSVKTK----------DSLYIILEYVEnGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKG 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  590 NNIFFDARNDIKIGDFGLAkfLKLEQLDQDggfSTDVagsgvdstgqAGTYFYTAPE-IEQDwpKIDEKADMYSLGVVFF 668
Cdd:cd06627  128 ANILTTKDGLVKLADFGVA--TKLNEVEKD---ENSV----------VGTPYWMAPEvIEMS--GVTTASDIWSVGCTVI 190
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30694992  669 ELW---------HPFgTAMERHVILTnlklkgELPLkwvnefPEQAS-----LLRRLMSPSPSDRPSATELLKH 728
Cdd:cd06627  191 ELLtgnppyydlQPM-AALFRIVQDD------HPPL------PENISpelrdFLLQCFQKDPTLRPSAKELLKH 251
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
423-728 5.99e-28

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: 114.35  E-value: 5.99e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYqawfetgvvdpfag 502
Cdd:cd14069    1 EDWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDCPENIKKEVCIQKMLSHKNVVRFY-------------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgsktagssmfsysgavsteipeqDNNLESTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQG 581
Cdd:cd14069   67 --------------------------GHRREGEFQYLFLEYASGgELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCG 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqdggfstdVAGSGVDSTGQAGTYFYTAPEIEQDWPKIDEKADMY 661
Cdd:cd14069  121 ITHRDIKPENLLLDENDNLKISDFGLATVFR-------------YKGKERLLNKMCGTLPYVAPELLAKKKYRAEPVDVW 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  662 SLGVVFFelwhpfgtAMerhviltnlkLKGELP-----------LKWV-NEFPEQA----------SLLRRLMSPSPSDR 719
Cdd:cd14069  188 SCGIVLF--------AM----------LAGELPwdqpsdscqeySDWKeNKKTYLTpwkkidtaalSLLRKILTENPNKR 249

                 ....*....
gi 30694992  720 PSATELLKH 728
Cdd:cd14069  250 ITIEDIKKH 258
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
427-726 9.46e-28

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: 113.97  E-value: 9.46e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  427 ELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDkeIPVNSRIVREVATLSRL-QHQHVVRYYqawfetgvvdpfaganw 505
Cdd:cd13985    4 VTKQLGEGGFSYVYLAHDVNTGRRYALKRMYFND--EEQLRVAIKEIEIMKRLcGHPNIVQYY----------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  506 gsktagssmfsySGAVSTEIPEQDnnlestyLYIQMEYCPRTLRQVFESY--NHFDKDFAWHLIRQIVEGLAHIHGQG-- 581
Cdd:cd13985   65 ------------DSAILSSEGRKE-------VLLLMEYCPGSLVDILEKSppSPLSEEEVLRIFYQICQAVGHLHSQSpp 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQDGgfstdvAGSGVDSTGQAGTYFYTAPEIEQDWPK--IDEKAD 659
Cdd:cd13985  126 IIHRDIKIENILFSNTGRFKLCDFGSATTEHYPLERAEE------VNIIEEEIQKNTTPMYRAPEMIDLYSKkpIGEKAD 199
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  660 MYSLGVVFFELW---HPFgtamERHVILTNLKLKGELPlKWVNEFPEQASLLRRLMSPSPSDRPSATELL 726
Cdd:cd13985  200 IWALGCLLYKLCffkLPF----DESSKLAIVAGKYSIP-EQPRYSPELHDLIRHMLTPDPAERPDIFQVI 264
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
423-730 1.17e-27

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: 113.88  E-value: 1.17e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSrIVREVATLSRLQHQHVVRYYqawfetgvvdpfag 502
Cdd:cd06609    1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEEAEDEIED-IQQEIQFLSQCDSPYITKYY-------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwGSKTAGSSmfsysgavsteipeqdnnlestyLYIQMEYCPR-TLRQVFESYNhFDKDFAWHLIRQIVEGLAHIHGQG 581
Cdd:cd06609   66 ---GSFLKGSK-----------------------LWIIMEYCGGgSVLDLLKPGP-LDETYIAFILREVLLGLEYLHSEG 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQDggfsTDVagsgvdstgqaGTYFYTAPE-IEQDwpKIDEKADM 660
Cdd:cd06609  119 KIHRDIKAANILLSEEGDVKLADFGVSGQLTSTMSKRN----TFV-----------GTPFWMAPEvIKQS--GYDEKADI 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  661 YSLGVVFFELwhpfgtamerhviltnlkLKGELPL------KWVNEFPEQA--SLLRRLMSPS------------PSDRP 720
Cdd:cd06609  182 WSLGITAIEL------------------AKGEPPLsdlhpmRVLFLIPKNNppSLEGNKFSKPfkdfvelclnkdPKERP 243
                        330
                 ....*....|
gi 30694992  721 SATELLKHAF 730
Cdd:cd06609  244 SAKELLKHKF 253
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
431-719 1.73e-27

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: 113.09  E-value: 1.73e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRlkdKEIPVNSR----IVREVATLSRLQHQHVVRYYQawfetgvvdpfaganwg 506
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTFALKCVK---KRHIVQTRqqehIFSEKEILEECNSPFIVKLYR----------------- 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  507 sktagssmfSYsgavsteipeQDNNlestYLYIQMEYCP-RTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHR 585
Cdd:cd05572   61 ---------TF----------KDKK----YLYMLMEYCLgGELWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYR 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  586 DFTPNNIFFDARNDIKIGDFGLAKflkleqldqdggfstdVAGSGVDSTGQAGTYFYTAPEIeqdwpkIDEK-----ADM 660
Cdd:cd05572  118 DLKPENLLLDSNGYVKLVDFGFAK----------------KLGSGRKTWTFCGTPEYVAPEI------ILNKgydfsVDY 175
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30694992  661 YSLGVVFFELWH---PFGTAMERHVILTNLKLKGELPLkwvnEFPEQAS-----LLRRLMSPSPSDR 719
Cdd:cd05572  176 WSLGILLYELLTgrpPFGGDDEDPMKIYNIILKGIDKI----EFPKYIDknaknLIKQLLRRNPEER 238
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
423-730 5.62e-27

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: 113.92  E-value: 5.62e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIR----LKDKEIpVNSRIVREVatLSRLQHQHVVRYYQAWfetgvvd 498
Cdd:cd05573    1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRksdmLKREQI-AHVRAERDI--LADADSPWIVRLHYAF------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  499 pfaganwgsktagssmfsysgavsteipeQDNNlestYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHI 577
Cdd:cd05573   71 -----------------------------QDED----HLYLVMEYMPGgDLMNLLIKYDVFPEETARFYIAELVLALDSL 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  578 HGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLK--------------LEQLDQDGGFSTDVAGSGVDSTGQAGTYFYT 643
Cdd:cd05573  118 HKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMNksgdresylndsvnTLFQDNVLARRRPHKQRRVRAYSAVGTPDYI 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  644 APEIEQDWPkIDEKADMYSLGVVFFELWH---PFgtaMERHVILTNLKLkgelpLKWVNEF---------PEQASLLRRL 711
Cdd:cd05573  198 APEVLRGTG-YGPECDWWSLGVILYEMLYgfpPF---YSDSLVETYSKI-----MNWKESLvfpddpdvsPEAIDLIRRL 268
                        330       340
                 ....*....|....*....|
gi 30694992  712 MSpSPSDR-PSATELLKHAF 730
Cdd:cd05573  269 LC-DPEDRlGSAEEIKAHPF 287
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
431-730 7.52e-27

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: 111.64  E-value: 7.52e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRL-----KDKEIPVNSRIVREVATLSRLQHQHVVRYYqawfetgvvDPFaganw 505
Cdd:cd13990    8 LGKGGFSEVYKAFDLVEQRYVACKIHQLnkdwsEEKKQNYIKHALREYEIHKSLDHPRIVKLY---------DVF----- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  506 gsktagssmfsysgavsteipEQDNNLESTYlyiqMEYCPRT-LRQVFESYNHFDKDFAWHLIRQIVEGLAHI--HGQGI 582
Cdd:cd13990   74 ---------------------EIDTDSFCTV----LEYCDGNdLDFYLKQHKSIPEREARSIIMQVVSALKYLneIKPPI 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  583 IHRDFTPNNIFFDARN---DIKIGDFGLAKflkleQLDQDggfstDVAGSGVDSTGQ-AGTYFYTAPEI---EQDWPKID 655
Cdd:cd13990  129 IHYDLKPGNILLHSGNvsgEIKITDFGLSK-----IMDDE-----SYNSDGMELTSQgAGTYWYLPPECfvvGKTPPKIS 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  656 EKADMYSLGVVFFELWH---PFGTAMERHVILTNL----KLKGELPLKwvnefP----EQASLLRRLMSPSPSDRPSATE 724
Cdd:cd13990  199 SKVDVWSVGVIFYQMLYgrkPFGHNQSQEAILEENtilkATEVEFPSK-----PvvssEAKDFIRRCLTYRKEDRPDVLQ 273

                 ....*.
gi 30694992  725 LLKHAF 730
Cdd:cd13990  274 LANDPY 279
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
424-730 1.30e-26

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: 111.27  E-value: 1.30e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQ-HQHVVRyyqawfetgVVDPFag 502
Cdd:cd07832    1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEGGIPNQALREIKALQACQgHPYVVK---------LRDVF-- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgsktagssmfsysgavsteipeqdnnLESTYLYIQMEYCPRTLRQVFESYNH-FDKDFAWHLIRQIVEGLAHIHGQG 581
Cdd:cd07832   70 -----------------------------PHGTGFVLVFEYMLSSLSEVLRDEERpLTEAQVKRYMRMLLKGVAYMHANR 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqdggfstdvAGSGVDSTGQAGTYFYTAPEIEQDWPKIDEKADMY 661
Cdd:cd07832  121 IMHRDLKPANLLISSTGVLKIADFGLARLFS--------------EEDPRLYSHQVATRWYRAPELLYGSRKYDEGVDLW 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  662 SLGVVFFELWH-----PFGTAME------RHVILTNLKLKGEL---------------PLKWVNEFP----EQASLLRRL 711
Cdd:cd07832  187 AVGCIFAELLNgsplfPGENDIEqlaivlRTLGTPNEKTWPELtslpdynkitfpeskGIRLEEIFPdcspEAIDLLKGL 266
                        330
                 ....*....|....*....
gi 30694992  712 MSPSPSDRPSATELLKHAF 730
Cdd:cd07832  267 LVYNPKKRLSAEEALRHPY 285
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
423-730 1.83e-26

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: 109.66  E-value: 1.83e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKdkeiPVNSRIVREVATLSRLQHQHVVRYYQAWFetgvvdpfag 502
Cdd:cd06612    3 EVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVE----EDLQEIIKEISILKQCDSPYIVKYYGSYF---------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgsktagssmfsysgavsteipeQDNNLestylYIQMEYCPR-TLRQVFESYNH-FDKDFAWHLIRQIVEGLAHIHGQ 580
Cdd:cd06612   69 -------------------------KNTDL-----WIVMEYCGAgSVSDIMKITNKtLTEEEIAAILYQTLKGLEYLHSN 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFDARNDIKIGDFGlakflkleqldqdggfstdVAGSGVDSTGQAGTY----FYTAPEIEQDwPKIDE 656
Cdd:cd06612  119 KKIHRDIKAGNILLNEEGQAKLADFG-------------------VSGQLTDTMAKRNTVigtpFWMAPEVIQE-IGYNN 178
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  657 KADMYSLGVVFFEL---------WHPFgTAMerHVILTNLKLKGELPLKWVNEFpeqASLLRRLMSPSPSDRPSATELLK 727
Cdd:cd06612  179 KADIWSLGITAIEMaegkppysdIHPM-RAI--FMIPNKPPPTLSDPEKWSPEF---NDFVKKCLVKDPEERPSAIQLLQ 252

                 ...
gi 30694992  728 HAF 730
Cdd:cd06612  253 HPF 255
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
429-730 1.96e-26

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


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 109.75  E-value: 1.96e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKLDGRQYAVKKIRLkDKEIPVNSRIVR----EVATLSRLQHQHVVRYYQAwfetgvvdpfagan 504
Cdd:cd06625    6 KLLGQGAFGQVYLCYDADTGRELAVKQVEI-DPINTEASKEVKalecEIQLLKNLQHERIVQYYGC-------------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysgavsteipEQDNNlestYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGII 583
Cdd:cd06625   71 ----------------------LQDEK----SLSIFMEYMPGgSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIV 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  584 HRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqdggfsTDVAGSGVDSTgqAGTYFYTAPEIeqdwpkID-----EKA 658
Cdd:cd06625  125 HRDIKGANILRDSNGNVKLGDFGASKRLQ-----------TICSSTGMKSV--TGTPYWMSPEV------INgegygRKA 185
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30694992  659 DMYSLGVVFFEL------WHPFGTAMERHVILTNlKLKGELPlkwvNEFPEQAS-LLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd06625  186 DIWSVGCTVVEMlttkppWAEFEPMAAIFKIATQ-PTNPQLP----PHVSEDARdFLSLIFVRNKKQRPSAEELLSHSF 259
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
422-728 2.09e-26

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: 109.78  E-value: 2.09e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEELK-PLGQGGFGHVVLCKNKLDGRQYAVK---KIRLKDkEIPvnsRIVREVATLSRLQHQHVVRYYQawfetgvv 497
Cdd:cd14078    1 LLKYYELHeTIGSGGFAKVKLATHILTGEKVAIKimdKKALGD-DLP---RVKTEIEALKNLSHQHICRLYH-------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  498 dpfaganwgsktagssmfsysgavsteIPEQDNNLestylYIQMEYCPRTlrQVFE---SYNHFDKDFAWHLIRQIVEGL 574
Cdd:cd14078   69 ---------------------------VIETDNKI-----FMVLEYCPGG--ELFDyivAKDRLSEDEARVFFRQIVSAV 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  575 AHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGL-AKflkleqldQDGGFSTDVAGSgvdstgqAGTYFYTAPEIEQDWPK 653
Cdd:cd14078  115 AYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLcAK--------PKGGMDHHLETC-------CGSPAYAAPELIQGKPY 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  654 IDEKADMYSLGVVFFEL---WHPFGTamERHVILTNLKLKG--ELPlKWVNefPEQASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14078  180 IGSEADVWSMGVLLYALlcgFLPFDD--DNVMALYRKIQSGkyEEP-EWLS--PSSKLLLDQMLQVDPKKRITVKELLNH 254
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
423-730 2.93e-26

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: 109.36  E-value: 2.93e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLK-DKEIpvNSRIVREVATLSRLQHQHVVRYYQAWFetgvvdpfa 501
Cdd:cd06605    1 DDLEYLGELGEGNGGVVSKVRHRPSGQIMAVKVIRLEiDEAL--QKQILRELDVLHKCNSPYIVGFYGAFY--------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 ganwgsktagssmfsYSGAVSteipeqdnnlestylyIQMEYCPRT-LRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQ 580
Cdd:cd06605   70 ---------------SEGDIS----------------ICMEYMDGGsLDKILKEVGRIPERILGKIAVAVVKGLIYLHEK 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 -GIIHRDFTPNNIFFDARNDIKIGDFGlakflkleqldqdggfstdVAGSGVDSTGQ--AGTYFYTAPEiEQDWPKIDEK 657
Cdd:cd06605  119 hKIIHRDVKPSNILVNSRGQVKLCDFG-------------------VSGQLVDSLAKtfVGTRSYMAPE-RISGGKYTVK 178
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  658 ADMYSLGVVFFELW-----HPFGTAMERHVILTNLK--LKGELPLKWVNEFPEQA-SLLRRLMSPSPSDRPSATELLKHA 729
Cdd:cd06605  179 SDIWSLGLSLVELAtgrfpYPPPNAKPSMMIFELLSyiVDEPPPLLPSGKFSPDFqDFVSQCLQKDPTERPSYKELMEHP 258

                 .
gi 30694992  730 F 730
Cdd:cd06605  259 F 259
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
424-729 3.13e-26

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: 109.28  E-value: 3.13e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPV-NSRIVREVATLSRLQHQHVVRYYQAWFEtgvvdpfag 502
Cdd:cd08224    1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFEMMDAKaRQDCLKEIDLLQQLNHPNIIKYLASFIE--------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgsktagssmfsysgavsteipeqdNNlestYLYIQMEYCP-----RTLRQVFESYNHFDKDFAWHLIRQIVEGLAHI 577
Cdd:cd08224   72 ---------------------------NN----ELNIVLELADagdlsRLIKHFKKQKRLIPERTIWKYFVQLCSALEHM 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  578 HGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFlkleqldqdggFS--TDVAGSGVdstgqaGTYFYTAPEI--EQDWpk 653
Cdd:cd08224  121 HSKRIMHRDIKPANVFITANGVVKLGDLGLGRF-----------FSskTTAAHSLV------GTPYYMSPERirEQGY-- 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  654 iDEKADMYSLGVVFFE---LWHPF-GTAMERHVILTNLKlKGELPLKWVNEFPEQ-ASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd08224  182 -DFKSDIWSLGCLLYEmaaLQSPFyGEKMNLYSLCKKIE-KCEYPPLPADLYSQElRDLVAACIQPDPEKRPDISYVLDV 259

                 .
gi 30694992  729 A 729
Cdd:cd08224  260 A 260
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
431-730 1.72e-25

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: 107.27  E-value: 1.72e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLC--KNKLDGRQYAVKKI-RLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAwFETGvvdpfaganwgs 507
Cdd:cd14080    8 IGEGSYSKVKLAeyTKSGLKEKVACKIIdKKKAPKDFLEKFLPRELEILRKLRHPNIIQVYSI-FERG------------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 ktagssmfsysgavsteipeqdnnlesTYLYIQMEYCPRT-LRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRD 586
Cdd:cd14080   75 ---------------------------SKVFIFMEYAEHGdLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRD 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  587 FTPNNIFFDARNDIKIGDFGLAKFLkleqLDQDGG-FSTDVAGSGvdstgqagtyFYTAPEIEQDWPKIDEKADMYSLGV 665
Cdd:cd14080  128 LKCENILLDSNNNVKLSDFGFARLC----PDDDGDvLSKTFCGSA----------AYAAPEILQGIPYDPKKYDIWSLGV 193
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30694992  666 VFFELWH---PFGTamerhvilTNLK--LKGELPLKWvnEFPEQAS--------LLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14080  194 ILYIMLCgsmPFDD--------SNIKkmLKDQQNRKV--RFPSSVKklspeckdLIDQLLEPDPTKRATIEEILNHPW 261
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
424-728 2.03e-25

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: 106.72  E-value: 2.03e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIrlkDKEIPVNSRIV----REVATLSRLQHQHVVRYYQAwfetgvvdp 499
Cdd:cd14663    1 RYELGRTLGEGTFAKVKFARNTKTGESVAIKII---DKEQVAREGMVeqikREIAIMKLLRHPNIVELHEV--------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  500 faganwgsktagssMFSysgavsteipeqdnnleSTYLYIQMEYCprTLRQVFE---SYNHFDKDFAWHLIRQIVEGLAH 576
Cdd:cd14663   69 --------------MAT-----------------KTKIFFVMELV--TGGELFSkiaKNGRLKEDKARKYFQQLIDAVDY 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  577 IHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFlkLEQLDQDGGFSTdvagsgvdstgQAGTYFYTAPEIEQDWPKIDE 656
Cdd:cd14663  116 CHSRGVFHRDLKPENLLLDEDGNLKISDFGLSAL--SEQFRQDGLLHT-----------TCGTPNYVAPEVLARRGYDGA 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  657 KADMYSLGVVFFEL---WHPFG----TAMERHViltnlkLKGELPL-KWVNefPEQASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14663  183 KADIWSCGVILFVLlagYLPFDdenlMALYRKI------MKGEFEYpRWFS--PGAKSLIKRILDPNPSTRITVEQIMAS 254
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
422-732 2.86e-25

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 113.68  E-value: 2.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   422 LNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIR---LKDKEipvNSRIVREVATLSRLQHQHVVRYyqawfetgvVD 498
Cdd:PTZ00266   12 LNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISyrgLKERE---KSQLVIEVNVMRELKHKNIVRY---------ID 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   499 PFAganwgsktagssmfsysgavsteipeqdnNLESTYLYIQMEYC-----PRTLRQVFESYNHFDKDFAWHLIRQIVEG 573
Cdd:PTZ00266   80 RFL-----------------------------NKANQKLYILMEFCdagdlSRNIQKCYKMFGKIEEHAIVDITRQLLHA 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   574 LAHIH-------GQGIIHRDFTPNNIFF-----------------DARNDIKIGDFGLAKFLKLEQLdqdggfstdvAGS 629
Cdd:PTZ00266  131 LAYCHnlkdgpnGERVLHRDLKPQNIFLstgirhigkitaqannlNGRPIAKIGDFGLSKNIGIESM----------AHS 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   630 GVdstgqaGTYFYTAPEIE-QDWPKIDEKADMYSLGVVFFELWH---PFGTAMERHVILTNLKLKGELPLKwvNEFPEQA 705
Cdd:PTZ00266  201 CV------GTPYYWSPELLlHETKSYDDKSDMWALGCIIYELCSgktPFHKANNFSQLISELKRGPDLPIK--GKSKELN 272
                         330       340       350
                  ....*....|....*....|....*....|..
gi 30694992   706 SLLRRLMSPSPSDRPSAT-----ELLKHAFPP 732
Cdd:PTZ00266  273 ILIKNLLNLSAKERPSALqclgyQIIKNVGPP 304
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
424-730 5.16e-25

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: 105.60  E-value: 5.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAWfetgvvdpfaga 503
Cdd:cd08223    1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKESF------------ 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssmfsysgavsteipeQDnnlESTYLYIQMEYC---------------PRTLRQVFEsynhfdkdfaWHLir 568
Cdd:cd08223   69 ------------------------EG---EDGFLYIVMGFCeggdlytrlkeqkgvLLEERQVVE----------WFV-- 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  569 QIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqdggFSTDVAgsgvdsTGQAGTYFYTAPEIE 648
Cdd:cd08223  110 QIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLE---------SSSDMA------TTLIGTPYYMSPELF 174
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  649 QDWPkIDEKADMYSLGVVFFE---LWHPFgTAMERHVILTNLkLKGELPLKWVNEFPEQASLLRRLMSPSPSDRPSATEL 725
Cdd:cd08223  175 SNKP-YNHKSDVWALGCCVYEmatLKHAF-NAKDMNSLVYKI-LEGKLPPMPKQYSPELGELIKAMLHQDPEKRPSVKRI 251

                 ....*
gi 30694992  726 LKHAF 730
Cdd:cd08223  252 LRQPY 256
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
423-730 5.94e-25

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: 107.27  E-value: 5.94e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIrLKDKEIPVNS-RIVREVATLSRLQHQHVVryyqawfetGVVDPFA 501
Cdd:cd07856   10 TRYSDLQPVGMGAFGLVCSARDQLTGQNVAVKKI-MKPFSTPVLAkRTYRELKLLKHLRHENII---------SLSDIFI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 GanwgsktagssmfsysgavsteiPEQDnnlestyLYIQMEYCPRTLRQVFESyNHFDKDFAWHLIRQIVEGLAHIHGQG 581
Cdd:cd07856   80 S-----------------------PLED-------IYFVTELLGTDLHRLLTS-RPLEKQFIQYFLYQILRGLKYVHSAG 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGLAKFlkleqldQDGGFstdvagsgvdsTGQAGTYFYTAPEIEQDWPKIDEKADMY 661
Cdd:cd07856  129 VIHRDLKPSNILVNENCDLKICDFGLARI-------QDPQM-----------TGYVSTRYYRAPEIMLTWQKYDVEVDIW 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  662 SLGVVFFELWH-----PFGTAMERHVILTNL----------KLKGELPLKWVNEFPEQ----------------ASLLRR 710
Cdd:cd07856  191 SAGCIFAEMLEgkplfPGKDHVNQFSIITELlgtppddvinTICSENTLRFVQSLPKRervpfsekfknadpdaIDLLEK 270
                        330       340
                 ....*....|....*....|
gi 30694992  711 LMSPSPSDRPSATELLKHAF 730
Cdd:cd07856  271 MLVFDPKKRISAAEALAHPY 290
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
430-727 6.60e-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: 105.51  E-value: 6.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  430 PLGQGGFGHVVLCKNKLDGRQYAVKKI-RLKDKEIPVNSRIV----REVATLSRL-QHQHVVRYYQAwFETGVvdpfaga 503
Cdd:cd13993    7 PIGEGAYGVVYLAVDLRTGRKYAIKCLyKSGPNSKDGNDFQKlpqlREIDLHRRVsRHPNIITLHDV-FETEV------- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssmfsysgavsteipeqdnnlestYLYIQMEYCPR-------TLRQVFESYNHFdkdfAWHLIRQIVEGLAH 576
Cdd:cd13993   79 --------------------------------AIYIVLEYCPNgdlfeaiTENRIYVGKTEL----IKNVFLQLIDAVKH 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  577 IHGQGIIHRDFTPNNIFFDARND-IKIGDFGLAkflkleqldQDGGFSTDVAgsgvdstgqAGTYFYTAPEIEQDWPKID 655
Cdd:cd13993  123 CHSLGIYHRDIKPENILLSQDEGtVKLCDFGLA---------TTEKISMDFG---------VGSEFYMAPECFDEVGRSL 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  656 E-----KADMYSLGVVFFELW---HPFGTAMERHVILTNLKLKGE-LPLKWVNEFPEQASLLRRLMSPSPSDRPSATELL 726
Cdd:cd13993  185 KgypcaAGDIWSLGIILLNLTfgrNPWKIASESDPIFYDYYLNSPnLFDVILPMSDDFYNLLRQIFTVNPNNRILLPELQ 264

                 .
gi 30694992  727 K 727
Cdd:cd13993  265 L 265
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
423-730 9.08e-25

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: 105.13  E-value: 9.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHV--VLCKNKldGRQYAVKKIRLKDKEIPVNSrIVREVATLSRLQHQHVVRYYqawfetgvvdpf 500
Cdd:cd06610    1 DDYELIEVIGSGATAVVyaAYCLPK--KEKVAIKRIDLEKCQTSMDE-LRKEIQAMSQCNHPNVVSYY------------ 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  501 aganwGSKTAGSSmfsysgavsteipeqdnnlestyLYIQMEY-----CPRTLRQVFeSYNHFDKDFAWHLIRQIVEGLA 575
Cdd:cd06610   66 -----TSFVVGDE-----------------------LWLVMPLlsggsLLDIMKSSY-PRGGLDEAIIATVLKEVLKGLE 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  576 HIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLkleqldQDGGFSTDVAGSGVdstgqAGTYFYTAPEIEQDWPKID 655
Cdd:cd06610  117 YLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSASL------ATGGDRTRKVRKTF-----VGTPCWMAPEVMEQVRGYD 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  656 EKADMYSLGVVFFELWH---PFGTAMERHVILtnLKLKGELP-LKWVNEFPEQASLLRRLMS----PSPSDRPSATELLK 727
Cdd:cd06610  186 FKADIWSFGITAIELATgaaPYSKYPPMKVLM--LTLQNDPPsLETGADYKKYSKSFRKMISlclqKDPSKRPTAEELLK 263

                 ...
gi 30694992  728 HAF 730
Cdd:cd06610  264 HKF 266
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
425-730 3.26e-24

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: 104.18  E-value: 3.26e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKE--IPVNSriVREVATLSRLQHQHVVRYYQAwfetgVVDPFAG 502
Cdd:cd07840    1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMENEKegFPITA--IREIKLLQKLDHPNVVRLKEI-----VTSKGSA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 ANWGSktagssmfsysgavsteipeqdnnlestyLYIQMEYCPRTLRQVFESYN-HFDKDFAWHLIRQIVEGLAHIHGQG 581
Cdd:cd07840   74 KYKGS-----------------------------IYMVFEYMDHDLTGLLDNPEvKFTESQIKCYMKQLLEGLQYLHSNG 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEqldQDGGFSTDVAgsgvdstgqagTYFYTAPEI---EQDW-PKIdek 657
Cdd:cd07840  125 ILHRDIKGSNILINNDGVLKLADFGLARPYTKE---NNADYTNRVI-----------TLWYRPPELllgATRYgPEV--- 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  658 aDMYSLGVVFFELWH-----PFGTAMER-HVIL--------------------TNLKLKGELPLKWVNEF----PEQA-S 706
Cdd:cd07840  188 -DMWSVGCILAELFTgkpifQGKTELEQlEKIFelcgspteenwpgvsdlpwfENLKPKKPYKRRLREVFknviDPSAlD 266
                        330       340
                 ....*....|....*....|....
gi 30694992  707 LLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd07840  267 LLDKLLTLDPKKRISADQALQHEY 290
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
425-728 6.05e-24

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: 102.47  E-value: 6.05e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRlKDK-EIPVNS-RIVREVATLSRLQHQHVVRYYQAwFETG----VVD 498
Cdd:cd14073    3 YELLETLGKGTYGKVKLAIERATGREVAIKSIK-KDKiEDEQDMvRIRREIEIMSSLNHPHIIRIYEV-FENKdkivIVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  499 PFAganwgsktAGSSMFSYSgAVSTEIPEQDnnlestylyiqmeycprtlrqvfesynhfdkdfAWHLIRQIVEGLAHIH 578
Cdd:cd14073   81 EYA--------SGGELYDYI-SERRRLPERE---------------------------------ARRIFRQIVSAVHYCH 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  579 GQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQDggFstdvagsgvdstgqAGTYFYTAPEIEQDWPKIDEKA 658
Cdd:cd14073  119 KNGVVHRDLKLENILLDQNGNAKIADFGLSNLYSKDKLLQT--F--------------CGSPLYASPEIVNGTPYQGPEV 182
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30694992  659 DMYSLGVVFFELWH---PFGTAmeRHVILTNLKLKGEL--PlkwvNEFPEQASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14073  183 DCWSLGVLLYTLVYgtmPFDGS--DFKRLVKQISSGDYreP----TQPSDASGLIRWMLTVNPKRRATIEDIANH 251
RWD_GCN2 cd23823
RWD domain of eIF-2-alpha kinase GCN2 and related proteins; GCN2 (EC 2.7.11.1), also called ...
32-148 8.82e-24

RWD domain of eIF-2-alpha kinase GCN2 and related proteins; GCN2 (EC 2.7.11.1), also called eukaryotic translation initiation factor 2-alpha kinase 4 (EIF2AK4), acts as a metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to low amino acid availability. It also plays a role in modulating the adaptive immune response to yellow fever virus infection and promotes dendritic cells to initiate autophagy and antigene presentation to both CD4(+) and CD8(+) T-cells under amino acid starvation.


Pssm-ID: 467659  Cd Length: 117  Bit Score: 97.29  E-value: 8.82e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   32 NELLSEEITALSAIFQEDCKVVS---DSRSPPQIAIKLRPYskDMGYEDTDISAMLIVRCLPGYPYKCPKLQITPEQGLT 108
Cdd:cd23823    1 EEEQEEELEALQSIYGDDFEDLSskkAVWSPPEFRIRLRPQ--EGESEENHVSVDLHVKFPPTYPDVPPEIELENVKGLS 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 30694992  109 TADAEKLLSLLEDQANSNarEGRVMIFNLVEAAQEFLSEI 148
Cdd:cd23823   79 DEQLEELLKELEELAKEL--LGEEMIFELAEAVQEFLEEH 116
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
425-730 1.11e-23

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: 102.45  E-value: 1.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIrLKDKEIPVNSRI-VREVATLSRLQHQHVVryyqawfetgvvdpfaga 503
Cdd:cd07847    3 YEKLSKIGEGSYGVVFKCRNRETGQIVAIKKF-VESEDDPVIKKIaLREIRMLKQLKHPNLV------------------ 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssmfsysgavsteipeqdnNLESTY-----LYIQMEYCPRTLRQVFESYNH-FDKDFAWHLIRQIVEGLAHI 577
Cdd:cd07847   64 ---------------------------NLIEVFrrkrkLHLVFEYCDHTVLNELEKNPRgVPEHLIKKIIWQTLQAVNFC 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  578 HGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLkleqldqdggfstdvAGSGVDSTGQAGTYFYTAPEIEQDWPKIDEK 657
Cdd:cd07847  117 HKHNCIHRDVKPENILITKQGQIKLCDFGFARIL---------------TGPGDDYTDYVATRWYRAPELLVGDTQYGPP 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  658 ADMYSLGVVFFE------LW-------------HPFGTAMERH--VILTNLKLKG----------ELPLKWVNEFPEQAS 706
Cdd:cd07847  182 VDVWAIGCVFAElltgqpLWpgksdvdqlylirKTLGDLIPRHqqIFSTNQFFKGlsipepetrePLESKFPNISSPALS 261
                        330       340
                 ....*....|....*....|....
gi 30694992  707 LLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd07847  262 FLKGCLQMDPTERLSCEELLEHPY 285
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
425-730 1.30e-23

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: 102.23  E-value: 1.30e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKI--RLKDKEIPVNsriVREVATLSRLQ-HQHVVRYYQawfetgvvdpfa 501
Cdd:cd07830    1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMkkKFYSWEECMN---LREVKSLRKLNeHPNIVKLKE------------ 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 ganwgsktagssMFsysgavsteipeqdnnLESTYLYIQMEYCPRTLRQVFESYNH--FDKDFAWHLIRQIVEGLAHIHG 579
Cdd:cd07830   66 ------------VF----------------RENDELYFVFEYMEGNLYQLMKDRKGkpFSESVIRSIIYQILQGLAHIHK 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  580 QGIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleqldqdggfstdvagsGVDS----TGQAGTYFYTAPEIEQDWPKID 655
Cdd:cd07830  118 HGFFHRDLKPENLLVSGPEVVKIADFGLAR--------------------EIRSrppyTDYVSTRWYRAPEILLRSTSYS 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  656 EKADMYSLGVVFFEL------------------------------WhPFGTAMERHVILTNLKLKGeLPLKWV--NEFPE 703
Cdd:cd07830  178 SPVDIWALGCIMAELytlrplfpgsseidqlykicsvlgtptkqdW-PEGYKLASKLGFRFPQFAP-TSLHQLipNASPE 255
                        330       340
                 ....*....|....*....|....*..
gi 30694992  704 QASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd07830  256 AIDLIKDMLRWDPKKRPTASQALQHPY 282
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
424-730 1.42e-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: 101.61  E-value: 1.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEipVNSRIVREVATLSRLQHQHVVRYYQAWFetgvvdpfaga 503
Cdd:cd06613    1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIKLEPGD--DFEIIQQEISMLKECRHPNIVAYFGSYL----------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nWGSKtagssmfsysgavsteipeqdnnlestyLYIQMEYCP-RTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGI 582
Cdd:cd06613   68 -RRDK----------------------------LWIVMEYCGgGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGK 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  583 IHRDFTPNNIFFDARNDIKIGDFGLAKFLKlEQLDQDGGFstdvagsgvdstgqAGTYFYTAPEI--EQDWPKIDEKADM 660
Cdd:cd06613  119 IHRDIKGANILLTEDGDVKLADFGVSAQLT-ATIAKRKSF--------------IGTPYWMAPEVaaVERKGGYDGKCDI 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  661 YSLGVVFFEL---------WHPfgtaMERHVILT-------NLKLKGelplKWVNEFpeqASLLRRLMSPSPSDRPSATE 724
Cdd:cd06613  184 WALGITAIELaelqppmfdLHP----MRALFLIPksnfdppKLKDKE----KWSPDF---HDFIKKCLTKNPKKRPTATK 252

                 ....*.
gi 30694992  725 LLKHAF 730
Cdd:cd06613  253 LLQHPF 258
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
423-730 1.72e-23

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: 103.08  E-value: 1.72e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKD---KEIPVNSRIVREVatLSRLQHQHVVRYYqawfetgvvdp 499
Cdd:cd05599    1 EDFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEmleKEQVAHVRAERDI--LAEADNPWVVKLY----------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  500 faganwgsktagssmfsYSGavsteipeQDNNlestYLYIQMEYCP----RTLrqvFESYNHFDKDFAWHLIRQIVEGLA 575
Cdd:cd05599   68 -----------------YSF--------QDEE----NLYLIMEFLPggdmMTL---LMKKDTLTEEETRFYIAETVLAIE 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  576 HIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLdqdgGFSTdvagsgvdstgqAGTYFYTAPEI-------- 647
Cdd:cd05599  116 SIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTGLKKSHL----AYST------------VGTPDYIAPEVflqkgygk 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  648 EQDWpkidekadmYSLGVVFFEL---WHPF--GTAME--RHVI--LTNLKLKGELPLKwvnefPEQASLLRRLMSpSPSD 718
Cdd:cd05599  180 ECDW---------WSLGVIMYEMligYPPFcsDDPQEtcRKIMnwRETLVFPPEVPIS-----PEAKDLIERLLC-DAEH 244
                        330
                 ....*....|....*
gi 30694992  719 R---PSATELLKHAF 730
Cdd:cd05599  245 RlgaNGVEEIKSHPF 259
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
425-730 1.81e-23

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: 101.35  E-value: 1.81e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIrlkdKEIPVNS-------RIVREVATLSRLQHQHVVRYYqawfetgvv 497
Cdd:cd08222    2 YRVVRKLGSGNFGTVYLVSDLKATADEELKVL----KEISVGElqpdetvDANREAKLLSKLDHPAIVKFH--------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  498 dpfaganwgsktagssmfsysgavsteipeqDNNLESTYLYIQMEYCP-RTLRQVFESYNHFDKDFAWHLIR----QIVE 572
Cdd:cd08222   69 -------------------------------DSFVEKESFCIVTEYCEgGDLDDKISEYKKSGTTIDENQILdwfiQLLL 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  573 GLAHIHGQGIIHRDFTPNNIFFdARNDIKIGDFGLAKFLKleqldqdggFSTDVAgsgvdsTGQAGTYFYTAPEIEQDwP 652
Cdd:cd08222  118 AVQYMHERRILHRDLKAKNIFL-KNNVIKVGDFGISRILM---------GTSDLA------TTFTGTPYYMSPEVLKH-E 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  653 KIDEKADMYSLGVVFFE---LWHPFGTAMERHVILTnlKLKGELPlkwvnEFPEQAS-----LLRRLMSPSPSDRPSATE 724
Cdd:cd08222  181 GYNSKSDIWSLGCILYEmccLKHAFDGQNLLSVMYK--IVEGETP-----SLPDKYSkelnaIYSRMLNKDPALRPSAAE 253

                 ....*.
gi 30694992  725 LLKHAF 730
Cdd:cd08222  254 ILKIPF 259
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
423-730 1.91e-23

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: 101.89  E-value: 1.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKK------IRLKDKEipvnsRIVREVATLSRLQHQHVVRYYQAWfetgv 496
Cdd:cd05580    1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKIlkkakiIKLKQVE-----HVLNEKRILSEVRHPFIVNLLGSF----- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  497 vdpfaganwgsktagssmfsysgavsteipeQDNNlestYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLA 575
Cdd:cd05580   71 -------------------------------QDDR----NLYMVMEYVPGgELFSLLRRSGRFPNDVAKFYAAEVVLALE 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  576 HIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqDGGFSTdvagsgvdstgqAGTYFYTAPEIEQDWPKiD 655
Cdd:cd05580  116 YLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVK------DRTYTL------------CGTPEYLAPEIILSKGH-G 176
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  656 EKADMYSLGVVFFEL---WHPF--GTAMERHviltNLKLKGElpLKWVNEFPEQA-SLLRRLMSPSPSDR-----PSATE 724
Cdd:cd05580  177 KAVDWWALGILIYEMlagYPPFfdENPMKIY----EKILEGK--IRFPSFFDPDAkDLIKRLLVVDLTKRlgnlkNGVED 250

                 ....*.
gi 30694992  725 LLKHAF 730
Cdd:cd05580  251 IKNHPW 256
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
429-730 2.06e-23

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: 101.27  E-value: 2.06e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKLDGRQYAVKKIRLkDKEIPVNSRIVR----EVATLSRLQHQHVVRYYQAwfetgVVDPfagan 504
Cdd:cd06652    8 KLLGQGAFGRVYLCYDADTGRELAVKQVQF-DPESPETSKEVNalecEIQLLKNLLHERIVQYYGC-----LRDP----- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysgavsteipeqdnnLESTyLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGII 583
Cdd:cd06652   77 ---------------------------QERT-LSIFMEYMPGgSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIV 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  584 HRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqdggfSTDVAGSGVDSTgqAGTYFYTAPEIEQDwPKIDEKADMYSL 663
Cdd:cd06652  129 HRDIKGANILRDSVGNVKLGDFGASKRLQ----------TICLSGTGMKSV--TGTPYWMSPEVISG-EGYGRKADIWSV 195
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30694992  664 GVVFFEL------WHPFgTAMERHVILTNLKLKGELPLKwVNEFPEQasLLRRLMSPSpSDRPSATELLKHAF 730
Cdd:cd06652  196 GCTVVEMltekppWAEF-EAMAAIFKIATQPTNPQLPAH-VSDHCRD--FLKRIFVEA-KLRPSADELLRHTF 263
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
428-726 2.24e-23

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 101.31  E-value: 2.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  428 LKPLGQGGFGHVVlcKNKLDGRQYAVKKIRlKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAwfETGVVDPFAGanwgs 507
Cdd:cd13979    8 QEPLGSGGFGSVY--KATYKGETVAVKIVR-RRRKNRASRQSFWAELNAARLRHENIVRVLAA--ETGTDFASLG----- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 ktagssmfsysgavsteipeqdnnlestylYIQMEYC-PRTLRQV-FESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHR 585
Cdd:cd13979   78 ------------------------------LIIMEYCgNGTLQQLiYEGSEPLPLAHRILISLDIARALRFCHSHGIVHL 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  586 DFTPNNIFFDARNDIKIGDFGLAKFLkleqldqdggFSTDVAGSGVdsTGQAGTYFYTAPE-IEQDWPKidEKADMYSLG 664
Cdd:cd13979  128 DVKPANILISEQGVCKLCDFGCSVKL----------GEGNEVGTPR--SHIGGTYTYRAPElLKGERVT--PKADIYSFG 193
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30694992  665 VVffeLWH------PFgtAMERHVILTNLKLKGELPLKWVNEFPEQA----SLLRRLMSPSPSDRPSATELL 726
Cdd:cd13979  194 IT---LWQmltrelPY--AGLRQHVLYAVVAKDLRPDLSGLEDSEFGqrlrSLISRCWSAQPAERPNADESL 260
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
425-728 2.42e-23

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: 101.88  E-value: 2.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIP---VNSRIVREVATLSRLQHQHVVryyqawfetGVVDPFa 501
Cdd:cd07841    2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEAkdgINFTALREIKLLQELKHPNII---------GLLDVF- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 ganwgsktagssmfsysgavsteiPEQDNnlestyLYIQMEYCPRTLRQVFEsynhfDKDF--------AWhlIRQIVEG 573
Cdd:cd07841   72 ------------------------GHKSN------INLVFEFMETDLEKVIK-----DKSIvltpadikSY--MLMTLRG 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  574 LAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLkleqldqdggfstdvAGSGVDSTGQAGTYFYTAPEI----EQ 649
Cdd:cd07841  115 LEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARSF---------------GSPNRKMTHQVVTRWYRAPELlfgaRH 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  650 DWPKIdekaDMYSLGVVFFEL-------------------WHPFGTAMER-----HVILTNLKLKGELPLKWVNEFPeQA 705
Cdd:cd07841  180 YGVGV----DMWSVGCIFAELllrvpflpgdsdidqlgkiFEALGTPTEEnwpgvTSLPDYVEFKPFPPTPLKQIFP-AA 254
                        330       340
                 ....*....|....*....|....*...
gi 30694992  706 S-----LLRRLMSPSPSDRPSATELLKH 728
Cdd:cd07841  255 SddaldLLQRLLTLNPNKRITARQALEH 282
RWD smart00591
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily ...
38-148 3.11e-23

domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily related to the UBCc domain;


Pssm-ID: 214735  Cd Length: 107  Bit Score: 95.50  E-value: 3.11e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992      38 EITALSAIFQEDCKVVSDSRSPPQIAIKLRPYSKDmgYEDTDISAMLIVRCLPGYPYKCPKLQITPEQGLTTADAEKLLS 117
Cdd:smart00591    1 ELEALESIYPEDFEVIDEDARIPEITIKLSPSSDE--GEDQYVSLTLQVKLPENYPDEAPPISLLNSEGLSDEQLAELLK 78
                            90       100       110
                    ....*....|....*....|....*....|.
gi 30694992     118 LLEDQANSNarEGRVMIFNLVEAAQEFLSEI 148
Cdd:smart00591   79 KLEEIAEEN--LGEVMIFELVEKLQEFLSEF 107
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
428-730 3.72e-23

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: 100.20  E-value: 3.72e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  428 LKPLGQGGFGHVVLCKNKLDGRQYAVKKI---RLKDKEipvNSRIVREVATLSRLQHQHVVRYYQAWfetgvvdpfagan 504
Cdd:cd08221    5 VRVLGRGAFGEAVLYRKTEDNSLVVWKEVnlsRLSEKE---RRDALNEIDILSLLNHDNIITYYNHF------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysgavsteipeqdnnLESTYLYIQMEYCP---------RTLRQVFEsynhfDKDFAWHLIrQIVEGLA 575
Cdd:cd08221   69 ---------------------------LDGESLFIEMEYCNggnlhdkiaQQKNQLFP-----EEVVLWYLY-QIVSAVS 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  576 HIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEqldqdggfstdvaGSGVDSTgqAGTYFYTAPEIEQDwPKID 655
Cdd:cd08221  116 HIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSE-------------SSMAESI--VGTPYYMSPELVQG-VKYN 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  656 EKADMYSLGVVFFELwhpfgTAMERHVILTN-LKL-----KGELPLKWVNEFPEQASLLRRLMSPSPSDRPSATELLKHA 729
Cdd:cd08221  180 FKSDIWAVGCVLYEL-----LTLKRTFDATNpLRLavkivQGEYEDIDEQYSEEIIQLVHDCLHQDPEDRPTAEELLERP 254

                 .
gi 30694992  730 F 730
Cdd:cd08221  255 L 255
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
424-725 3.95e-23

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: 100.65  E-value: 3.95e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQ-YAVKKIRL-----------KDKEIpvnSRIVREVATL-SRLQHQHVVRYYQA 490
Cdd:cd08528    1 EYAVLELLGSGAFGCVYKVRKKSNGQTlLALKEINMtnpafgrteqeRDKSV---GDIISEVNIIkEQLRHPNIVRYYKT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  491 WfetgvvdpfaganwgsktagssmfsysgavsteipeqdnnLESTYLYIQMEY---CPrtLRQVF----ESYNHFDKDFA 563
Cdd:cd08528   78 F----------------------------------------LENDRLYIVMELiegAP--LGEHFsslkEKNEHFTEDRI 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  564 WHLIRQIVEGLAHIHGQ-GIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleQLDQDGGFSTDVagsgvdstgqAGTYFY 642
Cdd:cd08528  116 WNIFVQMVLALRYLHKEkQIVHRDLKPNNIMLGEDDKVTITDFGLAK-----QKGPESSKMTSV----------VGTILY 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  643 TAPEIEQDWPkIDEKADMYSLGVVFFE---LWHPF-GTAMerhVILTNLKLKGEL-PLKWVNEFPEQASLLRRLMSPSPS 717
Cdd:cd08528  181 SCPEIVQNEP-YGEKADIWALGCILYQmctLQPPFySTNM---LTLATKIVEAEYePLPEGMYSDDITFVIRSCLTPDPE 256

                 ....*...
gi 30694992  718 DRPSATEL 725
Cdd:cd08528  257 ARPDIVEV 264
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
428-727 5.23e-23

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 99.91  E-value: 5.23e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992     428 LKPLGQGGFGHVVLC--KNKLDGRQY--AVKKIRlKDKEIPVNSRIVREVATLSRLQHQHVVRYYqawfetGVVdpfaga 503
Cdd:smart00219    4 GKKLGEGAFGEVYKGklKGKGGKKKVevAVKTLK-EDASEQQIEEFLREARIMRKLDHPNVVKLL------GVC------ 70
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992     504 nwgsktagssmfsysgavsteipeqdnnLESTYLYIQMEYCP--------RTLRQVFesyNHFDK-DFAWhlirQIVEGL 574
Cdd:smart00219   71 ----------------------------TEEEPLYIVMEYMEggdllsylRKNRPKL---SLSDLlSFAL----QIARGM 115
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992     575 AHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLdqdggfstdvagsgVDSTGQAGTYFYTAPE-IEQDwpK 653
Cdd:smart00219  116 EYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDY--------------YRKRGGKLPIRWMAPEsLKEG--K 179
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992     654 IDEKADMYSLGVVFFELWH----PFGtAMERHVILTNLKLKGELPlkwvneFPEQASL-LRRLMS----PSPSDRPSATE 724
Cdd:smart00219  180 FTSKSDVWSFGVLLWEIFTlgeqPYP-GMSNEEVLEYLKNGYRLP------QPPNCPPeLYDLMLqcwaEDPEDRPTFSE 252

                    ...
gi 30694992     725 LLK 727
Cdd:smart00219  253 LVE 255
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
423-730 9.99e-23

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: 98.86  E-value: 9.99e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLK---DKEIpVNSRivREVATLSRLQHQHVVRYYQAwFETGvvDP 499
Cdd:cd14002    1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRgksEKEL-RNLR--QEIEILRKLNHPNIIEMLDS-FETK--KE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  500 FAganwgsktagssmfsysgaVSTEipeqdnnlestylYIQMEycprtLRQVFESynhfDKDFAWHLIR----QIVEGLA 575
Cdd:cd14002   75 FV-------------------VVTE-------------YAQGE-----LFQILED----DGTLPEEEVRsiakQLVSALH 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  576 HIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqdggFSTDVAgsgvdsTGQAGTYFYTAPEIEQDWPkID 655
Cdd:cd14002  114 YLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMS---------CNTLVL------TSIKGTPLYMAPELVQEQP-YD 177
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30694992  656 EKADMYSLGVVFFELWH---PFGTamerHVILTNLKLKGELPLKWVNEF-PEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14002  178 HTADLWSLGCILYELFVgqpPFYT----NSIYQLVQMIVKDPVKWPSNMsPEFKSFLQGLLNKDPSKRLSWPDLLEHPF 252
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
429-730 1.05e-22

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 98.86  E-value: 1.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKLDGRQYAVKKI-RLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAWfETgvvdpfaganwgs 507
Cdd:cd14081    7 KTLGKGQTGLVKLAKHCVTGQKVAIKIVnKEKLSKESVLMKVEREIAIMKLIEHPNVLKLYDVY-EN------------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 ktagssmfsysgavsteipeqdnnleSTYLYIQMEYCPRTlrQVFE---SYNHFDKDFAWHLIRQIVEGLAHIHGQGIIH 584
Cdd:cd14081   73 --------------------------KKYLYLVLEYVSGG--ELFDylvKKGRLTEKEARKFFRQIISALDYCHSHSICH 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  585 RDFTPNNIFFDARNDIKIGDFGLAkflkleqldqdggfSTDVAGSGVDSTgqAGTYFYTAPEIEQDWPKIDEKADMYSLG 664
Cdd:cd14081  125 RDLKPENLLLDEKNNIKIADFGMA--------------SLQPEGSLLETS--CGSPHYACPEVIKGEKYDGRKADIWSCG 188
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30694992  665 VVFFELWH---PFGTAMERHVILTNLKLKGELPlkwvnEF--PEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14081  189 VILYALLVgalPFDDDNLRQLLEKVKRGVFHIP-----HFisPDAQDLLRRMLEVNPEKRITIEEIKKHPW 254
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
424-729 1.41e-22

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: 99.02  E-value: 1.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREV---ATLSrlQHQHVVRYYQAWFETGvvdpf 500
Cdd:cd14051    1 EFHEVEKIGSGEFGSVYKCINRLDGCVYAIKKSKKPVAGSVDEQNALNEVyahAVLG--KHPHVVRYYSAWAEDD----- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  501 aganwgsktagssmfsysgavsteipeqdnnlestYLYIQMEYC-----PRTLRQVFESYNHFDKDFAWHLIRQIVEGLA 575
Cdd:cd14051   74 -----------------------------------HMIIQNEYCnggslADAISENEKAGERFSEAELKDLLLQVAQGLK 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  576 HIHGQGIIHRDFTPNNIFFDARNDI------------------------KIGDFGLAKFLKLEQLDQdggfstdvagsgv 631
Cdd:cd14051  119 YIHSQNLVHMDIKPGNIFISRTPNPvsseeeeedfegeednpesnevtyKIGDLGHVTSISNPQVEE------------- 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  632 dstgqaGTYFYTAPEIEQDWPKIDEKADMYSLGVVFFEL------------WHpfgtamerhviltNLKlKGELP-LKWV 698
Cdd:cd14051  186 ------GDCRFLANEILQENYSHLPKADIFALALTVYEAagggplpkngdeWH-------------EIR-QGNLPpLPQC 245
                        330       340       350
                 ....*....|....*....|....*....|.
gi 30694992  699 NefPEQASLLRRLMSPSPSDRPSATELLKHA 729
Cdd:cd14051  246 S--PEFNELLRSMIHPDPEKRPSAAALLQHP 274
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
428-727 1.42e-22

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: 98.39  E-value: 1.42e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992     428 LKPLGQGGFGHVVLC--KNKLDGRQY--AVKKIRlKDKEIPVNSRIVREVATLSRLQHQHVVRYYqawfetgvvdpfaga 503
Cdd:smart00221    4 GKKLGEGAFGEVYKGtlKGKGDGKEVevAVKTLK-EDASEQQIEEFLREARIMRKLDHPNIVKLL--------------- 67
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992     504 nwgsktagssmfsysGAVSTEIPeqdnnlestyLYIQMEYCP--------RTLRQVFESYNHFdKDFAWhlirQIVEGLA 575
Cdd:smart00221   68 ---------------GVCTEEEP----------LMIVMEYMPggdlldylRKNRPKELSLSDL-LSFAL----QIARGME 117
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992     576 HIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLdqdggfstdvagsgVDSTGQAGTYFYTAPE-IEQDwpKI 654
Cdd:smart00221  118 YLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDY--------------YKVKGGKLPIRWMAPEsLKEG--KF 181
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992     655 DEKADMYSLGVVFFELWH----PFGtAMERHVILTNLKLKGELPlkwvneFPEQASL-LRRLMS----PSPSDRPSATEL 725
Cdd:smart00221  182 TSKSDVWSFGVLLWEIFTlgeePYP-GMSNAEVLEYLKKGYRLP------KPPNCPPeLYKLMLqcwaEDPEDRPTFSEL 254

                    ..
gi 30694992     726 LK 727
Cdd:smart00221  255 VE 256
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
424-728 3.21e-22

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: 97.93  E-value: 3.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKI-RLKDKEIPVNSRIV-REVATLSRLQHQHVVRYYQaWFEtgvvdpfa 501
Cdd:cd14098    1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIvKRKVAGNDKNLQLFqREINILKSLEHPGIVRLID-WYE-------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 ganwgsktagssmfsysgavsteipeqdnnlESTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQ 580
Cdd:cd14098   72 -------------------------------DDQHIYLVMEYVEGgDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSM 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFDARND--IKIGDFGLAKflkleqldqdggfstdVAGSGVDSTGQAGTYFYTAPEI-----EQDWPK 653
Cdd:cd14098  121 GITHRDLKPENILITQDDPviVKISDFGLAK----------------VIHTGTFLVTFCGTMAYLAPEIlmskeQNLQGG 184
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30694992  654 IDEKADMYSLGVVFFEL---WHPF-GTAMERHVILTNLKLKGELPLKWVNEFPEQASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14098  185 YSNLVDMWSVGCLVYVMltgALPFdGSSQLPVEKRIRKGRYTQPPLVDFNISEEAIDFILRLLDVDPEKRMTAAQALDH 263
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
429-728 3.39e-22

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: 97.61  E-value: 3.39e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCK---NKLDGRQYAVKKIRlKDKEIPVNSRIVREVATLSRLQHQHVVRYYqawfetgvvdpfaganw 505
Cdd:cd00192    1 KKLGEGAFGEVYKGKlkgGDGKTVDVAVKTLK-EDASESERKDFLKEARVMKKLGHPNVVRLL----------------- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  506 gsktagssmfsysGAVSTEIPeqdnnlestyLYIQMEYCPRT-----LRQVFESYNHFDKD---------FAWhlirQIV 571
Cdd:cd00192   63 -------------GVCTEEEP----------LYLVMEYMEGGdlldfLRKSRPVFPSPEPStlslkdllsFAI----QIA 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  572 EGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLkleqldqdggfstDVAGSGVDSTGQAGTYFYTAPEIEQDw 651
Cdd:cd00192  116 KGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDI-------------YDDDYYRKKTGGKLPIRWMAPESLKD- 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  652 PKIDEKADMYSLGVVFFELW----HPFGTaMERHVILTNLKlKGELPlkwvnEFPEQAS-LLRRLM----SPSPSDRPSA 722
Cdd:cd00192  182 GIFTSKSDVWSFGVLLWEIFtlgaTPYPG-LSNEEVLEYLR-KGYRL-----PKPENCPdELYELMlscwQLDPEDRPTF 254

                 ....*.
gi 30694992  723 TELLKH 728
Cdd:cd00192  255 SELVER 260
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
418-728 3.76e-22

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: 97.81  E-value: 3.76e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  418 SSRYLNDFEEL--KPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQ-HQHVVRYYQAwFET 494
Cdd:cd14106    1 STENINEVYTVesTPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCRNEILHEIAVLELCKdCPRVVNLHEV-YET 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  495 gvvdpfaganwgsktagssmfsysgavsteipeqdnnleSTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEG 573
Cdd:cd14106   80 ---------------------------------------RSELILILELAAGgELQTLLDEEECLTEADVRRLMRQILEG 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  574 LAHIHGQGIIHRDFTPNNIFF---DARNDIKIGDFGLAKFLkleqldqdggfstdvaGSGVDSTGQAGTYFYTAPEIEQD 650
Cdd:cd14106  121 VQYLHERNIVHLDLKPQNILLtseFPLGDIKLCDFGISRVI----------------GEGEEIREILGTPDYVAPEILSY 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  651 WPkIDEKADMYSLGVVFFEL---WHPFG--TAMERHVILTNLKLkgELPLKWVNEFPEQA-SLLRRLMSPSPSDRPSATE 724
Cdd:cd14106  185 EP-ISLATDMWSIGVLTYVLltgHSPFGgdDKQETFLNISQCNL--DFPEELFKDVSPLAiDFIKRLLVKDPEKRLTAKE 261

                 ....
gi 30694992  725 LLKH 728
Cdd:cd14106  262 CLEH 265
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
429-730 4.19e-22

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: 97.46  E-value: 4.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKLDGRQYAVKKIRLkDKEIPVNSRIVR----EVATLSRLQHQHVVRYYQAWFETGvvdpfagan 504
Cdd:cd06651   13 KLLGQGAFGRVYLCYDVDTGRELAAKQVQF-DPESPETSKEVSalecEIQLLKNLQHERIVQYYGCLRDRA--------- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysgavsteipeqdnnlESTyLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGII 583
Cdd:cd06651   83 ----------------------------EKT-LTIFMEYMPGgSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIV 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  584 HRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqdggfSTDVAGSGVDSTgqAGTYFYTAPEIEQDwPKIDEKADMYSL 663
Cdd:cd06651  134 HRDIKGANILRDSAGNVKLGDFGASKRLQ----------TICMSGTGIRSV--TGTPYWMSPEVISG-EGYGRKADVWSL 200
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30694992  664 GVVFFEL------WHPFgTAMERHVILTNLKLKGELPlkwvNEFPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd06651  201 GCTVVEMltekppWAEY-EAMAAIFKIATQPTNPQLP----SHISEHARDFLGCIFVEARHRPSAEELLRHPF 268
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
425-736 4.59e-22

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: 98.18  E-value: 4.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEiPVNSRIVrEVATLSRLQHQHVVRYYQAWFetgvvdpfagan 504
Cdd:cd06644   14 WEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKSEE-ELEDYMV-EIEILATCNHPYIVKLLGAFY------------ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 WGSKTAGSSMFSYSGAVSTEIPEQDNNLESTYLYIqmeycprtlrqvfesynhfdkdfawhLIRQIVEGLAHIHGQGIIH 584
Cdd:cd06644   80 WDGKLWIMIEFCPGGAVDAIMLELDRGLTEPQIQV--------------------------ICRQMLEALQYLHSMKIIH 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  585 RDFTPNNIFFDARNDIKIGDFGL-AKFLKleQLDQDGGFstdvagsgvdstgqAGTYFYTAPEI-----EQDWPkIDEKA 658
Cdd:cd06644  134 RDLKAGNVLLTLDGDIKLADFGVsAKNVK--TLQRRDSF--------------IGTPYWMAPEVvmcetMKDTP-YDYKA 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  659 DMYSLGVVFFELWHPFGTAMERHVILTNLKL-KGE-----LPLKWVNEFPEqasLLRRLMSPSPSDRPSATELLKHAFPP 732
Cdd:cd06644  197 DIWSLGITLIEMAQIEPPHHELNPMRVLLKIaKSEpptlsQPSKWSMEFRD---FLKTALDKHPETRPSAAQLLEHPFVS 273

                 ....
gi 30694992  733 RMES 736
Cdd:cd06644  274 SVTS 277
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
425-730 4.94e-22

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: 97.73  E-value: 4.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKE--IPVNsrIVREVATLSRLQ---HQHVVRYYqawfetgvvDP 499
Cdd:cd07838    1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRVPLSEegIPLS--TIREIALLKQLEsfeHPNVVRLL---------DV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  500 FAGANWGSKTAGSSMFsysgavstEIPEQDnnlESTYLyiqmEYCPRTlrqvfesynHFDKDFAWHLIRQIVEGLAHIHG 579
Cdd:cd07838   70 CHGPRTDRELKLTLVF--------EHVDQD---LATYL----DKCPKP---------GLPPETIKDLMRQLLRGLDFLHS 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  580 QGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEqldqdggfstdvagsgVDSTGQAGTYFYTAPEI----EQDWPkid 655
Cdd:cd07838  126 HRIVHRDLKPQNILVTSDGQVKLADFGLARIYSFE----------------MALTSVVVTLWYRAPEVllqsSYATP--- 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  656 ekADMYSLGVVFFELWH-----PFGTAMER-HVILTNLKLKGE------LPLKWVNeFP----------------EQASL 707
Cdd:cd07838  187 --VDMWSVGCIFAELFNrrplfRGSSEADQlGKIFDVIGLPSEeewprnSALPRSS-FPsytprpfksfvpeideEGLDL 263
                        330       340
                 ....*....|....*....|...
gi 30694992  708 LRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd07838  264 LKKMLTFNPHKRISAFEALQHPY 286
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
431-728 4.99e-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: 96.94  E-value: 4.99e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVvlcKNKLDG---RQYAVKKI-RLKDKEIPvN--SRIVREVATLSRLQHQHVVRyyqawfetgVVDPFagan 504
Cdd:cd14119    1 LGEGSYGKV---KEVLDTetlCRRAVKILkKRKLRRIP-NgeANVKREIQILRRLNHRNVIK---------LVDVL---- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysgavsteipeqdNNLESTYLYIQMEYCPRTLRQVFESYNhfDKDF----AWHLIRQIVEGLAHIHGQ 580
Cdd:cd14119   64 -------------------------YNEEKQKLYMVMEYCVGGLQEMLDSAP--DKRLpiwqAHGYFVQLIDGLEYLHSQ 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFDARNDIKIGDFGLAkflklEQLDQdggfstdVAGSGVDSTGQaGTYFYTAPEIEQDWPKIDE-KAD 659
Cdd:cd14119  117 GIIHKDIKPGNLLLTTDGTLKISDFGVA-----EALDL-------FAEDDTCTTSQ-GSPAFQPPEIANGQDSFSGfKVD 183
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30694992  660 MYSLGVVFFELW---HPF-GTAMERhvILTNLklkGELPLKWVNEFPEQ-ASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14119  184 IWSAGVTLYNMTtgkYPFeGDNIYK--LFENI---GKGEYTIPDDVDPDlQDLLRGMLEKDPEKRFTIEQIRQH 252
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
424-729 1.01e-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: 1.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYqawfetgvvdpfaga 503
Cdd:cd08220    1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQAALNEVKVLSMLHHPNIIEYY--------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssmfsysgavsteipeqDNNLESTYLYIQMEYCPR-TLRQVFESYNH--FDKDFAWHLIRQIVEGLAHIHGQ 580
Cdd:cd08220   66 -------------------------ESFLEDKALMIVMEYAPGgTLFEYIQQRKGslLSEEEILHFFVQILLALHHVHSK 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFDA-RNDIKIGDFGLAKFLkleqldqdggfSTDVAGSGVdstgqAGTYFYTAPEIEQDWPkIDEKAD 659
Cdd:cd08220  121 QILHRDLKTQNILLNKkRTVVKIGDFGISKIL-----------SSKSKAYTV-----VGTPCYISPELCEGKP-YNQKSD 183
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30694992  660 MYSLGVVFFELwhpfgTAMERHVILTNLK------LKGELPLKWVNEFPEQASLLRRLMSPSPSDRPSATELLKHA 729
Cdd:cd08220  184 IWALGCVLYEL-----ASLKRAFEAANLPalvlkiMRGTFAPISDRYSEELRHLILSMLHLDPNKRPTLSEIMAQP 254
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
424-728 1.14e-21

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: 96.34  E-value: 1.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVV-LCKNKLDGRQYAVKKIR-----LKDKEipvnsRIVREVATLSRLQ---HQHVVRYYQAWFET 494
Cdd:cd14052    1 RFANVELIGSGEFSQVYkVSERVPTGKVYAVKKLKpnyagAKDRL-----RRLEEVSILRELTldgHDNIVQLIDSWEYH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  495 GvvdpfaganwgsktagssmfsysgavsteipeqdnnlestYLYIQMEYCPRTLRQVFESYN----HFDKDFAWHLIRQI 570
Cdd:cd14052   76 G----------------------------------------HLYIQTELCENGSLDVFLSELgllgRLDEFRVWKILVEL 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  571 VEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEqldqdggfstdvagSGVDSTGQAgtyFYTAPEIEQD 650
Cdd:cd14052  116 SLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMATVWPLI--------------RGIEREGDR---EYIAPEILSE 178
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  651 wPKIDEKADMYSLGVVFFEL------------WH----------PFGTAMERHVILTNLKLKGELPLKWVNEFPEQASLL 708
Cdd:cd14052  179 -HMYDKPADIFSLGLILLEAaanvvlpdngdaWQklrsgdlsdaPRLSSTDLHSASSPSSNPPPDPPNMPILSGSLDRVV 257
                        330       340
                 ....*....|....*....|
gi 30694992  709 RRLMSPSPSDRPSATELLKH 728
Cdd:cd14052  258 RWMLSPEPDRRPTADDVLAT 277
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
431-721 2.12e-21

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: 95.21  E-value: 2.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYqawfetGVVDpfaganwgskta 510
Cdd:cd13978    1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLPLL------GVCV------------ 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  511 gssmfsysgavsteipeqdnnlESTYLYIQMEYCPR-TLRQVFESYNhfdKDFAWHL----IRQIVEGLAHIHG--QGII 583
Cdd:cd13978   63 ----------------------ERRSLGLVMEYMENgSLKSLLEREI---QDVPWSLrfriIHEIALGMNFLHNmdPPLL 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  584 HRDFTPNNIFFDARNDIKIGDFGLAKFlkleqldqdGGFSTDVAGSGvDSTGQAGTYFYTAPE-IEQDWPKIDEKADMYS 662
Cdd:cd13978  118 HHDLKPENILLDNHFHVKISDFGLSKL---------GMKSISANRRR-GTENLGGTPIYMAPEaFDDFNKKPTSKSDVYS 187
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30694992  663 LGVVffeLW------HPFGTAMERHVILTnLKLKGELP-------LKWVNEFPEQASLLRRLMSPSPSDRPS 721
Cdd:cd13978  188 FAIV---IWavltrkEPFENAINPLLIMQ-IVSKGDRPslddigrLKQIENVQELISLMIRCWDGNPDARPT 255
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
451-730 2.26e-21

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: 95.44  E-value: 2.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  451 YAVKKIRlKDKEipvnSRIVREVATLSRLQHQHVVRYYqAWFETgvvdpfaganwgsktagssmfsysgavsteipeqdn 530
Cdd:cd14010   28 VAIKCVD-KSKR----PEVLNEVRLTHELKHPNVLKFY-EWYET------------------------------------ 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  531 nleSTYLYIQMEYCP-RTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAk 609
Cdd:cd14010   66 ---SNHLWLVVEYCTgGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLA- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  610 flKLEQLDQDGGFSTDVAGSGVDSTGQA----GTYFYTAPEIEQDwPKIDEKADMYSLGVVFFELW--HP--FGTAMERh 681
Cdd:cd14010  142 --RREGEILKELFGQFSDEGNVNKVSKKqakrGTPYYMAPELFQG-GVHSFASDLWALGCVLYEMFtgKPpfVAESFTE- 217
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 30694992  682 viLTNLKLKGELPLKWVNEF----PEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14010  218 --LVEKILNEDPPPPPPKVSskpsPDFKSLLKGLLEKDPAKRLSWDELVKHPF 268
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
424-728 5.72e-21

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: 93.99  E-value: 5.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIR---------LKDK---EIPVNSRIVrevATLSRLQHQHVVRyyqaw 491
Cdd:cd14004    1 DYTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFkerilvdtwVRDRklgTVPLEIHIL---DTLNKRSHPNIVK----- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  492 fetgVVDPFAganwgsktagSSMFSYsgavsTEIPEQDNNLEstyLYIQMEYCPRtlrqvfesynhFDKDFAWHLIRQIV 571
Cdd:cd14004   73 ----LLDFFE----------DDEFYY-----LVMEKHGSGMD---LFDFIERKPN-----------MDEKEAKYIFRQVA 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  572 EGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqDGGFSTDVagsgvdstgqaGTYFYTAPEIEQDW 651
Cdd:cd14004  120 DAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSAAYIK------SGPFDTFV-----------GTIDYAAPEVLRGN 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  652 PKIDEKADMYSLGV-----VFFElwHPFGTAMErhviltnlKLKGEL-PLKWVNEfpEQASLLRRLMSPSPSDRPSATEL 725
Cdd:cd14004  183 PYGGKEQDIWALGVllytlVFKE--NPFYNIEE--------ILEADLrIPYAVSE--DLIDLISRMLNRDVGDRPTIEEL 250

                 ...
gi 30694992  726 LKH 728
Cdd:cd14004  251 LTD 253
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
425-670 5.95e-21

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: 94.66  E-value: 5.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYqawfetgvvdpfagan 504
Cdd:cd07835    1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIRLETEDEGVPSTAIREISLLKELNHPNIVRLL---------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysgavstEIPEQDNNLestylYIQMEYCPRTLRQVFESYNHFDKDFAwhLIR----QIVEGLAHIHGQ 580
Cdd:cd07835   65 -------------------DVVHSENKL-----YLVFEFLDLDLKKYMDSSPLTGLDPP--LIKsylyQLLQGIAFCHSH 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleqldqdgGFSTDVAGsgvdSTGQAGTYFYTAPEIEQDWPKIDEKADM 660
Cdd:cd07835  119 RVLHRDLKPQNLLIDTEGALKLADFGLAR-----------AFGVPVRT----YTHEVVTLWYRAPEILLGSKHYSTPVDI 183
                        250
                 ....*....|
gi 30694992  661 YSLGVVFFEL 670
Cdd:cd07835  184 WSVGCIFAEM 193
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
431-728 6.89e-21

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: 93.88  E-value: 6.89e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKlDGRQYAVKKIRLKDKEIPVnSRIVREVATLSRLQHQHVVRYYqawfetgvvdpfaganwgskta 510
Cdd:cd14066    1 IGSGGFGTVYKGVLE-NGTVVAVKRLNEMNCAASK-KEFLTELEMLGRLRHPNLVRLL---------------------- 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  511 GSSMfsysgavsteipEQDNNLestYLYiqmEYCP-RTLRQVFeSYNHFDKDFAWH----LIRQIVEGLAHIHGQG---I 582
Cdd:cd14066   57 GYCL------------ESDEKL---LVY---EYMPnGSLEDRL-HCHKGSPPLPWPqrlkIAKGIARGLEYLHEECpppI 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  583 IHRDFTPNNIFFDARNDIKIGDFGLAKFLkleqldqdggfstDVAGSGVDSTGQAGTYFYTAPEIEQDWpKIDEKADMYS 662
Cdd:cd14066  118 IHGDIKSSNILLDEDFEPKLTDFGLARLI-------------PPSESVSKTSAVKGTIGYLAPEYIRTG-RVSTKSDVYS 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  663 LGVVFFEL------WHPFGTAMERHVILTNLKLKGEL---------PLKWVNEFPEQASLLRRL----MSPSPSDRPSAT 723
Cdd:cd14066  184 FGVVLLELltgkpaVDENRENASRKDLVEWVESKGKEeledildkrLVDDDGVEEEEVEALLRLallcTRSDPSLRPSMK 263

                 ....*
gi 30694992  724 ELLKH 728
Cdd:cd14066  264 EVVQM 268
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
419-729 1.24e-20

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. 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 Wee1a 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: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 93.55  E-value: 1.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  419 SRYLNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRL-QHQHVVRYYQAWfetgvv 497
Cdd:cd14138    1 SRYATEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHSHVVRYYSAW------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  498 dpfaganwgsktagssmfsysgavsteipeqdnnLESTYLYIQMEYC-----PRTLRQVFESYNHFDKDFAWHLIRQIVE 572
Cdd:cd14138   75 ----------------------------------AEDDHMLIQNEYCnggslADAISENYRIMSYFTEPELKDLLLQVAR 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  573 GLAHIHGQGIIHRDFTPNNIFFdARNDI--------------------KIGDFGLAKFLKLEQLDQdggfstdvagsgvd 632
Cdd:cd14138  121 GLKYIHSMSLVHMDIKPSNIFI-SRTSIpnaaseegdedewasnkvifKIGDLGHVTRVSSPQVEE-------------- 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  633 stgqaGTYFYTAPEIEQDWPKIDEKADMYSLG--VVFFELWHPFGTAMER-HVIltnlkLKGELPlkwvnEFP-----EQ 704
Cdd:cd14138  186 -----GDSRFLANEVLQENYTHLPKADIFALAltVVCAAGAEPLPTNGDQwHEI-----RQGKLP-----RIPqvlsqEF 250
                        330       340
                 ....*....|....*....|....*
gi 30694992  705 ASLLRRLMSPSPSDRPSATELLKHA 729
Cdd:cd14138  251 LDLLKVMIHPDPERRPSAVALVKHS 275
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
425-730 1.45e-20

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: 93.27  E-value: 1.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYqawfetgvvdpfagan 504
Cdd:cd07839    2 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLY---------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysgavsteipeqDNNLESTYLYIQMEYCPRTLRQVFESYN-HFDKDFAWHLIRQIVEGLAHIHGQGII 583
Cdd:cd07839   66 ------------------------DVLHSDKKLTLVFEYCDQDLKKYFDSCNgDIDPEIVKSFMFQLLKGLAFCHSHNVL 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  584 HRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQldqdGGFSTDVAgsgvdstgqagTYFYTAPEIEQDWPKIDEKADMYSL 663
Cdd:cd07839  122 HRDLKPQNLLINKNGELKLADFGLARAFGIPV----RCYSAEVV-----------TLWYRPPDVLFGAKLYSTSIDMWSA 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  664 GVVFFEL--------------------WHPFGTAMERH-VILTNLKLKGELPL-----KWVNEFPEQAS----LLRRLMS 713
Cdd:cd07839  187 GCIFAELanagrplfpgndvddqlkriFRLLGTPTEESwPGVSKLPDYKPYPMypattSLVNVVPKLNStgrdLLQNLLV 266
                        330
                 ....*....|....*..
gi 30694992  714 PSPSDRPSATELLKHAF 730
Cdd:cd07839  267 CNPVQRISAEEALQHPY 283
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
431-728 2.58e-20

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: 91.56  E-value: 2.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVK--KIRLKDKEipvnsRIVREVATLSRLQHQHVVRYYQAwFETGvvdpfaganwgsk 508
Cdd:cd14006    1 LGRGRFGVVKRCIEKATGREFAAKfiPKRDKKKE-----AVLREISILNQLQHPRIIQLHEA-YESP------------- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  509 tagssmfsysgavsteipeqdnnlesTYLYIQMEYC--PRTLRQVFESYNHFDKDFAWHlIRQIVEGLAHIHGQGIIHRD 586
Cdd:cd14006   62 --------------------------TELVLILELCsgGELLDRLAERGSLSEEEVRTY-MRQLLEGLQYLHNHHILHLD 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  587 FTPNNIFFDAR--NDIKIGDFGLAKflkleQLDQDGGFSTdvagsgvdstgQAGTYFYTAPEIEQDWPkIDEKADMYSLG 664
Cdd:cd14006  115 LKPENILLADRpsPQIKIIDFGLAR-----KLNPGEELKE-----------IFGTPEFVAPEIVNGEP-VSLATDMWSIG 177
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30694992  665 VVFFELW---HPFGTAMERHvILTNLkLKGElpLKWVNEFPEQAS-----LLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14006  178 VLTYVLLsglSPFLGEDDQE-TLANI-SACR--VDFSEEYFSSVSqeakdFIRKLLVKEPRKRPTAQEALQH 245
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
420-730 2.61e-20

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 91.90  E-value: 2.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  420 RYLNdFEELkpLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAWFetgvvdp 499
Cdd:cd13983    1 RYLK-FNEV--LGRGSFKTVYRAFDTEEGIEVAWNEIKLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDSWE------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  500 faganwgsktagssmfsysgavsteipeqdNNLESTYLYIQmEYCPR-TLRQVFESYNHFDkdfaWHLI----RQIVEGL 574
Cdd:cd13983   71 ------------------------------SKSKKEVIFIT-ELMTSgTLKQYLKRFKRLK----LKVIkswcRQILEGL 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  575 AHIHGQG--IIHRDFTPNNIFFD-ARNDIKIGDFGLAKFLKleqldqdGGFSTDVagsgvdstgqAGTYFYTAPEIEQDw 651
Cdd:cd13983  116 NYLHTRDppIIHRDLKCDNIFINgNTGEVKIGDLGLATLLR-------QSFAKSV----------IGTPEFMAPEMYEE- 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  652 pKIDEKADMYSLGVVFFEL------WHPFGTAME--RHVIltnlklKGELP--LKWVNEfPEQASLLRRLMSPsPSDRPS 721
Cdd:cd13983  178 -HYDEKVDIYAFGMCLLEMatgeypYSECTNAAQiyKKVT------SGIKPesLSKVKD-PELKDFIEKCLKP-PDERPS 248

                 ....*....
gi 30694992  722 ATELLKHAF 730
Cdd:cd13983  249 ARELLEHPF 257
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
33-145 2.78e-20

RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. The function of this domain is unknown. GCN2 is the alpha-subunit of the only translation initiation factor (eIF2 alpha) kinase that appears in all eukaryotes. Its function requires an interaction with GCN1 via the domain at its N-terminus, which is termed the RWD domain after three major RWD-containing proteins: RING finger-containing proteins, WD-repeat-containing proteins, and yeast DEAD (DEXD)-like helicases. The structure forms an alpha + beta sandwich fold consisting of two layers: a four-stranded antiparallel beta-sheet, and three side-by-side alpha-helices.


Pssm-ID: 399058  Cd Length: 111  Bit Score: 87.38  E-value: 2.78e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992     33 ELLSEEITALSAIFQEDCKVVSDSR-SPPQIAIKLRPYSKDMGyEDTDISAMLIVRCLPGYPYKCPKLQITPEQGLTTAD 111
Cdd:pfam05773    1 EEQEEELEALESIYPDEFEVISDSPyESLEIEIKLSLDSDESD-SSHLPPLVLKFTLPEDYPDEPPKISLSSPWNLSDEQ 79
                           90       100       110
                   ....*....|....*....|....*....|....
gi 30694992    112 AEKLLSLLEDQANSNarEGRVMIFNLVEAAQEFL 145
Cdd:pfam05773   80 VLSLLEELEELAEEN--LGEVMIFELIEWLQENL 111
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
423-740 3.37e-20

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: 92.49  E-value: 3.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIrLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAWFEtgvvdpfag 502
Cdd:cd06621    1 DKIVELSSLGEGAGGSVTKCRLRNTKTIFALKTI-TTDPNPDVQKQILRELEINKSCASPYIVKYYGAFLD--------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgsktagssmfsysgavsteipEQDNNLestylYIQMEYCP-----RTLRQVFESYNHFDKDFAWHLIRQIVEGLAHI 577
Cdd:cd06621   71 ------------------------EQDSSI-----GIAMEYCEggsldSIYKKVKKKGGRIGEKVLGKIAESVLKGLSYL 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  578 HGQGIIHRDFTPNNIFFDARNDIKIGDFGLAkflkleqldqdGGFSTDVAGSGVdstgqaGTYFYTAPEIEQDWP-KIde 656
Cdd:cd06621  122 HSRKIIHRDIKPSNILLTRKGQVKLCDFGVS-----------GELVNSLAGTFT------GTSYYMAPERIQGGPySI-- 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  657 KADMYSLGVVFFELWH---PFGTAMERHV--------ILT--NLKLKGE--LPLKWVNEFpeqASLLRRLMSPSPSDRPS 721
Cdd:cd06621  183 TSDVWSLGLTLLEVAQnrfPFPPEGEPPLgpiellsyIVNmpNPELKDEpeNGIKWSESF---KDFIEKCLEKDGTRRPG 259
                        330
                 ....*....|....*....
gi 30694992  722 ATELLKHAFPPRMESELLD 740
Cdd:cd06621  260 PWQMLAHPWIKAQEKKKVN 278
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
425-739 3.51e-20

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: 92.15  E-value: 3.51e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVnSRIVREVATLSRLQH---QHVVRYYQAWfetgvvdpfa 501
Cdd:cd06917    3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNLDTDDDDV-SDIQKEVALLSQLKLgqpKNIIKYYGSY---------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 ganwgsktagssmfsysgavsteipeqdnnLESTYLYIQMEYCP----RTLRQVfesyNHFDKDFAWHLIRQIVEGLAHI 577
Cdd:cd06917   72 ------------------------------LKGPSLWIIMDYCEggsiRTLMRA----GPIAERYIAVIMREVLVALKFI 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  578 HGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLkleqldqdggfstdVAGSGVDSTgQAGTYFYTAPEIEQDWPKIDEK 657
Cdd:cd06917  118 HKDGIIHRDIKAANILVTNTGNVKLCDFGVAASL--------------NQNSSKRST-FVGTPYWMAPEVITEGKYYDTK 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  658 ADMYSLGVVFFELWH---PF-GTAMERHVILTNLKLKGELPLkwvNEF-PEQASLLRRLMSPSPSDRPSATELLK----- 727
Cdd:cd06917  183 ADIWSLGITTYEMATgnpPYsDVDALRAVMLIPKSKPPRLEG---NGYsPLLKEFVAACLDEEPKDRLSADELLKskwik 259
                        330
                 ....*....|....
gi 30694992  728 -HAFPPRME-SELL 739
Cdd:cd06917  260 qHSKTPTSVlKELI 273
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
428-730 4.39e-20

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: 91.39  E-value: 4.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  428 LKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKD---KEIPVNSRIVREVATLSRlQHQHVVRYYQAwFETGvvdpfagan 504
Cdd:cd05611    1 LKPISKGAFGSVYLAKKRSTGDYFAIKVLKKSDmiaKNQVTNVKAERAIMMIQG-ESPYVAKLYYS-FQSK--------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysgavsteipeqdnnlesTYLYIQMEYCP----RTLRQVFesyNHFDKDFAWHLIRQIVEGLAHIHGQ 580
Cdd:cd05611   70 ------------------------------DYLYLVMEYLNggdcASLIKTL---GGLPEDWAKQYIAEVVLGVEDLHQR 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQDggFStdvagsgvdstgqaGTYFYTAPEIEQDWPKiDEKADM 660
Cdd:cd05611  117 GIIHRDIKPENLLIDQTGHLKLTDFGLSRNGLEKRHNKK--FV--------------GTPDYLAPETILGVGD-DKMSDW 179
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30694992  661 YSLGVVFFEL---WHPFGTAMERHVILTNLKLKGELPlKWVNEF--PEQASLLRRLMSPSPSDRPSAT---ELLKHAF 730
Cdd:cd05611  180 WSLGCVIFEFlfgYPPFHAETPDAVFDNILSRRINWP-EEVKEFcsPEAVDLINRLLCMDPAKRLGANgyqEIKSHPF 256
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
431-728 5.24e-20

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


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 91.65  E-value: 5.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVK---KIRLKDK----------------EIPVNS--RIVREVATLSRLQHQHVVRYYQ 489
Cdd:cd14118    2 IGKGSYGIVKLAYNEEDNTLYAMKilsKKKLLKQagffrrppprrkpgalGKPLDPldRVYREIAILKKLDHPNVVKLVE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  490 awfetgVVDPfaganwgsktagssmfsysgavsteiPEQDNnlestyLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIRQ 569
Cdd:cd14118   82 ------VLDD--------------------------PNEDN------LYMVFELVDKGAVMEVPTDNPLSEETARSYFRD 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  570 IVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLakflkleqldqdggfSTDVAGSGVDSTGQAGTYFYTAPE-IE 648
Cdd:cd14118  124 IVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFGV---------------SNEFEGDDALLSSTAGTPAFMAPEaLS 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  649 QDWPKIDEKA-DMYSLGVVFFELWH---PFgtaMERHVILTNLKLKGElPLKWVNEF---PEQASLLRRLMSPSPSDRPS 721
Cdd:cd14118  189 ESRKKFSGKAlDIWAMGVTLYCFVFgrcPF---EDDHILGLHEKIKTD-PVVFPDDPvvsEQLKDLILRMLDKNPSERIT 264

                 ....*..
gi 30694992  722 ATELLKH 728
Cdd:cd14118  265 LPEIKEH 271
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
431-730 6.37e-20

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: 91.71  E-value: 6.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAWFETG----VVDPFAGanwg 506
Cdd:cd14086    9 LGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGfhylVFDLVTG---- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  507 sktagssmfsysGAVSTEIpeqdnnlestylyIQMEYcprtlrqvfesYNHFDkdfAWHLIRQIVEGLAHIHGQGIIHRD 586
Cdd:cd14086   85 ------------GELFEDI-------------VAREF-----------YSEAD---ASHCIQQILESVNHCHQNGIVHRD 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  587 FTPNNIFFDARN---DIKIGDFGLAkflkleqldqdggfsTDVAGSGVDSTGQAGTYFYTAPEIEQDWPkIDEKADMYSL 663
Cdd:cd14086  126 LKPENLLLASKSkgaAVKLADFGLA---------------IEVQGDQQAWFGFAGTPGYLSPEVLRKDP-YGKPVDIWAC 189
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30694992  664 GVVFFEL---WHPFGTamERHVILTNLKLKGEL---PLKWVNEFPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14086  190 GVILYILlvgYPPFWD--EDQHRLYAQIKAGAYdypSPEWDTVTPEAKDLINQMLTVNPAKRITAAEALKHPW 260
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
428-725 1.06e-19

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: 90.90  E-value: 1.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  428 LKPLGQGGFGHVVLCK----NKLDGRQYAVKKIRlKDKEIPVNSRIVREVATLSRLQHQHVVRYyqawfeTGVVDPFAGA 503
Cdd:cd05038    9 IKQLGEGHFGSVELCRydplGDNTGEQVAVKSLQ-PSGEEQHMSDFKREIEILRTLDHEYIVKY------KGVCESPGRR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 NwgsktagssmfsysgavsteipeqdnnlestyLYIQMEYCPR-TLRQVFEsyNHFDKDFAWHLIR---QIVEGLAHIHG 579
Cdd:cd05038   82 S--------------------------------LRLIMEYLPSgSLRDYLQ--RHRDQIDLKRLLLfasQICKGMEYLGS 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  580 QGIIHRDFTPNNIFFDARNDIKIGDFGLAKFlkleqLDQDGGFSTdvagsgVDSTGQAGTYFYtAPE-IEQDwpKIDEKA 658
Cdd:cd05038  128 QRYIHRDLAARNILVESEDLVKISDFGLAKV-----LPEDKEYYY------VKEPGESPIFWY-APEcLRES--RFSSAS 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  659 DMYSLGVVFFELW-------HPFGTAMER---------HVILTNLKLKGE-LPLkwvnefPEQA-----SLLRRLMSPSP 716
Cdd:cd05038  194 DVWSFGVTLYELFtygdpsqSPPALFLRMigiaqgqmiVTRLLELLKSGErLPR------PPSCpdevyDLMKECWEYEP 267

                 ....*....
gi 30694992  717 SDRPSATEL 725
Cdd:cd05038  268 QDRPSFSDL 276
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
422-725 1.10e-19

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: 91.22  E-value: 1.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKD-KE-IPVNSriVREVATLSRLQHQHVVRyyqawfetgVVDP 499
Cdd:cd07866    7 LRDYEILGKLGEGTFGEVYKARQIKTGRVVALKKILMHNeKDgFPITA--LREIKILKKLKHPNVVP---------LIDM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  500 FaganwgsktagssmFSYSGAVSTEIPEqdnnlestyLYIQMEYCPRTLRQVFESYN-HFDKDFAWHLIRQIVEGLAHIH 578
Cdd:cd07866   76 A--------------VERPDKSKRKRGS---------VYMVTPYMDHDLSGLLENPSvKLTESQIKCYMLQLLEGINYLH 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  579 GQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKleqlDQDGGFSTDVAGSGVDSTGQAGTYFYTAPEIEQDWPKIDEKA 658
Cdd:cd07866  133 ENHILHRDIKAANILIDNQGILKIADFGLARPYD----GPPPNPKGGGGGGTRKYTNLVVTRWYRPPELLLGERRYTTAV 208
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30694992  659 DMYSLGVVFFELWhpfgtamERHVILTNlklKGELplkwvnefpEQASLLRRLM-SPSPSDRPSATEL 725
Cdd:cd07866  209 DIWGIGCVFAEMF-------TRRPILQG---KSDI---------DQLHLIFKLCgTPTEETWPGWRSL 257
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
425-730 1.18e-19

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: 91.05  E-value: 1.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQ-HVVRYyqawfetgvvdpfaga 503
Cdd:cd07837    3 YEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRLEMEEEGVPSTALREVSLLQMLSQSiYIVRL---------------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssmfsysgaVSTEIPEQDNNlesTYLYIQMEYCPRTLRQVFESY-----NHFDKDFAWHLIRQIVEGLAHIH 578
Cdd:cd07837   67 -----------------LDVEHVEENGK---PLLYLVFEYLDTDLKKFIDSYgrgphNPLPAKTIQSFMYQLCKGVAHCH 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  579 GQGIIHRDFTPNNIFFD-ARNDIKIGDFGLAKflkleqldqdgGFSTDVAGsgvdSTGQAGTYFYTAPEIEQDWPKIDEK 657
Cdd:cd07837  127 SHGVMHRDLKPQNLLVDkQKGLLKIADLGLGR-----------AFTIPIKS----YTHEIVTLWYRAPEVLLGSTHYSTP 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  658 ADMYSLGVVFFE----------------LWHPF---GTAMERHVI-LTNLKLKGELPlKWVNE---------FPEQASLL 708
Cdd:cd07837  192 VDMWSVGCIFAEmsrkqplfpgdselqqLLHIFrllGTPNEEVWPgVSKLRDWHEYP-QWKPQdlsravpdlEPEGVDLL 270
                        330       340
                 ....*....|....*....|..
gi 30694992  709 RRLMSPSPSDRPSATELLKHAF 730
Cdd:cd07837  271 TKMLAYDPAKRISAKAALQHPY 292
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
431-730 1.26e-19

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: 90.57  E-value: 1.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEiPVNSRIVrEVATLSRLQHQHVVRYYQAWFetgvvdpfaganwgskta 510
Cdd:cd06611   13 LGDGAFGKVYKAQHKETGLFAAAKIIQIESEE-ELEDFMV-EIDILSECKHPNIVGLYEAYF------------------ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  511 gssmfsysgavsteipeQDNNLestylYIQMEYCPR-TLRQVFESYNH-FDKDFAWHLIRQIVEGLAHIHGQGIIHRDFT 588
Cdd:cd06611   73 -----------------YENKL-----WILIEFCDGgALDSIMLELERgLTEPQIRYVCRQMLEALNFLHSHKVIHRDLK 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  589 PNNIFFDARNDIKIGDFGLAKFLKLEQLDQDggfsTDVagsgvdstgqaGTYFYTAPEI-----EQDWPkIDEKADMYSL 663
Cdd:cd06611  131 AGNILLTLDGDVKLADFGVSAKNKSTLQKRD----TFI-----------GTPYWMAPEVvacetFKDNP-YDYKADIWSL 194
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30694992  664 GVVFFELWHPFGTAMERHVILTNLK-LKGELPL-----KWVNEFPEqasLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd06611  195 GITLIELAQMEPPHHELNPMRVLLKiLKSEPPTldqpsKWSSSFND---FLKSCLVKDPDDRPTAAELLKHPF 264
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
418-670 1.26e-19

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: 91.76  E-value: 1.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  418 SSRYLndfeELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEiPVNSRIvREVATLSRLQHQHVVRYYQAWFETGvv 497
Cdd:cd07854    4 GSRYM----DLRPLGCGSNGLVFSAVDSDCDKRVAVKKIVLTDPQ-SVKHAL-REIKIIRRLDHDNIVKVYEVLGPSG-- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  498 dpfaganwgsktagssmfsysgavsTEIPEQDNNL-ESTYLYIQMEYCPRTLRQVFE----SYNHFdKDFAWHLIRqive 572
Cdd:cd07854   76 -------------------------SDLTEDVGSLtELNSVYIVQEYMETDLANVLEqgplSEEHA-RLFMYQLLR---- 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  573 GLAHIHGQGIIHRDFTPNNIFFDARNDI-KIGDFGLAKFlkleqLDQdggfstDVAGSGVDSTGQAgTYFYTAPEIEQDW 651
Cdd:cd07854  126 GLKYIHSANVLHRDLKPANVFINTEDLVlKIGDFGLARI-----VDP------HYSHKGYLSEGLV-TKWYRSPRLLLSP 193
                        250
                 ....*....|....*....
gi 30694992  652 PKIDEKADMYSLGVVFFEL 670
Cdd:cd07854  194 NNYTKAIDMWAAGCIFAEM 212
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
431-728 1.38e-19

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: 89.59  E-value: 1.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYA---VKKIRLKDKEipvnsRIVREVATLSRLQHQHVVRYYQAwFETG-----VVDPFAG 502
Cdd:cd14103    1 LGRGKFGTVYRCVEKATGKELAakfIKCRKAKDRE-----DVRNEIEIMNQLRHPRLLQLYDA-FETPremvlVMEYVAG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 AnwgsktagssmfsysgavstEIPEqdnnlestylyiqmeycprtlRQVFESYNHFDKDFAwHLIRQIVEGLAHIHGQGI 582
Cdd:cd14103   75 G--------------------ELFE---------------------RVVDDDFELTERDCI-LFMRQICEGVQYMHKQGI 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  583 IHRDFTPNNIFFDAR--NDIKIGDFGLAKFLKLEQldqdggfSTDVagsgvdstgQAGTYFYTAPEIeQDWPKIDEKADM 660
Cdd:cd14103  113 LHLDLKPENILCVSRtgNQIKIIDFGLARKYDPDK-------KLKV---------LFGTPEFVAPEV-VNYEPISYATDM 175
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  661 YSLGVVFFEL---WHPF--GTAMErhvILTNLklkgeLPLKWvnEFPEQA---------SLLRRLMSPSPSDRPSATELL 726
Cdd:cd14103  176 WSVGVICYVLlsgLSPFmgDNDAE---TLANV-----TRAKW--DFDDEAfddisdeakDFISKLLVKDPRKRMSAAQCL 245

                 ..
gi 30694992  727 KH 728
Cdd:cd14103  246 QH 247
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
412-730 1.41e-19

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: 90.89  E-value: 1.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  412 PNASLPSSRYLNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRL-KDKE-IPVNSriVREVATLSRLQHQHVVRYYQ 489
Cdd:cd07865    1 DQVEFPFCDEVSKYEKLAKIGQGTFGEVFKARHRKTGQIVALKKVLMeNEKEgFPITA--LREIKILQLLKHENVVNLIE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  490 awfetgvvdpfaganwgsktagssmfsysgaVSTEIPEQDNNLESTYlYIQMEYCPRTLRQVFESYN-HFDKDFAWHLIR 568
Cdd:cd07865   79 -------------------------------ICRTKATPYNRYKGSI-YLVFEFCEHDLAGLLSNKNvKFTLSEIKKVMK 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  569 QIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleqldqdgGFSTDVAGSGVDSTGQAGTYFYTAPEI- 647
Cdd:cd07865  127 MLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLAR-----------AFSLAKNSQPNRYTNRVVTLWYRPPELl 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  648 --EQDW-PKIdekaDMYSLGVVFFELW--HPF--GTAmERHVI-----------------LTNLKL--KGELP------- 694
Cdd:cd07865  196 lgERDYgPPI----DMWGAGCIMAEMWtrSPImqGNT-EQHQLtlisqlcgsitpevwpgVDKLELfkKMELPqgqkrkv 270
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 30694992  695 ---LKWVNEFPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd07865  271 kerLKPYVKDPYALDLIDKLLVLDPAKRIDADTALNHDF 309
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
431-730 1.54e-19

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: 89.70  E-value: 1.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVK---KIRLKDKEIPVNSRivrEVATLSRLQHQHVVRYYQAwfetgvvdpfaganwgs 507
Cdd:cd14075   10 LGSGNFSQVKLGIHQLTKEKVAIKildKTKLDQKTQRLLSR---EISSMEKLHHPNIIRLYEV----------------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 ktagssmfsysgaVSTEipeqdnnlesTYLYIQMEYCPRTlrqvfESYNH------FDKDFAWHLIRQIVEGLAHIHGQG 581
Cdd:cd14075   70 -------------VETL----------SKLHLVMEYASGG-----ELYTKistegkLSESEAKPLFAQIVSAVKHMHENN 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQ-LDQdggFstdvagsgvdstgqAGTYFYTAPEIEQDWPKIDEKADM 660
Cdd:cd14075  122 IIHRDLKAENVFYASNNCVKVGDFGFSTHAKRGEtLNT---F--------------CGSPPYAAPELFKDEHYIGIYVDI 184
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30694992  661 YSLGVVFFelwhpF---GTAMERHVILTNLK---LKGE--LPlKWVNEfpEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14075  185 WALGVLLY-----FmvtGVMPFRAETVAKLKkciLEGTytIP-SYVSE--PCQELIRGILQPVPSDRYSIDEIKNSEW 254
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
425-728 1.90e-19

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: 89.48  E-value: 1.90e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992    425 FEELKPLGQGGFGHVVLCKNKLDGRQY----AVKKIRLKDKEIPVNSrIVREVATLSRLQHQHVVRYYqawfetgvvdpf 500
Cdd:pfam07714    1 LTLGEKLGEGAFGEVYKGTLKGEGENTkikvAVKTLKEGADEEERED-FLEEASIMKKLDHPNIVKLL------------ 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992    501 aganwgsktagssmfsysGAVSTEIPeqdnnlestyLYIQMEYCP----RT-LRQVFESYNHFDK-DFAWhlirQIVEGL 574
Cdd:pfam07714   68 ------------------GVCTQGEP----------LYIVTEYMPggdlLDfLRKHKRKLTLKDLlSMAL----QIAKGM 115
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992    575 AHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleqlDQDGGFSTDVAGSGVDStgqagtYFYTAPEIEQDWpKI 654
Cdd:pfam07714  116 EYLESKNFVHRDLAARNCLVSENLVVKISDFGLSR-------DIYDDDYYRKRGGGKLP------IKWMAPESLKDG-KF 181
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992    655 DEKADMYSLGVVFFElwhpfgtamerhvILTNlklkGELPLKWVN--------------EFPEQAS-----LLRRLMSPS 715
Cdd:pfam07714  182 TSKSDVWSFGVLLWE-------------IFTL----GEQPYPGMSneevlefledgyrlPQPENCPdelydLMKQCWAYD 244
                          330
                   ....*....|...
gi 30694992    716 PSDRPSATELLKH 728
Cdd:pfam07714  245 PEDRPTFSELVED 257
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
431-728 3.06e-19

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: 88.92  E-value: 3.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVK-----KIRLKDkeipvnsrIVREVA-TLSRLQHQHVVRYYQAWFETgvvdpfagan 504
Cdd:cd13987    1 LGEGTYGKVLLAVHKGSGTKMALKfvpkpSTKLKD--------FLREYNiSLELSVHPHIIKTYDVAFET---------- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysgavsteipeqdnnlESTYLYIQmEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGII 583
Cdd:cd13987   63 ----------------------------EDYYVFAQ-EYAPYgDLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLV 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  584 HRDFTPNNIF-FDAR-NDIKIGDFGLakflkleqldqdggfsTDVAGSGVDSTgqAGTYFYTAPEIEQ----DWPKIDEK 657
Cdd:cd13987  114 HRDIKPENVLlFDKDcRRVKLCDFGL----------------TRRVGSTVKRV--SGTIPYTAPEVCEakknEGFVVDPS 175
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  658 ADMYSLGVVFFEL---WHPFGTAM------ERHVILTNLKLKGeLPLKWVNEFPEQASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd13987  176 IDVWAFGVLLFCCltgNFPWEKADsddqfyEEFVRWQKRKNTA-VPSQWRRFTPKALRMFKKLLAPEPERRCSIKEVFKY 254
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
422-728 3.56e-19

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: 88.86  E-value: 3.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVK---KIRLKDKEipVNSRIVREVATLSRLQHQHVVRYYqAWFEtgvvd 498
Cdd:cd14116    4 LEDFEIGRPLGKGKFGNVYLAREKQSKFILALKvlfKAQLEKAG--VEHQLRREVEIQSHLRHPNILRLY-GYFH----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  499 pfaganwgsktagssmfsysgavsteipeqdnnlESTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHI 577
Cdd:cd14116   76 ----------------------------------DATRVYLILEYAPLgTVYRELQKLSKFDEQRTATYITELANALSYC 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  578 HGQGIIHRDFTPNNIFFDARNDIKIGDFGLAkflkleqldqdggfstdVAGSGVDSTGQAGTYFYTAPEIEQDWPKiDEK 657
Cdd:cd14116  122 HSKRVIHRDIKPENLLLGSAGELKIADFGWS-----------------VHAPSSRRTTLCGTLDYLPPEMIEGRMH-DEK 183
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30694992  658 ADMYSLGVVFFELW---HPFGTAMERHVILTNLKLKGELPLkWVNEfpEQASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14116  184 VDLWSLGVLCYEFLvgkPPFEANTYQETYKRISRVEFTFPD-FVTE--GARDLISRLLKHNPSQRPMLREVLEH 254
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
425-674 5.39e-19

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: 88.09  E-value: 5.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKlDGRQYAVKKIR---LKDKEIPVNSRivREVATLSRLQHQHVVRYYQAwFETgvvdpfa 501
Cdd:cd14161    5 YEFLETLGKGTYGRVKKARDS-SGRLVAIKSIRkdrIKDEQDLLHIR--REIEIMSSLNHPHIISVYEV-FEN------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 ganwgsktagssmfsysgavsteipeqdnnleSTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQ 580
Cdd:cd14161   74 --------------------------------SSKIVIVMEYASRgDLYDYISERQRLSELEARHFFRQIVSAVHYCHAN 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQDggfstdvagsgvdstgQAGTYFYTAPEIEQDWPKIDEKADM 660
Cdd:cd14161  122 GIVHRDLKLENILLDANGNIKIADFGLSNLYNQDKFLQT----------------YCGSPLYASPEIVNGRPYIGPEVDS 185
                        250
                 ....*....|....*..
gi 30694992  661 YSLGVVFFELWH---PF 674
Cdd:cd14161  186 WSLGVLLYILVHgtmPF 202
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
429-729 5.98e-19

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: 88.12  E-value: 5.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKLDGRQYAVKKI-RLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAwFETgvvdpfaganwgs 507
Cdd:cd14162    6 KTLGHGSYAVVKKAYSTKHKCKVAIKIVsKKKAPEDYLQKFLPREIEVIKGLKHPNLICFYEA-IET------------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 ktagssmfsysgavsteipeqdnnleSTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRD 586
Cdd:cd14162   72 --------------------------TSRVYIIMELAENgDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRD 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  587 FTPNNIFFDARNDIKIGDFGLAKflkleqldqdgGFSTDVAGSGVDSTGQAGTYFYTAPEIEQDWPKIDEKADMYSLGVV 666
Cdd:cd14162  126 LKCENLLLDKNNNLKITDFGFAR-----------GVMKTKDGKPKLSETYCGSYAYASPEILRGIPYDPFLSDIWSMGVV 194
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30694992  667 FFELWH---PFGTamERHVILtnlklkgelpLKWVNE---FP-------EQASLLRRLMSPSPSdRPSATELLKHA 729
Cdd:cd14162  195 LYTMVYgrlPFDD--SNLKVL----------LKQVQRrvvFPknptvseECKDLILRMLSPVKK-RITIEEIKRDP 257
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
431-730 5.99e-19

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 88.23  E-value: 5.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKkirlkdkEIPV-NSRIVR----EVATLSRLQHQHVVRYYQAWFETGVVDPFAganw 505
Cdd:cd06624   16 LGKGTFGVVYAARDLSTQVRIAIK-------EIPErDSREVQplheEIALHSRLSHKNIVQYLGSVSEDGFFKIFM---- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  506 gSKTAGSSMFSYsgAVSTEIPEQDNnlESTYLYiqmeycprtlrqvfesYNhfdkdfawhliRQIVEGLAHIHGQGIIHR 585
Cdd:cd06624   85 -EQVPGGSLSAL--LRSKWGPLKDN--ENTIGY----------------YT-----------KQILEGLKYLHDNKIVHR 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  586 DFTPNNIFFDARND-IKIGDFGLAKFLkleqldqdggfstdvAGSGVDSTGQAGTYFYTAPEIeqdwpkIDE-------K 657
Cdd:cd06624  133 DIKGDNVLVNTYSGvVKISDFGTSKRL---------------AGINPCTETFTGTLQYMAPEV------IDKgqrgygpP 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  658 ADMYSLGVV----------FFELWHP----FGTAMerhviltnLKLKGELPlkwvNEFPEQA-SLLRRLMSPSPSDRPSA 722
Cdd:cd06624  192 ADIWSLGCTiiematgkppFIELGEPqaamFKVGM--------FKIHPEIP----ESLSEEAkSFILRCFEPDPDKRATA 259

                 ....*...
gi 30694992  723 TELLKHAF 730
Cdd:cd06624  260 SDLLQDPF 267
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
424-730 6.00e-19

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: 89.67  E-value: 6.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIpVNSRIVREVATLSRLQHQHVVryyqawfetGVVDpfaga 503
Cdd:cd07849    6 RYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISPFEHQT-YCLRTLREIKILLRFKHENII---------GILD----- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssmfsysgavsTEIPEQDNNLESTYLyIQmEYCPRTLRQVFESYNHFDkDFAWHLIRQIVEGLAHIHGQGII 583
Cdd:cd07849   71 -------------------IQRPPTFESFKDVYI-VQ-ELMETDLYKLIKTQHLSN-DHIQYFLYQILRGLKYIHSANVL 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  584 HRDFTPNNIFFDARNDIKIGDFGLAKfLKLEQLDQDGGFSTDVAgsgvdstgqagTYFYTAPEIEQDWPKIDEKADMYSL 663
Cdd:cd07849  129 HRDLKPSNLLLNTNCDLKICDFGLAR-IADPEHDHTGFLTEYVA-----------TRWYRAPEIMLNSKGYTKAIDIWSV 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  664 GVVFFE----------------LWHPF---GTA-MERHVILTNLKLKG---ELPLK----WVNEFPEQAS----LLRRLM 712
Cdd:cd07849  197 GCILAEmlsnrplfpgkdylhqLNLILgilGTPsQEDLNCIISLKARNyikSLPFKpkvpWNKLFPNADPkaldLLDKML 276
                        330
                 ....*....|....*...
gi 30694992  713 SPSPSDRPSATELLKHAF 730
Cdd:cd07849  277 TFNPHKRITVEEALAHPY 294
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
429-729 6.16e-19

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: 88.22  E-value: 6.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKD------KEIPVNSRIVREVATLSRLQHQHVVRYYQaWFETgvvdpfag 502
Cdd:cd14084   12 RTLGSGACGEVKLAYDKSTCKKVAIKIINKRKftigsrREINKPRNIETEIEILKKLSHPCIIKIED-FFDA-------- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgsktagssmfsysgavsteipeqdnnleSTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQG 581
Cdd:cd14084   83 -------------------------------EDDYYIVLELMEGgELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNG 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARND---IKIGDFGLAKFlkleqLDQDGGFSTdvagsgvdstgQAGTYFYTAPEIEQDWPKI--DE 656
Cdd:cd14084  132 IIHRDLKPENVLLSSQEEeclIKITDFGLSKI-----LGETSLMKT-----------LCGTPTYLAPEVLRSFGTEgyTR 195
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30694992  657 KADMYSLGVVFFEL---WHPFGTAMERhVILTNLKLKGEL---PLKWVNEFPEQASLLRRLMSPSPSDRPSATELLKHA 729
Cdd:cd14084  196 AVDCWSLGVILFIClsgYPPFSEEYTQ-MSLKEQILSGKYtfiPKAWKNVSEEAKDLVKKMLVVDPSRRPSIEEALEHP 273
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
424-728 8.53e-19

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: 87.43  E-value: 8.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELkpLGQGGFGHVVLCKNKLDGRQYAVKKIR---LKDKEIPVNSrivrEVATLSRLQHQHVVRYYqawfetgvvdpf 500
Cdd:cd14083    6 EFKEV--LGTGAFSEVVLAEDKATGKLVAIKCIDkkaLKGKEDSLEN----EIAVLRKIKHPNIVQLL------------ 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  501 aganwgsktagssmfsysgavstEIPEQDNNLestYLYIQMEYCPRTLRQVFESYNHFDKDfAWHLIRQIVEGLAHIHGQ 580
Cdd:cd14083   68 -----------------------DIYESKSHL---YLVMELVTGGELFDRIVEKGSYTEKD-ASHLIRQVLEAVDYLHSL 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFF---DARNDIKIGDFGLAKflkleqLDQDGGFSTdvagsgvdstgQAGTYFYTAPEIEQDWPKIDEk 657
Cdd:cd14083  121 GIVHRDLKPENLLYyspDEDSKIMISDFGLSK------MEDSGVMST-----------ACGTPGYVAPEVLAQKPYGKA- 182
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30694992  658 ADMYSLGVVFFEL---WHPFGTAMERHVILTNLKLKGELPLKWVNEFPEQA-SLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14083  183 VDCWSIGVISYILlcgYPPFYDENDSKLFAQILKAEYEFDSPYWDDISDSAkDFIRHLMEKDPNKRYTCEQALEH 257
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
431-730 8.99e-19

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: 87.29  E-value: 8.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIP-VNSRIVREVATLSRLQHQHVVRYyqawfetgvvdpfaganwgskt 509
Cdd:cd14189    9 LGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKPhQREKIVNEIELHRDLHHKHVVKF---------------------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  510 agssmfsysgavSTEIPEQDNnlestyLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFT 588
Cdd:cd14189   67 ------------SHHFEDAEN------IYIFLELCSRkSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLK 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  589 PNNIFFDARNDIKIGDFGLAKflKLEQLDQdggfstdvagsgvDSTGQAGTYFYTAPEIEQDWPKIDEkADMYSLGVVFF 668
Cdd:cd14189  129 LGNFFINENMELKVGDFGLAA--RLEPPEQ-------------RKKTICGTPNYLAPEVLLRQGHGPE-SDVWSLGCVMY 192
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30694992  669 ELW---HPFGTAMERHVILTNLKLKGELPLKWVnefPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14189  193 TLLcgnPPFETLDLKETYRCIKQVKYTLPASLS---LPARHLLAGILKRNPGDRLTLDQILEHEF 254
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
424-671 9.07e-19

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: 88.25  E-value: 9.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYyqawfetgvvdpfaga 503
Cdd:cd07861    1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEEGVPSTAIREISLLKELQHPNIVCL---------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssmfsysgavsteipeQDNNLESTYLYIQMEYCPRTLRQVFESY---NHFDKDFAWHLIRQIVEGLAHIHGQ 580
Cdd:cd07861   65 ------------------------EDVLMQENRLYLVFEFLSMDLKKYLDSLpkgKYMDAELVKSYLYQILQGILFCHSR 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFDARNDIKIGDFGLAKFLkleqldqdgGFSTDVagsgvdSTGQAGTYFYTAPEIEQDWPKIDEKADM 660
Cdd:cd07861  121 RVLHRDLKPQNLLIDNKGVIKLADFGLARAF---------GIPVRV------YTHEVVTLWYRAPEVLLGSPRYSTPVDI 185
                        250
                 ....*....|.
gi 30694992  661 YSLGVVFFELW 671
Cdd:cd07861  186 WSIGTIFAEMA 196
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
424-730 1.24e-18

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: 87.22  E-value: 1.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKD-KEIPVNSRIVREVATLSRLQHQHVVRYYQaWFEtgvvdpfag 502
Cdd:cd14186    2 DFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAmQKAGMVQRVRNEVEIHCQLKHPSILELYN-YFE--------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgsktagssmfsysgavsteipeqdnnlESTYLYIQMEYC--PRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQ 580
Cdd:cd14186   72 ------------------------------DSNYVYLVLEMChnGEMSRYLKNRKKPFTEDEARHFMHQIVTGMLYLHSH 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQldqDGGFStdvagsgvdstgQAGTYFYTAPEIEQDWPKIDEkADM 660
Cdd:cd14186  122 GILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPH---EKHFT------------MCGTPNYISPEIATRSAHGLE-SDV 185
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30694992  661 YSLGVVFFELW---HPFGTAMERH----VILTNLKLKGELPLkwvnefpEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14186  186 WSLGCMFYTLLvgrPPFDTDTVKNtlnkVVLADYEMPAFLSR-------EAQDLIHQLLRKNPADRLSLSSVLDHPF 255
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
424-728 1.95e-18

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. 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 Wee1b 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: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 86.91  E-value: 1.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRL-QHQHVVRYYQAWfetgvvdpfag 502
Cdd:cd14139    1 EFLELEKIGVGEFGSVYKCIKRLDGCVYAIKRSMRPFAGSSNEQLALHEVYAHAVLgHHPHVVRYYSAW----------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgsktagssmfsysgavsteipeqdnnLESTYLYIQMEYC-----PRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHI 577
Cdd:cd14139   70 -----------------------------AEDDHMIIQNEYCnggslQDAISENTKSGNHFEEPELKDILLQVSMGLKYI 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  578 HGQGIIHRDFTPNNIFFDARNDI----------------------KIGDFGLAKFLKLEQLDQdggfstdvagsgvdstg 635
Cdd:cd14139  121 HNSGLVHLDIKPSNIFICHKMQSssgvgeevsneedeflsanvvyKIGDLGHVTSINKPQVEE----------------- 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  636 qaGTYFYTAPEIEQDWPKIDEKADMYSLGVVFF------------ELWHpfgtamerHViltnlkLKGELPlKWVNEFPE 703
Cdd:cd14139  184 --GDSRFLANEILQEDYRHLPKADIFALGLTVAlaagaeplptngAAWH--------HI------RKGNFP-DVPQELPE 246
                        330       340
                 ....*....|....*....|....*.
gi 30694992  704 Q-ASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14139  247 SfSSLLKNMIQPDPEQRPSATALARH 272
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
424-728 2.06e-18

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


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 86.97  E-value: 2.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELkpLGQGGFGHVVLCKNKLDGRQYAVKKIrlKDKEIPVNSRIVREVATLSRLQHQHVVryyqawfetGVVDPFaga 503
Cdd:cd14166    6 IFMEV--LGSGAFSEVYLVKQRSTGKLYALKCI--KKSPLSRDSSLENEIAVLKRIKHENIV---------TLEDIY--- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssmfsysgavsteipeqdnnlEST---YLYIQMEYCPRTLRQVFESYNHFDKDfAWHLIRQIVEGLAHIHGQ 580
Cdd:cd14166   70 -----------------------------ESTthyYLVMQLVSGGELFDRILERGVYTEKD-ASRVINQVLSAVKYLHEN 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFF---DARNDIKIGDFGLAKflkleqLDQDGGFSTdvagsgvdstgQAGTYFYTAPEIEQDWPkIDEK 657
Cdd:cd14166  120 GIVHRDLKPENLLYltpDENSKIMITDFGLSK------MEQNGIMST-----------ACGTPGYVAPEVLAQKP-YSKA 181
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30694992  658 ADMYSLGVVFFEL---WHPFGTAMERHVILTNLKLKGELPLKWVNEFPEQAS-LLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14166  182 VDCWSIGVITYILlcgYPPFYEETESRLFEKIKEGYYEFESPFWDDISESAKdFIRHLLEKNPSKRYTCEKALSH 256
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
419-733 2.15e-18

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: 87.55  E-value: 2.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  419 SRYLNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLK-DKE-IPVNSriVREVATLSRLQHQHVVRYYQAwfetgv 496
Cdd:cd07864    3 KRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDnEKEgFPITA--IREIKILRQLNHRSVVNLKEI------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  497 vdpfaganwgsktagssmfsysgaVSTEIPEQDNNLESTYLYIQMEYCPRTLRQVFES-YNHFDKDFAWHLIRQIVEGLA 575
Cdd:cd07864   75 ------------------------VTDKQDALDFKKDKGAFYLVFEYMDHDLMGLLESgLVHFSEDHIKSFMKQLLEGLN 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  576 HIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEqldqdggfstdvagSGVDSTGQAGTYFYTAPEI----EQDW 651
Cdd:cd07864  131 YCHKKNFLHRDIKCSNILLNNKGQIKLADFGLARLYNSE--------------ESRPYTNKVITLWYRPPELllgeERYG 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  652 PKIdekaDMYSLGVVFFELWhpfgtamerhviltnlklkGELPLKWVNEFPEQASLLRRLM-SPSPSDRPSATEL-LKHA 729
Cdd:cd07864  197 PAI----DVWSCGCILGELF-------------------TKKPIFQANQELAQLELISRLCgSPCPAVWPDVIKLpYFNT 253

                 ....
gi 30694992  730 FPPR 733
Cdd:cd07864  254 MKPK 257
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
424-730 3.12e-18

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: 85.96  E-value: 3.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKI-------------RLKDKEIPVNSRIVREVATLSRLQHQHVVRYYqa 490
Cdd:cd14077    2 NWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIprasnaglkkereKRLEKEISRDIRTIREAALSSLLNHPHICRLR-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  491 wfetgvvdpfaganwgsktagssmfsysgavsteipeqDNNLESTYLYIQMEYCP-RTLRQVFESYNHFDKDFAWHLIRQ 569
Cdd:cd14077   80 --------------------------------------DFLRTPNHYYMLFEYVDgGQLLDYIISHGKLKEKQARKFARQ 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  570 IVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFlkleqLDQDGGFSTdvagsgvdstgQAGTYFYTAPEIEQ 649
Cdd:cd14077  122 IASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGLSNL-----YDPRRLLRT-----------FCGSLYFAAPELLQ 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  650 DWPKIDEKADMYSLGVVFFELWH---PFGtamERHVILTNLKLKgelplKWVNEFP-----EQASLLRRLMSPSPSDRPS 721
Cdd:cd14077  186 AQPYTGPEVDVWSFGVVLYVLVCgkvPFD---DENMPALHAKIK-----KGKVEYPsylssECKSLISRMLVVDPKKRAT 257

                 ....*....
gi 30694992  722 ATELLKHAF 730
Cdd:cd14077  258 LEQVLNHPW 266
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
537-796 3.75e-18

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 89.31  E-value: 3.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   537 LYIQMEY-----CPRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKfl 611
Cdd:PTZ00267  140 LLLIMEYgsggdLNKQIKQRLKEHLPFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSK-- 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   612 kleqlDQDGGFSTDVAGSGvdstgqAGTYFYTAPEIeqdW--PKIDEKADMYSLGVVFFELW---HPFGTAMERHVILTN 686
Cdd:PTZ00267  218 -----QYSDSVSLDVASSF------CGTPYYLAPEL---WerKRYSKKADMWSLGVILYELLtlhRPFKGPSQREIMQQV 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   687 LKLKgelplkwVNEFPEQAS-----LLRRLMSPSPSDRPSATELLKHAFpPRMESELLDNILRimqTSEDSSVYDRvvsv 761
Cdd:PTZ00267  284 LYGK-------YDPFPCPVSsgmkaLLDPLLSKNPALRPTTQQLLHTEF-LKYVANLFQDIVR---HSETISPHDR---- 348
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 30694992   762 ifdEEVLemKSHQSSRSRLCADDSyIQYTEINTEL 796
Cdd:PTZ00267  349 ---EEIL--RQLQESGERAPPPSS-IRYGVVTSDV 377
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
429-728 3.78e-18

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


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 85.78  E-value: 3.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKLDGRQYAVKKI-RLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQawfetgVVDpfaganwgs 507
Cdd:cd14079    8 KTLGVGSFGKVKLAEHELTGHKVAVKILnRQKIKSLDMEEKIRREIQILKLFRHPHIIRLYE------VIE--------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 ktagssmfsysgaVSTEIpeqdnnlestylYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRD 586
Cdd:cd14079   73 -------------TPTDI------------FMVMEYVSGgELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRD 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  587 FTPNNIFFDARNDIKIGDFGLAKFLKleqldqDGGFSTDVAGSGVdstgqagtyfYTAPEIeqdwpkIDEK------ADM 660
Cdd:cd14079  128 LKPENLLLDSNMNVKIADFGLSNIMR------DGEFLKTSCGSPN----------YAAPEV------ISGKlyagpeVDV 185
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30694992  661 YSLGVVFFELW---HPFGtamERHVILTNLKLKG---ELPlKWVNefPEQASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14079  186 WSCGVILYALLcgsLPFD---DEHIPNLFKKIKSgiyTIP-SHLS--PGARDLIKRMLVVDPLKRITIPEIRQH 253
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
392-730 4.08e-18

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 87.57  E-value: 4.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   392 QNMASTSVPQFWEPPSDSCEPNASLPSSRY-------LNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIrLKDKEIP 464
Cdd:PLN00034   36 QRDPSLAVPLPLPPPSSSSSSSSSSSASGSapsaaksLSELERVNRIGSGAGGTVYKVIHRPTGRLYALKVI-YGNHEDT 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   465 VNSRIVREVATLSRLQHQHVVRYYQawfetgvvdpfaganwgsktagssMFSYSGAVSTEIPEQDN-NLESTYLYiqmey 543
Cdd:PLN00034  115 VRRQICREIEILRDVNHPNVVKCHD------------------------MFDHNGEIQVLLEFMDGgSLEGTHIA----- 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   544 cprtlrqvfesynhfDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLeqldqdggfS 623
Cdd:PLN00034  166 ---------------DEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQ---------T 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   624 TDVAGSGVdstgqaGTYFYTAPE-IEQDWP--KIDEKA-DMYSLGVVFFELW---HPFGTAMERH-VILTNLKLKGELPL 695
Cdd:PLN00034  222 MDPCNSSV------GTIAYMSPErINTDLNhgAYDGYAgDIWSLGVSILEFYlgrFPFGVGRQGDwASLMCAICMSQPPE 295
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 30694992   696 KWVNEFPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:PLN00034  296 APATASREFRHFISCCLQREPAKRWSAMQLLQHPF 330
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
431-728 4.76e-18

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: 85.68  E-value: 4.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRlKDKEIPVNSRIV-REVATLSRLQHQHVVrYYQAWFETgvvdpfaganwgskt 509
Cdd:cd14097    9 LGQGSFGVVIEATHKETQTKWAIKKIN-REKAGSSAVKLLeREVDILKHVNHAHII-HLEEVFET--------------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  510 agssmfsysgavsteipeqdnnleSTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFT 588
Cdd:cd14097   72 ------------------------PKRMYLVMELCEDgELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLK 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  589 PNNIFFDA-------RNDIKIGDFGLAKflkleqldQDGGFSTDVAgsgvdsTGQAGTYFYTAPEI--EQDWpkiDEKAD 659
Cdd:cd14097  128 LENILVKSsiidnndKLNIKVTDFGLSV--------QKYGLGEDML------QETCGTPIYMAPEVisAHGY---SQQCD 190
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30694992  660 MYSLGVVFFELWH---PFGTAMERHviLTNLKLKGELPLK---WVNEFPEQASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14097  191 IWSIGVIMYMLLCgepPFVAKSEEK--LFEEIRKGDLTFTqsvWQSVSDAAKNVLQQLLKVDPAHRMTASELLDN 263
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
423-730 5.23e-18

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: 87.60  E-value: 5.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKkirlkdkeipvnSRIVREVATLSRLQHQHVVRyyqawfetgvvDPFAG 502
Cdd:cd05629    1 EDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMK------------TLLKSEMFKKDQLAHVKAER-----------DVLAE 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 AN--WgsktagssmfsysgAVSTEIPEQDnnleSTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHG 579
Cdd:cd05629   58 SDspW--------------VVSLYYSFQD----AQYLYLIMEFLPGgDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHK 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  580 QGIIHRDFTPNNIFFDARNDIKIGDFGL----------AKFLKLEQLDQDGGFSTDVAGSGVDST--------------- 634
Cdd:cd05629  120 LGFIHRDIKPDNILIDRGGHIKLSDFGLstgfhkqhdsAYYQKLLQGKSNKNRIDNRNSVAVDSInltmsskdqiatwkk 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  635 -------GQAGTYFYTAPEI--------EQDWpkidekadmYSLGVVFFEL---WHPF--GTAMERHVILTNLKLKGELP 694
Cdd:cd05629  200 nrrlmaySTVGTPDYIAPEIflqqgygqECDW---------WSLGAIMFECligWPPFcsENSHETYRKIINWRETLYFP 270
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 30694992  695 LKwVNEFPEQASLLRRLMSPSPS--DRPSATELLKHAF 730
Cdd:cd05629  271 DD-IHLSVEAEDLIRRLITNAENrlGRGGAHEIKSHPF 307
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
425-670 5.87e-18

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: 87.02  E-value: 5.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVryyqawfetGVVDPFagan 504
Cdd:cd07877   19 YQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVI---------GLLDVF---- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsySGAVSTEipeqdnnlESTYLYIQMEYCPRTLRQVFESYNHFDkDFAWHLIRQIVEGLAHIHGQGIIH 584
Cdd:cd07877   86 -------------TPARSLE--------EFNDVYLVTHLMGADLNNIVKCQKLTD-DHVQFLIYQILRGLKYIHSADIIH 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  585 RDFTPNNIFFDARNDIKIGDFGLAKFLKLEQldqdggfstdvagsgvdsTGQAGTYFYTAPEIEQDWPKIDEKADMYSLG 664
Cdd:cd07877  144 RDLKPSNLAVNEDCELKILDFGLARHTDDEM------------------TGYVATRWYRAPEIMLNWMHYNQTVDIWSVG 205

                 ....*.
gi 30694992  665 VVFFEL 670
Cdd:cd07877  206 CIMAEL 211
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
420-730 6.93e-18

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: 85.74  E-value: 6.93e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  420 RYLNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRL-KDKE-IPVNSriVREVATLSRLQHQHVVRYYQAwfetgVV 497
Cdd:cd07843    2 RSVDEYEKLNRIEEGTYGVVYRARDKKTGEIVALKKLKMeKEKEgFPITS--LREINILLKLQHPNIVTVKEV-----VV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  498 dpfaganwgsktaGSSMfsysgavsteipeqdnnlesTYLYIQMEYCPRTLRQVFEsynHFDKDFAWH----LIRQIVEG 573
Cdd:cd07843   75 -------------GSNL--------------------DKIYMVMEYVEHDLKSLME---TMKQPFLQSevkcLMLQLLSG 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  574 LAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLA-KFlkleqldqdgGFSTDVAGSGVdstgqaGTYFYTAPEIEQDWP 652
Cdd:cd07843  119 VAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLArEY----------GSPLKPYTQLV------VTLWYRAPELLLGAK 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  653 KIDEKADMYSLGVVFFEL-------------------WHPFGTAMER---------HVILTNLKLKGELPLKwvNEFPEQ 704
Cdd:cd07843  183 EYSTAIDMWSVGCIFAELltkkplfpgkseidqlnkiFKLLGTPTEKiwpgfselpGAKKKTFTKYPYNQLR--KKFPAL 260
                        330       340       350
                 ....*....|....*....|....*....|..
gi 30694992  705 A------SLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd07843  261 SlsdngfDLLNRLLTYDPAKRISAEDALKHPY 292
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
420-728 8.25e-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: 84.69  E-value: 8.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  420 RYLNDFEELkpLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSrIVREVATLSRLQHQHVVRYyqawfetgvvdp 499
Cdd:cd14167    2 RDIYDFREV--LGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKETS-IENEIAVLHKIKHPNIVAL------------ 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  500 faganwgsktagssmfsysgavsTEIPEQDNNLestYLYIQMEYCPRTLRQVFESYNHFDKDfAWHLIRQIVEGLAHIHG 579
Cdd:cd14167   67 -----------------------DDIYESGGHL---YLIMQLVSGGELFDRIVEKGFYTERD-ASKLIFQILDAVKYLHD 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  580 QGIIHRDFTPNNIFF---DARNDIKIGDFGLAKflkleqldqdggfstdVAGSGVDSTGQAGTYFYTAPEIEQDWPkIDE 656
Cdd:cd14167  120 MGIVHRDLKPENLLYyslDEDSKIMISDFGLSK----------------IEGSGSVMSTACGTPGYVAPEVLAQKP-YSK 182
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30694992  657 KADMYSLGVVFFEL---WHPFGTAMERHVILTNLKLKGELPLKWVNEFPEQAS-LLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14167  183 AVDCWSIGVIAYILlcgYPPFYDENDAKLFEQILKAEYEFDSPYWDDISDSAKdFIQHLMEKDPEKRFTCEQALQH 258
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
429-730 1.31e-17

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: 84.31  E-value: 1.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKLDGRQYAVKKIRLkDKEIPVNSRIVR----EVATLSRLQHQHVVRYYQAwfetgVVDPfagan 504
Cdd:cd06653    8 KLLGRGAFGEVYLCYDADTGRELAVKQVPF-DPDSQETSKEVNalecEIQLLKNLRHDRIVQYYGC-----LRDP----- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysgavsteipeqdnnlESTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGII 583
Cdd:cd06653   77 ----------------------------EEKKLSIFVEYMPGgSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIV 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  584 HRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqdggfSTDVAGSGVDSTgqAGTYFYTAPEIEQDwPKIDEKADMYSL 663
Cdd:cd06653  129 HRDIKGANILRDSAGNVKLGDFGASKRIQ----------TICMSGTGIKSV--TGTPYWMSPEVISG-EGYGRKADVWSV 195
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30694992  664 GVVFFELWHPFGTAMERHVILTNLKLKGElPLKwvNEFPEQAS-----LLRRLMSPSpSDRPSATELLKHAF 730
Cdd:cd06653  196 ACTVVEMLTEKPPWAEYEAMAAIFKIATQ-PTK--PQLPDGVSdacrdFLRQIFVEE-KRRPTAEFLLRHPF 263
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
423-728 1.46e-17

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: 84.80  E-value: 1.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVV-LCKNKLDGRQYAVKKIR---LKDKEIPVNSR--IVREVATLSRLQHQHVVRYYqAWFETGV 496
Cdd:cd14096    1 ENYRLINKIGEGAFSNVYkAVPLRNTGKPVAIKVVRkadLSSDNLKGSSRanILKEVQIMKRLSHPNIVKLL-DFQESDE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  497 vdpfaganwgsktagssmfsysgavsteipeqdnnlestYLYIQMEYCP--RTLRQVFEsYNHFDKDFAWHLIRQIVEGL 574
Cdd:cd14096   80 ---------------------------------------YYYIVLELADggEIFHQIVR-LTYFSEDLSRHVITQVASAV 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  575 AHIHGQGIIHRDFTPNNIFFDA-----------RND----------------------IKIGDFGLAKFLKLEQLDQdgg 621
Cdd:cd14096  120 KYLHEIGVVHRDIKPENLLFEPipfipsivklrKADddetkvdegefipgvggggigiVKLADFGLSKQVWDSNTKT--- 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  622 fstdvagsgvdstgQAGTYFYTAPEIEQDWpKIDEKADMYSLGVVFFEL---WHPFGTamERHVILTNLKLKGELP-LK- 696
Cdd:cd14096  197 --------------PCGTVGYTAPEVVKDE-RYSKKVDMWALGCVLYTLlcgFPPFYD--ESIETLTEKISRGDYTfLSp 259
                        330       340       350
                 ....*....|....*....|....*....|...
gi 30694992  697 WVNEFPEQA-SLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14096  260 WWDEISKSAkDLISHLLTVDPAKRYDIDEFLAH 292
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
431-730 1.52e-17

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: 84.50  E-value: 1.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKI---RLKDKE---IPVNSRIVrevatLSRLQHQHVVRYYQAwFETgvvdpfagan 504
Cdd:cd05577    1 LGRGGFGEVCACQVKATGKMYACKKLdkkRIKKKKgetMALNEKII-----LEKVSSPFIVSLAYA-FET---------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsKTAGSSMFSYSGAVSTEipeqdnnlestylyiqmeycprtlrqvFESYNH----FDKDFAWHLIRQIVEGLAHIHGQ 580
Cdd:cd05577   65 ---KDKLCLVLTLMNGGDLK---------------------------YHIYNVgtrgFSEARAIFYAAEIICGLEHLHNR 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqdggfstdvagSGVDSTGQAGTYFYTAPEIEQDWPKIDEKADM 660
Cdd:cd05577  115 FIVYRDLKPENILLDDHGHVRISDLGLAVEFK----------------GGKKIKGRVGTHGYMAPEVLQKEVAYDFSVDW 178
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  661 YSLGVVFFELWH---PF---GTAMERHVILTNLKlkgELPLKWVNEF-PEQASLLRRLMSPSPSDR-----PSATELLKH 728
Cdd:cd05577  179 FALGCMLYEMIAgrsPFrqrKEKVDKEELKRRTL---EMAVEYPDSFsPEARSLCEGLLQKDPERRlgcrgGSADEVKEH 255

                 ..
gi 30694992  729 AF 730
Cdd:cd05577  256 PF 257
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
425-670 1.64e-17

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: 85.49  E-value: 1.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVryyqawfetGVVDPFAGAN 504
Cdd:cd07878   17 YQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRPFQSLIHARRTYRELRLLKHMKHENVI---------GLLDVFTPAT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 WGSKtagssmFSYSGAVSTEIPEQDNNLEStylyiqmeyCPRtlrqvfesynhFDKDFAWHLIRQIVEGLAHIHGQGIIH 584
Cdd:cd07878   88 SIEN------FNEVYLVTNLMGADLNNIVK---------CQK-----------LSDEHVQFLIYQLLRGLKYIHSAGIIH 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  585 RDFTPNNIFFDARNDIKIGDFGLAKflkleQLDQdggfstdvagsgvDSTGQAGTYFYTAPEIEQDWPKIDEKADMYSLG 664
Cdd:cd07878  142 RDLKPSNVAVNEDCELRILDFGLAR-----QADD-------------EMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVG 203

                 ....*.
gi 30694992  665 VVFFEL 670
Cdd:cd07878  204 CIMAEL 209
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
431-730 1.83e-17

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: 84.03  E-value: 1.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGhVVLCKNKLDGRQYAVKKIRL----KDKEIPVNSRIVREVATLSRLQHQHVVRYYQAWFETGVVDPFaganwg 506
Cdd:cd06631    9 LGKGAYG-TVYCGLTSTGQLIAVKQVELdtsdKEKAEKEYEKLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIF------ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  507 sktagssmfsysgavsteipeqdnnlestylyiqMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHR 585
Cdd:cd06631   82 ----------------------------------MEFVPGgSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHR 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  586 DFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDqdgGFSTDVAGSgvdstgQAGTYFYTAPEIeqdwpkIDE-----KADM 660
Cdd:cd06631  128 DIKGNNIMLMPNGVIKLIDFGCAKRLCINLSS---GSQSQLLKS------MRGTPYWMAPEV------INEtghgrKSDI 192
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30694992  661 YSLGVVFFELW--HPFGTAMER----HVILTNLKLKGELPLKWVnefPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd06631  193 WSIGCTVFEMAtgKPPWADMNPmaaiFAIGSGRKPVPRLPDKFS---PEARDFVHACLTRDQDERPSAEQLLKHPF 265
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
431-730 2.06e-17

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: 83.94  E-value: 2.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKI-RLKDKEIP-----VNSRIVREVATLSRLQ-HQHVVRYYQAwFETgvvdpfaga 503
Cdd:cd14093   11 LGRGVSSTVRRCIEKETGQEFAVKIIdITGEKSSEneaeeLREATRREIEILRQVSgHPNIIELHDV-FES--------- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssmfsysgavsteipeqdnnleSTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGI 582
Cdd:cd14093   81 ------------------------------PTFIFLVFELCRKgELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNI 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  583 IHRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqDGGFSTDVagsgvdstgqAGTYFYTAPEI-----EQDWPKIDEK 657
Cdd:cd14093  131 VHRDLKPENILLDDNLNVKISDFGFATRLD------EGEKLREL----------CGTPGYLAPEVlkcsmYDNAPGYGKE 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  658 ADMYSLGVVFFEL-------WHPFGTAMERHVILTNLKLKGElplKWVNEFPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14093  195 VDMWACGVIMYTLlagcppfWHRKQMVMLRNIMEGKYEFGSP---EWDDISDTAKDLISKLLVVDPKKRLTAEEALEHPF 271
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
425-725 2.43e-17

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


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 83.91  E-value: 2.43e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEE-----LKPLGQGGFGHVVLCK----NKLDGRQYAVKKIR------LKDKEipvnsrivREVATLSRLQHQHVVRYYQ 489
Cdd:cd14205    1 FEErhlkfLQQLGKGNFGSVEMCRydplQDNTGEVVAVKKLQhsteehLRDFE--------REIEILKSLQHDNIVKYKG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  490 AWFETGvvdpfaganwgsktagssmfsysgavsteipeqDNNLEstylyIQMEYCPR-TLRQVFESY-NHFDKDFAWHLI 567
Cdd:cd14205   73 VCYSAG---------------------------------RRNLR-----LIMEYLPYgSLRDYLQKHkERIDHIKLLQYT 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  568 RQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldQDGGFSTdvagsgVDSTGQAGTYFYtAPEI 647
Cdd:cd14205  115 SQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLP-----QDKEYYK------VKEPGESPIFWY-APES 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  648 EQDwPKIDEKADMYSLGVVFFELW-------HPFGTAMER------------HVIlTNLKLKGELPLKwvNEFPEQA-SL 707
Cdd:cd14205  183 LTE-SKFSVASDVWSFGVVLYELFtyiekskSPPAEFMRMigndkqgqmivfHLI-ELLKNNGRLPRP--DGCPDEIyMI 258
                        330
                 ....*....|....*...
gi 30694992  708 LRRLMSPSPSDRPSATEL 725
Cdd:cd14205  259 MTECWNNNVNQRPSFRDL 276
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
425-670 3.88e-17

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: 84.27  E-value: 3.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVryyqawfetGVVDPFagan 504
Cdd:cd07851   17 YQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRPFQSAIHAKRTYRELRLLKHMKHENVI---------GLLDVF---- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgskTAGSSMfsysgavsteipeqdNNLESTYLYiqMEYCPRTLRQVFESyNHFDKDFAWHLIRQIVEGLAHIHGQGIIH 584
Cdd:cd07851   84 ----TPASSL---------------EDFQDVYLV--THLMGADLNNIVKC-QKLSDDHIQFLVYQILRGLKYIHSAGIIH 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  585 RDFTPNNIFFDARNDIKIGDFGLAKflkleQLDQdggfstdvagsgvDSTGQAGTYFYTAPEIEQDWPKIDEKADMYSLG 664
Cdd:cd07851  142 RDLKPSNLAVNEDCELKILDFGLAR-----HTDD-------------EMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVG 203

                 ....*.
gi 30694992  665 VVFFEL 670
Cdd:cd07851  204 CIMAEL 209
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
425-730 3.92e-17

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: 83.32  E-value: 3.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAwfetgvvdpfagan 504
Cdd:cd07860    2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDV-------------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysgaVSTEipeqdnnlesTYLYIQMEYCPRTLRQVFESYNhfDKDFAWHLIR----QIVEGLAHIHGQ 580
Cdd:cd07860   68 ----------------IHTE----------NKLYLVFEFLHQDLKKFMDASA--LTGIPLPLIKsylfQLLQGLAFCHSH 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleqldqdgGFSTDVAgsgvDSTGQAGTYFYTAPEIEQDWPKIDEKADM 660
Cdd:cd07860  120 RVLHRDLKPQNLLINTEGAIKLADFGLAR-----------AFGVPVR----TYTHEVVTLWYRAPEILLGCKYYSTAVDI 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  661 YSLGVVF-------------------FELWHPFGTAMErhVI---LTNLK-LKGELPlKW-VNEF--------PEQASLL 708
Cdd:cd07860  185 WSLGCIFaemvtrralfpgdseidqlFRIFRTLGTPDE--VVwpgVTSMPdYKPSFP-KWaRQDFskvvppldEDGRDLL 261
                        330       340
                 ....*....|....*....|..
gi 30694992  709 RRLMSPSPSDRPSATELLKHAF 730
Cdd:cd07860  262 SQMLHYDPNKRISAKAALAHPF 283
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
422-730 4.45e-17

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: 82.46  E-value: 4.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEElkPLGQGGFGHVVLCKNKLDGRQYAVKKI-RLKDKEIPvNSRIVREVATLSRLQHQHVVRYYQawfetgVVDP- 499
Cdd:cd14074    4 LYDLEE--TLGRGHFAVVKLARHVFTGEKVAVKVIdKTKLDDVS-KAHLFQEVRCMKLVQHPNVVRLYE------VIDTq 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  500 ---FAGANWGsktAGSSMFSYsgavsteIPEQDNNLestylyiqmeycprtlrqvfesynhfDKDFAWHLIRQIVEGLAH 576
Cdd:cd14074   75 tklYLILELG---DGGDMYDY-------IMKHENGL--------------------------NEDLARKYFRQIVSAISY 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  577 IHGQGIIHRDFTPNN-IFFDARNDIKIGDFGLA-KFLKLEQLDQdggfstdvagsgvdstgQAGTYFYTAPEI----EQD 650
Cdd:cd14074  119 CHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSnKFQPGEKLET-----------------SCGSLAYSAPEIllgdEYD 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  651 WPKIdekaDMYSLGVVFFEL---WHPFGTAMERHVILTNLKLKGELPlKWVNefPEQASLLRRLMSPSPSDRPSATELLK 727
Cdd:cd14074  182 APAV----DIWSLGVILYMLvcgQPPFQEANDSETLTMIMDCKYTVP-AHVS--PECKDLIRRMLIRDPKKRASLEEIEN 254

                 ...
gi 30694992  728 HAF 730
Cdd:cd14074  255 HPW 257
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
429-730 4.74e-17

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: 82.37  E-value: 4.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIP-VNSRIVREVATLSRLQHQHVVRYYQaWFEtgvvdpfaganwgs 507
Cdd:cd14188    7 KVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKPhQREKIDKEIELHRILHHKHVVQFYH-YFE-------------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 ktagssmfsysgavsteipEQDNnlestyLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRD 586
Cdd:cd14188   72 -------------------DKEN------IYILLEYCSRrSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRD 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  587 FTPNNIFFDARNDIKIGDFGLAKflKLEQLDQdggfstdvagsgvDSTGQAGTYFYTAPEIEQDWPKIDEkADMYSLGVV 666
Cdd:cd14188  127 LKLGNFFINENMELKVGDFGLAA--RLEPLEH-------------RRRTICGTPNYLSPEVLNKQGHGCE-SDIWALGCV 190
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30694992  667 FFELW---HPFGTAMERHVILTNLKLKGELPlkwvNEFPEQAS-LLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14188  191 MYTMLlgrPPFETTNLKETYRCIREARYSLP----SSLLAPAKhLIASMLSKNPEDRPSLDEIIRHDF 254
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
425-728 4.98e-17

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: 83.36  E-value: 4.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRL-KDKEIP--VNSRIVREVATLSRLQHQHVVRYYqawfetgvvdpfa 501
Cdd:cd14094    5 YELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVaKFTSSPglSTEDLKREASICHMLKHPHIVELL------------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 ganwgsKTAGSSMfsysgavsteipeqdnnlestYLYIQMEY------CPRTLRQVFESYNhFDKDFAWHLIRQIVEGLA 575
Cdd:cd14094   72 ------ETYSSDG---------------------MLYMVFEFmdgadlCFEIVKRADAGFV-YSEAVASHYMRQILEALR 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  576 HIHGQGIIHRDFTPNNIFFDARND---IKIGDFGLAKflkleqldqdggfstDVAGSGVDSTGQAGTYFYTAPEIEQDWP 652
Cdd:cd14094  124 YCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAI---------------QLGESGLVAGGRVGTPHFMAPEVVKREP 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  653 kIDEKADMYSLGVVFFELWH---PFGTAMERhviLTNLKLKGELPLK---WVNEFPEQASLLRRLMSPSPSDRPSATELL 726
Cdd:cd14094  189 -YGKPVDVWGCGVILFILLSgclPFYGTKER---LFEGIIKGKYKMNprqWSHISESAKDLVRRMLMLDPAERITVYEAL 264

                 ..
gi 30694992  727 KH 728
Cdd:cd14094  265 NH 266
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
425-727 5.25e-17

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: 82.30  E-value: 5.25e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRlKDKEIPVNS--RIVREVATLSRLQHQHVVRYYQAWfetgvvdpfag 502
Cdd:cd05578    2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMN-KQKCIEKDSvrNVLNELEILQELEHPFLVNLWYSF----------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgsktagssmfsysgavsteipeQDNnlesTYLYIQMEYC-PRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQG 581
Cdd:cd05578   70 -------------------------QDE----EDMYMVVDLLlGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKN 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLdqdggfstdvagsgvdSTGQAGTYFYTAPEI--------EQDWpk 653
Cdd:cd05578  121 IIHRDIKPDNILLDEQGHVHITDFNIATKLTDGTL----------------ATSTSGTKPYMAPEVfmragysfAVDW-- 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  654 idekadmYSLGVVFFELW-----HPFGTAMERHVILTNLKLKGEL-PLKWVnefPEQASLLRRLMSPSPSDRPSATELLK 727
Cdd:cd05578  183 -------WSLGVTAYEMLrgkrpYEIHSRTSIEEIRAKFETASVLyPAGWS---EEAIDLINKLLERDPQKRLGDLSDLK 252
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
417-739 5.75e-17

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: 83.19  E-value: 5.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  417 PSSRYLNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLkDKE---IPVNSriVREVATLSRLQHQHVVRYYQawfe 493
Cdd:cd07845    1 GRCRSVTEFEKLNRIGEGTYGIVYRARDTTSGEIVALKKVRM-DNErdgIPISS--LREITLLLNLRHPNIVELKE---- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  494 tgVVdpfaganwgsktagssmfsysgavsteipeQDNNLESTYLYiqMEYCPRTLRQVFESY-NHFDKDFAWHLIRQIVE 572
Cdd:cd07845   74 --VV------------------------------VGKHLDSIFLV--MEYCEQDLASLLDNMpTPFSESQVKCLMLQLLR 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  573 GLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleqldqdgGFSTDVAgsgvDSTGQAGTYFYTAPEIEQDWP 652
Cdd:cd07845  120 GLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLAR-----------TYGLPAK----PMTPKVVTLWYRAPELLLGCT 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  653 KIDEKADMYSLGVVFFELW--HP-FGTAMERHVILTNLKLKG-----------ELPLKWVNEFPEQA------------- 705
Cdd:cd07845  185 TYTTAIDMWAVGCILAELLahKPlLPGKSEIEQLDLIIQLLGtpnesiwpgfsDLPLVGKFTLPKQPynnlkhkfpwlse 264
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 30694992  706 ---SLLRRLMSPSPSDRPSATELLKHAF----PPRMESELL 739
Cdd:cd07845  265 aglRLLNFLLMYDPKKRATAEEALESSYfkekPLPCEPEMM 305
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
425-728 6.88e-17

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: 82.79  E-value: 6.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVK---KIRLKDKEipvnSRIVREVATLSRLQHQHVVRYyqawfetgvvdpfa 501
Cdd:cd14168   12 FEFKEVLGTGAFSEVVLAEERATGKLFAVKcipKKALKGKE----SSIENEIAVLRKIKHENIVAL-------------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 ganwgsktagssmfsysgavsTEIPEQDNNLestYLYIQMEYCPRTLRQVFESYNHFDKDfAWHLIRQIVEGLAHIHGQG 581
Cdd:cd14168   74 ---------------------EDIYESPNHL---YLVMQLVSGGELFDRIVEKGFYTEKD-ASTLIRQVLDAVYYLHRMG 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARND---IKIGDFGLAKflkleqldqdggfstdVAGSGVDSTGQAGTYFYTAPEIEQDWPkIDEKA 658
Cdd:cd14168  129 IVHRDLKPENLLYFSQDEeskIMISDFGLSK----------------MEGKGDVMSTACGTPGYVAPEVLAQKP-YSKAV 191
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30694992  659 DMYSLGVVFFEL---WHPFGTAMERHVILTNLKLKGELPLKWVNEFPEQAS-LLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14168  192 DCWSIGVIAYILlcgYPPFYDENDSKLFEQILKADYEFDSPYWDDISDSAKdFIRNLMEKDPNKRYTCEQALRH 265
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
431-730 7.55e-17

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: 82.14  E-value: 7.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIrlKDKEIP---VNSRIVREVATLSRLQHQHVVRYYQAwFETgvvdpfaganwgs 507
Cdd:cd14165    9 LGEGSYAKVKSAYSERLKCNVAIKII--DKKKAPddfVEKFLPRELEILARLNHKSIIKTYEI-FET------------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 ktagssmfsysgavsteipeqdnnlESTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRD 586
Cdd:cd14165   73 -------------------------SDGKVYIVMELGVQgDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRD 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  587 FTPNNIFFDARNDIKIGDFGLAKFLkleqldqdggfSTDVAGSGVDSTGQAGTYFYTAPEIEQDWPKIDEKADMYSLGVV 666
Cdd:cd14165  128 LKCENLLLDKDFNIKLTDFGFSKRC-----------LRDENGRIVLSKTFCGSAAYAAPEVLQGIPYDPRIYDIWSLGVI 196
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30694992  667 FFELW---HPFGTAMERHVILTNLKLKGELPlKWVNEFPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14165  197 LYIMVcgsMPYDDSNVKKMLKIQKEHRVRFP-RSKNLTSECKDLIYRLLQPDVSQRLCIDEVLSHPW 262
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
421-728 7.96e-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: 82.73  E-value: 7.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  421 YLNDFEElKPLGQGGFGHVVLCKNKLDGRQYAVKkirlkdkeIpVNSRI--VREVATLSRLQ-HQHVVRYYQAWfetgvV 497
Cdd:cd14092    5 YELDLRE-EALGDGSFSVCRKCVHKKTGQEFAVK--------I-VSRRLdtSREVQLLRLCQgHPNIVKLHEVF-----Q 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  498 DPFaganwgsktagssmfsysgavsteipeqdnnlestYLYIQMEYcprtLR--QVFE---SYNHFDKDFAWHLIRQIVE 572
Cdd:cd14092   70 DEL-----------------------------------HTYLVMEL----LRggELLErirKKKRFTESEASRIMRQLVS 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  573 GLAHIHGQGIIHRDFTPNNIFFDARND---IKIGDFGLAKFLKLEQLDQDGGFstdvagsgvdstgqagTYFYTAPEI-E 648
Cdd:cd14092  111 AVSFMHSKGVVHRDLKPENLLFTDEDDdaeIKIVDFGFARLKPENQPLKTPCF----------------TLPYAAPEVlK 174
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  649 QDWPK--IDEKADMYSLGVVFFELWH---PFGTA---------MERhvILT-NLKLKGElplKWVNEFPEQASLLRRLMS 713
Cdd:cd14092  175 QALSTqgYDESCDLWSLGVILYTMLSgqvPFQSPsrnesaaeiMKR--IKSgDFSFDGE---EWKNVSSEAKSLIQGLLT 249
                        330
                 ....*....|....*
gi 30694992  714 PSPSDRPSATELLKH 728
Cdd:cd14092  250 VDPSKRLTMSELRNH 264
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
471-730 8.07e-17

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: 81.64  E-value: 8.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  471 REVATLSRLQHQHVVRYYqawfetgvvdpfaganwgsktagssmfsysgAVSTEIPEQDNNLEstyLYIQMEYCPR-TLR 549
Cdd:cd14012   47 KELESLKKLRHPNLVSYL-------------------------------AFSIERRGRSDGWK---VYLLTEYAPGgSLS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  550 QVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARN---DIKIGDFGLAKFLkleqLDQDGGFSTDV 626
Cdd:cd14012   93 ELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAgtgIVKLTDYSLGKTL----LDMCSRGSLDE 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  627 AGSgvdstgqagTYFYtAPEIEQDWPKIDEKADMYSLGVVFFELWhpFGT-AMERHVILTNLKLKGELPlkwvnefPEQA 705
Cdd:cd14012  169 FKQ---------TYWL-PPELAQGSKSPTRKTDVWDLGLLFLQML--FGLdVLEKYTSPNPVLVSLDLS-------ASLQ 229
                        250       260
                 ....*....|....*....|....*
gi 30694992  706 SLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14012  230 DFLSKCLSLDPKKRPTALELLPHEF 254
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
548-768 8.09e-17

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 84.92  E-value: 8.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   548 LRQVFESYNHFDKDFAWH----LIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFlkleqldqdggFS 623
Cdd:PTZ00283  126 LRQEIKSRAKTNRTFREHeaglLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKM-----------YA 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   624 TDVAgsgvDSTGQA--GTYFYTAPEIEQDWPkIDEKADMYSLGVVFFELW---HPF-GTAMERhviLTNLKLKGEL-PLK 696
Cdd:PTZ00283  195 ATVS----DDVGRTfcGTPYYVAPEIWRRKP-YSKKADMFSLGVLLYELLtlkRPFdGENMEE---VMHKTLAGRYdPLP 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   697 wVNEFPEQASLLRRLMSPSPSDRPSATELLKHAF--------------PPRMESELLDNILRIMQTSEDSSVYDRVVSVI 762
Cdd:PTZ00283  267 -PSISPEMQEIVTALLSSDPKRRPSSSKLLNMPIcklfisglleivqtQPGFSGPLRDTISRQIQQTKQLLQVERRRIVR 345

                  ....*.
gi 30694992   763 FDEEVL 768
Cdd:PTZ00283  346 QMEESL 351
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
425-744 9.66e-17

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: 82.04  E-value: 9.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSrIVREVATLSRLQHQHVVRYYQAWfetgvvdpfagan 504
Cdd:cd06641    6 FTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEIED-IQQEITVLSQCDSPYVTKYYGSY------------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysgavsteipeqdnnLESTYLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIH 584
Cdd:cd06641   72 ---------------------------LKDTKLWIIMEYLGGGSALDLLEPGPLDETQIATILREILKGLDYLHSEKKIH 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  585 RDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQDGGfstdvagsgvdstgqAGTYFYTAPEIEQDwPKIDEKADMYSLG 664
Cdd:cd06641  125 RDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRN*F---------------VGTPFWMAPEVIKQ-SAYDSKADIWSLG 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  665 VVFFELWHPFGTAMERHVI-LTNLKLKGELPLKWVNEFPEQASLLRRLMSPSPSDRPSATELLKHAFPPRME------SE 737
Cdd:cd06641  189 ITAIELARGEPPHSELHPMkVLFLIPKNNPPTLEGNYSKPLKEFVEACLNKEPSFRPTAKELLKHKFILRNAkktsylTE 268

                 ....*..
gi 30694992  738 LLDNILR 744
Cdd:cd06641  269 LIDRYKR 275
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
538-726 9.72e-17

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 85.23  E-value: 9.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   538 YIQMEYCP-RTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFlkleql 616
Cdd:NF033483   83 YIVMEYVDgRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARA------ 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   617 dqdggfstdVAGSGVDSTGQA-GTYFYTAPE-IEQDwpKIDEKADMYSLGVVFFELwhpfgtamerhviLTnlklkGELP 694
Cdd:NF033483  157 ---------LSSTTMTQTNSVlGTVHYLSPEqARGG--TVDARSDIYSLGIVLYEM-------------LT-----GRPP 207
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 30694992   695 ----------LKWVNEFPEQASLLR------------RLMSPSPSDRP-SATELL 726
Cdd:NF033483  208 fdgdspvsvaYKHVQEDPPPPSELNpgipqsldavvlKATAKDPDDRYqSAAEMR 262
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
424-730 9.93e-17

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: 81.88  E-value: 9.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNkLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQ-HVVRYYQAwfetgvvdpfag 502
Cdd:cd14131    2 PYEILKQLGKGGSSKVYKVLN-PKKKIYALKRVDLEGADEQTLQSYKNEIELLKKLKGSdRIIQLYDY------------ 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgsktagssmfsysgavsteipeqDNNLESTYLYIQMEYCPRTLRQVFESYNH--FDKDFAWHLIRQIVEGLAHIHGQ 580
Cdd:cd14131   69 --------------------------EVTDEDDYLYMVMECGEIDLATILKKKRPkpIDPNFIRYYWKQMLEAVHTIHEE 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNiFFDARNDIKIGDFGLAKflkleqldqdgGFSTDVAGSGVDStgQAGTYFYTAPE----------IEQD 650
Cdd:cd14131  123 GIVHSDLKPAN-FLLVKGRLKLIDFGIAK-----------AIQNDTTSIVRDS--QVGTLNYMSPEaikdtsasgeGKPK 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  651 WpKIDEKADMYSLGVVFFELWH---PFGtamerHVILTNLKLKGELPLKWVNEFPEQAS-----LLRRLMSPSPSDRPSA 722
Cdd:cd14131  189 S-KIGRPSDVWSLGCILYQMVYgktPFQ-----HITNPIAKLQAIIDPNHEIEFPDIPNpdlidVMKRCLQRDPKKRPSI 262

                 ....*...
gi 30694992  723 TELLKHAF 730
Cdd:cd14131  263 PELLNHPF 270
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
425-670 1.08e-16

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: 83.08  E-value: 1.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVryyqawfetGVVDPFAgan 504
Cdd:cd07880   17 YRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYRPFQSELFAKRAYRELRLLKHMKHENVI---------GLLDVFT--- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysgavsteipeQDNNLES-TYLYIQMEYCPRTLRQVFEsYNHFDKDFAWHLIRQIVEGLAHIHGQGII 583
Cdd:cd07880   85 -----------------------PDLSLDRfHDFYLVMPFMGTDLGKLMK-HEKLSEDRIQFLVYQMLKGLKYIHAAGII 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  584 HRDFTPNNIFFDARNDIKIGDFGLAKflkleQLDQdggfstdvagsgvDSTGQAGTYFYTAPEIEQDWPKIDEKADMYSL 663
Cdd:cd07880  141 HRDLKPGNLAVNEDCELKILDFGLAR-----QTDS-------------EMTGYVVTRWYRAPEVILNWMHYTQTVDIWSV 202

                 ....*..
gi 30694992  664 GVVFFEL 670
Cdd:cd07880  203 GCIMAEM 209
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
425-730 1.10e-16

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: 81.44  E-value: 1.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKI-RLKDKEIPVNSRIVREVATLSRLQHQHVVRyyqawfetgvvdpfaga 503
Cdd:cd14164    2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVdRRRASPDFVQKFLPRELSILRRVNHPNIVQ----------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssMFsysgavstEIPEQDNNLestyLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGII 583
Cdd:cd14164   65 ----------MF--------ECIEVANGR----LYIVMEAAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIV 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  584 HRDFTPNNIFFDARND-IKIGDFGLAKFlkleqldqdggfstdVAGSGVDSTGQAGTYFYTAPEIEQDWPKIDEKADMYS 662
Cdd:cd14164  123 HRDLKCENILLSADDRkIKIADFGFARF---------------VEDYPELSTTFCGSRAYTPPEVILGTPYDPKKYDVWS 187
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30694992  663 LGVVFFEL---WHPFGTAMERhviLTNLKLKGELPLKWVNEFPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14164  188 LGVVLYVMvtgTMPFDETNVR---RLRLQQRGVLYPSGVALEEPCRALIRTLLQFNPSTRPSIQQVAGNSW 255
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
424-728 1.18e-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: 81.91  E-value: 1.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIrlkDKEipvnSRIVR-EVATLSRL-QHQHVVRYYqawfetGVVDpfa 501
Cdd:cd14091    1 EYEIKEEIGKGSYSVCKRCIHKATGKEYAVKII---DKS----KRDPSeEIEILLRYgQHPNIITLR------DVYD--- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 ganwgsktagssmfsysgavsteipeqdnnlESTYLYIQMEYC------PRTLRQvfesyNHFDKDFAWHLIRQIVEGLA 575
Cdd:cd14091   65 -------------------------------DGNSVYLVTELLrggellDRILRQ-----KFFSEREASAVMKTLTKTVE 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  576 HIHGQGIIHRDFTPNNIFF-DARND---IKIGDFGLAKflkleQLDQDGGFSTdvagsgvdstgqagTYFYT----APEI 647
Cdd:cd14091  109 YLHSQGVVHRDLKPSNILYaDESGDpesLRICDFGFAK-----QLRAENGLLM--------------TPCYTanfvAPEV 169
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  648 --EQDWpkiDEKADMYSLGVVFFEL---WHPFGTAME--RHVILTNLKlKGELPL---KWVNEFPEQASLLRRLMSPSPS 717
Cdd:cd14091  170 lkKQGY---DAACDIWSLGVLLYTMlagYTPFASGPNdtPEVILARIG-SGKIDLsggNWDHVSDSAKDLVRKMLHVDPS 245
                        330
                 ....*....|.
gi 30694992  718 DRPSATELLKH 728
Cdd:cd14091  246 QRPTAAQVLQH 256
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
422-740 1.19e-16

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: 82.04  E-value: 1.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKI-RLKDKEipVNSRIVREVATLSrLQHQ--HVVRYYqawfetgvvd 498
Cdd:cd06618   14 LNDLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMrRSGNKE--ENKRILMDLDVVL-KSHDcpYIVKCY---------- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  499 pfaganwgsktaGSSMFSYSGAVSTEIpeqdnnlestylyiqMEYCPRTLRQvfESYNHFDKDFAWHLIRQIVEGLAHI- 577
Cdd:cd06618   81 ------------GYFITDSDVFICMEL---------------MSTCLDKLLK--RIQGPIPEDILGKMTVSIVKALHYLk 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  578 HGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLkleqldqdggfstdvagsgVDS---TGQAGTYFYTAPE-IE-QDWP 652
Cdd:cd06618  132 EKHGVIHRDVKPSNILLDESGNVKLCDFGISGRL-------------------VDSkakTRSAGCAAYMAPErIDpPDNP 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  653 KIDEKADMYSLGVVFFEL---WHPF-GTAMERHViLTNLkLKGELPLKWVNE-F-PEQASLLRRLMSPSPSDRPSATELL 726
Cdd:cd06618  193 KYDIRADVWSLGISLVELatgQFPYrNCKTEFEV-LTKI-LNEEPPSLPPNEgFsPDFCSFVDLCLTKDHRYRPKYRELL 270
                        330
                 ....*....|....
gi 30694992  727 KHAFPPRMESELLD 740
Cdd:cd06618  271 QHPFIRRYETAEVD 284
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
423-730 1.20e-16

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 81.70  E-value: 1.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVryyqawfetgvvdpfag 502
Cdd:cd07846    1 EKYENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMVKKIAMREIKMLKQLRHENLV----------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgsktagssmfsysgavsteipeqdnNLESTY-----LYIQMEYCPRTLRQVFESY-NHFDKDFAWHLIRQIVEGLAH 576
Cdd:cd07846   64 ----------------------------NLIEVFrrkkrWYLVFEFVDHTVLDDLEKYpNGLDESRVRKYLFQILRGIDF 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  577 IHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLkleqldqdggfstdvAGSGVDSTGQAGTYFYTAPEIEQDWPKIDE 656
Cdd:cd07846  116 CHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTL---------------AAPGEVYTDYVATRWYRAPELLVGDTKYGK 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  657 KADMYSLGVVFFE----------------LWH---PFGTAMERH------------VILTNLKLKGELPLKWVNEFPEQA 705
Cdd:cd07846  181 AVDVWAVGCLVTEmltgeplfpgdsdidqLYHiikCLGNLIPRHqelfqknplfagVRLPEVKEVEPLERRYPKLSGVVI 260
                        330       340
                 ....*....|....*....|....*
gi 30694992  706 SLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd07846  261 DLAKKCLHIDPDKRPSCSELLHHEF 285
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
425-670 1.32e-16

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: 82.64  E-value: 1.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKI-RLKDKEIpVNSRIVREVATLSRLQHQHVVryyqawfetGVVDPFAga 503
Cdd:cd07879   17 YTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLsRPFQSEI-FAKRAYRELTLLKHMQHENVI---------GLLDVFT-- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgSKTAGSSMFSYsgavsteipeqdnnlestylYIQMEYCPRTLRQVFEsyNHFDKDFAWHLIRQIVEGLAHIHGQGII 583
Cdd:cd07879   85 ---SAVSGDEFQDF--------------------YLVMPYMQTDLQKIMG--HPLSEDKVQYLVYQMLCGLKYIHSAGII 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  584 HRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQldqdggfstdvagsgvdsTGQAGTYFYTAPEIEQDWPKIDEKADMYSL 663
Cdd:cd07879  140 HRDLKPGNLAVNEDCELKILDFGLARHADAEM------------------TGYVVTRWYRAPEVILNWMHYNQTVDIWSV 201

                 ....*..
gi 30694992  664 GVVFFEL 670
Cdd:cd07879  202 GCIMAEM 208
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
431-728 1.36e-16

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: 81.48  E-value: 1.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIR---LKDKEIPVNSrivrEVATLSRLQHQHVVRYYQAWfetgvvdpfaganwgs 507
Cdd:cd14169   11 LGEGAFSEVVLAQERGSQRLVALKCIPkkaLRGKEAMVEN----EIAVLRRINHENIVSLEDIY---------------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 ktagssmfsysgavstEIPeqdnnlesTYLYIQMEYCP--RTLRQVFESYNHFDKDfAWHLIRQIVEGLAHIHGQGIIHR 585
Cdd:cd14169   71 ----------------ESP--------THLYLAMELVTggELFDRIIERGSYTEKD-ASQLIGQVLQAVKYLHQLGIVHR 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  586 DFTPNNIFF-----DARndIKIGDFGLAKFlkleqlDQDGGFSTdvagsgvdstgQAGTYFYTAPEIEQDWPkIDEKADM 660
Cdd:cd14169  126 DLKPENLLYatpfeDSK--IMISDFGLSKI------EAQGMLST-----------ACGTPGYVAPELLEQKP-YGKAVDV 185
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30694992  661 YSLGVVFFEL---WHPFGTAMERHVILTNLKLKGELPLKWVNEFPEQAS-LLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14169  186 WAIGVISYILlcgYPPFYDENDSELFNQILKAEYEFDSPYWDDISESAKdFIRHLLERDPEKRFTCEQALQH 257
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
422-728 1.45e-16

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


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 81.12  E-value: 1.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEEL--KPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLS------RLQHQHVVryYQAWFE 493
Cdd:cd14198    5 FNNFYILtsKELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAEILHEIAVLElaksnpRVVNLHEV--YETTSE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  494 TGVVDPFAganwgsktAGSSMFSYSgavsteIPEQDNNLESTYLYiqmeycprtlrqvfesynhfdkdfawHLIRQIVEG 573
Cdd:cd14198   83 IILILEYA--------AGGEIFNLC------VPDLAEMVSENDII--------------------------RLIRQILEG 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  574 LAHIHGQGIIHRDFTPNNIFFDARN---DIKIGDFGLAKFLkleqldqdggfstdvaGSGVDSTGQAGTYFYTAPEIeQD 650
Cdd:cd14198  123 VYYLHQNNIVHLDLKPQNILLSSIYplgDIKIVDFGMSRKI----------------GHACELREIMGTPEYLAPEI-LN 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  651 WPKIDEKADMYSLGVVFFELW---HPFGTAMERHVILTNLKLKGELPLKWVNEFPEQAS-LLRRLMSPSPSDRPSATELL 726
Cdd:cd14198  186 YDPITTATDMWNIGVIAYMLLtheSPFVGEDNQETFLNISQVNVDYSEETFSSVSQLATdFIQKLLVKNPEKRPTAEICL 265

                 ..
gi 30694992  727 KH 728
Cdd:cd14198  266 SH 267
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
431-724 1.47e-16

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: 81.39  E-value: 1.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGrQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAWFETGvvdpfaganwgskta 510
Cdd:cd14027    1 LDSGGFGKVSLCFHRTQG-LVVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEG--------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  511 gssmfSYSgavsteipeqdnnlestylyIQMEYCPR-TLRQVFESYNhFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTP 589
Cdd:cd14027   65 -----KYS--------------------LVMEYMEKgNLMHVLKKVS-VPLSVKGRIILEIIEGMAYLHGKGVIHKDLKP 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  590 NNIFFDARNDIKIGDFGLAKFLKLEQLDQDggfsTDVAGSGVDSTGQ--AGTYFYTAPEIEQDW-PKIDEKADMYSLGVV 666
Cdd:cd14027  119 ENILVDNDFHIKIADLGLASFKMWSKLTKE----EHNEQREVDGTAKknAGTLYYMAPEHLNDVnAKPTEKSDVYSFAIV 194
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30694992  667 FFELW---HPFGTAMERHVILTNLKlKGELP-LKWVNEF--PEQASLLRRLMSPSPSDRPSATE 724
Cdd:cd14027  195 LWAIFankEPYENAINEDQIIMCIK-SGNRPdVDDITEYcpREIIDLMKLCWEANPEARPTFPG 257
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
431-730 1.57e-16

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


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 81.13  E-value: 1.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNkLDGRQYAVKKIRLKDKEIPVNSR--IVREVATLSRLQHQHVVRYyQAWFEtgvvdpfaganwgsk 508
Cdd:cd14187   15 LGKGGFAKCYEITD-ADTKEVFAGKIVPKSLLLKPHQKekMSMEIAIHRSLAHQHVVGF-HGFFE--------------- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  509 tagssmfsysgavsteipeqDNNlestYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDF 587
Cdd:cd14187   78 --------------------DND----FVYVVLELCRRrSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  588 TPNNIFFDARNDIKIGDFGLAkflkleqldqdggfsTDVAGSGVDSTGQAGTYFYTAPEIEQDWPKIDEkADMYSLGVVF 667
Cdd:cd14187  134 KLGNLFLNDDMEVKIGDFGLA---------------TKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFE-VDIWSIGCIM 197
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30694992  668 FELW---HPFGTAMERHVILTNLKLKGELPlKWVNefPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14187  198 YTLLvgkPPFETSCLKETYLRIKKNEYSIP-KHIN--PVAASLIQKMLQTDPTARPTINELLNDEF 260
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
418-730 1.74e-16

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 82.12  E-value: 1.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   418 SSRY--LNDFeelkpLGQGGFGHVVLCKNKLDGRQYAVKKIRLKD------------KEIPVNSRIVREVATLSRLQHQH 483
Cdd:PTZ00024    7 SERYiqKGAH-----LGEGTYGKVEKAYDTLTGKIVAIKKVKIIEisndvtkdrqlvGMCGIHFTTLRELKIMNEIKHEN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   484 VVryyqawfetGVVDPFAganwgsktagssmfsysgavsteipEQDnnlestYLYIQMEYCPRTLRQVFESYNHFDKDFA 563
Cdd:PTZ00024   82 IM---------GLVDVYV-------------------------EGD------FINLVMDIMASDLKKVVDRKIRLTESQV 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   564 WHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLdQDGGFSTDVAGSGVDSTGQAGTYFYT 643
Cdd:PTZ00024  122 KCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARRYGYPPY-SDTLSKDETMQRREEMTSKVVTLWYR 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   644 APEIEQDWPKIDEKADMYSLGVVFFEL-------------------WHPFGTAMErhvilTNLKLKGELPL--------- 695
Cdd:PTZ00024  201 APELLMGAEKYHFAVDMWSVGCIFAELltgkplfpgeneidqlgriFELLGTPNE-----DNWPQAKKLPLyteftprkp 275
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 30694992   696 -KWVNEFPEQAS----LLRRLMSPSPSDRPSATELLKHAF 730
Cdd:PTZ00024  276 kDLKTIFPNASDdaidLLQSLLKLNPLERISAKEALKHEY 315
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
425-730 1.83e-16

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: 81.37  E-value: 1.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLkDKEIPVNSRIVREVATLSRLQHQHVVRYYQAwfetgvvdpfagan 504
Cdd:cd07836    2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIHL-DAEEGTPSTAIREISLMKELKHENIVRLHDV-------------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysgaVSTEipeqdnnlesTYLYIQMEYCPRTLRQVFESYNH---FDKDFAWHLIRQIVEGLAHIHGQG 581
Cdd:cd07836   67 ----------------IHTE----------NKLMLVFEYMDKDLKKYMDTHGVrgaLDPNTVKSFTYQLLKGIAFCHENR 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQldqdGGFSTDVAgsgvdstgqagTYFYTAPEIEQDWPKIDEKADMY 661
Cdd:cd07836  121 VLHRDLKPQNLLINKRGELKLADFGLARAFGIPV----NTFSNEVV-----------TLWYRAPDVLLGSRTYSTSIDIW 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  662 SLGVVFFELW--HPF--GTAMERHV--ILTNLKLKGELPLKWVNEFPE-------------QA----------SLLRRLM 712
Cdd:cd07836  186 SVGCIMAEMItgRPLfpGTNNEDQLlkIFRIMGTPTESTWPGISQLPEykptfpryppqdlQQlfphadplgiDLLHRLL 265
                        330
                 ....*....|....*...
gi 30694992  713 SPSPSDRPSATELLKHAF 730
Cdd:cd07836  266 QLNPELRISAHDALQHPW 283
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
423-730 2.02e-16

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: 81.19  E-value: 2.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVK---KIRLKDKEIPVNSRIVREVAtlsrlQHQHVVRYYQAWFETGvvdp 499
Cdd:cd06639   22 DTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKildPISDVDEEIEAEYNILRSLP-----NHPNVVKFYGMFYKAD---- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  500 faganwgsktagssmfSYSGAVSTEIPEQDNNLESTYLYIQMEYCPRTLRQVFESYnhfdkdfawhLIRQIVEGLAHIHG 579
Cdd:cd06639   93 ----------------QYVGGQLWLVLELCNGGSVTELVKGLLKCGQRLDEAMISY----------ILYGALLGLQHLHN 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  580 QGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQDggfsTDVagsgvdstgqaGTYFYTAPEI---EQDWP-KID 655
Cdd:cd06639  147 NRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSARLRRN----TSV-----------GTPFWMAPEViacEQQYDySYD 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  656 EKADMYSLGVVFFELWHPFGTAMERHVILTNLKLKGEL------PLKWVNEFpeqASLLRRLMSPSPSDRPSATELLKHA 729
Cdd:cd06639  212 ARCDVWSLGITAIELADGDPPLFDMHPVKALFKIPRNPpptllnPEKWCRGF---SHFISQCLIKDFEKRPSVTHLLEHP 288

                 .
gi 30694992  730 F 730
Cdd:cd06639  289 F 289
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
424-730 2.04e-16

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 80.93  E-value: 2.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKdkeipVNS----RIVREVATLSRLQH-QHVVRYYQAWFETGVVd 498
Cdd:cd06617    2 DLEVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRAT-----VNSqeqkRLLMDLDISMRSVDcPYTVTFYGALFREGDV- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  499 pfaganWgsktagssmfsysgaVSTEIpeQDNNLESTYlyiqmeycprtlRQVFESYNHFDKDFAWHLIRQIVEGLAHIH 578
Cdd:cd06617   76 ------W---------------ICMEV--MDTSLDKFY------------KKVYDKGLTIPEDILGKIAVSIVKALEYLH 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  579 GQ-GIIHRDFTPNNIFFDARNDIKIGDFGLAKFLkleqldqdggfstdvagsgVDS---TGQAGTYFYTAPE---IEQDW 651
Cdd:cd06617  121 SKlSVIHRDVKPSNVLINRNGQVKLCDFGISGYL-------------------VDSvakTIDAGCKPYMAPErinPELNQ 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  652 PKIDEKADMYSLGVVFFELW---HPF---GTAMERhviltnLK--LKGELPLKWVNEF-PEQASLLRRLMSPSPSDRPSA 722
Cdd:cd06617  182 KGYDVKSDVWSLGITMIELAtgrFPYdswKTPFQQ------LKqvVEEPSPQLPAEKFsPEFQDFVNKCLKKNYKERPNY 255

                 ....*...
gi 30694992  723 TELLKHAF 730
Cdd:cd06617  256 PELLQHPF 263
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
425-730 2.32e-16

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: 80.57  E-value: 2.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVN-SRIVREVATLSRLQHQHVVRYYQAWfetgvvdpfaga 503
Cdd:cd06607    3 FEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTEKwQDIIKEVKFLRQLRHPNTIEYKGCY------------ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssmfsysgavsteipeqdnnLESTYLYIQMEYCPRTLRQVFESYNHFDKDFAWHLI-RQIVEGLAHIHGQGI 582
Cdd:cd06607   71 ----------------------------LREHTAWLVMEYCLGSASDIVEVHKKPLQEVEIAAIcHGALQGLAYLHSHNR 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  583 IHRDFTPNNIFFDARNDIKIGDFGLAKFLkleqldqdggfstDVAGSGVdstgqaGTYFYTAPEI--EQDWPKIDEKADM 660
Cdd:cd06607  123 IHRDVKAGNILLTEPGTVKLADFGSASLV-------------CPANSFV------GTPYWMAPEVilAMDEGQYDGKVDV 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  661 YSLGVVFFELwhpfgtaMERHVILTNLKLKGEL------------PLKWVNEFpeqASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd06607  184 WSLGITCIEL-------AERKPPLFNMNAMSALyhiaqndsptlsSGEWSDDF---RNFVDSCLQKIPQDRPSAEDLLKH 253

                 ..
gi 30694992  729 AF 730
Cdd:cd06607  254 PF 255
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
429-670 2.80e-16

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: 81.65  E-value: 2.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVryyqawfetgvvdpfaganwgsk 508
Cdd:cd07858   11 KPIGRGAYGIVCSAKNSETNEKVAIKKIANAFDNRIDAKRTLREIKLLRHLDHENVI----------------------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  509 tagssmfsysgAVSTEI-PEQDNNLEStyLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDF 587
Cdd:cd07858   68 -----------AIKDIMpPPHREAFND--VYIVYELMDTDLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDL 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  588 TPNNIFFDARNDIKIGDFGLAKflkleQLDQDGGFSTD-VAgsgvdstgqagTYFYTAPEIEQDWPKIDEKADMYSLGVV 666
Cdd:cd07858  135 KPSNLLLNANCDLKICDFGLAR-----TTSEKGDFMTEyVV-----------TRWYRAPELLLNCSEYTTAIDVWSVGCI 198

                 ....
gi 30694992  667 FFEL 670
Cdd:cd07858  199 FAEL 202
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
425-730 3.31e-16

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: 80.48  E-value: 3.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSrIVREVATLSRLQHQHVVRYYQAWfetgvvdpfagan 504
Cdd:cd06640    6 FTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEDEIED-IQQEITVLSQCDSPYVTKYYGSY------------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysgavsteipeqdnnLESTYLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIH 584
Cdd:cd06640   72 ---------------------------LKGTKLWIIMEYLGGGSALDLLRAGPFDEFQIATMLKEILKGLDYLHSEKKIH 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  585 RDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQDGGfstdvagsgvdstgqAGTYFYTAPEIEQDwPKIDEKADMYSLG 664
Cdd:cd06640  125 RDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTF---------------VGTPFWMAPEVIQQ-SAYDSKADIWSLG 188
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30694992  665 VVFFELWHPFGTAMERHVILTNLKLKGELPLKWVNEFPEQ-ASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd06640  189 ITAIELAKGEPPNSDMHPMRVLFLIPKNNPPTLVGDFSKPfKEFIDACLNKDPSFRPTAKELLKHKF 255
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
422-670 5.27e-16

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 80.25  E-value: 5.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   422 LNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYyqawfetgvvdpfa 501
Cdd:PLN00009    1 MDQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHGNIVRL-------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   502 ganwgsktagssmfsysgavsteipeQDNNLESTYLYIQMEYCPRTLRQVFESYNHFDKDFawHLIR----QIVEGLAHI 577
Cdd:PLN00009   67 --------------------------QDVVHSEKRLYLVFEYLDLDLKKHMDSSPDFAKNP--RLIKtylyQILRGIAYC 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   578 HGQGIIHRDFTPNNIFFDAR-NDIKIGDFGLAKflkleqldqdgGFSTDVAGsgvdSTGQAGTYFYTAPEIEQDWPKIDE 656
Cdd:PLN00009  119 HSHRVLHRDLKPQNLLIDRRtNALKLADFGLAR-----------AFGIPVRT----FTHEVVTLWYRAPEILLGSRHYST 183
                         250
                  ....*....|....
gi 30694992   657 KADMYSLGVVFFEL 670
Cdd:PLN00009  184 PVDIWSVGCIFAEM 197
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
422-728 5.83e-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: 79.52  E-value: 5.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKI-RLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAWFEtgvvdpf 500
Cdd:cd14117    5 IDDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLfKSQIEKEGVEHQLRREIEIQSHLRHPNILRLYNYFHD------- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  501 aganwgsktagssmfsysgavsteipeqdnnleSTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHG 579
Cdd:cd14117   78 ---------------------------------RKRIYLILEYAPRgELYKELQKHGRFDEQRTATFMEELADALHYCHE 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  580 QGIIHRDFTPNNIFFDARNDIKIGDFGLAkflkleqldqdggfstdVAGSGVDSTGQAGTYFYTAPEIEQDWPKiDEKAD 659
Cdd:cd14117  125 KKVIHRDIKPENLLMGYKGELKIADFGWS-----------------VHAPSLRRRTMCGTLDYLPPEMIEGRTH-DEKVD 186
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30694992  660 MYSLGVVFFEL---WHPFGTA--MERHVILTNLKLKgelplkwvneFPEQAS-----LLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14117  187 LWCIGVLCYELlvgMPPFESAshTETYRRIVKVDLK----------FPPFLSdgsrdLISKLLRYHPSERLPLKGVMEH 255
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
425-727 6.87e-16

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: 79.10  E-value: 6.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAwfetgvvdpfagan 504
Cdd:cd14072    2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEV-------------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysgaVSTEipeqdnnlesTYLYIQMEYCprTLRQVFE---SYNHFDKDFAWHLIRQIVEGLAHIHGQG 581
Cdd:cd14072   68 ----------------IETE----------KTLYLVMEYA--SGGEVFDylvAHGRMKEKEARAKFRQIVSAVQYCHQKR 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFglakflkleqldqdgGFSTD-VAGSGVDSTgqAGTYFYTAPEIEQ----DWPKIde 656
Cdd:cd14072  120 IVHRDLKAENLLLDADMNIKIADF---------------GFSNEfTPGNKLDTF--CGSPPYAAPELFQgkkyDGPEV-- 180
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30694992  657 kaDMYSLGVVFFELWH---PFGTAmerhviltNLKLKGELPLKWVNEFP-----EQASLLRRLMSPSPSDRPSATELLK 727
Cdd:cd14072  181 --DVWSLGVILYTLVSgslPFDGQ--------NLKELRERVLRGKYRIPfymstDCENLLKKFLVLNPSKRGTLEQIMK 249
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
567-728 7.26e-16

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: 78.78  E-value: 7.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  567 IRQIVEGLAHIHGQGIIHRDFTPNNIF--FDARNDIKIGDFGLAKFLKLEQLDqdggFStdvagsgvdstgQAGTYFYTA 644
Cdd:cd14107  104 IQQVLEGIGYLHGMNILHLDIKPDNILmvSPTREDIKICDFGFAQEITPSEHQ----FS------------KYGSPEFVA 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  645 PEIEQDWPkIDEKADMYSLGVVFF---ELWHPFGTAMERHVILTnlKLKGElpLKWVNefPEQASL-------LRRLMSP 714
Cdd:cd14107  168 PEIVHQEP-VSAATDIWALGVIAYlslTCHSPFAGENDRATLLN--VAEGV--VSWDT--PEITHLsedakdfIKRVLQP 240
                        170
                 ....*....|....
gi 30694992  715 SPSDRPSATELLKH 728
Cdd:cd14107  241 DPEKRPSASECLSH 254
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
425-730 7.32e-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: 79.69  E-value: 7.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEiPVNSRIVrEVATLSRLQHQHVVRYYQAWFetgvvdpfagan 504
Cdd:cd06643    7 WEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKSEE-ELEDYMV-EIDILASCDHPNIVKLLDAFY------------ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 WGSKTAGSSMFSYSGAVSTEIPEQDNNLESTYLYIqmeycprtlrqvfesynhfdkdfawhLIRQIVEGLAHIHGQGIIH 584
Cdd:cd06643   73 YENNLWILIEFCAGGAVDAVMLELERPLTEPQIRV--------------------------VCKQTLEALVYLHENKIIH 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  585 RDFTPNNIFFDARNDIKIGDFGL-AKFLKleQLDQDGGFstdvagsgvdstgqAGTYFYTAPEI-----EQDWPkIDEKA 658
Cdd:cd06643  127 RDLKAGNILFTLDGDIKLADFGVsAKNTR--TLQRRDSF--------------IGTPYWMAPEVvmcetSKDRP-YDYKA 189
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30694992  659 DMYSLGVVFFELWHPFGTAMERHVILTNLKL-KGELPL-----KWVNEFPEqasLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd06643  190 DVWSLGVTLIEMAQIEPPHHELNPMRVLLKIaKSEPPTlaqpsRWSPEFKD---FLRKCLEKNVDARWTTSQLLQHPF 264
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
430-668 7.93e-16

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: 79.38  E-value: 7.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  430 PLGQGGFGHVVLCKNKLDGRQYAVKKIrlkdKEIPVNSR--IVREVATLSRLQ-HQHVVRYYQaWFETGvvdpfaganwg 506
Cdd:cd14090    9 LLGEGAYASVQTCINLYTGKEYAVKII----EKHPGHSRsrVFREVETLHQCQgHPNILQLIE-YFEDD----------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  507 sktagssmfsysgavsteipeqdnnlESTYLYIQMEYCPRTLRQVfESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRD 586
Cdd:cd14090   73 --------------------------ERFYLVFEKMRGGPLLSHI-EKRVHFTEQEASLVVRDIASALDFLHDKGIAHRD 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  587 FTPNNIFFDARNDI---KIGDFGLAKFLKLeqldqDGGFSTDVAGSgvDSTGQAGTYFYTAPEIEQDW----PKIDEKAD 659
Cdd:cd14090  126 LKPENILCESMDKVspvKICDFDLGSGIKL-----SSTSMTPVTTP--ELLTPVGSAEYMAPEVVDAFvgeaLSYDKRCD 198

                 ....*....
gi 30694992  660 MYSLGVVFF 668
Cdd:cd14090  199 LWSLGVILY 207
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
425-739 8.50e-16

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: 79.70  E-value: 8.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVN-SRIVREVATLSRLQHQHVVRYYQAWfetgvvdpfaga 503
Cdd:cd06633   23 FVDLHEIGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKwQDIIKEVKFLQQLKHPNTIEYKGCY------------ 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssmfsysgavsteipeqdnnLESTYLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIRQ-IVEGLAHIHGQGI 582
Cdd:cd06633   91 ----------------------------LKDHTAWLVMEYCLGSASDLLEVHKKPLQEVEIAAITHgALQGLAYLHSHNM 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  583 IHRDFTPNNIFFDARNDIKIGDFGLAKFlkleqldqdggfsTDVAGSGVdstgqaGTYFYTAPEI--EQDWPKIDEKADM 660
Cdd:cd06633  143 IHRDIKAGNILLTEPGQVKLADFGSASI-------------ASPANSFV------GTPYWMAPEVilAMDEGQYDGKVDI 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  661 YSLGVVFFELwhpfgtaMERHVILTNLKLKGELPLKWVNEFP-----EQASLLRRL----MSPSPSDRPSATELLKHAF- 730
Cdd:cd06633  204 WSLGITCIEL-------AERKPPLFNMNAMSALYHIAQNDSPtlqsnEWTDSFRGFvdycLQKIPQERPSSAELLRHDFv 276
                        330
                 ....*....|...
gi 30694992  731 ----PPRMESELL 739
Cdd:cd06633  277 rrerPPRVLIDLI 289
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
424-670 1.67e-15

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: 79.79  E-value: 1.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAwFETGVVDPFaga 503
Cdd:cd07853    1 DVEPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDI-LQPPHIDPF--- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagSSMFsysgaVSTEIPEQDnnlestylyiqmeycprtLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGII 583
Cdd:cd07853   77 --------EEIY-----VVTELMQSD------------------LHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGIL 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  584 HRDFTPNNIFFDARNDIKIGDFGLAkflKLEQLDQDGGFSTDVAgsgvdstgqagTYFYTAPEIEQDWPKIDEKADMYSL 663
Cdd:cd07853  126 HRDIKPGNLLVNSNCVLKICDFGLA---RVEEPDESKHMTQEVV-----------TQYYRAPEILMGSRHYTSAVDIWSV 191

                 ....*..
gi 30694992  664 GVVFFEL 670
Cdd:cd07853  192 GCIFAEL 198
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
422-720 1.77e-15

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: 78.15  E-value: 1.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDK-EIPVNSRIVREVATLSRLQHQHVVRYYQAWF---ETGVV 497
Cdd:cd08228    1 LANFQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMmDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIednELNIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  498 DPFAGANwgsktAGSSMFSYSGAVSTEIPEqdnnlestylyiqmeycpRTLrqvfesynhfdkdfaWHLIRQIVEGLAHI 577
Cdd:cd08228   81 LELADAG-----DLSQMIKYFKKQKRLIPE------------------RTV---------------WKYFVQLCSAVEHM 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  578 HGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEqldqdggfsTDVAGSGVdstgqaGTYFYTAPEieqdwpKIDE- 656
Cdd:cd08228  123 HSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSK---------TTAAHSLV------GTPYYMSPE------RIHEn 181
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30694992  657 ----KADMYSLGVVFFE---LWHPF-GTAMERHVILTNLKLKGELPLKWVNEFPEQASLLRRLMSPSPSDRP 720
Cdd:cd08228  182 gynfKSDIWSLGCLLYEmaaLQSPFyGDKMNLFSLCQKIEQCDYPPLPTEHYSEKLRELVSMCIYPDPDQRP 253
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
425-730 1.86e-15

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: 78.51  E-value: 1.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVK---KIRLKDKEIPVNSRIVREVAtlsrlQHQHVVRYYQAWFETGVVDpfa 501
Cdd:cd06638   20 WEIIETIGKGTYGKVFKVLNKKNGSKAAVKildPIHDIDEEIEAEYNILKALS-----DHPNVVKFYGMYYKKDVKN--- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 ganwGSKtagssmfsysgavsteipeqdnnlestyLYIQMEYC-----PRTLRQVFESYNHFDKDFAWHLIRQIVEGLAH 576
Cdd:cd06638   92 ----GDQ----------------------------LWLVLELCnggsvTDLVKGFLKRGERMEEPIIAYILHEALMGLQH 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  577 IHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQDggfsTDVagsgvdstgqaGTYFYTAPEI----EQDWP 652
Cdd:cd06638  140 LHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLRRN----TSV-----------GTPFWMAPEViaceQQLDS 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  653 KIDEKADMYSLGVVFFEL---------WHPFGTAMErhvILTNLKLKGELPLKWVNEFPEqasLLRRLMSPSPSDRPSAT 723
Cdd:cd06638  205 TYDARCDVWSLGITAIELgdgdppladLHPMRALFK---IPRNPPPTLHQPELWSNEFND---FIRKCLTKDYEKRPTVS 278

                 ....*..
gi 30694992  724 ELLKHAF 730
Cdd:cd06638  279 DLLQHVF 285
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
431-681 2.22e-15

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: 78.26  E-value: 2.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRL------KDKEipvnsRIVREVATLSRLQHQHVVRYYQAWFETGVVDPfagan 504
Cdd:cd13989    1 LGSGGFGYVTLWKHQDTGEYVAIKKCRQelspsdKNRE-----RWCLEVQIMKKLNHPNVVSARDVPPELEKLSP----- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysgavsTEIPeqdnnlestylYIQMEYCPR-TLRQV---FESYNHFDKDFAWHLIRQIVEGLAHIHGQ 580
Cdd:cd13989   71 ------------------NDLP-----------LLAMEYCSGgDLRKVlnqPENCCGLKESEVRTLLSDISSAISYLHEN 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFDARND---IKIGDFGLAKflkleQLDQdggfstdvaGSGVDSTgqAGTYFYTAPEI-EQDwpKIDE 656
Cdd:cd13989  122 RIIHRDLKPENIVLQQGGGrviYKLIDLGYAK-----ELDQ---------GSLCTSF--VGTLQYLAPELfESK--KYTC 183
                        250       260       270
                 ....*....|....*....|....*....|.
gi 30694992  657 KADMYSLGVVFFEL---WHPF---GTAMERH 681
Cdd:cd13989  184 TVDYWSFGTLAFECitgYRPFlpnWQPVQWH 214
HisS COG0124
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ...
794-1231 2.53e-15

Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439894 [Multi-domain]  Cd Length: 422  Bit Score: 79.78  E-value: 2.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  794 TELRDYVVEITKEVFRQHCAKHLEvipMRLLSDCPQFSRK-----TVKLL----TNGGDMLELCYELRLPFVHwiSVNQK 864
Cdd:COG0124   18 SAKWQYVEDTIREVFERYGFQEIR---TPIFEYTELFARKigediVEKEMytfeDRGGRSLTLRPEGTAPVAR--AVAEH 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  865 SS-----FKRYEISHVYRraigHSPPNPC-----LQADFDIVGGTLSLTEAEVLKVIVDItthiFHR---GSCDIHLNH- 930
Cdd:COG0124   93 GNelpfpFKLYYIGPVFR----YERPQKGryrqfHQFGVEVIGSDSPLADAEVIALAADL----LKAlglKDFTLEINSr 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  931 -------GDLLDAIwswagiKAEHRRKVAELLSmmgslrpQSSERKLKWVFIRRQLlqELKLPEavvnrlqtvasrfCGD 1003
Cdd:COG0124  165 glpeeraEALLRYL------DKLDKIGHEDVLD-------EDSQRRLETNPLRAIL--DSKGPD-------------CQE 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992 1004 ADQALPRLrgalrADRPTRKALDELSNLLTYLRVWRIEehVHIDvlmpPTE----SYHRNLFFQVFLTKENSSGTsndgv 1079
Cdd:COG0124  217 VLADAPKL-----LDYLGEEGLAHFEEVLELLDALGIP--YVID----PRLvrglDYYTGTVFEIVTDGLGAQGS----- 280
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992 1080 lLAVGGRYDWLVQEVCDREhkmnLPgAVGVSLALETIFQHLPMDLRPIRNEVSTSVLVCSRGGGGLLvQRMELVAELWEK 1159
Cdd:COG0124  281 -VCGGGRYDGLVEQLGGPP----TP-AVGFAIGLERLLLLLEELGLLPAAEPPPDVYVVPLGEEARA-EALKLAQELRAA 353
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30694992 1160 SIKAEFVPTPDpSLTEQYEYANEHEIKCLVIITESGVAQNQiefVKVRHLELKKEKVVGREELVKFLLDAMA 1231
Cdd:COG0124  354 GIRVELDLGGR-KLKKQLKYADKSGAPFVLILGEDELANGT---VTLKDLATGEQETVPLDELVEYLKELLA 421
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
424-728 3.10e-15

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: 77.48  E-value: 3.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIpVNSRIVREVATLSRLQHQHVVRYYqawfetgvvdpfaga 503
Cdd:cd06620    6 DLETLKDLGAGNGGSVSKVLHIPTGTIMAKKVIHIDAKSS-VRKQILRELQILHECHSPYIVSFY--------------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssmfsysGAVSTEIPEqdnnlestyLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQ-G 581
Cdd:cd06620   70 ---------------GAFLNENNN---------IIICMEYMDCgSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVhR 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGlakflkleqldqdggfstdVAGSGVDSTGQA--GTYFYTAPE-IEQDwpKIDEKA 658
Cdd:cd06620  126 IIHRDIKPSNILVNSKGQIKLCDFG-------------------VSGELINSIADTfvGTSTYMSPErIQGG--KYSVKS 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  659 DMYSLGVVFFELW---HPFgtAMERHVILTNLKLKGELPL--KWVNE----------FPEQASLL-RRLMSPSPSDRPSA 722
Cdd:cd06620  185 DVWSLGLSIIELAlgeFPF--AGSNDDDDGYNGPMGILDLlqRIVNEppprlpkdriFPKDLRDFvDRCLLKDPRERPSP 262

                 ....*.
gi 30694992  723 TELLKH 728
Cdd:cd06620  263 QLLLDH 268
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
432-726 3.17e-15

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: 76.53  E-value: 3.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  432 GQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVnsrivrevatLSRLQHQHVVRYYQAWFET---GVVDPFAGAnwgsk 508
Cdd:cd14060    2 GGGSFGSVYRAIWVSQDKEVAVKKLLKIEKEAEI----------LSVLSHRNIIQFYGAILEApnyGIVTEYASY----- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  509 tagSSMFSYSGAVSTEipeqdnnlestylyiQMEycprtlrqvfesynhFDKDFAWHliRQIVEGLAHIHGQG---IIHR 585
Cdd:cd14060   67 ---GSLFDYLNSNESE---------------EMD---------------MDQIMTWA--TDIAKGMHYLHMEApvkVIHR 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  586 DFTPNNIFFDARNDIKIGDFGLAKFlkleqldqdggFSTDVAGSGVdstgqaGTYFYTAPEIEQDWPkIDEKADMYSLGV 665
Cdd:cd14060  112 DLKSRNVVIAADGVLKICDFGASRF-----------HSHTTHMSLV------GTFPWMAPEVIQSLP-VSETCDTYSYGV 173
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30694992  666 VFFELwhpfgtaMERHVILTNLKlkgELPLKWV----NEFP--------EQASLLRRLMSPSPSDRPSATELL 726
Cdd:cd14060  174 VLWEM-------LTREVPFKGLE---GLQVAWLvvekNERPtipsscprSFAELMRRCWEADVKERPSFKQII 236
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
429-719 3.77e-15

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: 77.77  E-value: 3.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKLDGRQYAVKKIrlkDKEIPVNSRivREVATLSRLQ-HQHVVRYYQAWfetgvvdpfaganwgs 507
Cdd:cd14179   13 KPLGEGSFSICRKCLHKKTNQEYAVKIV---SKRMEANTQ--REIAALKLCEgHPNIVKLHEVY---------------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 ktagssmfsysgavsteipeqdNNLESTYLYIQMEYCPRTLRQVfESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDF 587
Cdd:cd14179   72 ----------------------HDQLHTFLVMELLKGGELLERI-KKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDL 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  588 TPNNIFFDARND---IKIGDFGLAKFLKLE-QLDQDGGFstdvagsgvdstgqagTYFYTAPEIeQDWPKIDEKADMYSL 663
Cdd:cd14179  129 KPENLLFTDESDnseIKIIDFGFARLKPPDnQPLKTPCF----------------TLHYAAPEL-LNYNGYDESCDLWSL 191
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30694992  664 GVVFFELWH---PFG------TAMERHVILTNLKlKGELPLK---WVNEFPEQASLLRRLMSPSPSDR 719
Cdd:cd14179  192 GVILYTMLSgqvPFQchdkslTCTSAEEIMKKIK-QGDFSFEgeaWKNVSQEAKDLIQGLLTVDPNKR 258
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
424-670 3.79e-15

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


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 77.48  E-value: 3.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKK------IRLKDKEIPVNSRIVrevatLSRLQHQHVVRYYQAWFEtgvv 497
Cdd:cd05612    2 DFERIKTIGTGTFGRVHLVRDRISEHYYALKVmaipevIRLKQEQHVHNEKRV-----LKEVSHPFIIRLFWTEHD---- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  498 dpfaganwgsktagssmfsysgavsteipeqdnnleSTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAH 576
Cdd:cd05612   73 ------------------------------------QRFLYMLMEYVPGgELFSYLRNSGRFSNSTGLFYASEIVCALEY 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  577 IHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLkleqldqdggfstdvagsgVDSTGQ-AGTYFYTAPEIEQDwpKID 655
Cdd:cd05612  117 LHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKL-------------------RDRTWTlCGTPEYLAPEVIQS--KGH 175
                        250
                 ....*....|....*.
gi 30694992  656 EKA-DMYSLGVVFFEL 670
Cdd:cd05612  176 NKAvDWWALGILIYEM 191
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
429-730 4.21e-15

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


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 77.83  E-value: 4.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKnKLDGRQ----YAVKKirLKDKEIPVNSRiVR---EVATLSRLQHQHVVRYYQAwFETG-----V 496
Cdd:cd05582    1 KVLGQGSFGKVFLVR-KITGPDagtlYAMKV--LKKATLKVRDR-VRtkmERDILADVNHPFIVKLHYA-FQTEgklylI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  497 VDPFAGANWGSKTAGSSMFSysgavsteipEQDNNLestYLyiqmeycprtlrqvfesynhfdkdfawhliRQIVEGLAH 576
Cdd:cd05582   76 LDFLRGGDLFTRLSKEVMFT----------EEDVKF---YL------------------------------AELALALDH 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  577 IHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKflklEQLDQDG-GFSTdvagsgvdstgqAGTYFYTAPEIeqdwpkID 655
Cdd:cd05582  113 LHSLGIIYRDLKPENILLDEDGHIKLTDFGLSK----ESIDHEKkAYSF------------CGTVEYMAPEV------VN 170
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  656 EK-----ADMYSLGVVFFELWH---PFGTAMERHVILTNLKLKGELPlkwvnEF--PEQASLLRRLMSPSPSDR----PS 721
Cdd:cd05582  171 RRghtqsADWWSFGVLMFEMLTgslPFQGKDRKETMTMILKAKLGMP-----QFlsPEAQSLLRALFKRNPANRlgagPD 245
                        330
                 ....*....|
gi 30694992  722 ATELLK-HAF 730
Cdd:cd05582  246 GVEEIKrHPF 255
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
423-730 6.24e-15

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: 76.57  E-value: 6.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIpvnSRIVREVATLSRL-QHQHVVRYYQAWFEtgvvdpfa 501
Cdd:cd06608    6 GIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEE---EEIKLEINILRKFsNHPNIATFYGAFIK-------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 ganwgsktagssmfsysgAVSTEIPEQdnnlestyLYIQMEYC-----PRTLRQVFESYNHFDKDFAWHLIRQIVEGLAH 576
Cdd:cd06608   75 ------------------KDPPGGDDQ--------LWLVMEYCgggsvTDLVKGLRKKGKRLKEEWIAYILRETLRGLAY 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  577 IHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQDggfsTDVagsgvdstgqaGTYFYTAPEI----EQDWP 652
Cdd:cd06608  129 LHENKVIHRDIKGQNILLTEEAEVKLVDFGVSAQLDSTLGRRN----TFI-----------GTPYWMAPEViacdQQPDA 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  653 KIDEKADMYSLGVVFFEL---------WHPFgTAMerHVILTNLKLKGELPLKWVNEFPEqasLLRRLMSPSPSDRPSAT 723
Cdd:cd06608  194 SYDARCDVWSLGITAIELadgkpplcdMHPM-RAL--FKIPRNPPPTLKSPEKWSKEFND---FISECLIKNYEQRPFTE 267

                 ....*..
gi 30694992  724 ELLKHAF 730
Cdd:cd06608  268 ELLEHPF 274
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
425-730 6.68e-15

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: 77.44  E-value: 6.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNK--LDGRQYAVKKI-RLKDKEIpVNSRIVREVATLSRLQ-HQHVvryyqawfeTGVVDpf 500
Cdd:cd07857    2 YELIKELGQGAYGIVCSARNAetSEEETVAIKKItNVFSKKI-LAKRALRELKLLRHFRgHKNI---------TCLYD-- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  501 aganwgsktagssmfsysgavsTEIPEQDNnLESTYLYIQ-MEYcprTLRQVFESYN-----HFdKDFawhlIRQIVEGL 574
Cdd:cd07857   70 ----------------------MDIVFPGN-FNELYLYEElMEA---DLHQIIRSGQpltdaHF-QSF----IYQILCGL 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  575 AHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQDGGFSTDVAgsgvdstgqagTYFYTAPEIEQDWPKI 654
Cdd:cd07857  119 KYIHSANVLHRDLKPGNLLVNADCELKICDFGLARGFSENPGENAGFMTEYVA-----------TRWYRAPEIMLSFQSY 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  655 DEKADMYSLGVVFFELW-------------------HPFGTAME---RHV-------ILTNLKLKGELPLKWVNEF--PE 703
Cdd:cd07857  188 TKAIDVWSVGCILAELLgrkpvfkgkdyvdqlnqilQVLGTPDEetlSRIgspkaqnYIRSLPNIPKKPFESIFPNanPL 267
                        330       340
                 ....*....|....*....|....*..
gi 30694992  704 QASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd07857  268 ALDLLEKLLAFDPTKRISVEEALEHPY 294
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
425-744 6.74e-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: 77.40  E-value: 6.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVN-SRIVREVATLSRLQHQHVVRYYQAWfetgvvdpfaga 503
Cdd:cd06635   27 FSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKwQDIIKEVKFLQRIKHPNSIEYKGCY------------ 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssmfsysgavsteipeqdnnLESTYLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIRQ-IVEGLAHIHGQGI 582
Cdd:cd06635   95 ----------------------------LREHTAWLVMEYCLGSASDLLEVHKKPLQEIEIAAITHgALQGLAYLHSHNM 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  583 IHRDFTPNNIFFDARNDIKIGDFGLAKFlkleqldqdggfsTDVAGSGVdstgqaGTYFYTAPEI--EQDWPKIDEKADM 660
Cdd:cd06635  147 IHRDIKAGNILLTEPGQVKLADFGSASI-------------ASPANSFV------GTPYWMAPEVilAMDEGQYDGKVDV 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  661 YSLGVVFFELwhpfgtaMERHVILTNLKLKGELPLKWVNEFP-----EQASLLRRLMSPS----PSDRPSATELLKHAF- 730
Cdd:cd06635  208 WSLGITCIEL-------AERKPPLFNMNAMSALYHIAQNESPtlqsnEWSDYFRNFVDSClqkiPQDRPTSEELLKHMFv 280
                        330
                 ....*....|....*
gi 30694992  731 -PPRMESELLDNILR 744
Cdd:cd06635  281 lRERPETVLIDLIQR 295
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
431-728 7.04e-15

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


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 76.21  E-value: 7.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVK---KIRLKDKEIPVNSrivrEVATLSRLQHQHVVRYYQAWFetgvvdpfaganwgs 507
Cdd:cd14095    8 IGDGNFAVVKECRDKATDKEYALKiidKAKCKGKEHMIEN----EVAILRRVKHPNIVQLIEEYD--------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 ktagssmfsysgaVSTEipeqdnnlestyLYIQMEYCprTLRQVFE---SYNHFDKDFAWHLIRQIVEGLAHIHGQGIIH 584
Cdd:cd14095   69 -------------TDTE------------LYLVMELV--KGGDLFDaitSSTKFTERDASRMVTDLAQALKYLHSLSIVH 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  585 RDFTPNNIFF----DARNDIKIGDFGLAKFLKlEQLdqdggFSTdvagsgvdstgqAGTYFYTAPEIeqdwpkIDE---- 656
Cdd:cd14095  122 RDIKPENLLVveheDGSKSLKLADFGLATEVK-EPL-----FTV------------CGTPTYVAPEI------LAEtgyg 177
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30694992  657 -KADMYSLGVVFFEL---WHPFGTAMERHVILTNLKLKGE---LPLKWVNEFPEQASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14095  178 lKVDIWAAGVITYILlcgFPPFRSPDRDQEELFDLILAGEfefLSPYWDNISDSAKDLISRMLVVDPEKRYSAGQVLDH 256
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
428-728 7.95e-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: 76.18  E-value: 7.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  428 LKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRivREVATLSRLQHQHVVRyyqawfetgVVDpfaganwgs 507
Cdd:cd13986    5 QRLLGEGGFSFVYLVEDLSTGRLYALKKILCHSKEDVKEAM--REIENYRLFNHPNILR---------LLD--------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 ktagssmfsysgavSTEIPEQDnnlESTYLYIQMEYCPR-TLRQVFESY----NHFDKDFAWHLIRQIVEGLAHIH---G 579
Cdd:cd13986   65 --------------SQIVKEAG---GKKEVYLLLPYYKRgSLQDEIERRlvkgTFFPEDRILHIFLGICRGLKAMHepeL 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  580 QGIIHRDFTPNNIFFDARNDIKIGDFG-------LAKFLKLEQLDQdggfstdvagsgvDSTGQAGTYFYTAPEI----- 647
Cdd:cd13986  128 VPYAHRDIKPGNVLLSEDDEPILMDLGsmnpariEIEGRREALALQ-------------DWAAEHCTMPYRAPELfdvks 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  648 EQDwpkIDEKADMYSLGVVFFELWH---PFGTAMERHVILTNLKLKGELPLKWVNEFPEQ-ASLLRRLMSPSPSDRPSAT 723
Cdd:cd13986  195 HCT---IDEKTDIWSLGCTLYALMYgesPFERIFQKGDSLALAVLSGNYSFPDNSRYSEElHQLVKSMLVVNPAERPSID 271

                 ....*
gi 30694992  724 ELLKH 728
Cdd:cd13986  272 DLLSR 276
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
447-722 9.04e-15

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


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 75.89  E-value: 9.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  447 DGRQYAVKKIRLKDKEipvNSRIVREVATLSRLQHQHVVRYYqawfetgvvdpfaganwgsktagssmfsysgAVSTEIP 526
Cdd:cd13992   24 GGRTVAIKHITFSRTE---KRTILQELNQLKELVHDNLNKFI-------------------------------GICINPP 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  527 EqdnnlestyLYIQMEYCPR-TLRQVFESYNH-FDKDFAWHLIRQIVEGLAHIHGQGII-HRDFTPNNIFFDARNDIKIG 603
Cdd:cd13992   70 N---------IAVVTEYCTRgSLQDVLLNREIkMDWMFKSSFIKDIVKGMNYLHSSSIGyHGRLKSSNCLVDSRWVVKLT 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  604 DFGLAKFLKlEQLDQDggfstdvagsgVDSTGQAGTYFYTAPEI---EQDWPKIDEKADMYSLGVVFFELWH---PFGT- 676
Cdd:cd13992  141 DFGLRNLLE-EQTNHQ-----------LDEDAQHKKLLWTAPELlrgSLLEVRGTQKGDVYSFAIILYEILFrsdPFALe 208
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 30694992  677 ---AMERHVILTNLKLKGELPLKWVNEFPEQ-ASLLRRLMSPSPSDRPSA 722
Cdd:cd13992  209 revAIVEKVISGGNKPFRPELAVLLDEFPPRlVLLVKQCWAENPEKRPSF 258
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
431-728 1.03e-14

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


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 75.65  E-value: 1.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKI--RLKDKEIpVNSrivrEVATLSRLQHQHVVRYYQAwFETgvvdpfaganwgsk 508
Cdd:cd14087    9 IGRGSFSRVVRVEHRVTRQPYAIKMIetKCRGREV-CES----ELNVLRRVRHTNIIQLIEV-FET-------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  509 tagssmfsysgavsteipeqdnnleSTYLYIQMEYCprTLRQVFE---SYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHR 585
Cdd:cd14087   69 -------------------------KERVYMVMELA--TGGELFDriiAKGSFTERDATRVLQMVLDGVKYLHGLGITHR 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  586 DFTPNN-IFFDARND--IKIGDFGLAKFLKleqldqdggfstdvAGSGVDSTGQAGTYFYTAPEIEQDWPKIdEKADMYS 662
Cdd:cd14087  122 DLKPENlLYYHPGPDskIMITDFGLASTRK--------------KGPNCLMKTTCGTPEYIAPEILLRKPYT-QSVDMWA 186
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30694992  663 LGVVFFELWH---PFG----TAMERHVILTNLKLKGElPLKWVNEFPEQasLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14087  187 VGVIAYILLSgtmPFDddnrTRLYRQILRAKYSYSGE-PWPSVSNLAKD--FIDRLLTVNPGERLSATQALKH 256
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
431-730 1.23e-14

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: 75.60  E-value: 1.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVL-----CKNKLDGRQYAVKKIRLKDKEIPVN-SRIVREVATLSRLQHQHVVRYY---QAWFETGVVDPFA 501
Cdd:cd14076    9 LGEGEFGKVKLgwplpKANHRSGVQVAIKLIRRDTQQENCQtSKIMREINILKGLTHPNIVRLLdvlKTKKYIGIVLEFV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 GanwgsktaGSSMFSYSgavsteipeqdnnLESTYLyiqmeycprtlrqvfesynhfdKD-FAWHLIRQIVEGLAHIHGQ 580
Cdd:cd14076   89 S--------GGELFDYI-------------LARRRL----------------------KDsVACRLFAQLISGVAYLHKK 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleQLDQDGG--FSTdvagsgvdstgQAGTYFYTAPE-IEQDWPKIDEK 657
Cdd:cd14076  126 GVVHRDLKLENLLLDKNRNLVITDFGFAN-----TFDHFNGdlMST-----------SCGSPCYAAPElVVSDSMYAGRK 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  658 ADMYSLGVVFFEL---WHPF---------GTAMERHVILTNLKLKgelplkwvneFPEQAS-----LLRRLMSPSPSDRP 720
Cdd:cd14076  190 ADIWSCGVILYAMlagYLPFdddphnpngDNVPRLYRYICNTPLI----------FPEYVTpkardLLRRILVPNPRKRI 259
                        330
                 ....*....|
gi 30694992  721 SATELLKHAF 730
Cdd:cd14076  260 RLSAIMRHAW 269
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
429-730 1.30e-14

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 75.78  E-value: 1.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRivREVATLSRLQ-HQHVVRYyqawfetgvVDpfaganwgs 507
Cdd:cd14037    9 KYLAEGGFAHVYLVKTSNGGNRAALKRVYVNDEHDLNVCK--REIEIMKRLSgHKNIVGY---------ID--------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 ktagsSMFSYSGAVSTEIpeqdnnlestylYIQMEYCPRtlRQVFESYN-HFDKDFAWHLIRQI----VEGLAHIHG--Q 580
Cdd:cd14037   69 -----SSANRSGNGVYEV------------LLLMEYCKG--GGVIDLMNqRLQTGLTESEILKIfcdvCEAVAAMHYlkP 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFDARNDIKIGDFGLA--KFLKLEQLDQDGGFSTDVAgsgVDSTGQagtyfYTAPEIEQDW--PKIDE 656
Cdd:cd14037  130 PLIHRDLKVENVLISDSGNYKLCDFGSAttKILPPQTKQGVTYVEEDIK---KYTTLQ-----YRAPEMIDLYrgKPITE 201
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30694992  657 KADMYSLGVVFFELWHpFGTAMERHVILTNLKLKGELPLKWVNEfPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14037  202 KSDIWALGCLLYKLCF-YTTPFEESGQLAILNGNFTFPDNSRYS-KRLHKLIRYMLEEDPEKRPNIYQVSYEAF 273
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
422-728 1.47e-14

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: 75.63  E-value: 1.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEEL-KPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKdkeipVNSRIVR-EVATLSRLQHQHVVRYyqawfetgvvdp 499
Cdd:cd14085    1 LEDFFEIeSELGRGATSVVYRCRQKGTQKPYAVKKLKKT-----VDKKIVRtEIGVLLRLSHPNIIKL------------ 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  500 faganwgsktagssmfsysgavsTEIPEQDNNLestYLYIQMEYCPRTLRQVFESYNHFDKDFAwHLIRQIVEGLAHIHG 579
Cdd:cd14085   64 -----------------------KEIFETPTEI---SLVLELVTGGELFDRIVEKGYYSERDAA-DAVKQILEAVAYLHE 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  580 QGIIHRDFTPNNIFF-DARND--IKIGDFGLAKFlkleqLDQDGGFSTdvagsgvdstgQAGTYFYTAPEIEQDWPkIDE 656
Cdd:cd14085  117 NGIVHRDLKPENLLYaTPAPDapLKIADFGLSKI-----VDQQVTMKT-----------VCGTPGYCAPEILRGCA-YGP 179
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30694992  657 KADMYSLGVVFFEL---WHPF-GTAMERHVILTNLKLKGELPLKWVNEFPEQAS-LLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14085  180 EVDMWSVGVITYILlcgFEPFyDERGDQYMFKRILNCDYDFVSPWWDDVSLNAKdLVKKLIVLDPKKRLTTQQALQH 256
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
404-723 1.86e-14

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: 75.45  E-value: 1.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  404 EPPSDSCEPNASL-PSSRY--LNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKD-KEIPVNSRIVREVATLSRL 479
Cdd:cd08229    2 GPPVPQFQPQKALrPDMGYntLANFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDlMDAKARADCIKEIDLLKQL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  480 QHQHVVRYYQAWFEtgvvdpfaganwgsktagssmfsysgavsteipeqDNNLESTYLYIQMEYCPRTLRQVFESYNHFD 559
Cdd:cd08229   82 NHPNVIKYYASFIE-----------------------------------DNELNIVLELADAGDLSRMIKHFKKQKRLIP 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  560 KDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEqldqdggfsTDVAGSGVdstgqaGT 639
Cdd:cd08229  127 EKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSK---------TTAAHSLV------GT 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  640 YFYTAPEieqdwpKIDE-----KADMYSLGVVFFE---LWHPF-GTAMERHVILTNLKLKGELPLKWVNEFPEQASLLRR 710
Cdd:cd08229  192 PYYMSPE------RIHEngynfKSDIWSLGCLLYEmaaLQSPFyGDKMNLYSLCKKIEQCDYPPLPSDHYSEELRQLVNM 265
                        330
                 ....*....|...
gi 30694992  711 LMSPSPSDRPSAT 723
Cdd:cd08229  266 CINPDPEKRPDIT 278
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
425-733 1.93e-14

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: 75.09  E-value: 1.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSrIVREVATLSRLQHQHVVRYYQAWfetgvvdpfagan 504
Cdd:cd06642    6 FTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAEDEIED-IQQEITVLSQCDSPYITRYYGSY------------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysgavsteipeqdnnLESTYLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIH 584
Cdd:cd06642   72 ---------------------------LKGTKLWIIMEYLGGGSALDLLKPGPLEETYIATILREILKGLDYLHSERKIH 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  585 RDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQDGGfstdvagsgvdstgqAGTYFYTAPEIEQDwPKIDEKADMYSLG 664
Cdd:cd06642  125 RDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTF---------------VGTPFWMAPEVIKQ-SAYDFKADIWSLG 188
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30694992  665 VVFFEL---------WHPFgtameRHVILTNLKLKGELPLKWVNEFPEqasLLRRLMSPSPSDRPSATELLKHAFPPR 733
Cdd:cd06642  189 ITAIELakgeppnsdLHPM-----RVLFLIPKNSPPTLEGQHSKPFKE---FVEACLNKDPRFRPTAKELLKHKFITR 258
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
425-730 2.27e-14

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: 75.66  E-value: 2.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKeipVNSRIVREVATLSRLQH------QHVVRYYqawfetgvvD 498
Cdd:cd14210   15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIRNKKR---FHQQALVEVKILKHLNDndpddkHNIVRYK---------D 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  499 PFaganwgsktagssMFSYSGAVSTEIPEQdnNLestYLYIQMeycprtlrqvfesyNHFdKDFAWHLIR----QIVEGL 574
Cdd:cd14210   83 SF-------------IFRGHLCIVFELLSI--NL---YELLKS--------------NNF-QGLSLSLIRkfakQILQAL 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  575 AHIHGQGIIHRDFTPNNIFF--DARNDIKIGDFGlakflkleqldqdggfstdvagSGVDSTGQAGTY----FYTAPEIe 648
Cdd:cd14210  130 QFLHKLNIIHCDLKPENILLkqPSKSSIKVIDFG----------------------SSCFEGEKVYTYiqsrFYRAPEV- 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  649 qdwpkI-----DEKADMYSLGVVFFELW--HP----------FGTAME------RHVILT----------NLKLKGELPL 695
Cdd:cd14210  187 -----IlglpyDTAIDMWSLGCILAELYtgYPlfpgeneeeqLACIMEvlgvppKSLIDKasrrkkffdsNGKPRPTTNS 261
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 30694992  696 KWVNEFPEQASL--------------LRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14210  262 KGKKRRPGSKSLaqvlkcddpsfldfLKKCLRWDPSERMTPEEALQHPW 310
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
431-726 2.59e-14

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: 74.85  E-value: 2.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKkiRLKDKEIPVNSRIVREVATLSRLQ-HQHVVRYYQAwfetgvvdpfaganwgskt 509
Cdd:cd14036    8 IAEGGFAFVYEAQDVGTGKEYALK--RLLSNEEEKNKAIIQEINFMKKLSgHPNIVQFCSA------------------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  510 agssmfsysgavSTEIPEQDNNLESTYLyIQMEYCPRTLRQVF---ESYNHFDKDFAWHLIRQIVEGLAHIHGQG--IIH 584
Cdd:cd14036   67 ------------ASIGKEESDQGQAEYL-LLTELCKGQLVDFVkkvEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIH 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  585 RDFTPNNIFFDARNDIKIGDFGLAkflKLEQLDQDGGFSTDVAGSGVDSTGQAGTYFYTAPEIEQDWPK--IDEKADMYS 662
Cdd:cd14036  134 RDLKIENLLIGNQGQIKLCDFGSA---TTEAHYPDYSWSAQKRSLVEDEITRNTTPMYRTPEMIDLYSNypIGEKQDIWA 210
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30694992  663 LGVVFFELW---HPFGTAMERHVILTNLKLKgELPLKWVNEFPeqasLLRRLMSPSPSDRPSATELL 726
Cdd:cd14036  211 LGCILYLLCfrkHPFEDGAKLRIINAKYTIP-PNDTQYTVFHD----LIRSTLKVNPEERLSITEIV 272
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
429-674 2.66e-14

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: 75.39  E-value: 2.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKLDGRQYAVK----KIRLKDKEipvNSRIVREVATLSR-LQHqhvvryyqawfetgvvdPF-AG 502
Cdd:cd05603    1 KVIGKGSFGKVLLAKRKCDGKFYAVKvlqkKTILKKKE---QNHIMAERNVLLKnLKH-----------------PFlVG 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 ANWGSKTAGSSMFSYSGAVSTEIpeqdnnlestYLYIQMEYCPRTLRQVFESynhfdkdfawhliRQIVEGLAHIHGQGI 582
Cdd:cd05603   61 LHYSFQTSEKLYFVLDYVNGGEL----------FFHLQRERCFLEPRARFYA-------------AEVASAIGYLHSLNI 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  583 IHRDFTPNNIFFDARNDIKIGDFGLAKflklEQLDQDGGFSTdvagsgvdstgQAGTYFYTAPEIEQDWPkIDEKADMYS 662
Cdd:cd05603  118 IYRDLKPENILLDCQGHVVLTDFGLCK----EGMEPEETTST-----------FCGTPEYLAPEVLRKEP-YDRTVDWWC 181
                        250
                 ....*....|....*
gi 30694992  663 LGVVFFELWH---PF 674
Cdd:cd05603  182 LGAVLYEMLYglpPF 196
HisRS-like_core cd00773
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ...
794-1121 2.77e-14

Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain.


Pssm-ID: 238396 [Multi-domain]  Cd Length: 261  Bit Score: 74.18  E-value: 2.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  794 TELRDYVVEITKEVFRQHCAKhlEVI-PMRLLSDCpqFSRK--------TVKLLTNGGDMLELCYELRLPFVHWISVNQK 864
Cdd:cd00773    2 AALRRYIEDTLREVFERYGYE--EIDtPVFEYTEL--FLRKsgdevskeMYRFKDKGGRDLALRPDLTAPVARAVAENLL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  865 S---SFKRYEISHVYRRaighspPNPCL-------QADFDIVGGTLSLTEAEVLKVIVDITTHIFHRGSCdIHLNHGDLL 934
Cdd:cd00773   78 SlplPLKLYYIGPVFRY------ERPQKgryrefyQVGVEIIGSDSPLADAEVIALAVEILEALGLKDFQ-IKINHRGIL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  935 DAIWSWAGIKAEHRRKVAELLsmmgslrpqsserklkwvfirrqllqelklpeavvnrlqtvasrfcgdadqalprlrga 1014
Cdd:cd00773  151 DGIAGLLEDREEYIERLIDKL----------------------------------------------------------- 171
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992 1015 lradrpTRKALDELSNLLTYLRVWRIEEHVHIDVLMPPTESYHRNLFFQVFLTKENSSGTsndgvlLAVGGRYDWLVQEV 1094
Cdd:cd00773  172 ------DKEALAHLEKLLDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQGS------IAGGGRYDGLLEEF 239
                        330       340
                 ....*....|....*....|....*..
gi 30694992 1095 CDREhkmnLPgAVGVSLALETIFQHLP 1121
Cdd:cd00773  240 GGED----VP-AVGFAIGLERLLLALE 261
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
425-725 3.32e-14

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: 75.29  E-value: 3.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLkdkEIPVNSRI-VREVATLSRLQHQH--VVRYYQAWFETGVVdpFA 501
Cdd:cd13977    2 YSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRC---NAPENVELaLREFWALSSIQRQHpnVIQLEECVLQRDGL--AQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 GANWGSKTAGSSMFSYSGAVSTEI---PEqdnnlESTYLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIH 578
Cdd:cd13977   77 RMSHGSSKSDLYLLLVETSLKGERcfdPR-----SACYLWFVMEFCDGGDMNEYLLSRRPDRQTNTSFMLQLSSALAFLH 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  579 GQGIIHRDFTPNNIFFDARND---IKIGDFGLAKFLKLEQLdqDGGFSTDVAGSGVDSTgqAGTYFYTAPEIeqdWP-KI 654
Cdd:cd13977  152 RNQIVHRDLKPDNILISHKRGepiLKVADFGLSKVCSGSGL--NPEEPANVNKHFLSSA--CGSDFYMAPEV---WEgHY 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  655 DEKADMYSLGVVFFELWHP------------FGTAMER--------HVILTNLKLKGELPLKWVNEFPEQ-ASLLRRLMS 713
Cdd:cd13977  225 TAKADIFALGIIIWAMVERitfrdgetkkelLGTYIQQgkeivplgEALLENPKLELQIPLKKKKSMNDDmKQLLRDMLA 304
                        330
                 ....*....|..
gi 30694992  714 PSPSDRPSATEL 725
Cdd:cd13977  305 ANPQERPDAFQL 316
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
425-730 3.61e-14

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: 74.27  E-value: 3.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEipvNSRIVREVATLSRL-QHQHVVRYYQAWfetgvvdpfaga 503
Cdd:cd06636   18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDE---EEEIKLEINMLKKYsHHRNIATYYGAF------------ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssmfsysgaVSTEIPEQDNNLestylYIQMEYC-PRTLRQVFESY--NHFDKDFAWHLIRQIVEGLAHIHGQ 580
Cdd:cd06636   83 -----------------IKKSPPGHDDQL-----WLVMEFCgAGSVTDLVKNTkgNALKEDWIAYICREILRGLAHLHAH 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleQLDQDGGFSTDVagsgvdstgqAGTYFYTAPEI----EQDWPKIDE 656
Cdd:cd06636  141 KVIHRDIKGQNVLLTENAEVKLVDFGVSA-----QLDRTVGRRNTF----------IGTPYWMAPEViacdENPDATYDY 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  657 KADMYSLGVVFFEL---------WHPFgtameRHVILTNL----KLKGElplKWVNEFPE--QASLLRRLMSpspsdRPS 721
Cdd:cd06636  206 RSDIWSLGITAIEMaegapplcdMHPM-----RALFLIPRnpppKLKSK---KWSKKFIDfiEGCLVKNYLS-----RPS 272

                 ....*....
gi 30694992  722 ATELLKHAF 730
Cdd:cd06636  273 TEQLLKHPF 281
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
425-730 3.80e-14

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: 74.61  E-value: 3.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKE--IPVNSriVREVATLSRLQ---HQHVVRyyqawfetgVVDP 499
Cdd:cd07863    2 YEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVQTNEdgLPLST--VREVALLKRLEafdHPNIVR---------LMDV 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  500 FAGANWGSKTAGSSMFSYSgavsteipeqDNNLEsTYLyiqmEYCP------RTLRQvfesynhfdkdfawhLIRQIVEG 573
Cdd:cd07863   71 CATSRTDRETKVTLVFEHV----------DQDLR-TYL----DKVPppglpaETIKD---------------LMRQFLRG 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  574 LAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFlkleqldqdggFSTDVAGSGVdstgqAGTYFYTAPEIEQDwPK 653
Cdd:cd07863  121 LDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARI-----------YSCQMALTPV-----VVTLWYRAPEVLLQ-ST 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  654 IDEKADMYSLGVVFFELWH-----------------------------PFGTAMERHviltNLKLKGELPL-KWVNEFPE 703
Cdd:cd07863  184 YATPVDMWSVGCIFAEMFRrkplfcgnseadqlgkifdliglppeddwPRDVTLPRG----AFSPRGPRPVqSVVPEIEE 259
                        330       340
                 ....*....|....*....|....*...
gi 30694992  704 Q-ASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd07863  260 SgAQLLLEMLTFNPHKRISAFRALQHPF 287
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
429-728 4.96e-14

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: 73.58  E-value: 4.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKLDGRQYAVK---KIRLKDKEIpvnSRIVREVATLSRLQHQHVVRYYQAwFETgvvdpfaganw 505
Cdd:cd14071    6 RTIGKGNFAVVKLARHRITKTEVAIKiidKSQLDEENL---KKIYREVQIMKMLNHPHIIKLYQV-MET----------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  506 gsktagssmfsysgavsteipeqdnnleSTYLYIQMEYCPRTlrQVFE---SYNHFDKDFAWHLIRQIVEGLAHIHGQGI 582
Cdd:cd14071   71 ----------------------------KDMLYLVTEYASNG--EIFDylaQHGRMSEKEARKKFWQILSAVEYCHKRHI 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  583 IHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLdqdggFSTdvagsgvdstgQAGTYFYTAPEI----EQDWPKIdeka 658
Cdd:cd14071  121 VHRDLKAENLLLDANMNIKIADFGFSNFFKPGEL-----LKT-----------WCGSPPYAAPEVfegkEYEGPQL---- 180
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30694992  659 DMYSLGVVFFEL---WHPF-GTAMErhvILTNLKLKGE--LPLkWVNEFPEQasLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14071  181 DIWSLGVVLYVLvcgALPFdGSTLQ---TLRDRVLSGRfrIPF-FMSTDCEH--LIRRMLVLDPSKRLTIEQIKKH 250
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
422-741 5.10e-14

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: 74.92  E-value: 5.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKeipVNSRIVREVAT----LSRLQHQHVVRYYqawfetgvv 497
Cdd:cd05610    3 IEEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADM---INKNMVHQVQAerdaLALSKSPFIVHLY--------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  498 dpfaganwgsktagssmfsYSgavsteipeqdnnLES-TYLYIQMEY-CPRTLRQVFESYNHFDKDFAWHLIRQIVEGLA 575
Cdd:cd05610   71 -------------------YS-------------LQSaNNVYLVMEYlIGGDVKSLLHIYGYFDEEMAVKYISEVALALD 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  576 HIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFL---KLEQLD-----------QDG--------------GFSTDV- 626
Cdd:cd05610  119 YLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTlnrELNMMDilttpsmakpkNDYsrtpgqvlslisslGFNTPTp 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  627 ---------AGSGVDSTGQAGTYFYTAPEIEQDWPKiDEKADMYSLGVVFFELWH---PFGTAMERHVILTNLKLKGELP 694
Cdd:cd05610  199 yrtpksvrrGAARVEGERILGTPDYLAPELLLGKPH-GPAVDWWALGVCLFEFLTgipPFNDETPQQVFQNILNRDIPWP 277
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 30694992  695 lkwvnEFPEQASLLRR-----LMSPSPSDRPSATELLKHAFPPRMESELLDN 741
Cdd:cd05610  278 -----EGEEELSVNAQnaieiLLTMDPTKRAGLKELKQHPLFHGVDWENLQN 324
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
428-730 5.23e-14

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


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 74.75  E-value: 5.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  428 LKPLGQGGFGHVVLCK---NKLDGRQYAVKKIRlkdkeipvNSRIVR----------EVATLSRLQHQHVVRYYQAwFET 494
Cdd:cd05584    1 LKVLGKGGYGKVFQVRkttGSDKGKIFAMKVLK--------KASIVRnqkdtahtkaERNILEAVKHPFIVDLHYA-FQT 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  495 GvvdpfaganwgsktaGSsmfsysgavsteipeqdnnlestyLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEG 573
Cdd:cd05584   72 G---------------GK------------------------LYLILEYLSGgELFMHLEREGIFMEDTACFYLAEITLA 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  574 LAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKflklEQLDQDGGFSTdvagsgvdstgQAGTYFYTAPEIEQDWPK 653
Cdd:cd05584  113 LGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCK----ESIHDGTVTHT-----------FCGTIEYMAPEILTRSGH 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  654 iDEKADMYSLGVVFFELWH---PFGTAMERHVILTNLKLKGELP--LKwvnefPEQASLLRRLMSPSPSDR----PS-AT 723
Cdd:cd05584  178 -GKAVDWWSLGALMYDMLTgapPFTAENRKKTIDKILKGKLNLPpyLT-----NEARDLLKKLLKRNVSSRlgsgPGdAE 251

                 ....*..
gi 30694992  724 ELLKHAF 730
Cdd:cd05584  252 EIKAHPF 258
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
567-730 6.49e-14

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: 73.07  E-value: 6.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  567 IRQIVEGLAHIHGQGIIHRDFTPNNIFF--DARNDIKIGDFGLAKFLkleqldqdggfsTDVAGSGVDSTgqagtyFYTA 644
Cdd:cd14133  108 AQQILEALVFLHSLGLIHCDLKPENILLasYSRCQIKIIDFGSSCFL------------TQRLYSYIQSR------YYRA 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  645 PEIEQDWPKiDEKADMYSLGVVFFELW--HP-FGTAMERHVILTNLKLKGELPLKWVNE----FPEQASLLRRLMSPSPS 717
Cdd:cd14133  170 PEVILGLPY-DEKIDMWSLGCILAELYtgEPlFPGASEVDQLARIIGTIGIPPAHMLDQgkadDELFVDFLKKLLEIDPK 248
                        170
                 ....*....|...
gi 30694992  718 DRPSATELLKHAF 730
Cdd:cd14133  249 ERPTASQALSHPW 261
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
425-728 6.76e-14

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: 73.04  E-value: 6.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKI-RLKDKE---IPVNSRIVREVATL---SRLQHQHVVRYYQaWFEtgvv 497
Cdd:cd14005    2 YEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVpKSRVTEwamINGPVPVPLEIALLlkaSKPGVPGVIRLLD-WYE---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  498 dpfaganwgsktagssmfsysgavsteipEQDNnlestYLYIqMEY---CpRTLRQVFESYNHFDKDFAWHLIRQIVEGL 574
Cdd:cd14005   77 -----------------------------RPDG-----FLLI-MERpepC-QDLFDFITERGALSENLARIIFRQVVEAV 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  575 AHIHGQGIIHRDFTPNNIFFDARN-DIKIGDFGLAKFLKleqldqDGGFSTdvagsgvdstgQAGTYFYTAPEIEQDWPK 653
Cdd:cd14005  121 RHCHQRGVLHRDIKDENLLINLRTgEVKLIDFGCGALLK------DSVYTD-----------FDGTRVYSPPEWIRHGRY 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  654 IDEKADMYSLGVVFFELwhpfgtamerhviltnlkLKGELP-------LKWVNEFPEQAS-----LLRRLMSPSPSDRPS 721
Cdd:cd14005  184 HGRPATVWSLGILLYDM------------------LCGDIPfendeqiLRGNVLFRPRLSkeccdLISRCLQFDPSKRPS 245

                 ....*..
gi 30694992  722 ATELLKH 728
Cdd:cd14005  246 LEQILSH 252
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
425-730 6.97e-14

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: 73.06  E-value: 6.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVK---KIRLKDKEIPVNSrivrEVATLSRLQHQHVVRYYQAwFETgvvdpfa 501
Cdd:cd14185    2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKiidKSKLKGKEDMIES----EILIIKSLSHPNIVKLFEV-YET------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 ganwgsktagssmfsysgavSTEIpeqdnnlestylYIQMEYCP--RTLRQVFESYNHFDKDFAWhLIRQIVEGLAHIHG 579
Cdd:cd14185   70 --------------------EKEI------------YLILEYVRggDLFDAIIESVKFTEHDAAL-MIIDLCEALVYIHS 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  580 QGIIHRDFTPNNIFF----DARNDIKIGDFGLAKFLKleqldqdGGFSTdvagsgvdstgQAGTYFYTAPEIEQDwPKID 655
Cdd:cd14185  117 KHIVHRDLKPENLLVqhnpDKSTTLKLADFGLAKYVT-------GPIFT-----------VCGTPTYVAPEILSE-KGYG 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  656 EKADMYSLGVVFFEL---WHPFGTAMERHVILTNLKLKGE---LPLKWVNEFPEQASLLRRLMSPSPSDRPSATELLKHA 729
Cdd:cd14185  178 LEVDMWAAGVILYILlcgFPPFRSPERDQEELFQIIQLGHyefLPPYWDNISEAAKDLISRLLVVDPEKRYTAKQVLQHP 257

                 .
gi 30694992  730 F 730
Cdd:cd14185  258 W 258
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
431-728 7.35e-14

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: 73.52  E-value: 7.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIpvNSRIVREVATLSRLQ-HQHVVRYYQaWFEtgvvdpfaganwgskt 509
Cdd:cd14173   10 LGEGAYARVQTCINLITNKEYAVKIIEKRPGHS--RSRVFREVEMLYQCQgHRNVLELIE-FFE---------------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  510 agssmfsysgavsteipEQDNnlestyLYIQME-YCPRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFT 588
Cdd:cd14173   71 -----------------EEDK------FYLVFEkMRGGSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLK 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  589 PNNIFFDARNDI---KIGDFGLAKFLKLEqldqdgGFSTDVagSGVDSTGQAGTYFYTAPEIEQDWPK----IDEKADMY 661
Cdd:cd14173  128 PENILCEHPNQVspvKICDFDLGSGIKLN------SDCSPI--STPELLTPCGSAEYMAPEVVEAFNEeasiYDKRCDLW 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  662 SLGVVFFEL---WHPF----GT-----------AMERHVILTNLKLKGELPLK-WVNEFPEQASLLRRLMSPSPSDRPSA 722
Cdd:cd14173  200 SLGVILYIMlsgYPPFvgrcGSdcgwdrgeacpACQNMLFESIQEGKYEFPEKdWAHISCAAKDLISKLLVRDAKQRLSA 279

                 ....*.
gi 30694992  723 TELLKH 728
Cdd:cd14173  280 AQVLQH 285
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
431-728 7.61e-14

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: 73.44  E-value: 7.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVK----KIRLKDKEIPVN--------------------SRIVREVATLSRLQHQHVVR 486
Cdd:cd14200    8 IGKGSYGVVKLAYNESDDKYYAMKvlskKKLLKQYGFPRRppprgskaaqgeqakplaplERVYQEIAILKKLDHVNIVK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  487 YYQawfetgVVDPfaganwgsktagssmfsysgavsteiPEQDNnlestyLYIQMEYCPRTLRQVFESYNHFDKDFAWHL 566
Cdd:cd14200   88 LIE------VLDD--------------------------PAEDN------LYMVFDLLRKGPVMEVPSDKPFSEDQARLY 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  567 IRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLakflkleqldqdggfSTDVAGSGVDSTGQAGTYFYTAPE 646
Cdd:cd14200  130 FRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGHVKIADFGV---------------SNQFEGNDALLSSTAGTPAFMAPE 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  647 IEQDWPK-IDEKA-DMYSLGVVFFELWH---PFgtaMERHVILTNLKLKGElplkwVNEFPEQAS-------LLRRLMSP 714
Cdd:cd14200  195 TLSDSGQsFSGKAlDVWAMGVTLYCFVYgkcPF---IDEFILALHNKIKNK-----PVEFPEEPEiseelkdLILKMLDK 266
                        330
                 ....*....|....
gi 30694992  715 SPSDRPSATELLKH 728
Cdd:cd14200  267 NPETRITVPEIKVH 280
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
397-670 7.67e-14

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: 74.34  E-value: 7.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  397 TSVPQF---WEPPSD---SCEPNAslpssrylNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKkirlkdkeipvnsriv 470
Cdd:cd05596    2 KNIENFlnrYEKPVNeitKLRMNA--------EDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMK---------------- 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  471 revaTLSRLQHqhVVRYYQAWF-ETGVVDPFAGANWgsktagssmfsysgAVSTEIPEQDnnleSTYLYIQMEYCPR-TL 548
Cdd:cd05596   58 ----LLSKFEM--IKRSDSAFFwEERDIMAHANSEW--------------IVQLHYAFQD----DKYLYMVMDYMPGgDL 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  549 RQVFESYNhFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleQLDQDGGFSTDVAg 628
Cdd:cd05596  114 VNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCM-----KMDKDGLVRSDTA- 186
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 30694992  629 sgvdstgqAGTYFYTAPEI------------EQDWpkidekadmYSLGVVFFEL 670
Cdd:cd05596  187 --------VGTPDYISPEVlksqggdgvygrECDW---------WSVGVFLYEM 223
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
425-719 8.28e-14

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 73.38  E-value: 8.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKI---RLKDKE----IPVNSRIvrevatLSRLQHQHVVRYYQAwFETgvv 497
Cdd:cd05608    3 FLDFRVLGKGGFGEVSACQMRATGKLYACKKLnkkRLKKRKgyegAMVEKRI------LAKVHSRFIVSLAYA-FQT--- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  498 dpfaganwgsKTAGSSMFSY--SGAVSTEIPEQDnnlestylyiqmeycprtlrqvfESYNHFDKDFAWHLIRQIVEGLA 575
Cdd:cd05608   73 ----------KTDLCLVMTImnGGDLRYHIYNVD-----------------------EENPGFQEPRACFYTAQIISGLE 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  576 HIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqDGGFSTdvagsgvdsTGQAGTYFYTAPEIEQDwPKID 655
Cdd:cd05608  120 HLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELK------DGQTKT---------KGYAGTPGFMAPELLLG-EEYD 183
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30694992  656 EKADMYSLGVVFFELWHPFGTAMERHVILTNLKLKGEL---PLKWVNEFPEQA-SLLRRLMSPSPSDR 719
Cdd:cd05608  184 YSVDYFTLGVTLYEMIAARGPFRARGEKVENKELKQRIlndSVTYSEKFSPASkSICEALLAKDPEKR 251
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
431-730 8.51e-14

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: 74.05  E-value: 8.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRyyqawfetgvvdpfaganwgskta 510
Cdd:cd07859    8 IGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHVSDATRILREIKLLRLLRHPDIVE------------------------ 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  511 gssmfsysgAVSTEIPEQDNNLEStyLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPN 590
Cdd:cd07859   64 ---------IKHIMLPPSRREFKD--IYVVFELMESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPK 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  591 NIFFDARNDIKIGDFGLAKflkleqldqdggFSTDVAGSGVDSTGQAGTYFYTAPEI-EQDWPKIDEKADMYSLGVVFFE 669
Cdd:cd07859  133 NILANADCKLKICDFGLAR------------VAFNDTPTAIFWTDYVATRWYRAPELcGSFFSKYTPAIDIWSIGCIFAE 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  670 -----------------------LWHPFGTAMER------HVILTNLKLKGELPL--KWVNEFPEQASLLRRLMSPSPSD 718
Cdd:cd07859  201 vltgkplfpgknvvhqldlitdlLGTPSPETISRvrnekaRRYLSSMRKKQPVPFsqKFPNADPLALRLLERLLAFDPKD 280
                        330
                 ....*....|..
gi 30694992  719 RPSATELLKHAF 730
Cdd:cd07859  281 RPTAEEALADPY 292
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
431-727 8.92e-14

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: 72.85  E-value: 8.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGhvVLCKNKLDGRQYAVKKIrlkdkEIPVNSR-IVREVATLSRLQHQHVVRYYqawfetgvvdpfaganwgskt 509
Cdd:cd14058    1 VGRGSFG--VVCKARWRNQIVAVKII-----ESESEKKaFEVEVRQLSRVDHPNIIKLY--------------------- 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  510 agssmfsysGAVSTEIPeqdnnlestyLYIQMEYCPR-TLRQVF---ESYNHFDKDFAWHLIRQIVEGLAHIHG---QGI 582
Cdd:cd14058   53 ---------GACSNQKP----------VCLVMEYAEGgSLYNVLhgkEPKPIYTAAHAMSWALQCAKGVAYLHSmkpKAL 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  583 IHRDFTPNN-IFFDARNDIKIGDFGLAkflkleqldqdggfsTDVAGSGVDSTGQAGtyfYTAPEIEQDwPKIDEKADMY 661
Cdd:cd14058  114 IHRDLKPPNlLLTNGGTVLKICDFGTA---------------CDISTHMTNNKGSAA---WMAPEVFEG-SKYSEKCDVF 174
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30694992  662 SLGVVFFELW---HPF---GTAMERHVILTNlklKGE-LPLkwVNEFPEQ-ASLLRRLMSPSPSDRPSATELLK 727
Cdd:cd14058  175 SWGIILWEVItrrKPFdhiGGPAFRIMWAVH---NGErPPL--IKNCPKPiESLMTRCWSKDPEKRPSMKEIVK 243
RWD_RWDD1 cd23816
RWD domain of RWD domain-containing protein 1 (RWDD1) and related proteins; RWDD1, also called ...
32-149 9.08e-14

RWD domain of RWD domain-containing protein 1 (RWDD1) and related proteins; RWDD1, also called DRG family-regulatory protein 2 (DFRP2), or PTD013, interacts with DRG2 and protects DRG2 from proteolytic degradation. It is an androgen receptor-interacting protein that functions as a coactivator of androgen-dependent transcription.


Pssm-ID: 467652  Cd Length: 118  Bit Score: 68.86  E-value: 9.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   32 NELLSEEITALSAIFQEDCKVVSdsRSPPqIAIKLRPYSKDMGYEDTDISAMLIVRCLPGYPYKCPKLQITPEQGLTTAD 111
Cdd:cd23816    2 KEEQRNELEALESIYPDEFTVLS--EEPP-ISFTITVTSEEEENEDETVSVTLKFTYTEKYPDEAPLIEIISHENLEDED 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 30694992  112 AEKLLSLLEDQANSNAreGRVMIFNLVEAAQEFLSEII 149
Cdd:cd23816   79 IEDLLELLEQQAEENL--GMVMVFTIVSAVQEKLNEIV 114
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
431-674 9.23e-14

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


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 73.41  E-value: 9.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRL----KDKEipvnsRIVREVATLSRLQHQHVVRyyqawfetgvvdpfaganwg 506
Cdd:cd14039    1 LGTGGFGNVCLYQNQETGEKIAIKSCRLelsvKNKD-----RWCHEIQIMKKLNHPNVVK-------------------- 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  507 sktagssmfsysgavSTEIPEQDNNLESTYLYIQMEYCP----RTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGI 582
Cdd:cd14039   56 ---------------ACDVPEEMNFLVNDVPLLAMEYCSggdlRKLLNKPENCCGLKESQVLSLLSDIGSGIQYLHENKI 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  583 IHRDFTPNNIFFDARNDI---KIGDFGLAKflkleQLDQdggfstdvagsGVDSTGQAGTYFYTAPEIEQDWPkIDEKAD 659
Cdd:cd14039  121 IHRDLKPENIVLQEINGKivhKIIDLGYAK-----DLDQ-----------GSLCTSFVGTLQYLAPELFENKS-YTVTVD 183
                        250
                 ....*....|....*...
gi 30694992  660 MYSLGVVFFEL---WHPF 674
Cdd:cd14039  184 YWSFGTMVFECiagFRPF 201
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
425-730 9.24e-14

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


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 73.94  E-value: 9.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVryyqawfetGVVDPFagan 504
Cdd:cd07855    7 YEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVTTAKRTLRELKILRHFKHDNII---------AIRDIL---- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsKTAGSsmfsysgavsteIPEQDNnlestyLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIH 584
Cdd:cd07855   74 ---RPKVP------------YADFKD------VYVVLDLMESDLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIH 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  585 RDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQDGGFSTDVAgsgvdstgqagTYFYTAPEIEQDWPKIDEKADMYSLG 664
Cdd:cd07855  133 RDLKPSNLLVNENCELKIGDFGMARGLCTSPEEHKYFMTEYVA-----------TRWYRAPELMLSLPEYTQAIDMWSVG 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  665 VVFFELW---------HPFGtamERHVILTNL---------KLKGELPLKWVNEFPEQA----------------SLLRR 710
Cdd:cd07855  202 CIFAEMLgrrqlfpgkNYVH---QLQLILTVLgtpsqavinAIGADRVRRYIQNLPNKQpvpwetlypkadqqalDLLSQ 278
                        330       340
                 ....*....|....*....|
gi 30694992  711 LMSPSPSDRPSATELLKHAF 730
Cdd:cd07855  279 MLRFDPSERITVAEALQHPF 298
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
423-730 9.63e-14

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: 72.64  E-value: 9.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLD-------GRQYAVKKIrlkdkeIPVNS--RIVREVATLSRLQHQHVVRYYqawfe 493
Cdd:cd14019    1 NKYRIIEKIGEGTFSSVYKAEDKLHdlydrnkGRLVALKHI------YPTSSpsRILNELECLERLGGSNNVSGL----- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  494 tgvvdpfaganwgsKTAgssmfsysgavsteIPEQDNNLestylyIQMEYCPRTLRQVFesYNHFD-KDFAWHLiRQIVE 572
Cdd:cd14019   70 --------------ITA--------------FRNEDQVV------AVLPYIEHDDFRDF--YRKMSlTDIRIYL-RNLFK 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  573 GLAHIHGQGIIHRDFTPNNIFFDARNdiKIG---DFGLAkflkleqldQDGGFSTDVAGSgvdstgQAGTYFYTAPEIEQ 649
Cdd:cd14019  113 ALKHVHSFGIIHRDVKPGNFLYNRET--GKGvlvDFGLA---------QREEDRPEQRAP------RAGTRGFRAPEVLF 175
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  650 DWPKIDEKADMYSLGVVFFEL----WHPFGTAMERHVILTNLKLKGElplkwvnefPEQASLLRRLMSPSPSDRPSATEL 725
Cdd:cd14019  176 KCPHQTTAIDIWSAGVILLSIlsgrFPFFFSSDDIDALAEIATIFGS---------DEAYDLLDKLLELDPSKRITAEEA 246

                 ....*
gi 30694992  726 LKHAF 730
Cdd:cd14019  247 LKHPF 251
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
423-773 1.03e-13

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: 74.66  E-value: 1.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKirLKDKEIpvnsrIVREVATLSRLQHQHVVRYYQAWFETgvvdpfag 502
Cdd:cd05624   72 DDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKI--LNKWEM-----LKRAETACFREERNVLVNGDCQWITT-------- 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgsktagssmFSYSGavsteipeQDNNlestYLYIQMEYCP----RTLRQVFEsyNHFDKDFAWHLIRQIVEGLAHIH 578
Cdd:cd05624  137 ------------LHYAF--------QDEN----YLYLVMDYYVggdlLTLLSKFE--DKLPEDMARFYIGEMVLAIHSIH 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  579 GQGIIHRDFTPNNIFFDARNDIKIGDFGlaKFLKleqLDQDGGFSTDVAgsgvdstgqAGTYFYTAPEI----EQDWPKI 654
Cdd:cd05624  191 QLHYVHRDIKPDNVLLDMNGHIRLADFG--SCLK---MNDDGTVQSSVA---------VGTPDYISPEIlqamEDGMGKY 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  655 DEKADMYSLGVVFFELWH---PF--GTAMERHVILTNLKLKGELPLKWVNEFPEQASLLRRLMSPSPS--DRPSATELLK 727
Cdd:cd05624  257 GPECDWWSLGVCMYEMLYgetPFyaESLVETYGKIMNHEERFQFPSHVTDVSEEAKDLIQRLICSRERrlGQNGIEDFKK 336
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 30694992  728 HAFPPRMESELLDNI----LRIMQTSEDSSVYDRVVSVIFDEEVLEMKSH 773
Cdd:cd05624  337 HAFFEGLNWENIRNLeapyIPDVSSPSDTSNFDVDDDVLRNPEILPPSSH 386
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
428-730 1.16e-13

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: 73.46  E-value: 1.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  428 LKPLGQGGFGHVVLCKNKLDGRQYAVKkirlkdkeipvnsrIVREVATLSRLQHQHVVRYYQAWFETgVVDPF-AGANWG 506
Cdd:cd05604    1 LKVIGKGSFGKVLLAKRKRDGKYYAVK--------------VLQKKVILNRKEQKHIMAERNVLLKN-VKHPFlVGLHYS 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  507 SKTAGSSMFSYSGAVSTEIpeqdnnlestYLYIQMEycprtlrqvfesyNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRD 586
Cdd:cd05604   66 FQTTDKLYFVLDFVNGGEL----------FFHLQRE-------------RSFPEPRARFYAAEIASALGYLHSINIVYRD 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  587 FTPNNIFFDARNDIKIGDFGLAKflkleqldqDGGFSTDVagsgvdSTGQAGTYFYTAPEIEQDWPkIDEKADMYSLGVV 666
Cdd:cd05604  123 LKPENILLDSQGHIVLTDFGLCK---------EGISNSDT------TTTFCGTPEYLAPEVIRKQP-YDNTVDWWCLGSV 186
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30694992  667 FFELWH---PFgTAMERHVILTNLkLKGELPLKWVNEFPeQASLLRRLMSPSPSDRPSAT----ELLKHAF 730
Cdd:cd05604  187 LYEMLYglpPF-YCRDTAEMYENI-LHKPLVLRPGISLT-AWSILEELLEKDRQLRLGAKedflEIKNHPF 254
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
431-670 1.24e-13

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: 72.53  E-value: 1.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVlcKNKL-DGRQYAVKkiRLKDKEIPVNSR-IVREVATLSRLQHQHVVRYYqawfetgvvdpfaganwgsk 508
Cdd:cd14664    1 IGRGGAGTVY--KGVMpNGTLVAVK--RLKGEGTQGGDHgFQAEIQTLGMIRHRNIVRLR-------------------- 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  509 tagssmfsysGAVSTeipeQDNNLeSTYLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQ---GIIHR 585
Cdd:cd14664   57 ----------GYCSN----PTTNL-LVYEYMPNGSLGELLHSRPESQPPLDWETRQRIALGSARGLAYLHHDcspLIIHR 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  586 DFTPNNIFFDARNDIKIGDFGLAKFLkleqldQDGGFSTdvagsgvdSTGQAGTYFYTAPEIEQDWpKIDEKADMYSLGV 665
Cdd:cd14664  122 DVKSNNILLDEEFEAHVADFGLAKLM------DDKDSHV--------MSSVAGSYGYIAPEYAYTG-KVSEKSDVYSYGV 186

                 ....*
gi 30694992  666 VFFEL 670
Cdd:cd14664  187 VLLEL 191
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
422-747 1.40e-13

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: 73.11  E-value: 1.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKE-IPVNSriVREVATLSRLQHQHVVRYYQAwfetgvvdpf 500
Cdd:cd07873    1 LETYIKLDKLGEGTYATVYKGRSKLTDNLVALKEIRLEHEEgAPCTA--IREVSLLKDLKHANIVTLHDI---------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  501 aganwgsktagssmfsysgaVSTEipeqdnnlesTYLYIQMEYCPRTLRQVFESYN-----HFDKDFAWHLIRqiveGLA 575
Cdd:cd07873   69 --------------------IHTE----------KSLTLVFEYLDKDLKQYLDDCGnsinmHNVKLFLFQLLR----GLA 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  576 HIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQldqdGGFSTDVAgsgvdstgqagTYFYTAPEIEQDWPKID 655
Cdd:cd07873  115 YCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSIPT----KTYSNEVV-----------TLWYRPPDILLGSTDYS 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  656 EKADMYSLGVVFFEL-----WHPFGTAMER-HVILTNLKLKGElplkwvNEFPEQASLLRRLMSPSPSDRPSAteLLKHA 729
Cdd:cd07873  180 TQIDMWGVGCIFYEMstgrpLFPGSTVEEQlHFIFRILGTPTE------ETWPGILSNEEFKSYNYPKYRADA--LHNHA 251
                        330
                 ....*....|....*...
gi 30694992  730 fpPRMESELLDNILRIMQ 747
Cdd:cd07873  252 --PRLDSDGADLLSKLLQ 267
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
431-728 1.44e-13

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: 71.76  E-value: 1.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLckNKLDGRQYAVKKIRlKDKEIpvnsrivrEVATLSRLQHQHVVRyyqawfetgvvdpFAGanwgskta 510
Cdd:cd14059    1 LGSGAQGAVFL--GKFRGEEVAVKKVR-DEKET--------DIKHLRKLNHPNIIK-------------FKG-------- 48
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  511 gssmfsysgaVSTEIPeqdnnlestyLY-IQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFT 588
Cdd:cd14059   49 ----------VCTQAP----------CYcILMEYCPYgQLYEVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLK 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  589 PNNIFFDARNDIKIGDFGLAKFLkleqldqdGGFSTDVAGsgvdstgqAGTYFYTAPEIEQDWPkIDEKADMYSLGVVFF 668
Cdd:cd14059  109 SPNVLVTYNDVLKISDFGTSKEL--------SEKSTKMSF--------AGTVAWMAPEVIRNEP-CSEKVDIWSFGVVLW 171
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  669 ELwhpfgtamerhviltnlkLKGELPLKWVNEF-------------------PEQASLLRRLM-SPSPSDRPSATELLKH 728
Cdd:cd14059  172 EL------------------LTGEIPYKDVDSSaiiwgvgsnslqlpvpstcPDGFKLLMKQCwNSKPRNRPSFRQILMH 233
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
431-728 1.68e-13

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: 71.94  E-value: 1.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKeipvnSRivREVATLSRL-QHQHVVRyyqawfetgVVDPFAGANWGSKt 509
Cdd:cd14089    9 LGLGINGKVLECFHKKTGEKFALKVLRDNPK-----AR--REVELHWRAsGCPHIVR---------IIDVYENTYQGRK- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  510 agssmfsysgavsteipeqdnnlestYLYIQMEYCP--RTLRQVFE-SYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRD 586
Cdd:cd14089   72 --------------------------CLLVVMECMEggELFSRIQErADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRD 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  587 FTPNNIFFDARND---IKIGDFGLAKflkleQLDQDGGFSTDVAgsgvdstgqagTYFYTAPEI---EqdwpKIDEKADM 660
Cdd:cd14089  126 LKPENLLYSSKGPnaiLKLTDFGFAK-----ETTTKKSLQTPCY-----------TPYYVAPEVlgpE----KYDKSCDM 185
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30694992  661 YSLGVVFFEL---WHPF----GTAME---RHVILTNlklKGELPLK-WVNEFPEQASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14089  186 WSLGVIMYILlcgYPPFysnhGLAISpgmKKRIRNG---QYEFPNPeWSNVSEEAKDLIRGLLKTDPSERLTIEEVMNH 261
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
423-730 1.78e-13

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: 73.11  E-value: 1.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDkeipvnsrivrevaTLSrlqhQHVVRYYQawfETGVVDPFAG 502
Cdd:cd05601    1 KDFEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSE--------------TLA----QEEVSFFE---EERDIMAKAN 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 ANWGSKTagssMFSYsgavsteipeQDNNlestYLYIQMEYCPR-TLRQVFESY-NHFDKDFAWHLIRQIVEGLAHIHGQ 580
Cdd:cd05601   60 SPWITKL----QYAF----------QDSE----NLYLVMEYHPGgDLLSLLSRYdDIFEESMARFYLAELVLAIHSLHSM 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleQLDQDGgfstdvagsGVDSTGQAGTYFYTAPEIEQdwpKIDEKA-- 658
Cdd:cd05601  122 GYVHRDIKPENILIDRTGHIKLADFGSAA-----KLSSDK---------TVTSKMPVGTPDYIAPEVLT---SMNGGSkg 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  659 ------DMYSLGVVFFELWH---PF--GTAMERHVILTNLKLKgelpLKwvneFPEQA-------SLLRRLMSpSPSDRP 720
Cdd:cd05601  185 tygvecDWWSLGIVAYEMLYgktPFteDTVIKTYSNIMNFKKF----LK----FPEDPkvsesavDLIKGLLT-DAKERL 255
                        330
                 ....*....|
gi 30694992  721 SATELLKHAF 730
Cdd:cd05601  256 GYEGLCCHPF 265
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
418-674 1.99e-13

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 72.93  E-value: 1.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   418 SSRYLNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIR----LKDKEIpvnSRIVREVATLSRLQHQHVVRYYQAWfe 493
Cdd:PTZ00263   13 SSWKLSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKkreiLKMKQV---QHVAQEKSILMELSHPFIVNMMCSF-- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   494 tgvvdpfaganwgsktagssmfsysgavsteipeQDNNlestYLYIQMEYCPRTlrqvfESYNH------FDKDFAWHLI 567
Cdd:PTZ00263   88 ----------------------------------QDEN----RVYFLLEFVVGG-----ELFTHlrkagrFPNDVAKFYH 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   568 RQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqDGGFSTdvagsgvdstgqAGTYFYTAPEI 647
Cdd:PTZ00263  125 AELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVP------DRTFTL------------CGTPEYLAPEV 186
                         250       260       270
                  ....*....|....*....|....*....|.
gi 30694992   648 EQDwpKIDEKA-DMYSLGVVFFEL---WHPF 674
Cdd:PTZ00263  187 IQS--KGHGKAvDWWTMGVLLYEFiagYPPF 215
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
425-730 2.36e-13

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: 71.55  E-value: 2.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKeipVNSRIVREVATLSRLQHQHVVRYYQAWfetgvvdpfagan 504
Cdd:cd14665    2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEK---IDENVQREIINHRSLRHPNIVRFKEVI------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysgavsteipeqdnnLESTYLYIQMEYCPRTlrQVFE---SYNHFDKDFAWHLIRQIVEGLAHIHGQG 581
Cdd:cd14665   66 ---------------------------LTPTHLAIVMEYAAGG--ELFEricNAGRFSEDEARFFFQQLISGVSYCHSMQ 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARN--DIKIGDFGLAKflkleqldqdggfsTDVAGSGVDSTgqAGTYFYTAPEIEQDWPKIDEKAD 659
Cdd:cd14665  117 ICHRDLKLENTLLDGSPapRLKICDFGYSK--------------SSVLHSQPKST--VGTPAYIAPEVLLKKEYDGKIAD 180
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30694992  660 MYSLGVVFFELW---HPFGTAME----RHVILTNLKLKGELPlKWVNEFPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14665  181 VWSCGVTLYVMLvgaYPFEDPEEprnfRKTIQRILSVQYSIP-DYVHISPECRHLISRIFVADPATRITIPEIRNHEW 257
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
423-674 2.65e-13

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: 72.74  E-value: 2.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKkirlkdkeipvnsrIVREVATLSRLQHQHVVRYYQAWFETgVVDPF-A 501
Cdd:cd05602    7 SDFHFLKVIGKGSFGKVLLARHKSDEKFYAVK--------------VLQKKAILKKKEEKHIMSERNVLLKN-VKHPFlV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 GANWGSKTAGSSMFsysgavsteIPEQDNNLESTYlYIQMEYCPRTLRQVFESynhfdkdfawhliRQIVEGLAHIHGQG 581
Cdd:cd05602   72 GLHFSFQTTDKLYF---------VLDYINGGELFY-HLQRERCFLEPRARFYA-------------AEIASALGYLHSLN 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGLAKflklEQLDQDGGFSTdvagsgvdstgQAGTYFYTAPEIEQDWPkIDEKADMY 661
Cdd:cd05602  129 IVYRDLKPENILLDSQGHIVLTDFGLCK----ENIEPNGTTST-----------FCGTPEYLAPEVLHKQP-YDRTVDWW 192
                        250
                 ....*....|....*.
gi 30694992  662 SLGVVFFELWH---PF 674
Cdd:cd05602  193 CLGAVLYEMLYglpPF 208
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
524-727 2.84e-13

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: 71.39  E-value: 2.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  524 EIPEQDNNLestylYIQMEYCP--RTLRQVFESyNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIK 601
Cdd:cd14070   70 DILETENSY-----YLVMELCPggNLMHRIYDK-KRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIK 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  602 IGDFGLAKFLKLEQLDQdgGFSTdvagsgvdstgQAGTYFYTAPEIEQDwPKIDEKADMYSLGVVFFELWH---PFGtam 678
Cdd:cd14070  144 LIDFGLSNCAGILGYSD--PFST-----------QCGSPAYAAPELLAR-KKYGPKVDVWSIGVNMYAMLTgtlPFT--- 206
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 30694992  679 erhVILTNLK-LKGELPLKWVNEFPEQAS-----LLRRLMSPSPSDRPSATELLK 727
Cdd:cd14070  207 ---VEPFSLRaLHQKMVDKEMNPLPTDLSpgaisFLRSLLEPDPLKRPNIKQALA 258
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
431-729 2.85e-13

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: 71.31  E-value: 2.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRL----KDKEIPVNSRIVREVATLSRLQHQHVVRYYQAWFETGVVDPFAgaNWg 506
Cdd:cd06630    8 LGTGAFSSCYQARDVKTGTLMAVKQVSFcrnsSSEQEEVVEAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFV--EW- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  507 skTAGssmfsysGAVSTeipeqdnnlestylyiqmeycprtlrqVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRD 586
Cdd:cd06630   85 --MAG-------GSVAS---------------------------LLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRD 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  587 FTPNNIFFDAR-NDIKIGDFGLAKFLkleqldqdggfSTDVAGSGvDSTGQ-AGTYFYTAPEI---EQdwpkIDEKADMY 661
Cdd:cd06630  129 LKGANLLVDSTgQRLRIADFGAAARL-----------ASKGTGAG-EFQGQlLGTIAFMAPEVlrgEQ----YGRSCDVW 192
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30694992  662 SLGVVFFELW---HPFG-TAMERHVILT-NLKLKGELPlkwvnEFPEQAS-----LLRRLMSPSPSDRPSATELLKHA 729
Cdd:cd06630  193 SVGCVIIEMAtakPPWNaEKISNHLALIfKIASATTPP-----PIPEHLSpglrdVTLRCLELQPEDRPPARELLKHP 265
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
566-730 2.92e-13

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: 71.54  E-value: 2.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  566 LIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFL----KLEQLdqdggfstdvagsgvdstgqAGTYF 641
Cdd:cd14181  121 IMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHLepgeKLREL--------------------CGTPG 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  642 YTAPEI-----EQDWPKIDEKADMYSLGVVFFEL-------WHpfgtamERHVILTNLKLKGELPL---KWVNEFPEQAS 706
Cdd:cd14181  181 YLAPEIlkcsmDETHPGYGKEVDLWACGVILFTLlagsppfWH------RRQMLMLRMIMEGRYQFsspEWDDRSSTVKD 254
                        170       180
                 ....*....|....*....|....
gi 30694992  707 LLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14181  255 LISRLLVVDPEIRLTAEQALQHPF 278
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
431-674 3.04e-13

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: 71.92  E-value: 3.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRlkdKEIPVNS--RIVREVATLSRLQHQHVVryyqawfetgvvdpfaganwgsk 508
Cdd:cd14038    2 LGTGGFGNVLRWINQETGEQVAIKQCR---QELSPKNreRWCLEIQIMKRLNHPNVV----------------------- 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  509 tagssmfsysgaVSTEIPEQDNNLESTYL-YIQMEYCP----RTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGII 583
Cdd:cd14038   56 ------------AARDVPEGLQKLAPNDLpLLAMEYCQggdlRKYLNQFENCCGLREGAILTLLSDISSALRYLHENRII 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  584 HRDFTPNNIFF---DARNDIKIGDFGLAKflkleQLDQdggfstdvagsGVDSTGQAGTYFYTAPE-IEQDwpKIDEKAD 659
Cdd:cd14038  124 HRDLKPENIVLqqgEQRLIHKIIDLGYAK-----ELDQ-----------GSLCTSFVGTLQYLAPElLEQQ--KYTVTVD 185
                        250
                 ....*....|....*...
gi 30694992  660 MYSLGVVFFEL---WHPF 674
Cdd:cd14038  186 YWSFGTLAFECitgFRPF 203
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
565-730 3.33e-13

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


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 71.58  E-value: 3.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  565 HLIRQIVEGLAHIHG-QGIIHRDFTPNNIFFDARNDIKIGDFGLAkfLKLEQ-LDQDGGFSTDVAGSGVDSTGqagTYFY 642
Cdd:cd14011  118 YGLLQISEALSFLHNdVKLVHGNICPESVVINSNGEWKLAGFDFC--ISSEQaTDQFPYFREYDPNLPPLAQP---NLNY 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  643 TAPEIEQDwPKIDEKADMYSLGVVFFELWHPFGTAMERHVILTNLKLK----GELPLKWVNEFP-EQASLLRRLMSPSPS 717
Cdd:cd14011  193 LAPEYILS-KTCDPASDMFSLGVLIYAIYNKGKPLFDCVNNLLSYKKNsnqlRQLSLSLLEKVPeELRDHVKTLLNVTPE 271
                        170
                 ....*....|...
gi 30694992  718 DRPSATELLKHAF 730
Cdd:cd14011  272 VRPDAEQLSKIPF 284
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
425-752 3.95e-13

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: 71.59  E-value: 3.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEipVNSR---IVREVATLSRLQHQHVVRYYQAWfetgvvdpfa 501
Cdd:cd06634   17 FSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQ--SNEKwqdIIKEVKFLQKLRHPNTIEYRGCY---------- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 ganwgsktagssmfsysgavsteipeqdnnLESTYLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIRQ-IVEGLAHIHGQ 580
Cdd:cd06634   85 ------------------------------LREHTAWLVMEYCLGSASDLLEVHKKPLQEVEIAAITHgALQGLAYLHSH 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqdggfstdvagsgvDSTGQAGTYFYTAPEI--EQDWPKIDEKA 658
Cdd:cd06634  135 NMIHRDVKAGNILLTEPGLVKLGDFGSASIMA-------------------PANSFVGTPYWMAPEVilAMDEGQYDGKV 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  659 DMYSLGVVFFELwhpfgtaMERHVILTNLKLKGELPLKWVNEFP-----EQASLLRRLMSPS----PSDRPSATELLKHA 729
Cdd:cd06634  196 DVWSLGITCIEL-------AERKPPLFNMNAMSALYHIAQNESPalqsgHWSEYFRNFVDSClqkiPQDRPTSDVLLKHR 268
                        330       340
                 ....*....|....*....|...
gi 30694992  730 FPPRMESELLdnILRIMQTSEDS 752
Cdd:cd06634  269 FLLRERPPTV--IMDLIQRTKDA 289
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
424-676 4.20e-13

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: 70.84  E-value: 4.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVvlcknkLDGRQYAVKKIRLKDKEIPVNSRIV---REVATLSRLQHQHVVRYYQAwfetgVVDPf 500
Cdd:cd14063    1 ELEIKEVIGKGRFGRV------HRGRWHGDVAIKLLNIDYLNEEQLEafkEEVAAYKNTRHDNLVLFMGA-----CMDP- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  501 aganwgsktagssmfsysgavsteipeqdnnlesTYLYIQMEYCP-RTLRQ-VFESYNHFDKDFAWHLIRQIVEGLAHIH 578
Cdd:cd14063   69 ----------------------------------PHLAIVTSLCKgRTLYSlIHERKEKFDFNKTVQIAQQICQGMGYLH 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  579 GQGIIHRDFTPNNIFFDaRNDIKIGDFGLAKFLKLEQLDQ-DGGFSTdvagsgvdstgQAGTYFYTAPEI----EQDWPK 653
Cdd:cd14063  115 AKGIIHKDLKSKNIFLE-NGRVVITDFGLFSLSGLLQPGRrEDTLVI-----------PNGWLCYLAPEIiralSPDLDF 182
                        250       260       270
                 ....*....|....*....|....*....|..
gi 30694992  654 ID-----EKADMYSLGVVFFEL----WhPFGT 676
Cdd:cd14063  183 EEslpftKASDVYAFGTVWYELlagrW-PFKE 213
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
541-719 4.29e-13

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: 71.63  E-value: 4.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  541 MEYCP-RTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIH--GQGIIHRDFTPNNIFF---DARNDIKIGDFGLAKFLkle 614
Cdd:cd14040   90 LEYCEgNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLvdgTACGEIKITDFGLSKIM--- 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  615 qldQDGGFSTDvagsGVDSTGQ-AGTYFYTAPE---IEQDWPKIDEKADMYSLGVVFFELWH---PFGTAMERHVILT-N 686
Cdd:cd14040  167 ---DDDSYGVD----GMDLTSQgAGTYWYLPPEcfvVGKEPPKISNKVDVWSVGVIFFQCLYgrkPFGHNQSQQDILQeN 239
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 30694992  687 LKLKG---ELPLKWVNEfPEQASLLRRLMSPSPSDR 719
Cdd:cd14040  240 TILKAtevQFPVKPVVS-NEAKAFIRRCLAYRKEDR 274
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
420-684 4.68e-13

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: 72.06  E-value: 4.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  420 RYLNdfeeLKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAWFETGVVDP 499
Cdd:cd07850    1 RYQN----LKPIGSGAQGIVCAAYDTVTGQNVAIKKLSRPFQNVTHAKRAYRELVLMKLVNHKNIIGLLNVFTPQKSLEE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  500 FaganwgsktagssmfsysgavsteipeQDnnlestyLYIQMEYCPRTLRQVFESynHFDKDFAWHLIRQIVEGLAHIHG 579
Cdd:cd07850   77 F---------------------------QD-------VYLVMELMDANLCQVIQM--DLDHERMSYLLYQMLCGIKHLHS 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  580 QGIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleqldqdggfstdVAGSGVDSTGQAGTYFYTAPEIEQDWPkIDEKAD 659
Cdd:cd07850  121 AGIIHRDLKPSNIVVKSDCTLKILDFGLAR----------------TAGTSFMMTPYVVTRYYRAPEVILGMG-YKENVD 183
                        250       260
                 ....*....|....*....|....*
gi 30694992  660 MYSLGVVFFElwhpfgtaMERHVIL 684
Cdd:cd07850  184 IWSVGCIMGE--------MIRGTVL 200
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
569-730 4.70e-13

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: 71.82  E-value: 4.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  569 QIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKflKLEQLDQDGGFS--TD-VAgsgvdstgqagTYFYTAP 645
Cdd:cd07852  115 QLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLAR--SLSQLEEDDENPvlTDyVA-----------TRWYRAP 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  646 EIEQDWPKIDEKADMYSLGVVFFEL---------------------------------WH-PFGTAM-ERhvilTNLKLK 690
Cdd:cd07852  182 EILLGSTRYTKGVDMWSVGCILGEMllgkplfpgtstlnqlekiievigrpsaediesIQsPFAATMlES----LPPSRP 257
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 30694992  691 GELPLKWVNEFPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd07852  258 KSLDELFPKASPDALDLLKKLLVFNPNKRLTAEEALRHPY 297
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
429-730 4.86e-13

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


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 71.65  E-value: 4.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKLDGRQYAVKKIR----LKDKEIPVnSRIVREVATLSRlQHQHVVRYYQAwFETgvvdpfagan 504
Cdd:cd05592    1 KVLGKGSFGKVMLAELKGTNQYFAIKALKkdvvLEDDDVEC-TMIERRVLALAS-QHPFLTHLFCT-FQT---------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysgavsteipeqdnnleSTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGII 583
Cdd:cd05592   68 -----------------------------ESHLFFVMEYLNGgDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGII 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  584 HRDFTPNNIFFDARNDIKIGDFGLAKflkleqldqdggfsTDVAGSGVDSTGqAGTYFYTAPEIEQDWpKIDEKADMYSL 663
Cdd:cd05592  119 YRDLKLDNVLLDREGHIKIADFGMCK--------------ENIYGENKASTF-CGTPDYIAPEILKGQ-KYNQSVDWWSF 182
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30694992  664 GVVFFELW---HPFGTAMERHVILTNLKLKGELPlKWVNEfpEQASLLRRLMSPSPSDR-----PSATELLKHAF 730
Cdd:cd05592  183 GVLLYEMLigqSPFHGEDEDELFWSICNDTPHYP-RWLTK--EAASCLSLLLERNPEKRlgvpeCPAGDIRDHPF 254
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
514-670 4.90e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 72.22  E-value: 4.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   514 MFSYSGAVSTEIPEQDNNLestYLYIQMEYCPRTLRQvfesynhfdkdfAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIF 593
Cdd:PHA03209  125 TLVSGAITCMVLPHYSSDL---YTYLTKRSRPLPIDQ------------ALIIEKQILEGLRYLHAQRIIHRDVKTENIF 189
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30694992   594 FDARNDIKIGDFGLAKFLKLEQLDqdggfstdvagsgvdsTGQAGTYFYTAPEI-EQDwpKIDEKADMYSLGVVFFEL 670
Cdd:PHA03209  190 INDVDQVCIGDLGAAQFPVVAPAF----------------LGLAGTVETNAPEVlARD--KYNSKADIWSAGIVLFEM 249
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
422-728 5.09e-13

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 70.69  E-value: 5.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLK---DKEIpvnsrIVREVATLSRLQHQHVVRYYQAWfetgvvd 498
Cdd:cd14114    1 YDHYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPhesDKET-----VRKEIQIMNQLHHPKLINLHDAF------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  499 pfaganwgsktagssmfsysgavsteipEQDNNLESTYLYIQmeyCPRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIH 578
Cdd:cd14114   69 ----------------------------EDDNEMVLILEFLS---GGELFERIAAEHYKMSEAEVINYMRQVCEGLCHMH 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  579 GQGIIHRDFTPNNIFFDAR--NDIKIGDFGLAKFLKLEQLdqdggfstdvagsgVDSTgqAGTYFYTAPEIEQDWPkIDE 656
Cdd:cd14114  118 ENNIVHLDIKPENIMCTTKrsNEVKLIDFGLATHLDPKES--------------VKVT--TGTAEFAAPEIVEREP-VGF 180
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30694992  657 KADMYSLGVVFFEL---WHPFGTAMERHViLTNLKL----KGELPLKWVNefPEQASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14114  181 YTDMWAVGVLSYVLlsgLSPFAGENDDET-LRNVKScdwnFDDSAFSGIS--EEAKDFIRKLLLADPNKRMTIHQALEH 256
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
425-730 5.49e-13

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: 70.87  E-value: 5.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKE-IPVNSriVREVATLSRLQHQHVVRYYQAwfetgvvdpfaga 503
Cdd:cd07844    2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEIRLEHEEgAPFTA--IREASLLKDLKHANIVTLHDI------------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssmfsysgaVSTEipeqdnnlesTYLYIQMEYCPRTLRQVFESYN-----HFDKDFAWHLIRqiveGLAHIH 578
Cdd:cd07844   67 -----------------IHTK----------KTLTLVFEYLDTDLKQYMDDCGgglsmHNVRLFLFQLLR----GLAYCH 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  579 GQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQldqdGGFSTDVAgsgvdstgqagTYFYTAPEIEQDWPKIDEKA 658
Cdd:cd07844  116 QRRVLHRDLKPQNLLISERGELKLADFGLARAKSVPS----KTYSNEVV-----------TLWYRPPDVLLGSTEYSTSL 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  659 DMYSLGVVFFEL--------------------WHPFGTAMER--HVILTNLKLKGE-----LPLKWVNEFP------EQA 705
Cdd:cd07844  181 DMWGVGCIFYEMatgrplfpgstdvedqlhkiFRVLGTPTEEtwPGVSSNPEFKPYsfpfyPPRPLINHAPrldripHGE 260
                        330       340
                 ....*....|....*....|....*
gi 30694992  706 SLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd07844  261 ELALKFLQYEPKKRISAAEAMKHPY 285
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
534-730 5.91e-13

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 70.48  E-value: 5.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  534 STYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARND---------IKIG 603
Cdd:cd14120   64 SSSVYLVMEYCNGgDLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGrkpspndirLKIA 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  604 DFGLAKFLkleqldQDGGFSTDVAGSGVdstgqagtyfYTAPEIEQDwPKIDEKADMYSLGVVFFELW---HPF--GTAM 678
Cdd:cd14120  144 DFGFARFL------QDGMMAATLCGSPM----------YMAPEVIMS-LQYDAKADLWSIGTIVYQCLtgkAPFqaQTPQ 206
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 30694992  679 E-RHVILTNLKLKGELPlKWVNefPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14120  207 ElKAFYEKNANLRPNIP-SGTS--PALKDLLLGLLKRNPKDRIDFEDFFSHPF 256
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
431-730 5.94e-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: 70.83  E-value: 5.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEipVNSRIVREVATLSRLQHQHVVRYYQAWFEtgvvDPFAGANWGSKTA 510
Cdd:cd14174   10 LGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGH--SRSRVFREVETLYQCQGNKNILELIEFFE----DDTRFYLVFEKLR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  511 GSSMFSYsgavsteipeqdnnlestylyiqmeycprtlrqvFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPN 590
Cdd:cd14174   84 GGSILAH----------------------------------IQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPE 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  591 NI---FFDARNDIKIGDFGLAKFLKLEqldqdggfSTDVAGSGVDSTGQAGTYFYTAPEIEQDWPK----IDEKADMYSL 663
Cdd:cd14174  130 NIlceSPDKVSPVKICDFDLGSGVKLN--------SACTPITTPELTTPCGSAEYMAPEVVEVFTDeatfYDKRCDLWSL 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  664 GVVFFEL---WHPF----GT--AMER----HVILTNL-----KLKGELPLK-WVNEFPEQASLLRRLMSPSPSDRPSATE 724
Cdd:cd14174  202 GVILYIMlsgYPPFvghcGTdcGWDRgevcRVCQNKLfesiqEGKYEFPDKdWSHISSEAKDLISKLLVRDAKERLSAAQ 281

                 ....*.
gi 30694992  725 LLKHAF 730
Cdd:cd14174  282 VLQHPW 287
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
424-730 6.12e-13

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: 70.16  E-value: 6.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKD---KEIPVNsrivrEVATLSRLQHQHVVRYYQAWF---ETGVV 497
Cdd:cd06648    8 DLDNFVKIGEGSTGIVCIATDKSTGRQVAVKKMDLRKqqrRELLFN-----EVVIMRDYQHPNIVEMYSSYLvgdELWVV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  498 dpfaganwgsktagssMFSYSGAVSTEIPEQDNNLESTYLYIqmeyCprtlrqvfesynhfdkdfawhliRQIVEGLAHI 577
Cdd:cd06648   83 ----------------MEFLEGGALTDIVTHTRMNEEQIATV----C-----------------------RAVLKALSFL 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  578 HGQGIIHRDFTPNNIFFDARNDIKIGDFGLAkflkleqldqdGGFSTDVAgsgvDSTGQAGTYFYTAPEIEQDWPkIDEK 657
Cdd:cd06648  120 HSQGVIHRDIKSDSILLTSDGRVKLSDFGFC-----------AQVSKEVP----RRKSLVGTPYWMAPEVISRLP-YGTE 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  658 ADMYSLGVVFFELWH---PFGT-----AMERhviltnlkLKGELPLKWVNEF---PEQASLLRRLMSPSPSDRPSATELL 726
Cdd:cd06648  184 VDIWSLGIMVIEMVDgepPYFNepplqAMKR--------IRDNEPPKLKNLHkvsPRLRSFLDRMLVRDPAQRATAAELL 255

                 ....
gi 30694992  727 KHAF 730
Cdd:cd06648  256 NHPF 259
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
432-730 6.48e-13

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: 70.24  E-value: 6.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  432 GQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEipvNSRIVREVATLSRLQHQHVVRYYQAWfetgvVDPfaganwgsktag 511
Cdd:cd14111   12 ARGRFGVIRRCRENATGKNFPAKIVPYQAEE---KQGVLQEYEILKSLHHERIMALHEAY-----ITP------------ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  512 ssmfsysgavsteipeqdnnlesTYLYIQMEYCP--RTLRQVFESYNHFDKDFAWHLIrQIVEGLAHIHGQGIIHRDFTP 589
Cdd:cd14111   72 -----------------------RYLVLIAEFCSgkELLHSLIDRFRYSEDDVVGYLV-QILQGLEYLHGRRVLHLDIKP 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  590 NNIFFDARNDIKIGDFGLAKF---LKLEQLDQdggfstdvagsgvdstgQAGTYFYTAPEIEQDWPkIDEKADMYSLGVV 666
Cdd:cd14111  128 DNIMVTNLNAIKIVDFGSAQSfnpLSLRQLGR-----------------RTGTLEYMAPEMVKGEP-VGPPADIWSIGVL 189
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  667 FFELW---HPFgtaMERHVILTNLKLKGEL--PLKWVNEFPEQASL-LRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14111  190 TYIMLsgrSPF---EDQDPQETEAKILVAKfdAFKLYPNVSQSASLfLKKVLSSYPWSRPTTKDCFAHAW 256
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
541-754 7.26e-13

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: 70.86  E-value: 7.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  541 MEYCP-RTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIH--GQGIIHRDFTPNNIFF---DARNDIKIGDFGLAKFLkle 614
Cdd:cd14041   90 LEYCEgNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNeiKPPIIHYDLKPGNILLvngTACGEIKITDFGLSKIM--- 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  615 qlDQDGGFSTDvagsGVDSTGQ-AGTYFYTAPE---IEQDWPKIDEKADMYSLGVVFFELWH---PFGTAMERHVILT-N 686
Cdd:cd14041  167 --DDDSYNSVD----GMELTSQgAGTYWYLPPEcfvVGKEPPKISNKVDVWSVGVIFYQCLYgrkPFGHNQSQQDILQeN 240
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30694992  687 LKLKG---ELPLKWVNEfPEQASLLRRLMSPSPSDRPSATELLKHAFpprmeseLLDNILRIMQTSEDSSV 754
Cdd:cd14041  241 TILKAtevQFPPKPVVT-PEAKAFIRRCLAYRKEDRIDVQQLACDPY-------LLPHIRKSVSTSSPAGA 303
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
568-726 7.41e-13

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: 70.11  E-value: 7.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  568 RQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleqldqdggFSTDVAGSGvDSTGQAGTYFYTAPEI 647
Cdd:cd14062   96 RQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLAT------------VKTRWSGSQ-QFEQPTGSILWMAPEV 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  648 --EQDWPKIDEKADMYSLGVVFFELWH---PFGTAMERHVILTNLKlKGELPLKWVNEFPEQASLLRRLMS----PSPSD 718
Cdd:cd14062  163 irMQDENPYSFQSDVYAFGIVLYELLTgqlPYSHINNRDQILFMVG-RGYLRPDLSKVRSDTPKALRRLMEdcikFQRDE 241

                 ....*...
gi 30694992  719 RPSATELL 726
Cdd:cd14062  242 RPLFPQIL 249
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
429-728 7.49e-13

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: 70.35  E-value: 7.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQ-HQHVVRYYQAWfetgvvdpfaganwgs 507
Cdd:cd14197   15 RELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRMEIIHEIAVLELAQaNPWVINLHEVY---------------- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 KTAGSSMFSYSGAVSTEIPEQdnnlestylyiqmeyCprtlrqVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDF 587
Cdd:cd14197   79 ETASEMILVLEYAAGGEIFNQ---------------C------VADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDL 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  588 TPNNIFFDARN---DIKIGDFGLAKFLK-LEQLDQdggfstdvagsgvdstgQAGTYFYTAPEIEQDWPkIDEKADMYSL 663
Cdd:cd14197  138 KPQNILLTSESplgDIKIVDFGLSRILKnSEELRE-----------------IMGTPEYVAPEILSYEP-ISTATDMWSI 199
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30694992  664 GVVFFELW---HPFGTAMERHVILT----NLKLKGElPLKWVNEfpEQASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14197  200 GVLAYVMLtgiSPFLGDDKQETFLNisqmNVSYSEE-EFEHLSE--SAIDFIKTLLIKKPENRATAEDCLKH 268
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
421-730 7.70e-13

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: 70.78  E-value: 7.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  421 YLNDFEELkplGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEipVNSRIVREVATLSRLQHQHVVRYYQAWFetgvvdpf 500
Cdd:cd06659   22 LLENYVKI---GEGSTGVVCIAREKHSGRQVAVKMMDLRKQQ--RRELLFNEVVIMRDYQHPNVVEMYKSYL-------- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  501 aganwgsktagssmfsysgaVSTEipeqdnnlestyLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQ 580
Cdd:cd06659   89 --------------------VGEE------------LWVLMEYLQGGALTDIVSQTRLNEEQIATVCEAVLQALAYLHSQ 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFDARNDIKIGDFGLAkflkleqldqdGGFSTDVAgsgvDSTGQAGTYFYTAPEIEQDWPKIDEkADM 660
Cdd:cd06659  137 GVIHRDIKSDSILLTLDGRVKLSDFGFC-----------AQISKDVP----KRKSLVGTPYWMAPEVISRCPYGTE-VDI 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  661 YSLGVVFFELWH---PFGT-----AMERhviltnlkLKGELPLKWVNEF---PEQASLLRRLMSPSPSDRPSATELLKHA 729
Cdd:cd06659  201 WSLGIMVIEMVDgepPYFSdspvqAMKR--------LRDSPPPKLKNSHkasPVLRDFLERMLVRDPQERATAQELLDHP 272

                 .
gi 30694992  730 F 730
Cdd:cd06659  273 F 273
pknD PRK13184
serine/threonine-protein kinase PknD;
431-737 7.89e-13

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 73.27  E-value: 7.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   431 LGQGGFGHVVLCKNKLDGRQYAVKKIR--LKDKEIpVNSRIVREVATLSRLQHQHVVRYYqawfetgvvdpfaganwgsk 508
Cdd:PRK13184   10 IGKGGMGEVYLAYDPVCSRRVALKKIRedLSENPL-LKKRFLREAKIAADLIHPGIVPVY-------------------- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   509 tagsSMFSYSGAVSTEIPeqdnnlestylYIQMEYCPRTLRQVFE----SYNHFDKDFAWHLIR---QIVEGLAHIHGQG 581
Cdd:PRK13184   69 ----SICSDGDPVYYTMP-----------YIEGYTLKSLLKSVWQkeslSKELAEKTSVGAFLSifhKICATIEYVHSKG 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   582 IIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQdggFSTDVAGSGVDSTGQA------GTYFYTAPEIEQDWPKiD 655
Cdd:PRK13184  134 VLHRDLKPDNILLGLFGEVVILDWGAAIFKKLEEEDL---LDIDVDERNICYSSMTipgkivGTPDYMAPERLLGVPA-S 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   656 EKADMYSLGVVFFE---LWHPFGTA-----MERHVILTNLKLKgelPLKWVNEFPEQASLlrRLMSPSPSDRPSATELLK 727
Cdd:PRK13184  210 ESTDIYALGVILYQmltLSFPYRRKkgrkiSYRDVILSPIEVA---PYREIPPFLSQIAM--KALAVDPAERYSSVQELK 284
                         330
                  ....*....|
gi 30694992   728 HAFPPRMESE 737
Cdd:PRK13184  285 QDLEPHLQGS 294
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
425-725 7.98e-13

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


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 70.31  E-value: 7.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEE-----LKPLGQGGFGHVVLCK----NKLDGRQYAVKKIR------LKDKEipvnsrivREVATLSRLQHQHVVRYYQ 489
Cdd:cd05081    1 FEErhlkyISQLGKGNFGSVELCRydplGDNTGALVAVKQLQhsgpdqQRDFQ--------REIQILKALHSDFIVKYRG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  490 AWFETGvvdpfaganwgsKTAGSSMFSY--SGAVSTEIPEQDNNLESTYLYIqmeycprtlrqvfesynhfdkdFAWhli 567
Cdd:cd05081   73 VSYGPG------------RRSLRLVMEYlpSGCLRDFLQRHRARLDASRLLL----------------------YSS--- 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  568 rQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKleqLDQDGGFstdvagsgVDSTGQAGTYFYtAPEI 647
Cdd:cd05081  116 -QICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLP---LDKDYYV--------VREPGQSPIFWY-APES 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  648 EQDwPKIDEKADMYSLGVVFFELW--------------HPFGTAMERHVILTNLKLkgelpLKWVNEFPEQAS------- 706
Cdd:cd05081  183 LSD-NIFSRQSDVWSFGVVLYELFtycdkscspsaeflRMMGCERDVPALCRLLEL-----LEEGQRLPAPPAcpaevhe 256
                        330
                 ....*....|....*....
gi 30694992  707 LLRRLMSPSPSDRPSATEL 725
Cdd:cd05081  257 LMKLCWAPSPQDRPSFSAL 275
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
569-730 9.45e-13

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: 70.16  E-value: 9.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  569 QIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAkflkleqldqdGGFSTDVAGSGVdstgqaGTYFYTAPEIE 648
Cdd:cd05606  106 EVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLA-----------CDFSKKKPHASV------GTHGYMAPEVL 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  649 QDWPKIDEKADMYSLGVVFFELWH---PF---GTAMERHVILTNLKLKGELPLKWVnefPEQASLLRRLMSPSPSDR--- 719
Cdd:cd05606  169 QKGVAYDSSADWFSLGCMLYKLLKghsPFrqhKTKDKHEIDRMTLTMNVELPDSFS---PELKSLLEGLLQRDVSKRlgc 245
                        170
                 ....*....|...
gi 30694992  720 --PSATELLKHAF 730
Cdd:cd05606  246 lgRGATEVKEHPF 258
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
423-708 1.14e-12

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: 70.02  E-value: 1.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAWFETGvvdpfag 502
Cdd:cd07848    1 NKFEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRG------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgsktagssmfsysgavsteipeqdnnlestYLYIQMEYCPRTLRQVFESY-NHFDKDFAWHLIRQIVEGLAHIHGQG 581
Cdd:cd07848   74 ---------------------------------KLYLVFEYVEKNMLELLEEMpNGVPPEKVRSYIYQLIKAIHWCHKND 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqdggfstdvAGSGVDSTGQAGTYFYTAPEIEQDWPkIDEKADMY 661
Cdd:cd07848  121 IVHRDIKPENLLISHNDVLKLCDFGFARNLS--------------EGSNANYTEYVATRWYRSPELLLGAP-YGKAVDMW 185
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 30694992  662 SLGVVFFEL--WHP-FGTAMERHVILTNLKLKGELPlkwvnefPEQASLL 708
Cdd:cd07848  186 SVGCILGELsdGQPlFPGESEIDQLFTIQKVLGPLP-------AEQMKLF 228
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
431-714 1.18e-12

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


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 70.60  E-value: 1.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIvREVATLSRLQHQHVVRYYqawfetgvvdpfaganwgskta 510
Cdd:cd13988    1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSFMRPLDVQM-REFEVLKKLNHKNIVKLF---------------------- 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  511 gssmfsysgAVSTEipeqdnnLESTYLYIQMEYCP-RTLRQVFE----SYNHFDKDFAwHLIRQIVEGLAHIHGQGIIHR 585
Cdd:cd13988   58 ---------AIEEE-------LTTRHKVLVMELCPcGSLYTVLEepsnAYGLPESEFL-IVLRDVVAGMNHLRENGIVHR 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  586 DFTPNNIFFDARND----IKIGDFGLAKflkleQLDQDGGFSTdvagsgvdstgQAGTYFYTAPEI-------EQDWPKI 654
Cdd:cd13988  121 DIKPGNIMRVIGEDgqsvYKLTDFGAAR-----ELEDDEQFVS-----------LYGTEEYLHPDMyeravlrKDHQKKY 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  655 DEKADMYSLGVVFFEL------WHPFGTAMER----HVILTNlKLKGEL---------PLKWVNEFPEQASL---LRRLM 712
Cdd:cd13988  185 GATVDLWSIGVTFYHAatgslpFRPFEGPRRNkevmYKIITG-KPSGAIsgvqksengPIEWSGELPVSCSLsqgLQTLL 263

                 ..
gi 30694992  713 SP 714
Cdd:cd13988  264 TP 265
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
424-730 1.29e-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: 70.33  E-value: 1.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKnKLDG----RQYAVKKIR----LKDKEIPVNSRIVREVATLSRlQHQHVVRYYQAwFETG 495
Cdd:cd05614    1 NFELLKVLGTGAYGKVFLVR-KVSGhdanKLYAMKVLRkaalVQKAKTVEHTRTERNVLEHVR-QSPFLVTLHYA-FQTD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  496 -----VVDpfaganwgsKTAGSSMFsysgavsteipeqdnnlesTYLYIQmeycprtlrqvfesyNHFDKDFAWHLIRQI 570
Cdd:cd05614   78 aklhlILD---------YVSGGELF-------------------THLYQR---------------DHFSEDEVRFYSGEI 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  571 VEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQDGGFstdvagsgvdstgqAGTYFYTAPEIEQD 650
Cdd:cd05614  115 ILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLTEEKERTYSF--------------CGTIEYMAPEIIRG 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  651 WPKIDEKADMYSLGVVFFELW---HPFGTAMERHVI--LTNLKLKGELPLKWVNEfPEQASLLRRLMSPSPSDR-----P 720
Cdd:cd05614  181 KSGHGKAVDWWSLGILMFELLtgaSPFTLEGEKNTQseVSRRILKCDPPFPSFIG-PVARDLLQKLLCKDPKKRlgagpQ 259
                        330
                 ....*....|
gi 30694992  721 SATELLKHAF 730
Cdd:cd05614  260 GAQEIKEHPF 269
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
533-722 1.63e-12

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: 69.83  E-value: 1.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  533 ESTYLYIQMEYCPRTLRQVFESyNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARND----IKIGDFG-- 606
Cdd:cd14018  111 HNRTLFLVMKNYPCTLRQYLWV-NTPSYRLARVMILQLLEGVDHLVRHGIAHRDLKSDNILLELDFDgcpwLVIADFGcc 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  607 LAkflkleqlDQDGGFSTDVAGSGVDSTGQAGTyfyTAPEIEQDWP----KID-EKADMYSLGVVFFELW---HPFGTAM 678
Cdd:cd14018  190 LA--------DDSIGLQLPFSSWYVDRGGNACL---MAPEVSTAVPgpgvVINySKADAWAVGAIAYEIFglsNPFYGLG 258
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 30694992  679 ERHVILTNLKlKGELPLKWVNEFPEQASLLRRLMSPSPSDRPSA 722
Cdd:cd14018  259 DTMLESRSYQ-ESQLPALPSAVPPDVRQVVKDLLQRDPNKRVSA 301
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
422-747 1.85e-12

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: 69.64  E-value: 1.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKE-IPVNSriVREVATLSRLQHQHVVRYYqawfetgvvdpf 500
Cdd:cd07872    5 METYIKLEKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEgAPCTA--IREVSLLKDLKHANIVTLH------------ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  501 aganwgsktagssmfsysgavstEIPEQDNNLESTYlyiqmEYCPRTLRQVFESYNHFdkdFAWHLIR----QIVEGLAH 576
Cdd:cd07872   71 -----------------------DIVHTDKSLTLVF-----EYLDKDLKQYMDDCGNI---MSMHNVKiflyQILRGLAY 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  577 IHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQldqdGGFSTDVAgsgvdstgqagTYFYTAPEIEQDWPKIDE 656
Cdd:cd07872  120 CHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSVPT----KTYSNEVV-----------TLWYRPPDVLLGSSEYST 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  657 KADMYSLGVVFFEL-----WHPFGTAM-ERHVILTNLKLKGELPLKWVNEFPEQASLLRRLMSPSPsdrpsateLLKHAf 730
Cdd:cd07872  185 QIDMWGVGCIFFEMasgrpLFPGSTVEdELHLIFRLLGTPTEETWPGISSNDEFKNYNFPKYKPQP--------LINHA- 255
                        330
                 ....*....|....*..
gi 30694992  731 pPRMESELLDNILRIMQ 747
Cdd:cd07872  256 -PRLDTEGIELLTKFLQ 271
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
425-740 2.24e-12

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: 69.28  E-value: 2.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKD-KEIPVNSRIVREVATLSRLQHQHVVRYYQAwFETgvvdpfaga 503
Cdd:cd05630    2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRiKKRKGEAMALNEKQILEKVNSRFVVSLAYA-YET--------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssmfsySGAVSTEIPEQDNNLESTYLYIQMEYCPRTLRQVFESynhfdkdfawhliRQIVEGLAHIHGQGII 583
Cdd:cd05630   72 --------------KDALCLVLTLMNGGDLKFHIYHMGQAGFPEARAVFYA-------------AEICCGLEDLHRERIV 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  584 HRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQdggfstdvagsgvdstGQAGTYFYTAPEIEQDwPKIDEKADMYSL 663
Cdd:cd05630  125 YRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIK----------------GRVGTVGYMAPEVVKN-ERYTFSPDWWAL 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  664 GVVFFEL---WHPFGTAMERHVILTNLKLKGELPLKWVNEFPEQA-SLLRRLMSPSPSDR-----PSATE-----LLKHA 729
Cdd:cd05630  188 GCLLYEMiagQSPFQQRKKKIKREEVERLVKEVPEEYSEKFSPQArSLCSMLLCKDPAERlgcrgGGAREvkehpLFKKL 267
                        330
                 ....*....|.
gi 30694992  730 FPPRMESELLD 740
Cdd:cd05630  268 NFKRLGAGMLE 278
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
558-728 2.65e-12

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: 68.48  E-value: 2.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  558 FDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARND---IKIGDFGLAKFLKLEQLDQDGGFstdvagsgvdst 634
Cdd:cd14172  100 FTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKdavLKLTDFGFAKETTVQNALQTPCY------------ 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  635 gqagTYFYTAPEIEQDwPKIDEKADMYSLGVVFFEL---WHPF----GTA----MERHVILTNLklkgELPLKWVNEFPE 703
Cdd:cd14172  168 ----TPYYVAPEVLGP-EKYDKSCDMWSLGVIMYILlcgFPPFysntGQAispgMKRRIRMGQY----GFPNPEWAEVSE 238
                        170       180
                 ....*....|....*....|....*.
gi 30694992  704 QA-SLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14172  239 EAkQLIRHLLKTDPTERMTITQFMNH 264
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
422-753 2.65e-12

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: 68.88  E-value: 2.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKE-IPVNSriVREVATLSRLQHQHVVRYYQAwfetgvvdpf 500
Cdd:cd07871    4 LETYVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEgAPCTA--IREVSLLKNLKHANIVTLHDI---------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  501 aganwgsktagssmfsysgaVSTEipeqdnnlesTYLYIQMEYCPRTLRQVFESYN-----HFDKDFAWHLIRqiveGLA 575
Cdd:cd07871   72 --------------------IHTE----------RCLTLVFEYLDSDLKQYLDNCGnlmsmHNVKIFMFQLLR----GLS 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  576 HIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQldqdGGFSTDVAgsgvdstgqagTYFYTAPEIEQDWPKID 655
Cdd:cd07871  118 YCHKRKILHRDLKPQNLLINEKGELKLADFGLARAKSVPT----KTYSNEVV-----------TLWYRPPDVLLGSTEYS 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  656 EKADMYSLGVVFFEL-----WHPFGTAMER-HVILTNLKLKGELPLKWVNEFPEQASLLRRLMSPSPsdrpsateLLKHA 729
Cdd:cd07871  183 TPIDMWGVGCILYEMatgrpMFPGSTVKEElHLIFRLLGTPTEETWPGVTSNEEFRSYLFPQYRAQP--------LINHA 254
                        330       340
                 ....*....|....*....|....*..
gi 30694992  730 fpPRMESE---LLDNILRIMQTSEDSS 753
Cdd:cd07871  255 --PRLDTDgidLLSSLLLYETKSRISA 279
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
557-730 3.04e-12

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: 68.57  E-value: 3.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  557 HFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQDGGFstdvagsgvdstgq 636
Cdd:cd05583   95 HFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLPGENDRAYSF-------------- 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  637 AGTYFYTAPE-IEQDWPKIDEKADMYSLGVVFFELW---HPFGTAMER--HVILTNLKLKGELPLKwvNEF-PEQASLLR 709
Cdd:cd05583  161 CGTIEYMAPEvVRGGSDGHDKAVDWWSLGVLTYELLtgaSPFTVDGERnsQSEISKRILKSHPPIP--KTFsAEAKDFIL 238
                        170       180
                 ....*....|....*....|....*.
gi 30694992  710 RLMSPSPSDR-----PSATELLKHAF 730
Cdd:cd05583  239 KLLEKDPKKRlgagpRGAHEIKEHPF 264
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
424-730 3.10e-12

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


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 68.53  E-value: 3.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIpvNSRIVREVATLSRLQHQHVVRYYQAWfetgvvdpfaga 503
Cdd:cd06645   12 DFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGED--FAVVQQEIIMMKDCKHSNIVAYFGSY------------ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssmfsysgavsteipeqdnnLESTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGI 582
Cdd:cd06645   78 ----------------------------LRRDKLWICMEFCGGgSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGK 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  583 IHRDFTPNNIFFDARNDIKIGDFGLakflkleqldqdggfSTDVAGSGVDSTGQAGTYFYTAPEIEQDWPK--IDEKADM 660
Cdd:cd06645  130 MHRDIKGANILLTDNGHVKLADFGV---------------SAQITATIAKRKSFIGTPYWMAPEVAAVERKggYNQLCDI 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  661 YSLGVVFFEL---------WHPfgtaMERHVILTNL-----KLKGElpLKWVNEFPEqasLLRRLMSPSPSDRPSATELL 726
Cdd:cd06645  195 WAVGITAIELaelqppmfdLHP----MRALFLMTKSnfqppKLKDK--MKWSNSFHH---FVKMALTKNPKKRPTAEKLL 265

                 ....
gi 30694992  727 KHAF 730
Cdd:cd06645  266 QHPF 269
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
422-730 3.48e-12

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: 68.45  E-value: 3.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKD-------------------KEIPVN-----SRIVREVATLS 477
Cdd:cd14199    1 LNQYKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKlmrqagfprrppprgaraaPEGCTQprgpiERVYQEIAILK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  478 RLQHQHVVRYYQawfetgVVDPfaganwgsktagssmfsysgavsteiPEQDnnlestYLYIQMEYCPRTLRQVFESYNH 557
Cdd:cd14199   81 KLDHPNVVKLVE------VLDD--------------------------PSED------HLYMVFELVKQGPVMEVPTLKP 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  558 FDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLakflkleqldqdggfSTDVAGSGVDSTGQA 637
Cdd:cd14199  123 LSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGEDGHIKIADFGV---------------SNEFEGSDALLTNTV 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  638 GTYFYTAPEIEQDWPKI--DEKADMYSLGVVFFELwhPFGTA--MERHVILTNLKLKGElPLkwvnEFPEQAS------- 706
Cdd:cd14199  188 GTPAFMAPETLSETRKIfsGKALDVWAMGVTLYCF--VFGQCpfMDERILSLHSKIKTQ-PL----EFPDQPDisddlkd 260
                        330       340
                 ....*....|....*....|....
gi 30694992  707 LLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14199  261 LLFRMLDKNPESRISVPEIKLHPW 284
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
431-756 3.53e-12

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: 69.14  E-value: 3.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKirLKDKEIPVNSRIVREVATLSRLQhqhvvryyqawfetgvvdpfaganwgSKTA 510
Cdd:cd05586    1 IGKGTFGQVYQVRKKDTRRIYAMKV--LSKKVIVAKKEVAHTIGERNILV--------------------------RTAL 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  511 GSSMFSYSGAVSTEIPeqdnnlesTYLYIQMEY-CPRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTP 589
Cdd:cd05586   53 DESPFIVGLKFSFQTP--------TDLYLVTDYmSGGELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKP 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  590 NNIFFDARNDIKIGDFGLAKflkleqldqdggfsTDVAGSGVDSTGqAGTYFYTAPEIEQDWPKIDEKADMYSLGVVFFE 669
Cdd:cd05586  125 ENILLDANGHIALCDFGLSK--------------ADLTDNKTTNTF-CGTTEYLAPEVLLDEKGYTKMVDFWSLGVLVFE 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  670 L---WHPF----GTAMERHVILTNLKL-KGELPLkwvnefpEQASLLRRLMSPSPSDR----PSATELLKHAFPPRMESE 737
Cdd:cd05586  190 MccgWSPFyaedTQQMYRNIAFGKVRFpKDVLSD-------EGRSFVKGLLNRNPKHRlgahDDAVELKEHPFFADIDWD 262
                        330       340
                 ....*....|....*....|....*
gi 30694992  738 LLDNIL------RIMQTSEDSSVYD 756
Cdd:cd05586  263 LLSKKKitppfkPIVDSDTDVSNFD 287
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
423-730 3.57e-12

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


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 69.27  E-value: 3.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDkeipvnsrivrevaTLSRLQHQHVvryyQAwfETgvvDPFAG 502
Cdd:cd05598    1 SMFEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKD--------------VLKRNQVAHV----KA--ER---DILAE 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 A--NWGSKTagssMFSYsgavsteipeQDnnleSTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHG 579
Cdd:cd05598   58 AdnEWVVKL----YYSF----------QD----KENLYFVMDYIPGgDLMSLLIKKGIFEEDLARFYIAELVCAIESVHK 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  580 QGIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleqldqdgGF------STDVAGSGVdstgqaGTYFYTAPEI------ 647
Cdd:cd05598  120 MGFIHRDIKPDNILIDRDGHIKLTDFGLCT-----------GFrwthdsKYYLAHSLV------GTPNYIAPEVllrtgy 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  648 EQ--DWpkidekadmYSLGVVFFEL---WHPF--GTAMErhvilTNLKLkgelpLKWVNEF---------PEQASLLRRL 711
Cdd:cd05598  183 TQlcDW---------WSVGVILYEMlvgQPPFlaQTPAE-----TQLKV-----INWRTTLkipheanlsPEAKDLILRL 243
                        330       340
                 ....*....|....*....|..
gi 30694992  712 MSpSPSDR---PSATELLKHAF 730
Cdd:cd05598  244 CC-DAEDRlgrNGADEIKAHPF 264
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
424-730 3.63e-12

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 69.30  E-value: 3.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIR----LKDKEIpvnSRIVREVATLSRLQHQHVVRYYQAWfetgvvdp 499
Cdd:cd05597    2 DFEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNkwemLKRAET---ACFREERDVLVNGDRRWITKLHYAF-------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  500 faganwgsktagssmfsysgavsteipeQDNNlestYLYIQMEYCP----RTLRQVFEsyNHFDKDFAWHLIRQIVEGLA 575
Cdd:cd05597   71 ----------------------------QDEN----YLYLVMDYYCggdlLTLLSKFE--DRLPEEMARFYLAEMVLAID 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  576 HIHGQGIIHRDFTPNNIFFDARNDIKIGDFGlaKFLKleqLDQDGgfstdvagsGVDSTGQAGTYFYTAPEI----EQDW 651
Cdd:cd05597  117 SIHQLGYVHRDIKPDNVLLDRNGHIRLADFG--SCLK---LREDG---------TVQSSVAVGTPDYISPEIlqamEDGK 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  652 PKIDEKADMYSLGVVFFELWH---PF--GTAMERHVILTNLKLKGELPLKwVNEFPEQA-SLLRRLMSPSPS--DRPSAT 723
Cdd:cd05597  183 GRYGPECDWWSLGVCMYEMLYgetPFyaESLVETYGKIMNHKEHFSFPDD-EDDVSEEAkDLIRRLICSRERrlGQNGID 261

                 ....*..
gi 30694992  724 ELLKHAF 730
Cdd:cd05597  262 DFKKHPF 268
PRK12420 PRK12420
histidyl-tRNA synthetase; Provisional
796-1225 3.67e-12

histidyl-tRNA synthetase; Provisional


Pssm-ID: 237097 [Multi-domain]  Cd Length: 423  Bit Score: 69.76  E-value: 3.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   796 LRDYVVEITKEVFRQHCAKHLEViPM----RLLSD----CPQFSRKTVKLLTNGGDMLELCYELRLPFVHWISVNQ--KS 865
Cdd:PRK12420   20 LRNKIKRALEDVFERYGCKPLET-PTlnmyELMSSkyggGDEILKEIYTLTDQGKRDLALRYDLTIPFAKVVAMNPniRL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   866 SFKRYEISHVYRRA-IGHSPPNPCLQADFDIVGGTLSLTEAEVLKVIVDitthIFHRGSCDIHL--NHGDLLDAIWSWAG 942
Cdd:PRK12420   99 PFKRYEIGKVFRDGpIKQGRFREFIQCDVDIVGVESVMAEAELMSMAFE----LFRRLNLEVTIqyNNRKLLNGILQAIG 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   943 IKAEhrrkvaELLSMMGSLrpqsseRKLKWVFI---RRQLLQELKLPEAVVNRLQTVASRFCGDADQALPRLRGALRADr 1019
Cdd:PRK12420  175 IPTE------LTSDVILSL------DKIEKIGIdgvRKDLLERGISEEMADTICNTVLSCLQLSIADFKEAFNNPLVAE- 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  1020 ptrkALDELSNLLTYLRVWRIEEHVHIDVLMPPTESYHRNLFFQVFLTkeNSSGTSNdgvlLAVGGRYDWLVQEVCDREh 1099
Cdd:PRK12420  242 ----GVNELQQLQQYLIALGINENCIFNPFLARGLTMYTGTVYEIFLK--DGSITSS----IGSGGRYDNIIGAFRGDD- 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  1100 kMNLPgAVGVSLALETIFQHLPMdlrpiRNEVSTS--VLVCSRG---GGGLLVQRMelvaeLWEKSIKAEFVPTpDPSLT 1174
Cdd:PRK12420  311 -MNYP-TVGISFGLDVIYTALSQ-----KETISSTadVFIIPLGtelQCLQIAQQL-----RSTTGLKVELELA-GRKLK 377
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 30694992  1175 EQYEYANEHEIKCLVIITESGVAQNQiefVKVRHLElkkekvVGREELVKF 1225
Cdd:PRK12420  378 KALNYANKENIPYVLIIGEEEVSTGT---VMLRNMK------EGSEVKVPL 419
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
423-730 3.77e-12

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: 68.55  E-value: 3.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLK--DKEipvNSRIVREVATLSRLQH-QHVVRYYQAWFETGVVdp 499
Cdd:cd06616    6 EDLKDLGEIGRGAFGTVNKMLHKPSGTIMAVKRIRSTvdEKE---QKRLLMDLDVVMRSSDcPYIVKFYGALFREGDC-- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  500 faganWgsktagssmfsysgaVSTEIpeQDNNLESTYLYIQMeycprTLRQvfesynHFDKDFAWHLIRQIVEGLAHIHG 579
Cdd:cd06616   81 -----W---------------ICMEL--MDISLDKFYKYVYE-----VLDS------VIPEEILGKIAVATVKALNYLKE 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  580 Q-GIIHRDFTPNNIFFDARNDIKIGDFGLAKFLkleqldqdggfstdvagsgVDS---TGQAGTYFYTAPE---IEQDWP 652
Cdd:cd06616  128 ElKIIHRDVKPSNILLDRNGNIKLCDFGISGQL-------------------VDSiakTRDAGCRPYMAPEridPSASRD 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  653 KIDEKADMYSLGVVFFELW---HPFGTAMERHVILTNLkLKGELP-LKWVNEF---PEQASLLRRLMSPSPSDRPSATEL 725
Cdd:cd06616  189 GYDVRSDVWSLGITLYEVAtgkFPYPKWNSVFDQLTQV-VKGDPPiLSNSEERefsPSFVNFVNLCLIKDESKRPKYKEL 267

                 ....*
gi 30694992  726 LKHAF 730
Cdd:cd06616  268 LKHPF 272
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
431-724 3.82e-12

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: 67.94  E-value: 3.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVV--LCKNKLdgrqYAVKKIRL------KDKEIpvnsrIVREVATLSRLQHQHVVRYYQAWFEtgvvDPFAG 502
Cdd:cd14064    1 IGSGSFGKVYkgRCRNKI----VAIKRYRAntycskSDVDM-----FCREVSILCRLNHPCVIQFVGACLD----DPSQF 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 ANWGSKTAGSSMFSYsgavsteIPEQDNNLestylyiqmeycprtlrqvfesynhfDKDFAWHLIRQIVEGLAHIHG--Q 580
Cdd:cd14064   68 AIVTQYVSGGSLFSL-------LHEQKRVI--------------------------DLQSKLIIAVDVAKGMEYLHNltQ 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKleQLDQDggfstdvagsgvDSTGQAGTYFYTAPEIEQDWPKIDEKADM 660
Cdd:cd14064  115 PIIHRDLNSHNILLYEDGHAVVADFGESRFLQ--SLDED------------NMTKQPGNLRWMAPEVFTQCTRYSIKADV 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  661 YSLGVVFFELwhpfgtamerhviltnlkLKGELPLKWV-------------------NEFPEQ-ASLLRRLMSPSPSDRP 720
Cdd:cd14064  181 FSYALCLWEL------------------LTGEIPFAHLkpaaaaadmayhhirppigYSIPKPiSSLLMRGWNAEPESRP 242

                 ....
gi 30694992  721 SATE 724
Cdd:cd14064  243 SFVE 246
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
429-730 3.93e-12

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: 68.88  E-value: 3.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKLDGRQYAVKKIRlkdKEIPVNSRIVREVATLSR-LQH-QHvvryyqawfetgvvdPFAGA-NW 505
Cdd:cd05595    1 KLLGKGTFGKVILVREKATGRYYAMKILR---KEVIIAKDEVAHTVTESRvLQNtRH---------------PFLTAlKY 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  506 GSKTAGSSMFSYSGAVSTEIpeqdnnlestYLYIQMEYCprtlrqvfesynhFDKDFAWHLIRQIVEGLAHIHGQGIIHR 585
Cdd:cd05595   63 AFQTHDRLCFVMEYANGGEL----------FFHLSRERV-------------FTEDRARFYGAEIVSALEYLHSRDVVYR 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  586 DFTPNNIFFDARNDIKIGDFGLAKflklEQLDQDGGFSTdvagsgvdstgQAGTYFYTAPEIEQDwPKIDEKADMYSLGV 665
Cdd:cd05595  120 DIKLENLMLDKDGHIKITDFGLCK----EGITDGATMKT-----------FCGTPEYLAPEVLED-NDYGRAVDWWGLGV 183
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30694992  666 VFFELW---HPFGTamERHVILTNLKLKGELPLKwVNEFPEQASLLRRLMSPSPSDR----PS-ATELLKHAF 730
Cdd:cd05595  184 VMYEMMcgrLPFYN--QDHERLFELILMEEIRFP-RTLSPEAKSLLAGLLKKDPKQRlgggPSdAKEVMEHRF 253
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
423-730 3.96e-12

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: 68.13  E-value: 3.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIpvNSRIVREVATLSRLQHQHVVRYYQAWfetgvvdpfag 502
Cdd:cd06646    9 HDYELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEPGDD--FSLIQQEIFMVKECKHCNIVAYFGSY----------- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgsktagssmfsysgavsteipeqdnnLESTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQG 581
Cdd:cd06646   76 -----------------------------LSREKLWICMEYCGGgSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKG 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGLAkflkleqldqdggfsTDVAGSGVDSTGQAGTYFYTAPEIE--QDWPKIDEKAD 659
Cdd:cd06646  127 KMHRDIKGANILLTDNGDVKLADFGVA---------------AKITATIAKRKSFIGTPYWMAPEVAavEKNGGYNQLCD 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  660 MYSLGVVFFEL---------WHPFgtameRHVILTNL------KLKGElpLKWVNEFpeqASLLRRLMSPSPSDRPSATE 724
Cdd:cd06646  192 IWAVGITAIELaelqppmfdLHPM-----RALFLMSKsnfqppKLKDK--TKWSSTF---HNFVKISLTKNPKKRPTAER 261

                 ....*.
gi 30694992  725 LLKHAF 730
Cdd:cd06646  262 LLTHLF 267
HisRS_anticodon cd00859
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ...
1132-1226 4.04e-12

HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.


Pssm-ID: 238436 [Multi-domain]  Cd Length: 91  Bit Score: 63.33  E-value: 4.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992 1132 STSVLVCSRGGGgLLVQRMELVAELWEKSIKAEFVPTpDPSLTEQYEYANEHEIKCLVIITESGVAQNQiefVKVRHLEL 1211
Cdd:cd00859    1 EVDVYVVPLGEG-ALSEALELAEQLRDAGIKAEIDYG-GRKLKKQFKYADRSGARFAVILGEDELAAGV---VTVKDLET 75
                         90
                 ....*....|....*
gi 30694992 1212 KKEKVVGREELVKFL 1226
Cdd:cd00859   76 GEQETVALDELVEEL 90
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
429-728 4.20e-12

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 67.71  E-value: 4.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKLDGRQYAVKKI-RLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAwfetgvvdpfaganwgs 507
Cdd:cd14163    6 KTIGEGTYSKVKEAFSKKHQRKVAIKIIdKSGGPEEFIQRFLPRELQIVERLDHKNIIHVYEM----------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 ktagssmfsysgavsteipeqdnnLEST--YLYIQMEYCPRTlrQVFESYNH---FDKDFAWHLIRQIVEGLAHIHGQGI 582
Cdd:cd14163   69 ------------------------LESAdgKIYLVMELAEDG--DVFDCVLHggpLPEHRAKALFRQLVEAIRYCHGCGV 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  583 IHRDFTPNNIFFDARNdIKIGDFGLAKFLKLEQLDQDGGFSTDVAgsgvdstgqagtyfYTAPEIEQDWPKIDEKADMYS 662
Cdd:cd14163  123 AHRDLKCENALLQGFT-LKLTDFGFAKQLPKGGRELSQTFCGSTA--------------YAAPEVLQGVPHDSRKGDIWS 187
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30694992  663 LGVVFFELW---HPFGTAMERHVILTNLK---LKGELPLKwvnefPEQASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14163  188 MGVVLYVMLcaqLPFDDTDIPKMLCQQQKgvsLPGHLGVS-----RTCQDLLKRLLEPDMVLRPSIEEVSWH 254
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
423-728 8.03e-12

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: 67.35  E-value: 8.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYA---VKKIRLKDKEIPVNSR-IVREVATLSRLQHQHVVRYYQAW-FETGVV 497
Cdd:cd14194    5 DYYDTGEELGSGQFAVVKKCREKSTGLQYAakfIKKRRTKSSRRGVSREdIEREVSILKEIQHPNVITLHEVYeNKTDVI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  498 DPFaganwgSKTAGSSMFSYsgavsteIPEQDNNLESTylyiqmeycprtlrqvfesynhfdkdfAWHLIRQIVEGLAHI 577
Cdd:cd14194   85 LIL------ELVAGGELFDF-------LAEKESLTEEE---------------------------ATEFLKQILNGVYYL 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  578 HGQGIIHRDFTPNNIFFDARN----DIKIGDFGLAkflklEQLDqdggfstdvagSGVDSTGQAGTYFYTAPEIEQDWPk 653
Cdd:cd14194  125 HSLQIAHFDLKPENIMLLDRNvpkpRIKIIDFGLA-----HKID-----------FGNEFKNIFGTPEFVAPEIVNYEP- 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  654 IDEKADMYSLGVVFFELW---HPFgTAMERHVILTNLKlkgELPLKWVNEFPEQASLL-----RRLMSPSPSDRPSATEL 725
Cdd:cd14194  188 LGLEADMWSIGVITYILLsgaSPF-LGDTKQETLANVS---AVNYEFEDEYFSNTSALakdfiRRLLVKDPKKRMTIQDS 263

                 ...
gi 30694992  726 LKH 728
Cdd:cd14194  264 LQH 266
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
425-730 8.21e-12

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: 67.70  E-value: 8.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNK--LDGRQYAVKKIR-LKDKEIPVNSRIVREVATLSRLQHQHVVryyqawfetgvvdpfa 501
Cdd:cd07842    2 YEIEGCIGRGTYGRVYKAKRKngKDGKEYAIKKFKgDKEQYTGISQSACREIALLRELKHENVV---------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 ganwgsktagssmfsysgavsteipeqdnnlestylyiqmeycprTLRQVFesYNHFDK------DFA----WHLIR--- 568
Cdd:cd07842   66 ---------------------------------------------SLVEVF--LEHADKsvyllfDYAehdlWQIIKfhr 98
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  569 -----------------QIVEGLAHIHGQGIIHRDFTPNNIF----FDARNDIKIGDFGLAKFLK--LEQLdqdggfstd 625
Cdd:cd07842   99 qakrvsippsmvksllwQILNGIHYLHSNWVLHRDLKPANILvmgeGPERGVVKIGDLGLARLFNapLKPL--------- 169
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  626 vagsgVDSTGQAGTYFYTAPEI---EQDWPKideKADMYSLGVVFFEL------WH----------PF------------ 674
Cdd:cd07842  170 -----ADLDPVVVTIWYRAPELllgARHYTK---AIDIWAIGCIFAELltlepiFKgreakikksnPFqrdqlerifevl 241
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30694992  675 GTA----------MERHVILTNLKLKGE----LPLKWVNEFPEQAS----LLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd07842  242 GTPtekdwpdikkMPEYDTLKSDTKASTypnsLLAKWMHKHKKPDSqgfdLLRKLLEYDPTKRITAEEALEHPY 315
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
428-730 9.14e-12

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


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 67.30  E-value: 9.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  428 LKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIP-VNSriVREVATLSRLQ-HQHVVRyyqawFETGVVDPFAGanw 505
Cdd:cd07831    4 LGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKHFKSLEqVNN--LREIQALRRLSpHPNILR-----LIEVLFDRKTG--- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  506 gsktagssmfsySGAVSTEIpeQDNNLestYLYIqmeycpRTLRQvfesynHFDKDFAWHLIRQIVEGLAHIHGQGIIHR 585
Cdd:cd07831   74 ------------RLALVFEL--MDMNL---YELI------KGRKR------PLPEKRVKNYMYQLLKSLDHMHRNGIFHR 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  586 DFTPNNIFFDArNDIKIGDFGLAKflkleqldqdggfstdvagsGVDS----TGQAGTYFYTAPEIEQDWPKIDEKADMY 661
Cdd:cd07831  125 DIKPENILIKD-DILKLADFGSCR--------------------GIYSkppyTEYISTRWYRAPECLLTDGYYGPKMDIW 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  662 SLGVVFFEL--WHPF-----------------GT------AMERHVILTNLKL---KG-ELPLKWVNEFPEQASLLRRLM 712
Cdd:cd07831  184 AVGCVFFEIlsLFPLfpgtneldqiakihdvlGTpdaevlKKFRKSRHMNYNFpskKGtGLRKLLPNASAEGLDLLKKLL 263
                        330
                 ....*....|....*...
gi 30694992  713 SPSPSDRPSATELLKHAF 730
Cdd:cd07831  264 AYDPDERITAKQALRHPY 281
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
424-730 9.99e-12

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: 67.65  E-value: 9.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIrlkDKE--IPVNS--RIVREVATLSRLQHQHVVRYYqAWFETgvvdp 499
Cdd:cd05574    2 HFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVL---DKEemIKRNKvkRVLTEREILATLDHPFLPTLY-ASFQT----- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  500 faganwgsktagssmfsysgavsteipeqdnnleSTYLYIQMEYCP-----RTLRQvfESYNHFDKDFAWHLIRQIVEGL 574
Cdd:cd05574   73 ----------------------------------STHLCFVMDYCPggelfRLLQK--QPGKRLPEEVARFYAAEVLLAL 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  575 AHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAK--------------FLKLEQLDQDGGFSTDVAGSGVDSTGQAGTY 640
Cdd:cd05574  117 EYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKqssvtpppvrkslrKGSRRSSVKSIEKETFVAEPSARSNSFVGTE 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  641 FYTAPEIEQ--------DWpkidekadmYSLGVVFFELWhpFGT----AMERHVILTNLkLKGELplkwvnEFPEQA--- 705
Cdd:cd05574  197 EYIAPEVIKgdghgsavDW---------WTLGILLYEML--YGTtpfkGSNRDETFSNI-LKKEL------TFPESPpvs 258
                        330       340       350
                 ....*....|....*....|....*....|...
gi 30694992  706 ----SLLRRLMSPSPSDR----PSATELLKHAF 730
Cdd:cd05574  259 seakDLIRKLLVKDPSKRlgskRGASEIKRHPF 291
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
422-684 1.11e-11

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: 67.81  E-value: 1.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAWFETGVVDPFa 501
Cdd:cd07874   16 LKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKSLEEF- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 ganwgsktagssmfsysgavsteipeQDnnlestyLYIQMEYCPRTLRQVFESynHFDKDFAWHLIRQIVEGLAHIHGQG 581
Cdd:cd07874   95 --------------------------QD-------VYLVMELMDANLCQVIQM--ELDHERMSYLLYQMLCGIKHLHSAG 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGLAKflkleqldqdggfstdVAGSGVDSTGQAGTYFYTAPEIEQDWpKIDEKADMY 661
Cdd:cd07874  140 IIHRDLKPSNIVVKSDCTLKILDFGLAR----------------TAGTSFMMTPYVVTRYYRAPEVILGM-GYKENVDIW 202
                        250       260
                 ....*....|....*....|...
gi 30694992  662 SLGVVFFElwhpfgtaMERHVIL 684
Cdd:cd07874  203 SVGCIMGE--------MVRHKIL 217
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
431-730 1.11e-11

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: 66.53  E-value: 1.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRlKDK-----EIPVNSRIVREVATLSRLQH--QHVVRYYQaWFETGvvDPFAga 503
Cdd:cd14100    8 LGSGGFGSVYSGIRVADGAPVAIKHVE-KDRvsewgELPNGTRVPMEIVLLKKVGSgfRGVIRLLD-WFERP--DSFV-- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssmfsysgaVSTEIPEQDNNLestYLYIqmeycprTLRQVFEsynhfdKDFAWHLIRQIVEGLAHIHGQGII 583
Cdd:cd14100   82 -----------------LVLERPEPVQDL---FDFI-------TERGALP------EELARSFFRQVLEAVRHCHNCGVL 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  584 HRDFTPNNIFFD-ARNDIKIGDFGLAKFLKleqldqdggfstDVAGSGVDstgqaGTYFYTAPEieqdWPKID----EKA 658
Cdd:cd14100  129 HRDIKDENILIDlNTGELKLIDFGSGALLK------------DTVYTDFD-----GTRVYSPPE----WIRFHryhgRSA 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  659 DMYSLGVVFFELwhpfgtamerhviltnlkLKGELPLKWVNEFPEQASLLRRLMSPS------------PSDRPSATELL 726
Cdd:cd14100  188 AVWSLGILLYDM------------------VCGDIPFEHDEEIIRGQVFFRQRVSSEcqhlikwclalrPSDRPSFEDIQ 249

                 ....
gi 30694992  727 KHAF 730
Cdd:cd14100  250 NHPW 253
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
566-730 1.12e-11

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: 66.86  E-value: 1.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  566 LIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleQLDQdggfstdvagsGVDSTGQAGTYFYTAP 645
Cdd:cd14182  115 IMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSC-----QLDP-----------GEKLREVCGTPGYLAP 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  646 EI-----EQDWPKIDEKADMYSLGVVFFEL-------WHPFGTAMERHVILTNLKLKGElplKWVNEFPEQASLLRRLMS 713
Cdd:cd14182  179 EIiecsmDDNHPGYGKEVDMWSTGVIMYTLlagsppfWHRKQMLMLRMIMSGNYQFGSP---EWDDRSDTVKDLISRFLV 255
                        170
                 ....*....|....*..
gi 30694992  714 PSPSDRPSATELLKHAF 730
Cdd:cd14182  256 VQPQKRYTAEEALAHPF 272
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
425-730 1.16e-11

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: 67.05  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEipvNSRIVREVATLSRLQHQHVVRYYqawfetgvvdpfagan 504
Cdd:cd06637    8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDE---EEEIKQEINMLKKYSHHRNIATY---------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsYSGAVSTEIPEQDNNLestylYIQMEYC-PRTLRQVFESY--NHFDKDFAWHLIRQIVEGLAHIHGQG 581
Cdd:cd06637   69 ------------YGAFIKKNPPGMDDQL-----WLVMEFCgAGSVTDLIKNTkgNTLKEEWIAYICREILRGLSHLHQHK 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGLAKflkleQLDQDGGFSTDVagsgvdstgqAGTYFYTAPEI----EQDWPKIDEK 657
Cdd:cd06637  132 VIHRDIKGQNVLLTENAEVKLVDFGVSA-----QLDRTVGRRNTF----------IGTPYWMAPEViacdENPDATYDFK 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  658 ADMYSLGVVFFELWHPFGTAMERHVILTNL--------KLKGElplKWVNEFpeqASLLRRLMSPSPSDRPSATELLKHA 729
Cdd:cd06637  197 SDLWSLGITAIEMAEGAPPLCDMHPMRALFliprnpapRLKSK---KWSKKF---QSFIESCLVKNHSQRPSTEQLMKHP 270

                 .
gi 30694992  730 F 730
Cdd:cd06637  271 F 271
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
422-670 1.36e-11

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: 67.75  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAWFETGVVDPFa 501
Cdd:cd07876   20 LKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKSLEEF- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 ganwgsktagssmfsysgavsteipeQDnnlestyLYIQMEYCPRTLRQVFesYNHFDKDFAWHLIRQIVEGLAHIHGQG 581
Cdd:cd07876   99 --------------------------QD-------VYLVMELMDANLCQVI--HMELDHERMSYLLYQMLCGIKHLHSAG 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGLAKflkleqldqdggfstdVAGSGVDSTGQAGTYFYTAPEIEQDWpKIDEKADMY 661
Cdd:cd07876  144 IIHRDLKPSNIVVKSDCTLKILDFGLAR----------------TACTNFMMTPYVVTRYYRAPEVILGM-GYKENVDIW 206

                 ....*....
gi 30694992  662 SLGVVFFEL 670
Cdd:cd07876  207 SVGCIMGEL 215
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
424-670 1.36e-11

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: 66.66  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIrlkDKEipvnsRIVRevatLSRLQHQH-VVRYYQAwfetgVVDPFAg 502
Cdd:cd14209    2 DFDRIKTLGTGSFGRVMLVRHKETGNYYAMKIL---DKQ-----KVVK----LKQVEHTLnEKRILQA-----INFPFL- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgsktagssmfsysgaVSTEIPEQDNnlesTYLYIQMEYCP-----RTLRQVfesyNHFDKDFAWHLIRQIVEGLAHI 577
Cdd:cd14209   64 ------------------VKLEYSFKDN----SNLYMVMEYVPggemfSHLRRI----GRFSEPHARFYAAQIVLAFEYL 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  578 HGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqdggfstdvagsGVDSTgQAGTYFYTAPEIEQDWPkIDEK 657
Cdd:cd14209  118 HSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVK-----------------GRTWT-LCGTPEYLAPEIILSKG-YNKA 178
                        250
                 ....*....|...
gi 30694992  658 ADMYSLGVVFFEL 670
Cdd:cd14209  179 VDWWALGVLIYEM 191
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
431-730 1.62e-11

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: 66.14  E-value: 1.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRL---KDKEipvnsRIVREVATLSRLQHQHVVRYYQAwFEtgvvdpfaganwgS 507
Cdd:cd14192   12 LGGGRFGQVHKCTELSTGLTLAAKIIKVkgaKERE-----EVKNEINIMNQLNHVNLIQLYDA-FE-------------S 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 KTAGSSMFSYsgavsteipeqdnnLESTYLYIqmeycprtlRQVFESYNHFDKDfAWHLIRQIVEGLAHIHGQGIIHRDF 587
Cdd:cd14192   73 KTNLTLIMEY--------------VDGGELFD---------RITDESYQLTELD-AILFTRQICEGVHYLHQHYILHLDL 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  588 TPNNIFF--DARNDIKIGDFGLA-KFLKLEQLDQDggfstdvagsgvdstgqAGTYFYTAPEIeQDWPKIDEKADMYSLG 664
Cdd:cd14192  129 KPENILCvnSTGNQIKIIDFGLArRYKPREKLKVN-----------------FGTPEFLAPEV-VNYDFVSFPTDMWSVG 190
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  665 VVFFEL---WHPFGTAMERHVILTNLKLKGELPLKWVNEFPEQAS-LLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14192  191 VITYMLlsgLSPFLGETDAETMNNIVNCKWDFDAEAFENLSEEAKdFISRLLVKEKSCRMSATQCLKHEW 260
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
429-730 1.79e-11

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: 66.69  E-value: 1.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHV--VLCKNKL---DGRQYAVKKIR-LKDKEIPVNSRIVREVAtlsrlqhQHVVRYYQAwFETGVVDPF-A 501
Cdd:cd14013    1 KKLGEGGFGTVykGSLLQKDpggEKRRVVLKKAKeYGEVEIWMNERVRRACP-------SSCAEFVGA-FLDTTSKKFtK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 GANW------GSKTAGSSM----FSYsgavsteipeqdnNLEStYLYIQMEYCPR-------TLRQVFesynhfdkdfaw 564
Cdd:cd14013   73 PSLWlvwkyeGDATLADLMqgkeFPY-------------NLEP-IIFGRVLIPPRgpkrenvIIKSIM------------ 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  565 hliRQIVEGLAHIHGQGIIHRDFTPNNIFFDARN-DIKIGDFGLAKFLKleqldqdggfstdvagSGVDSTGQagtYF-- 641
Cdd:cd14013  127 ---RQILVALRKLHSTGIVHRDVKPQNIIVSEGDgQFKIIDLGAAADLR----------------IGINYIPK---EFll 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  642 ---YTAPE---IEQDWPKIDEKA------------------DMYSLGVVFFELWHPfGTAMERHVILTNLKLKG---ELP 694
Cdd:cd14013  185 dprYAPPEqyiMSTQTPSAPPAPvaaalspvlwqmnlpdrfDMYSAGVILLQMAFP-NLRSDSNLIAFNRQLKQcdyDLN 263
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 30694992  695 lKWVNEFPEQAS-------------------LLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14013  264 -AWRMLVEPRASadlregfeildlddgagwdLVTKLIRYKPRGRLSASAALAHPY 317
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
431-728 2.19e-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: 65.64  E-value: 2.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRlKDK-----EIPVNSRIVREVATLSRL----QHQHVVRYYQaWFETgvvdpfa 501
Cdd:cd14101    8 LGKGGFGTVYAGHRISDGLQVAIKQIS-RNRvqqwsKLPGVNPVPNEVALLQSVgggpGHRGVIRLLD-WFEI------- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 ganwgsktagssmfsysgavsteiPEqdnnlESTYLYIQMEYCPRTLRQVFESyNHFDKDFAWHLIRQIVEGLAHIHGQG 581
Cdd:cd14101   79 ------------------------PE-----GFLLVLERPQHCQDLFDYITER-GALDESLARRFFKQVVEAVQHCHSKG 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARN-DIKIGDFGLAKFLKLEQLdqdggfsTDVAGSGVdstgqagtyfYTAPEieqdWPKIDE---- 656
Cdd:cd14101  129 VVHRDIKDENILVDLRTgDIKLIDFGSGATLKDSMY-------TDFDGTRV----------YSPPE----WILYHQyhal 187
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30694992  657 KADMYSLGVVFFELWH---PFgtamERHVILTNLKLKGELPLKwvnefPEQASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14101  188 PATVWSLGILLYDMVCgdiPF----ERDTDILKAKPSFNKRVS-----NDCRSLIRSCLAYNPSDRPSLEQILLH 253
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
422-670 2.20e-11

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: 66.99  E-value: 2.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVryyqawfetGVVDPFa 501
Cdd:cd07875   23 LKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNII---------GLLNVF- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 ganwgskTAGSSMFSYsgavsteipeQDnnlestyLYIQMEYCPRTLRQVFESynHFDKDFAWHLIRQIVEGLAHIHGQG 581
Cdd:cd07875   93 -------TPQKSLEEF----------QD-------VYIVMELMDANLCQVIQM--ELDHERMSYLLYQMLCGIKHLHSAG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGLAKflkleqldqdggfstdVAGSGVDSTGQAGTYFYTAPEIEQDWpKIDEKADMY 661
Cdd:cd07875  147 IIHRDLKPSNIVVKSDCTLKILDFGLAR----------------TAGTSFMMTPYVVTRYYRAPEVILGM-GYKENVDIW 209

                 ....*....
gi 30694992  662 SLGVVFFEL 670
Cdd:cd07875  210 SVGCIMGEM 218
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
432-670 2.50e-11

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: 65.92  E-value: 2.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  432 GQGGFGHVVlcKNKLDGRQYAVKKIRLKDKEIPVNSRivrEVATLSRLQHQHVVRYYQAwfetgvvdpfaganwgsktag 511
Cdd:cd13998    4 GKGRFGEVW--KASLKNEPVAVKIFSSRDKQSWFREK---EIYRTPMLKHENILQFIAA--------------------- 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  512 ssmfsysgavsteiPEQDNNLESTYLYIqMEYCPRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIH------GQG---I 582
Cdd:cd13998   58 --------------DERDTALRTELWLV-TAFHPNGSL*DYLSLHTIDWVSLCRLALSVARGLAHLHseipgcTQGkpaI 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  583 IHRDFTPNNIFFDARNDIKIGDFGLAkfLKLEQLDQDGgfstDVAGSgvdstGQAGTYFYTAPEIEQDWPKID-----EK 657
Cdd:cd13998  123 AHRDLKSKNILVKNDGTCCIADFGLA--VRLSPSTGEE----DNANN-----GQVGTKRYMAPEVLEGAINLRdfesfKR 191
                        250
                 ....*....|...
gi 30694992  658 ADMYSLGVVFFEL 670
Cdd:cd13998  192 VDIYAMGLVLWEM 204
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
422-730 2.54e-11

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: 65.75  E-value: 2.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEEL-KPLGQGGFGHVVLCKNKLDGRQYAVKKIrlKDKEIPVNSR------IVREVATLSRLQHQHVVRYYQAW-FE 493
Cdd:cd14196    3 VEDFYDIgEELGSGQFAIVKKCREKSTGLEYAAKFI--KKRQSRASRRgvsreeIEREVSILRQVLHPNIITLHDVYeNR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  494 TGVVDPFaganwgSKTAGSSMFSYSgAVSTEIPEQDnnlestylyiqmeycprtlrqvfesynhfdkdfAWHLIRQIVEG 573
Cdd:cd14196   81 TDVVLIL------ELVSGGELFDFL-AQKESLSEEE---------------------------------ATSFIKQILDG 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  574 LAHIHGQGIIHRDFTPNNIFFDARN----DIKIGDFGLAKflKLEQldqdggfstdvagsGVDSTGQAGTYFYTAPEIEQ 649
Cdd:cd14196  121 VNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAH--EIED--------------GVEFKNIFGTPEFVAPEIVN 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  650 DWPkIDEKADMYSLGVVFFELW---HPFGTAMERHVILTNLKLKGELPLKWVNEFPEQA-SLLRRLMSPSPSDRPSATEL 725
Cdd:cd14196  185 YEP-LGLEADMWSIGVITYILLsgaSPFLGDTKQETLANITAVSYDFDEEFFSHTSELAkDFIRKLLVKETRKRLTIQEA 263

                 ....*
gi 30694992  726 LKHAF 730
Cdd:cd14196  264 LRHPW 268
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
567-730 2.59e-11

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: 66.18  E-value: 2.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  567 IRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQDGGFstdvagsgvdstgqAGTYFYTAPE 646
Cdd:cd05613  111 IGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFLLDENERAYSF--------------CGTIEYMAPE 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  647 IEQDWPKIDEKA-DMYSLGVVFFELW---HPFGTAMER--HVILTNLKLKGELPlkwvneFPEQAS-----LLRRLMSPS 715
Cdd:cd05613  177 IVRGGDSGHDKAvDWWSLGVLMYELLtgaSPFTVDGEKnsQAEISRRILKSEPP------YPQEMSalakdIIQRLLMKD 250
                        170       180
                 ....*....|....*....|
gi 30694992  716 PSDR----PS-ATELLKHAF 730
Cdd:cd05613  251 PKKRlgcgPNgADEIKKHPF 270
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
425-733 3.22e-11

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


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 65.82  E-value: 3.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKN-KLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQ---HQHVVRYYqawfetgvvDPF 500
Cdd:cd07862    3 YECVAEIGEGAYGKVFKARDlKNGGRFVALKRVRVQTGEEGMPLSTIREVAVLRHLEtfeHPNVVRLF---------DVC 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  501 AGANWGSKTAGSSMFSYSgavsteipeqDNNLeSTYLYIQME--YCPRTLRQvfesynhfdkdfawhLIRQIVEGLAHIH 578
Cdd:cd07862   74 TVSRTDRETKLTLVFEHV----------DQDL-TTYLDKVPEpgVPTETIKD---------------MMFQLLRGLDFLH 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  579 GQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFlkleqldqdggFSTDVAGSGVdstgqAGTYFYTAPEIEQDwPKIDEKA 658
Cdd:cd07862  128 SHRVVHRDLKPQNILVTSSGQIKLADFGLARI-----------YSFQMALTSV-----VVTLWYRAPEVLLQ-SSYATPV 190
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30694992  659 DMYSLGVVFFELWHpfgtamerhviltnlklkgELPLKWVNEFPEQASLLRRLMS-PSPSDRPSATELLKHAFPPR 733
Cdd:cd07862  191 DLWSVGCIFAEMFR-------------------RKPLFRGSSDVDQLGKILDVIGlPGEEDWPRDVALPRQAFHSK 247
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
420-670 3.23e-11

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: 65.69  E-value: 3.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  420 RYLndfEELKPLGQGGFGHVVLCK----NKLDGRQYAVKKIRlKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAWFETG 495
Cdd:cd05080    4 RYL---KKIRDLGEGHFGKVSLYCydptNDGTGEMVAVKALK-ADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  496 vvdpfaganwgSKTAGSSM-FSYSGAVSTEIPEQDNNLESTYLYIQmeycprtlrqvfesynhfdkdfawhlirQIVEGL 574
Cdd:cd05080   80 -----------GKSLQLIMeYVPLGSLRDYLPKHSIGLAQLLLFAQ----------------------------QICEGM 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  575 AHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqDGGFSTDVAGSGvDStgqagTYFYTAPEIEQDWpKI 654
Cdd:cd05080  121 AYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVP------EGHEYYRVREDG-DS-----PVFWYAPECLKEY-KF 187
                        250
                 ....*....|....*.
gi 30694992  655 DEKADMYSLGVVFFEL 670
Cdd:cd05080  188 YYASDVWSFGVTLYEL 203
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
431-670 3.35e-11

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: 65.22  E-value: 3.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNsrIVREVATLSRLQHQHVVRyyqawfetgvvdpFAGANWGSKTa 510
Cdd:cd14154    1 LGKGFFGQAIKVTHRETGEVMVMKELIRFDEEAQRN--FLKEVKVMRSLDHPNVLK-------------FIGVLYKDKK- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  511 gssmfsysgavsteipeqdnnlestyLYIQMEYCPR-TLRQVFESynhFDKDFAW----HLIRQIVEGLAHIHGQGIIHR 585
Cdd:cd14154   65 --------------------------LNLITEYIPGgTLKDVLKD---MARPLPWaqrvRFAKDIASGMAYLHSMNIIHR 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  586 DFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQDGGFSTDVAGSGVDSTGQ-----AGTYFYTAPEIEQDwPKIDEKADM 660
Cdd:cd14154  116 DLNSHNCLVREDKTVVVADFGLARLIVEERLPSGNMSPSETLRHLKSPDRKkrytvVGNPYWMAPEMLNG-RSYDEKVDI 194
                        250
                 ....*....|
gi 30694992  661 YSLGVVFFEL 670
Cdd:cd14154  195 FSFGIVLCEI 204
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
423-670 3.48e-11

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: 65.64  E-value: 3.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKirLKdkeiPVN-SRIVREVATLSRLQ-HQHVVRYYQAwfetgVVDPf 500
Cdd:cd14132   18 DDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKV--LK----PVKkKKIKREIKILQNLRgGPNIVKLLDV-----VKDP- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  501 aganwGSKTAgSSMFSYsgavsteipeqdnnLESTylyiqmeycprTLRQVFESYNHFDKDFawhLIRQIVEGLAHIHGQ 580
Cdd:cd14132   86 -----QSKTP-SLIFEY--------------VNNT-----------DFKTLYPTLTDYDIRY---YMYELLKALDYCHSK 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFD-ARNDIKIGDFGLAKFLKLEQldqdgGFSTDVAgsgvdstgqagTYFYTAPEIEQDWPKIDEKAD 659
Cdd:cd14132  132 GIMHRDVKPHNIMIDhEKRKLRLIDWGLAEFYHPGQ-----EYNVRVA-----------SRYYKGPELLVDYQYYDYSLD 195
                        250
                 ....*....|.
gi 30694992  660 MYSLGVVFFEL 670
Cdd:cd14132  196 MWSLGCMLASM 206
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
534-730 4.03e-11

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: 64.86  E-value: 4.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  534 STYLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARND--IKIGDFGLAKfl 611
Cdd:cd14112   72 SNFAYLVMEKLQEDVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSwqVKLVDFGRAQ-- 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  612 kleqldqdggfstdvAGSGVDSTGQAGTYFYTAPEIEQDWPKIDEKADMYSLGVVFFEL---WHPFGTAMERHVI----L 684
Cdd:cd14112  150 ---------------KVSKLGKVPVDGDTDWASPEFHNPETPITVQSDIWGLGVLTFCLlsgFHPFTSEYDDEEEtkenV 214
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 30694992  685 TNLKLKGELPLKWVNefPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14112  215 IFVKCRPNLIFVEAT--QEALRFATWALKKSPTRRMRTDEALEHRW 258
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
425-724 4.16e-11

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: 65.40  E-value: 4.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKD-KEIPVNSRIVREVATLSRLQHQHVVRYYQAwFETgvvdpfaga 503
Cdd:cd05631    2 FRHYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRiKKRKGEAMALNEKRILEKVNSRFVVSLAYA-YET--------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsKTAGSSMFSYSGAvsteipeqdNNLEstylyiqmeycprtlrqvFESYNH----FDKDFAWHLIRQIVEGLAHIHG 579
Cdd:cd05631   72 ----KDALCLVLTIMNG---------GDLK------------------FHIYNMgnpgFDEQRAIFYAAELCCGLEDLQR 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  580 QGIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleQLDQdggfstdvagsGVDSTGQAGTYFYTAPEIEQDwPKIDEKAD 659
Cdd:cd05631  121 ERIVYRDLKPENILLDDRGHIRISDLGLAV-----QIPE-----------GETVRGRVGTVGYMAPEVINN-EKYTFSPD 183
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30694992  660 MYSLGVVFFELWH---PFGTAME---RHVILTNLKLKGElplKWVNEFPEQA-SLLRRLMSPSPSDRPSATE 724
Cdd:cd05631  184 WWGLGCLIYEMIQgqsPFRKRKErvkREEVDRRVKEDQE---EYSEKFSEDAkSICRMLLTKNPKERLGCRG 252
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
404-730 4.61e-11

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


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 65.82  E-value: 4.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  404 EPPSDSCEPNASLPSSRY---LNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRlkdKEIPVNSRIVREVATLSRlq 480
Cdd:cd05594    3 SDNSGAEEMEVSLTKPKHkvtMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILK---KEVIVAKDEVAHTLTENR-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  481 hqhVVRYYQAWFETGVVDPFaganwgsKTAGSSMFSYSGAVSTEIpeqdnnlestYLYIQMEYCprtlrqvfesynhFDK 560
Cdd:cd05594   78 ---VLQNSRHPFLTALKYSF-------QTHDRLCFVMEYANGGEL----------FFHLSRERV-------------FSE 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  561 DFAWHLIRQIVEGLAHIHGQ-GIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleqldqdggfstDVAGSGVDSTGQAGT 639
Cdd:cd05594  125 DRARFYGAEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGLCK---------------EGIKDGATMKTFCGT 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  640 YFYTAPEIEQDwPKIDEKADMYSLGVVFFELW---HPFGTamERHVILTNLKLKGELPLKWVNEfPEQASLLRRLMSPSP 716
Cdd:cd05594  190 PEYLAPEVLED-NDYGRAVDWWGLGVVMYEMMcgrLPFYN--QDHEKLFELILMEEIRFPRTLS-PEAKSLLSGLLKKDP 265
                        330
                 ....*....|....*....
gi 30694992  717 SDR-----PSATELLKHAF 730
Cdd:cd05594  266 KQRlgggpDDAKEIMQHKF 284
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
431-730 5.17e-11

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: 64.62  E-value: 5.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQY-AVKKIrlKDKEIPVNSR--IVREVATLSRLQHQHVVRYyqawfetgvvdpfaganwgs 507
Cdd:cd14121    3 LGSGTYATVYKAYRKSGAREVvAVKCV--SKSSLNKASTenLLTEIELLKKLKHPHIVEL-------------------- 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 ktagssmfsysgavsteipeQDNNLESTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRD 586
Cdd:cd14121   61 --------------------KDFQWDEEHIYLIMEYCSGgDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMD 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  587 FTPNNIFFDARND--IKIGDFGLAKFLKLEQldqdggFSTDVAGSGVdstgqagtyfYTAPEIEQDwPKIDEKADMYSLG 664
Cdd:cd14121  121 LKPQNLLLSSRYNpvLKLADFGFAQHLKPND------EAHSLRGSPL----------YMAPEMILK-KKYDARVDLWSVG 183
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30694992  665 VVFFELWhpFGTAMERHVILTNLKLK------GELPLKwVNEFPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14121  184 VILYECL--FGRAPFASRSFEELEEKirsskpIEIPTR-PELSADCRDLLLRLLQRDPDRRISFEEFFAHPF 252
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
431-671 5.79e-11

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


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 65.08  E-value: 5.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVvlCKNKLDGRQYAVKKIRLKDKEIPVNSRivrEVATLSRLQHQHVVRYYqawfetgvvdpfaganwgskta 510
Cdd:cd14054    3 IGQGRYGTV--WKGSLDERPVAVKVFPARHRQNFQNEK---DIYELPLMEHSNILRFI---------------------- 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  511 gssmfsysgaVSTEIPEQDNNLEstYLyIQMEYCPRTLRQVFESYNHFDkdfaWH----LIRQIVEGLAHIHGQ------ 580
Cdd:cd14054   56 ----------GADERPTADGRME--YL-LVLEYAPKGSLCSYLRENTLD----WMsscrMALSLTRGLAYLHTDlrrgdq 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 ---GIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQDGGFSTDVAgsgvdSTGQAGTYFYTAPEI------EQDW 651
Cdd:cd14054  119 ykpAIAHRDLNSRNVLVKADGSCVICDFGLAMVLRGSSLVRGRPGAAENA-----SISEVGTLRYMAPEVlegavnLRDC 193
                        250       260
                 ....*....|....*....|
gi 30694992  652 PKIDEKADMYSLGVVFFELW 671
Cdd:cd14054  194 ESALKQVDVYALGLVLWEIA 213
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
423-670 5.83e-11

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 66.18  E-value: 5.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKkirlkdkeipvnsrivrevaTLSRLQHqhVVRYYQAWF-ETGVVDPFA 501
Cdd:cd05622   73 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMK--------------------LLSKFEM--IKRSDSAFFwEERDIMAFA 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 GANWgsktagssmfsysgAVSTEIPEQDNNlestYLYIQMEYCPR-TLRQVFESYNHFDKdFAWHLIRQIVEGLAHIHGQ 580
Cdd:cd05622  131 NSPW--------------VVQLFYAFQDDR----YLYMVMEYMPGgDLVNLMSNYDVPEK-WARFYTAEVVLALDAIHSM 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleQLDQDGGFSTDVAgsgvdstgqAGTYFYTAPEIEQDWPK---IDEK 657
Cdd:cd05622  192 GFIHRDVKPDNMLLDKSGHLKLADFGTCM-----KMNKEGMVRCDTA---------VGTPDYISPEVLKSQGGdgyYGRE 257
                        250
                 ....*....|...
gi 30694992  658 ADMYSLGVVFFEL 670
Cdd:cd05622  258 CDWWSVGVFLYEM 270
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
548-725 6.09e-11

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


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 64.56  E-value: 6.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  548 LRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIF---FDARN--DIKIGDFGLAKFlkleqldqdgGF 622
Cdd:cd14000   99 LQQDSRSFASLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLvwtLYPNSaiIIKIADYGISRQ----------CC 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  623 STDVAGSGvdstgqaGTYFYTAPEIEQDWPKIDEKADMYSLGVVFFELWHPFGTAMERHVILTNLKLKGEL--PLKWVNE 700
Cdd:cd14000  169 RMGAKGSE-------GTPGFRAPEIARGNVIYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIHGGLrpPLKQYEC 241
                        170       180
                 ....*....|....*....|....*..
gi 30694992  701 --FPEQASLLRRLMSPSPSDRPSATEL 725
Cdd:cd14000  242 apWPEVEVLMKKCWKENPQQRPTAVTV 268
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
421-730 6.14e-11

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


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 64.98  E-value: 6.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  421 YLNdfeeLKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKE-IPVNSriVREVATLSRLQHQHVVRYYqawfetgvvdp 499
Cdd:cd07870    2 YLN----LEKLGEGSYATVYKGISRINGQLVALKVISMKTEEgVPFTA--IREASLLKGLKHANIVLLH----------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  500 faganwgsktagssmfsysgavstEIPEQDNNLESTYLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIRqiveGLAHIHG 579
Cdd:cd07870   65 ------------------------DIIHTKETLTFVFEYMHTDLAQYMIQHPGGLHPYNVRLFMFQLLR----GLAYIHG 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  580 QGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDqdggFSTDVAgsgvdstgqagTYFYTAPEIEQDWPKIDEKAD 659
Cdd:cd07870  117 QHILHRDLKPQNLLISYLGELKLADFGLARAKSIPSQT----YSSEVV-----------TLWYRPPDVLLGATDYSSALD 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  660 MYSLGVVFFEL--------------------WHPFGTAMERH----VILTNLKLKGELPLK-------W--VNEFPEQAS 706
Cdd:cd07870  182 IWGAGCIFIEMlqgqpafpgvsdvfeqlekiWTVLGVPTEDTwpgvSKLPNYKPEWFLPCKpqqlrvvWkrLSRPPKAED 261
                        330       340
                 ....*....|....*....|....
gi 30694992  707 LLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd07870  262 LASQMLMMFPKDRISAQDALLHPY 285
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
431-728 6.36e-11

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: 64.16  E-value: 6.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRL---KDKEIPVNsrivrEVATLSRLQHQHVVRYYQAWfetgvvdpfaganwgs 507
Cdd:cd14193   12 LGGGRFGQVHKCEEKSSGLKLAAKIIKArsqKEKEEVKN-----EIEVMNQLNHANLIQLYDAF---------------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 ktagssmfsysgavsteipEQDNNLESTYLYIQM-EYCPRTLRqvfESYNHFDKDfAWHLIRQIVEGLAHIHGQGIIHRD 586
Cdd:cd14193   71 -------------------ESRNDIVLVMEYVDGgELFDRIID---ENYNLTELD-TILFIKQICEGIQYMHQMYILHLD 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  587 FTPNNIFFDAR--NDIKIGDFGLAKFLK-LEQLDQDggfstdvagsgvdstgqAGTYFYTAPEIeQDWPKIDEKADMYSL 663
Cdd:cd14193  128 LKPENILCVSReaNQVKIIDFGLARRYKpREKLRVN-----------------FGTPEFLAPEV-VNYEFVSFPTDMWSL 189
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30694992  664 GVVFFEL---WHPFGTAMERHVILTNLKLKGELPLKWVNEFPEQAS-LLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14193  190 GVIAYMLlsgLSPFLGEDDNETLNNILACQWDFEDEEFADISEEAKdFISKLLIKEKSWRMSASEALKH 258
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
424-670 6.97e-11

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 65.79  E-value: 6.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKkirlkdkeipvnsrivrevaTLSRLQHqhVVRYYQAWF-ETGVVDPFAG 502
Cdd:cd05621   53 DYDVVKVIGRGAFGEVQLVRHKASQKVYAMK--------------------LLSKFEM--IKRSDSAFFwEERDIMAFAN 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 ANWgsktagssmfsysgAVSTEIPEQDNNlestYLYIQMEYCPR-TLRQVFESYNHFDKdFAWHLIRQIVEGLAHIHGQG 581
Cdd:cd05621  111 SPW--------------VVQLFCAFQDDK----YLYMVMEYMPGgDLVNLMSNYDVPEK-WAKFYTAEVVLALDAIHSMG 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGLAKflkleQLDQDGGFSTDVAgsgvdstgqAGTYFYTAPEIEQDWPK---IDEKA 658
Cdd:cd05621  172 LIHRDVKPDNMLLDKYGHLKLADFGTCM-----KMDETGMVHCDTA---------VGTPDYISPEVLKSQGGdgyYGREC 237
                        250
                 ....*....|..
gi 30694992  659 DMYSLGVVFFEL 670
Cdd:cd05621  238 DWWSVGVFLFEM 249
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
420-725 7.10e-11

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


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 64.89  E-value: 7.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  420 RYLNDFEElKPLGQGGFGHVVLCKNKLDGRQYAVKKIrlkDKEIPVNSRivREVATLSRLQ-HQHVVRYYQAWfetgvvd 498
Cdd:cd14180    4 CYELDLEE-PALGEGSFSVCRKCRHRQSGQEYAVKII---SRRMEANTQ--REVAALRLCQsHPNIVALHEVL------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  499 pfaganwgsktagssmfsysgavsteipeqdNNLESTYLYIQM----EYCPRTLRQvfesyNHFDKDFAWHLIRQIVEGL 574
Cdd:cd14180   71 -------------------------------HDQYHTYLVMELlrggELLDRIKKK-----ARFSESEASQLMRSLVSAV 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  575 AHIHGQGIIHRDFTPNNIFFDARND---IKIGDFGLAKFLKleqldqdggfstdvAGSGVDSTgQAGTYFYTAPEIEQDw 651
Cdd:cd14180  115 SFMHEAGVVHRDLKPENILYADESDgavLKVIDFGFARLRP--------------QGSRPLQT-PCFTLQYAAPELFSN- 178
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  652 PKIDEKADMYSLGVVFFELWH---PF------GTAMERHVILTNLKlKGELPLK---WVNEFPEQASLLRRLMSPSPSDR 719
Cdd:cd14180  179 QGYDESCDLWSLGVILYTMLSgqvPFqskrgkMFHNHAADIMHKIK-EGDFSLEgeaWKGVSEEAKDLVRGLLTVDPAKR 257

                 ....*.
gi 30694992  720 PSATEL 725
Cdd:cd14180  258 LKLSEL 263
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
414-730 7.14e-11

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: 64.36  E-value: 7.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  414 ASLPSSRYLN-DFEelkpLGQGGFGHVVlckNKLDGRQYA-VKKIRLKDKEI--PVNSRIVREVATLSRLQHQHVVRYYQ 489
Cdd:cd14031    4 ATSPGGRFLKfDIE----LGRGAFKTVY---KGLDTETWVeVAWCELQDRKLtkAEQQRFKEEAEMLKGLQHPNIVRFYD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  490 AWfetgvvdpfaganwgsktagSSMFSYSGAVSTEIPEQDNNLESTYLYIQMEYCPRTLRqvfesynhfdkdfAWhlIRQ 569
Cdd:cd14031   77 SW--------------------ESVLKGKKCIVLVTELMTSGTLKTYLKRFKVMKPKVLR-------------SW--CRQ 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  570 IVEGLAHIHGQG--IIHRDFTPNNIFFDA-RNDIKIGDFGLAKFLKleqldqdggfsTDVAGSGVdstgqaGTYFYTAPE 646
Cdd:cd14031  122 ILKGLQFLHTRTppIIHRDLKCDNIFITGpTGSVKIGDLGLATLMR-----------TSFAKSVI------GTPEFMAPE 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  647 IEQDwpKIDEKADMYSLGVVFFELW---HPFGTAMERHVILTNLKlKGELPLKWvNEF--PEQASLLRRLMSPSPSDRPS 721
Cdd:cd14031  185 MYEE--HYDESVDVYAFGMCMLEMAtseYPYSECQNAAQIYRKVT-SGIKPASF-NKVtdPEVKEIIEGCIRQNKSERLS 260

                 ....*....
gi 30694992  722 ATELLKHAF 730
Cdd:cd14031  261 IKDLLNHAF 269
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
568-670 7.71e-11

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: 64.27  E-value: 7.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  568 RQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAkflkleqldqdggfSTDVAGSGVDSTGQ-AGTYFYTAPE 646
Cdd:cd14150  103 RQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLA--------------TVKTRWSGSQQVEQpSGSILWMAPE 168
                         90       100
                 ....*....|....*....|....*.
gi 30694992  647 I--EQDWPKIDEKADMYSLGVVFFEL 670
Cdd:cd14150  169 VirMQDTNPYSFQSDVYAYGVVLYEL 194
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
423-740 9.19e-11

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


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 64.61  E-value: 9.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKD-KEIPVNSRIVREVATLSRLQHQHVVRYYQAwFETgvvdpfa 501
Cdd:cd05632    2 NTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRiKKRKGESMALNEKQILEKVNSQFVVNLAYA-YET------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 ganwgsKTAGSSMFSYSGAVSTEipeqdnnlestylyiqmeycprtlrqvFESYNH----FDKDFAWHLIRQIVEGLAHI 577
Cdd:cd05632   74 ------KDALCLVLTIMNGGDLK---------------------------FHIYNMgnpgFEEERALFYAAEILCGLEDL 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  578 HGQGIIHRDFTPNNIFFDARNDIKIGDFGLAkfLKLEQldqdggfstdvagsGVDSTGQAGTYFYTAPEIEQDwPKIDEK 657
Cdd:cd05632  121 HRENTVYRDLKPENILLDDYGHIRISDLGLA--VKIPE--------------GESIRGRVGTVGYMAPEVLNN-QRYTLS 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  658 ADMYSLGVVFFELWH---PFGTAMERHVILTNLKLKGELPLKWVNEFPEQA-SLLRRLMSPSPSDR-----PSATELLKH 728
Cdd:cd05632  184 PDYWGLGCLIYEMIEgqsPFRGRKEKVKREEVDRRVLETEEVYSAKFSEEAkSICKMLLTKDPKQRlgcqeEGAGEVKRH 263
                        330
                 ....*....|....*..
gi 30694992  729 AFP-----PRMESELLD 740
Cdd:cd05632  264 PFFrnmnfKRLEAGMLD 280
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
425-730 1.17e-10

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: 63.41  E-value: 1.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKeiPVNSRIVREVATLSRLQHQHVVRYYqawfetgvvdpfagan 504
Cdd:cd06647    9 YTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQ--PKKELIINEILVMRENKNPNIVNYL---------------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysgavsteipeqDNNLESTYLYIQMEYCPR-TLRQVFESYNHFDKDFAwHLIRQIVEGLAHIHGQGII 583
Cdd:cd06647   71 ------------------------DSYLVGDELWVVMEYLAGgSLTDVVTETCMDEGQIA-AVCRECLQALEFLHSNQVI 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  584 HRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQdggfstdvagsgvdsTGQAGTYFYTAPEI---EQDWPKIdekaDM 660
Cdd:cd06647  126 HRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR---------------STMVGTPYWMAPEVvtrKAYGPKV----DI 186
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30694992  661 YSLGVVFFELWH---PF---GTAMERHVILTNLKLKGELPLKWVNEFPEqasLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd06647  187 WSLGIMAIEMVEgepPYlneNPLRALYLIATNGTPELQNPEKLSAIFRD---FLNRCLEMDVEKRGSAKELLQHPF 259
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
568-669 1.18e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 65.30  E-value: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   568 RQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqdGGFSTDVagsgvdSTGQAGTYFYTAPEI 647
Cdd:PHA03211  267 RQLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFGAACFAR-------GSWSTPF------HYGIAGTVDTNAPEV 333
                          90       100
                  ....*....|....*....|..
gi 30694992   648 EQDWPkIDEKADMYSLGVVFFE 669
Cdd:PHA03211  334 LAGDP-YTPSVDIWSAGLVIFE 354
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
530-728 1.27e-10

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 63.89  E-value: 1.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  530 NNLESTYLYIQM----EYCPRTLRQVFesYNHFDKDFAWHLIRQIVEglaHIHGQGIIHRDFTPNNIFF-DARND---IK 601
Cdd:cd14175   65 DDGKHVYLVTELmrggELLDKILRQKF--FSEREASSVLHTICKTVE---YLHSQGVVHRDLKPSNILYvDESGNpesLR 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  602 IGDFGLAKflkleQLDQDGGFSTDvagsgvdstgQAGTYFYTAPEI--EQDWpkiDEKADMYSLGVVFFEL---WHPFGT 676
Cdd:cd14175  140 ICDFGFAK-----QLRAENGLLMT----------PCYTANFVAPEVlkRQGY---DEGCDIWSLGILLYTMlagYTPFAN 201
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 30694992  677 AMER--HVILTNLKlKGELPLK---WVNEFPEQASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14175  202 GPSDtpEEILTRIG-SGKFTLSggnWNTVSDAAKDLVSKMLHVDPHQRLTAKQVLQH 257
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
422-674 1.52e-10

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: 64.31  E-value: 1.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKeipvnsrIVREVATLSRLQHQHVVRYYQAWfetgVVDPFa 501
Cdd:cd05627    1 LDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADM-------LEKEQVAHIRAERDILVEADGAW----VVKMF- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 ganwgsktagssmFSYsgavsteipeQDNNlestYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQ 580
Cdd:cd05627   69 -------------YSF----------QDKR----NLYLIMEFLPGgDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQL 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQ-----DGGFSTDVAGSGVDSTGQA---------------GTY 640
Cdd:cd05627  122 GFIHRDIKPDNLLLDAKGHVKLSDFGLCTGLKKAHRTEfyrnlTHNPPSDFSFQNMNSKRKAetwkknrrqlaystvGTP 201
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 30694992  641 FYTAPEI--EQDWPKIdekADMYSLGVVFFEL---WHPF 674
Cdd:cd05627  202 DYIAPEVfmQTGYNKL---CDWWSLGVIMYEMligYPPF 237
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
422-730 1.55e-10

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: 64.31  E-value: 1.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVK-----KIRLKDKE-IPVNSRIVREVATLSRLQHQHVVRYYqawFETG 495
Cdd:cd05633    4 MNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldkkRIKMKQGEtLALNERIMLSLVSTGDCPFIVCMTYA---FHTP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  496 -----VVDPFAGANWGSKTAGSSMFSysgavsteipEQDNNLESTylyiqmeycprtlrqvfesynhfdkdfawhlirQI 570
Cdd:cd05633   81 dklcfILDLMNGGDLHYHLSQHGVFS----------EKEMRFYAT---------------------------------EI 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  571 VEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAkflkleqldqdGGFSTDVAGSGVdstgqaGTYFYTAPEIEQD 650
Cdd:cd05633  118 ILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLA-----------CDFSKKKPHASV------GTHGYMAPEVLQK 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  651 WPKIDEKADMYSLGVVFFELWH---PF---GTAMERHVILTNLKLKGELPLKWVnefPEQASLLRRLMSPSPSDR----- 719
Cdd:cd05633  181 GTAYDSSADWFSLGCMLFKLLRghsPFrqhKTKDKHEIDRMTLTVNVELPDSFS---PELKSLLEGLLQRDVSKRlgchg 257
                        330
                 ....*....|.
gi 30694992  720 PSATELLKHAF 730
Cdd:cd05633  258 RGAQEVKEHSF 268
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
537-730 1.60e-10

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: 63.11  E-value: 1.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  537 LYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARND---------IKIGDFG 606
Cdd:cd14202   76 VYLVMEYCNGgDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGGrksnpnnirIKIADFG 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  607 LAKFLkleqldQDGGFSTDVAGSGVdstgqagtyfYTAPEI--EQDWpkiDEKADMYSLGVVFFELW---HPFGTAMERH 681
Cdd:cd14202  156 FARYL------QNNMMAATLCGSPM----------YMAPEVimSQHY---DAKADLWSIGTIIYQCLtgkAPFQASSPQD 216
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 30694992  682 VILTNLKLKGELPlkwvnEFPEQAS-----LLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14202  217 LRLFYEKNKSLSP-----NIPRETSshlrqLLLGLLQRNQKDRMDFDEFFHHPF 265
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
425-728 1.63e-10

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


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 63.28  E-value: 1.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYA---VKKIRLKDKEIPVN-SRIVREVATLSRLQHQHVVRYYQAwFE--TGVVD 498
Cdd:cd14105    7 YDIGEELGSGQFAVVKKCREKSTGLEYAakfIKKRRSKASRRGVSrEDIEREVSILRQVLHPNIITLHDV-FEnkTDVVL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  499 PFaganwgSKTAGSSMFSYsgavsteIPEQDNNLEstylyiqmeycprtlrqvfesynhfdkDFAWHLIRQIVEGLAHIH 578
Cdd:cd14105   86 IL------ELVAGGELFDF-------LAEKESLSE---------------------------EEATEFLKQILDGVNYLH 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  579 GQGIIHRDFTPNNIFFDARN----DIKIGDFGLAKflKLEqldqdggfstdvagSGVDSTGQAGTYFYTAPEIEQDWPkI 654
Cdd:cd14105  126 TKNIAHFDLKPENIMLLDKNvpipRIKLIDFGLAH--KIE--------------DGNEFKNIFGTPEFVAPEIVNYEP-L 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  655 DEKADMYSLGVVFFELW---HPFgTAMERHVILTNLKlkgELPLKWVNEFPEQASLL-----RRLMSPSPSDRPSATELL 726
Cdd:cd14105  189 GLEADMWSIGVITYILLsgaSPF-LGDTKQETLANIT---AVNYDFDDEYFSNTSELakdfiRQLLVKDPRKRMTIQESL 264

                 ..
gi 30694992  727 KH 728
Cdd:cd14105  265 RH 266
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
558-728 1.75e-10

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: 63.05  E-value: 1.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  558 FDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARN-DIKIGDFGLAKFLKleqldqdggfstDVAGSGVDstgq 636
Cdd:cd14102  102 LDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLRTgELKLIDFGSGALLK------------DTVYTDFD---- 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  637 aGTYFYTAPEieqdWPKID----EKADMYSLGVVFFELWH---PFgtAMERHVILTNLKLKGELPlkwvnefPEQASLLR 709
Cdd:cd14102  166 -GTRVYSPPE----WIRYHryhgRSATVWSLGVLLYDMVCgdiPF--EQDEEILRGRLYFRRRVS-------PECQQLIK 231
                        170
                 ....*....|....*....
gi 30694992  710 RLMSPSPSDRPSATELLKH 728
Cdd:cd14102  232 WCLSLRPSDRPTLEQIFDH 250
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
429-730 1.90e-10

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


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 63.88  E-value: 1.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKLDGRQYAVK----KIRLKDKEIpvnSRIVREVATL-SRLQHQHVVRYYQAwFETG-----VVD 498
Cdd:cd05575    1 KVIGKGSFGKVLLARHKAEGKLYAVKvlqkKAILKRNEV---KHIMAERNVLlKNVKHPFLVGLHYS-FQTKdklyfVLD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  499 PFAGanwgsktaGSSMFsysgavsteipeqdnnlestylYIQMEYCPRTLRQVFESynhfdkdfawhliRQIVEGLAHIH 578
Cdd:cd05575   77 YVNG--------GELFF----------------------HLQRERHFPEPRARFYA-------------AEIASALGYLH 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  579 GQGIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleqldqdggfsTDVAGSGVDSTGqAGTYFYTAPEIEQDWPkIDEKA 658
Cdd:cd05575  114 SLNIIYRDLKPENILLDSQGHVVLTDFGLCK--------------EGIEPSDTTSTF-CGTPEYLAPEVLRKQP-YDRTV 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  659 DMYSLGVVFFELWH---PF---GTA-MERHVILTNLKLKGELPlkwvnefPEQASLLRRLMSPSPSDRPSA----TELLK 727
Cdd:cd05575  178 DWWCLGAVLYEMLYglpPFysrDTAeMYDNILHKPLRLRTNVS-------PSARDLLEGLLQKDRTKRLGSgndfLEIKN 250

                 ...
gi 30694992  728 HAF 730
Cdd:cd05575  251 HSF 253
tRNA-synt_His pfam13393
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ...
889-1116 1.94e-10

Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP phosphoribosyltransferase regulatory subunits.


Pssm-ID: 433170 [Multi-domain]  Cd Length: 309  Bit Score: 63.37  E-value: 1.94e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992    889 LQADFDIVGGTLSLTEAEVLKVIVDITTHIfhrGSCDIH--LNHGDLLDAIWSWAGIKAEHRRKVAELLsmmgslrpqss 966
Cdd:pfam13393  112 LQVGAELIGHAGIEADAEIISLLLEALAAA---GVPGVTldLGHVGLVRALLEAAGLSEALEEALRAAL----------- 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992    967 ERKlKWVFIRrQLLQELKLPEAVVNRLQTVASrFCGDADqALPRLRGALRADRPTRKALDELSNLLTYLRVWRIEEHVHI 1046
Cdd:pfam13393  178 QRK-DAAELA-ELAAEAGLPPALRRALLALPD-LYGGPE-VLDEARAALPGLPALQEALDELEALAALLEALGDGVRLTF 253
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30694992   1047 DvlmpPTE----SYHRNLFFQVFltkenssgTSNDGVLLAVGGRYDWLVQEVcdrehKMNLPgAVGVSLALETI 1116
Cdd:pfam13393  254 D----LAElrgyEYYTGIVFAAY--------APGVGEPLARGGRYDDLGAAF-----GRARP-ATGFSLDLEAL 309
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
423-734 1.95e-10

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: 63.56  E-value: 1.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKE-IPVNSriVREVATLSRLQHQHVVRYYqawfetgvvdpfa 501
Cdd:cd07869    5 DSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEgTPFTA--IREASLLKGLKHANIVLLH------------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 ganwgsktagssmfsysgavstEIPEQDNNLESTYLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIRqiveGLAHIHGQG 581
Cdd:cd07869   70 ----------------------DIIHTKETLTLVFEYVHTDLCQYMDKHPGGLHPENVKLFLFQLLR----GLSYIHQRY 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQldqdGGFSTDVAgsgvdstgqagTYFYTAPEIEQDWPKIDEKADMY 661
Cdd:cd07869  124 ILHRDLKPQNLLISDTGELKLADFGLARAKSVPS----HTYSNEVV-----------TLWYRPPDVLLGSTEYSTCLDMW 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  662 SLGVVFFEL--------------------WHPFGTAM---------------ERHVILTNLKLKGEL-PLKWVNEFPEQA 705
Cdd:cd07869  189 GVGCIFVEMiqgvaafpgmkdiqdqleriFLVLGTPNedtwpgvhslphfkpERFTLYSPKNLRQAWnKLSYVNHAEDLA 268
                        330       340       350
                 ....*....|....*....|....*....|...
gi 30694992  706 SllrRLMSPSPSDRPSATELLKHAF----PPRM 734
Cdd:cd07869  269 S---KLLQCFPKNRLSAQAALSHEYfsdlPPRL 298
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
566-731 1.97e-10

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: 63.13  E-value: 1.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  566 LIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAkflkleqldqdggfSTDVAGSGVDSTGQ-AGTYFYTA 644
Cdd:cd14149  113 IARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLA--------------TVKSRWSGSQQVEQpTGSILWMA 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  645 PEI--EQDWPKIDEKADMYSLGVVFFELWH---PFGTAMERHVILTNLKLKGELP--LKWVNEFPE-QASLLRRLMSPSP 716
Cdd:cd14149  179 PEVirMQDNNPFSFQSDVYSYGIVLYELMTgelPYSHINNRDQIIFMVGRGYASPdlSKLYKNCPKaMKRLVADCIKKVK 258
                        170       180
                 ....*....|....*....|.
gi 30694992  717 SDRP------SATELLKHAFP 731
Cdd:cd14149  259 EERPlfpqilSSIELLQHSLP 279
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
425-730 2.16e-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: 63.14  E-value: 2.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKI---RLKDKEipVNSRIVREVATLSRLQHQHVVRYYQAwFETgvvdpfa 501
Cdd:cd05605    2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLekkRIKKRK--GEAMALNEKQILEKVNSRFVVSLAYA-YET------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 ganwgsKTAGSsmfsysgAVSTEIPEQDnnlestylyiqmeycprtLRqvFESYN----HFDKDFAWHLIRQIVEGLAHI 577
Cdd:cd05605   72 ------KDALC-------LVLTIMNGGD------------------LK--FHIYNmgnpGFEEERAVFYAAEITCGLEHL 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  578 HGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQdggfstdvagsgvdstGQAGTYFYTAPEIeqdwpkIDEK 657
Cdd:cd05605  119 HSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPEGETIR----------------GRVGTVGYMAPEV------VKNE 176
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  658 -----ADMYSLGVVFFELWH---PFGT--------AMERHVIltnlklkgELPLKWVNEFPEQA-SLLRRLMSPSPSDR- 719
Cdd:cd05605  177 rytfsPDWWGLGCLIYEMIEgqaPFRArkekvkreEVDRRVK--------EDQEEYSEKFSEEAkSICSQLLQKDPKTRl 248
                        330
                 ....*....|....*
gi 30694992  720 ----PSATELLKHAF 730
Cdd:cd05605  249 gcrgEGAEDVKSHPF 263
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
425-740 2.41e-10

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


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 63.00  E-value: 2.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIrlkDKEipvnsrivrevatlsRLQhqhvvryyqawfetgvvdpfagan 504
Cdd:cd05607    4 FYEFRVLGKGGFGEVCAVQVKNTGQMYACKKL---DKK---------------RLK------------------------ 41
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsKTAGSSMfsysGAVSTEIPEQDNNLestylYIQmeycprTLRQVFESYNHF--------DKDFAWHLIR-------- 568
Cdd:cd05607   42 ---KKSGEKM----ALLEKEILEKVNSP-----FIV------SLAYAFETKTHLclvmslmnGGDLKYHIYNvgergiem 103
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  569 --------QIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqdggfstdvagSGVDSTGQAGTY 640
Cdd:cd05607  104 ervifysaQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVK----------------EGKPITQRAGTN 167
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  641 FYTAPEIEQDWPkIDEKADMYSLGVVFFELWH---PFGTAMERhVILTNLK---LKGELPLKWVNEFPEQASLLR----- 709
Cdd:cd05607  168 GYMAPEILKEES-YSYPVDWFAMGCSIYEMVAgrtPFRDHKEK-VSKEELKrrtLEDEVKFEHQNFTEEAKDICRlflak 245
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 30694992  710 ----RLMSPSPSDRPSATELLKHAFPPRMESELLD 740
Cdd:cd05607  246 kpenRLGSRTNDDDPRKHEFFKSINFPRLEAGLID 280
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
420-730 2.99e-10

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: 62.75  E-value: 2.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  420 RYLNDFEELkplGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEipVNSRIVREVATLSRLQHQHVVRYYQAWfetgvvdp 499
Cdd:cd06658   22 EYLDSFIKI---GEGSTGIVCIATEKHTGKQVAVKKMDLRKQQ--RRELLFNEVVIMRDYHHENVVDMYNSY-------- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  500 faganwgsktagssmfsysgavsteipeqdnnLESTYLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHG 579
Cdd:cd06658   89 --------------------------------LVGDELWVVMEFLEGGALTDIVTHTRMNEEQIATVCLSVLRALSYLHN 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  580 QGIIHRDFTPNNIFFDARNDIKIGDFglakflkleqldqdgGFSTDVAGSGVDSTGQAGTYFYTAPEIEQDWPKIDEkAD 659
Cdd:cd06658  137 QGVIHRDIKSDSILLTSDGRIKLSDF---------------GFCAQVSKEVPKRKSLVGTPYWMAPEVISRLPYGTE-VD 200
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30694992  660 MYSLGVVFFELWHPFGTAMERHVILTNLKLKGELPLKwVNEFPEQASLLRR----LMSPSPSDRPSATELLKHAF 730
Cdd:cd06658  201 IWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDNLPPR-VKDSHKVSSVLRGfldlMLVREPSQRATAQELLQHPF 274
hisZ PRK12292
ATP phosphoribosyltransferase regulatory subunit; Provisional
977-1185 3.13e-10

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 237043 [Multi-domain]  Cd Length: 391  Bit Score: 63.73  E-value: 3.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   977 RQLLQELKLPEAVVNRLQT-------VA-SRFCGDAD-------QALPRLRG---------ALRADRPTRKALDELSNLL 1032
Cdd:PRK12292  167 RALLEAAGLSEELEEVLRRalankdyVAlEELVLDLSeelrdalLALPRLRGgrevleearKLLPSLPIKRALDELEALA 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  1033 TYLRVWRIEEHVHIDVLMPPTESYHRNLFFQVFltkenssgTSNDGVLLAVGGRYDWLVqEVCDRehkmNLPgAVGVSLA 1112
Cdd:PRK12292  247 EALEKYGYGIPLSLDLGLLRHLDYYTGIVFEGY--------VDGVGNPIASGGRYDDLL-GRFGR----ARP-ATGFSLD 312
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30694992  1113 LETIfqhlpMDLRPIRNEVSTSVLVCSRGGGGlLVQRMELVAELWEKSIKAEFVPTPDpSLTEQYEYANEHEI 1185
Cdd:PRK12292  313 LDRL-----LELQLELPVEARKDLVIAPDSEA-LAAALAAAQELRKKGEIVVLALPGR-NFEDAREYARDRQI 378
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
431-670 3.24e-10

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: 62.12  E-value: 3.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEipvnSRIVREVATLSRLQHQHVVRYyqawfeTGVVdpfaganwgskta 510
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVMVMKELKRFDEQ----RSFLKEVKLMRRLSHPNILRF------IGVC------------- 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  511 gssmfsysgavsteipEQDNNLESTYLYIQmeycPRTLRQVFESYnhfDKDFAW----HLIRQIVEGLAHIHGQGIIHRD 586
Cdd:cd14065   58 ----------------VKDNKLNFITEYVN----GGTLEELLKSM---DEQLPWsqrvSLAKDIASGMAYLHSKNIIHRD 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  587 FTPNNIFFDARNDIK---IGDFGLAKFL-KLEQLDQDGGFSTDVAGSGvdstgqagtyFYTAPEIEQDWPkIDEKADMYS 662
Cdd:cd14065  115 LNSKNCLVREANRGRnavVADFGLAREMpDEKTKKPDRKKRLTVVGSP----------YWMAPEMLRGES-YDEKVDVFS 183

                 ....*...
gi 30694992  663 LGVVFFEL 670
Cdd:cd14065  184 FGIVLCEI 191
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
422-730 3.38e-10

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: 62.33  E-value: 3.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEELKP--LGQGGFGHVVLCKN-KLDGRQYAVKKIRLKDKEipvNSRIV--REVATLSRLQHQHVVRYYqawfetgv 496
Cdd:cd14201    3 VGDFEYSRKdlVGHGAFAVVFKGRHrKKTDWEVAIKSINKKNLS---KSQILlgKEIKILKELQHENIVALY-------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  497 vdpfaganwgsktagssmfsysgavstEIPEQDNNLestylYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLA 575
Cdd:cd14201   72 ---------------------------DVQEMPNSV-----FLVMEYCNGgDLADYLQAKGTLSEDTIRVFLQQIAAAMR 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  576 HIHGQGIIHRDFTPNNIFFDARN---------DIKIGDFGLAKFLKleqldqdggfstdvagSGVDSTGQAGTYFYTAPE 646
Cdd:cd14201  120 ILHSKGIIHRDLKPQNILLSYASrkkssvsgiRIKIADFGFARYLQ----------------SNMMAATLCGSPMYMAPE 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  647 I--EQDWpkiDEKADMYSLGVVFFELW---HPFGTAMERHVILTNLKLKGELPLKWVNEFPEQASLLRRLMSPSPSDRPS 721
Cdd:cd14201  184 VimSQHY---DAKADLWSIGTVIYQCLvgkPPFQANSPQDLRMFYEKNKNLQPSIPRETSPYLADLLLGLLQRNQKDRMD 260

                 ....*....
gi 30694992  722 ATELLKHAF 730
Cdd:cd14201  261 FEAFFSHPF 269
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
431-740 3.54e-10

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


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 63.00  E-value: 3.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIR----LKDKEIPVnSRIVREVATLSRlQHQHVVRYYQAwFETgvvdpfaganwg 506
Cdd:cd05590    3 LGKGSFGKVMLARLKESGRLYAVKVLKkdviLQDDDVEC-TMTEKRILSLAR-NHPFLTQLYCC-FQT------------ 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  507 sktagssmfsysgavsteiPEQdnnlestyLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHR 585
Cdd:cd05590   68 -------------------PDR--------LFFVMEFVNGgDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYR 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  586 DFTPNNIFFDARNDIKIGDFGLAKflkleqldqDGGFstdvagSGVDSTGQAGTYFYTAPEIEQDW---PKIdekaDMYS 662
Cdd:cd05590  121 DLKLDNVLLDHEGHCKLADFGMCK---------EGIF------NGKTTSTFCGTPDYIAPEILQEMlygPSV----DWWA 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  663 LGVVFFELW---HPFGTAMERHVILTNLKLKGELPlKWVNEfpEQASLLRRLMSPSPSDRPSATEL------LKHAFPPR 733
Cdd:cd05590  182 MGVLLYEMLcghAPFEAENEDDLFEAILNDEVVYP-TWLSQ--DAVDILKAFMTKNPTMRLGSLTLggeeaiLRHPFFKE 258

                 ....*..
gi 30694992  734 MESELLD 740
Cdd:cd05590  259 LDWEKLN 265
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
565-780 3.60e-10

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 64.34  E-value: 3.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   565 HLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKigdFGLAKFLKLEQLDQDGGFSTDVAGSG-------------- 630
Cdd:PLN00181   84 HVFRQIVEIVNAAHSQGIVVHNVRPSCFVMSSFNHVS---FIESASCSDSGSDEDATTKSREIGSSrreeilserriekl 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   631 ---------VDSTGQAGTYFYTAPEiEQDWPKIDEKADMYSLGVVFFELWHPFGTAMERHVILTNLK---LKGELPLKWv 698
Cdd:PLN00181  161 eevkkqpfpMKQILAMEMSWYTSPE-EDNGSSSNCASDVYRLGVLLFELFCPVSSREEKSRTMSSLRhrvLPPQILLNW- 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   699 nefPEQASLLRRLMSPSPSDRPSATELLKHAF--PPR----------------MESELLDNILRIMQTSEDSSVY----- 755
Cdd:PLN00181  239 ---PKEASFCLWLLHPEPSCRPSMSELLQSEFinEPRenleereaamelrdriEEQELLLEFLFLIQQRKQEAADklqdt 315
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 30694992   756 --------DRVV--SVIFDEEVLEMKSHQSSRSRL 780
Cdd:PLN00181  316 isllssdiDQVVkrQLVLQQKGSDVRSFLASRKRI 350
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
422-727 3.91e-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: 61.98  E-value: 3.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEELKPLGQGGFGHVVLCKNKldGRQYAVKKirLKDKEIPVNSrIVREVATLSRLQHQHVVRYyqawfeTGVVdpfa 501
Cdd:cd05039    5 KKDLKLGELIGKGEFGDVMLGDYR--GQKVAVKC--LKDDSTAAQA-FLAEASVMTTLRHPNLVQL------LGVV---- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 ganwgsktagssmfsysgavsteipeqdnnLESTYLYIQMEYCPRT-----LRQVFESYNHFD--KDFAwhliRQIVEGL 574
Cdd:cd05039   70 ------------------------------LEGNGLYIVTEYMAKGslvdyLRSRGRAVITRKdqLGFA----LDVCEGM 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  575 AHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFlklEQLDQDGG-FSTDvagsgvdstgqagtyfYTAPEIEQDwPK 653
Cdd:cd05039  116 EYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKE---ASSNQDGGkLPIK----------------WTAPEALRE-KK 175
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  654 IDEKADMYSLGVVFFELWhPFGTA---------MERHVIltnlklKG---ELPLKWVnefPEQASLLRRLMSPSPSDRPS 721
Cdd:cd05039  176 FSTKSDVWSFGILLWEIY-SFGRVpypriplkdVVPHVE------KGyrmEAPEGCP---PEVYKVMKNCWELDPAKRPT 245

                 ....*.
gi 30694992  722 ATELLK 727
Cdd:cd05039  246 FKQLRE 251
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
420-670 4.82e-10

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: 61.87  E-value: 4.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  420 RYLndfEELKPLGQGGFGHVVLCKNKLDG----RQYAVKKIRLKDKEIPVNSrIVREVATLSRLQHQHVVRYYQAWFETG 495
Cdd:cd05079    4 RFL---KRIRDLGEGHFGKVELCRYDPEGdntgEQVAVKSLKPESGGNHIAD-LKKEIEILRNLYHENIVKYKGICTEDG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  496 vvdpfaganwGSKTAGSSMFSYSGAVSTEIPEQDNNLEstyLYIQMEYCPrtlrqvfesynhfdkdfawhlirQIVEGLA 575
Cdd:cd05079   80 ----------GNGIKLIMEFLPSGSLKEYLPRNKNKIN---LKQQLKYAV-----------------------QICKGMD 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  576 HIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldQDGGFSTdvAGSGVDStgqagTYFYTAPEIEQDwPKID 655
Cdd:cd05079  124 YLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIE-----TDKEYYT--VKDDLDS-----PVFWYAPECLIQ-SKFY 190
                        250
                 ....*....|....*
gi 30694992  656 EKADMYSLGVVFFEL 670
Cdd:cd05079  191 IASDVWSFGVTLYEL 205
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
429-612 5.52e-10

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: 61.59  E-value: 5.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHV---VLCKNKLDGRQYAVK---KIRLKDKEIPvnSRIVREVATLSRLQHQHVVRYYqawfetGVVdpfag 502
Cdd:cd05040    1 EKLGDGSFGVVrrgEWTTPSGKVIQVAVKclkSDVLSQPNAM--DDFLKEVNAMHSLDHPNLIRLY------GVV----- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgsktagssmFSYSGAVSTEIPEQDNNLEstylyiqmeycprTLRqvfESYNHFDKDFAWHLIRQIVEGLAHIHGQGI 582
Cdd:cd05040   68 ------------LSSPLMMVTELAPLGSLLD-------------RLR---KDQGHFLISTLCDYAVQIANGMAYLESKRF 119
                        170       180       190
                 ....*....|....*....|....*....|
gi 30694992  583 IHRDFTPNNIFFDARNDIKIGDFGLAKFLK 612
Cdd:cd05040  120 IHRDLAARNILLASKDKVKIGDFGLMRALP 149
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
424-742 5.71e-10

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 62.07  E-value: 5.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEiPVNSRIVREVATLSRLQHQHVVRYYQAWFETGvvdpfaga 503
Cdd:cd06615    2 DFEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHLEIKP-AIRNQIIRELKVLHECNSPYIVGFYGAFYSDG-------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssmfsysgavstEIPeqdnnlestylyIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQ-G 581
Cdd:cd06615   73 --------------------EIS------------ICMEHMDGgSLDQVLKKAGRIPENILGKISIAVLRGLTYLREKhK 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGlakflkleqldqdggfstdVAGSGVDSTGQA--GTYFYTAPEIEQDwPKIDEKAD 659
Cdd:cd06615  121 IMHRDVKPSNILVNSRGEIKLCDFG-------------------VSGQLIDSMANSfvGTRSYMSPERLQG-THYTVQSD 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  660 MYSLGVVFFELwhpfgtAMERHVILTNLKlKGELPLKWVNEFPEQASLLRRLMSPSPSDRPsatellkhafPPRMESELL 739
Cdd:cd06615  181 IWSLGLSLVEM------AIGRYPIPPPDA-KELEAMFGRPVSEGEAKESHRPVSGHPPDSP----------RPMAIFELL 243

                 ...
gi 30694992  740 DNI 742
Cdd:cd06615  244 DYI 246
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
424-674 6.06e-10

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: 62.75  E-value: 6.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKkirlkdkeipvnsrIVREVATLSRLQHQHVVRYYQAWFEtgvvdpfAGA 503
Cdd:cd05628    2 DFESLKVIGRGAFGEVRLVQKKDTGHVYAMK--------------ILRKADMLEKEQVGHIRAERDILVE-------ADS 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 NWGSKTagssMFSYSGAVSteipeqdnnlestyLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGI 582
Cdd:cd05628   61 LWVVKM----FYSFQDKLN--------------LYLIMEFLPGgDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGF 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  583 IHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQ-----DGGFSTDVAGSGVDSTGQA---------------GTYFY 642
Cdd:cd05628  123 IHRDIKPDNLLLDSKGHVKLSDFGLCTGLKKAHRTEfyrnlNHSLPSDFTFQNMNSKRKAetwkrnrrqlafstvGTPDY 202
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 30694992  643 TAPEI--EQDWPKIdekADMYSLGVVFFEL---WHPF 674
Cdd:cd05628  203 IAPEVfmQTGYNKL---CDWWSLGVIMYEMligYPPF 236
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
566-670 6.25e-10

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: 61.62  E-value: 6.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  566 LIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAkflkleqldqdggfSTDVAGSGVDSTGQ-AGTYFYTA 644
Cdd:cd14151  109 IARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLA--------------TVKSRWSGSHQFEQlSGSILWMA 174
                         90       100
                 ....*....|....*....|....*...
gi 30694992  645 PEI--EQDWPKIDEKADMYSLGVVFFEL 670
Cdd:cd14151  175 PEVirMQDKNPYSFQSDVYAFGIVLYEL 202
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
531-670 6.37e-10

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 63.13  E-value: 6.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   531 NLESTYLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIR----QIVEGLAHIHGQGIIHRDFTPNNIFFDAR-NDIKIGDF 605
Cdd:PTZ00036  136 NEKNIFLNVVMEFIPQTVHKYMKHYARNNHALPLFLVKlysyQLCRALAYIHSKFICHRDLKPQNLLIDPNtHTLKLCDF 215
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30694992   606 GLAKFLKleqldqdggfstdvagSGVDSTGQAGTYFYTAPEIEQDWPKIDEKADMYSLGVVFFEL 670
Cdd:PTZ00036  216 GSAKNLL----------------AGQRSVSYICSRFYRAPELMLGATNYTTHIDLWSLGCIIAEM 264
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
429-730 6.47e-10

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


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 61.99  E-value: 6.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKLDGRQYAVKKIRlkdKEIPVNSRIVREVATLSR-LQHQHvvryyqawfetgvvDPFAGAnwgs 507
Cdd:cd05571    1 KVLGKGTFGKVILCREKATGELYAIKILK---KEVIIAKDEVAHTLTENRvLQNTR--------------HPFLTS---- 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 ktagssmFSYSGavsteipeQDNNlestYLYIQMEYCPRTlrqvfESYNH------FDKDFAWHLIRQIVEGLAHIHGQG 581
Cdd:cd05571   60 -------LKYSF--------QTND----RLCFVMEYVNGG-----ELFFHlsrervFSEDRTRFYGAEIVLALGYLHSQG 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGLAKflklEQLDqdggfstdvagSGVDSTGQAGTYFYTAPEIEQDwPKIDEKADMY 661
Cdd:cd05571  116 IVYRDLKLENLLLDKDGHIKITDFGLCK----EEIS-----------YGATTKTFCGTPEYLAPEVLED-NDYGRAVDWW 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  662 SLGVVFFELWH---PFGTamERHVILTNLKLKGELplkwvnEFP-----EQASLLRRLMSPSPSDR----PS-ATELLKH 728
Cdd:cd05571  180 GLGVVMYEMMCgrlPFYN--RDHEVLFELILMEEV------RFPstlspEAKSLLAGLLKKDPKKRlgggPRdAKEIMEH 251

                 ..
gi 30694992  729 AF 730
Cdd:cd05571  252 PF 253
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
423-743 8.13e-10

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 61.61  E-value: 8.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEiPVNSRIVREVATLSRLQHQHVVRYYQAWFEtgvvdpfag 502
Cdd:cd06650    5 DDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKP-AIRNQIIRELQVLHECNSPYIVGFYGAFYS--------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgsktagssmfsySGAVSTEIPEQDNNlestylyiqmeycprTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQ-G 581
Cdd:cd06650   75 ---------------DGEISICMEHMDGG---------------SLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKhK 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGlakflkleqldqdggfstdVAGSGVDSTGQA--GTYFYTAPEIEQDwPKIDEKAD 659
Cdd:cd06650  125 IMHRDVKPSNILVNSRGEIKLCDFG-------------------VSGQLIDSMANSfvGTRSYMSPERLQG-THYSVQSD 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  660 MYSLGVVFFELwhpfgtAMERHVILTNLKLKGELPLKWVNEFPEQASLLRrlmsPSPSDRPSATELLKhAFPPRMESELL 739
Cdd:cd06650  185 IWSMGLSLVEM------AVGRYPIPPPDAKELELMFGCQVEGDAAETPPR----PRTPGRPLSSYGMD-SRPPMAIFELL 253

                 ....
gi 30694992  740 DNIL 743
Cdd:cd06650  254 DYIV 257
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
429-730 8.52e-10

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: 61.54  E-value: 8.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNklDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAWFETG---VVDPFaganw 505
Cdd:cd08216    8 KCFKGGGVVHLAKHKP--TNTLVAVKKINLESDSKEDLKFLQQEILTSRQLQHPNILPYVTSFVVDNdlyVVTPL----- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  506 gsktagssmfsysgavsteipeqdnnlestylyiqMEY--CPRTLRqvfesyNHFDKDFAWHLIRQI----VEGLAHIHG 579
Cdd:cd08216   81 -----------------------------------MAYgsCRDLLK------THFPEGLPELAIAFIlrdvLNALEYIHS 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  580 QGIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleQLDQDGGFSTDVAGSGVDSTgqaGTYFYTAPEI-EQDWPKIDEKA 658
Cdd:cd08216  120 KGYIHRSVKASHILISGDGKVVLSGLRYAY-----SMVKHGKRQRVVHDFPKSSE---KNLPWLSPEVlQQNLLGYNEKS 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  659 DMYSLGVVFFELWH---PFgTAMERHVILTNlKLKGELPLKW----------VNEFPEQASLLR------------RLMS 713
Cdd:cd08216  192 DIYSVGITACELANgvvPF-SDMPATQMLLE-KVRGTTPQLLdcstypleedSMSQSEDSSTEHpnnrdtrdipyqRTFS 269
                        330       340
                 ....*....|....*....|....*....
gi 30694992  714 PS------------PSDRPSATELLKHAF 730
Cdd:cd08216  270 EAfhqfvelclqrdPELRPSASQLLAHSF 298
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
422-669 8.81e-10

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: 62.36  E-value: 8.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRlkdKEIPVNSRIVREVAT----LSRLQHQHVVRYYQAWfetgvv 497
Cdd:cd05600   10 LSDFQILTQVGQGGYGSVFLARKKDTGEICALKIMK---KKVLFKLNEVNHVLTerdiLTTTNSPWLVKLLYAF------ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  498 dpfaganwgsktagssmfsysgavsteipeQDNNlestYLYIQMEYCP----RTLRQvfesyNH--FDKDFAWHLIRQIV 571
Cdd:cd05600   81 ------------------------------QDPE----NVYLAMEYVPggdfRTLLN-----NSgiLSEEHARFYIAEMF 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  572 EGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAK----------------------FLKLEQLDQDGGFSTDVAGS 629
Cdd:cd05600  122 AAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASgtlspkkiesmkirleevkntaFLELTAKERRNIYRAMRKED 201
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 30694992  630 GVDSTGQAGTYFYTAPEIEQDwPKIDEKADMYSLGVVFFE 669
Cdd:cd05600  202 QNYANSVVGSPDYMAPEVLRG-EGYDLTVDYWSLGCILFE 240
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
429-730 1.00e-09

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


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 61.46  E-value: 1.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKLDGRQYAVKKIRlKDkeipvnsRIVREVATLSRLQHQHVvryyqawFETGVVDPFAganwgsk 508
Cdd:cd05570    1 KVLGKGSFGKVMLAERKKTDELYAIKVLK-KE-------VIIEDDDVECTMTEKRV-------LALANRHPFL------- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  509 TAGSSMFsysgavsteipeQDnnleSTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDF 587
Cdd:cd05570   59 TGLHACF------------QT----EDRLYFVMEYVNGgDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDL 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  588 TPNNIFFDARNDIKIGDFGLAKflkleqldqdggfsTDVAGSGVDSTgQAGTYFYTAPEI--EQDWpkiDEKADMYSLGV 665
Cdd:cd05570  123 KLDNVLLDAEGHIKIADFGMCK--------------EGIWGGNTTST-FCGTPDYIAPEIlrEQDY---GFSVDWWALGV 184
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30694992  666 VFFELW---HPFGTAMERHVILTNLKLKGELPlKWVNefPEQASLLRRLMSPSPSDR----PS-ATELLKHAF 730
Cdd:cd05570  185 LLYEMLagqSPFEGDDEDELFEAILNDEVLYP-RWLS--REAVSILKGLLTKDPARRlgcgPKgEADIKAHPF 254
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
424-712 1.06e-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: 61.95  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKkirlkdkeipvnsrIVREVATLSRLQhqhvvryyQAWF--ETGVVdpfa 501
Cdd:cd05623   73 DFEILKVIGRGAFGEVAVVKLKNADKVFAMK--------------ILNKWEMLKRAE--------TACFreERDVL---- 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 gANWGSKTAGSSMFSYsgavsteipEQDNNLestylYIQMEYCP----RTLRQVFEsyNHFDKDFAWHLIRQIVEGLAHI 577
Cdd:cd05623  127 -VNGDSQWITTLHYAF---------QDDNNL-----YLVMDYYVggdlLTLLSKFE--DRLPEDMARFYLAEMVLAIDSV 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  578 HGQGIIHRDFTPNNIFFDARNDIKIGDFGlaKFLKLEqldQDGGFSTDVAgsgvdstgqAGTYFYTAPEIEQDWP----K 653
Cdd:cd05623  190 HQLHYVHRDIKPDNILMDMNGHIRLADFG--SCLKLM---EDGTVQSSVA---------VGTPDYISPEILQAMEdgkgK 255
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30694992  654 IDEKADMYSLGVVFFELWH---PF--GTAMERHVILTNLKLKGELPLKWVNEFPEQASLLRRLM 712
Cdd:cd05623  256 YGPECDWWSLGVCMYEMLYgetPFyaESLVETYGKIMNHKERFQFPTQVTDVSENAKDLIRRLI 319
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
420-730 1.12e-09

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: 61.64  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  420 RYLNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRlkdKEIPVNSRIVREVATLSRlqhqhVVRYYQAWFETGVVDP 499
Cdd:cd05593   12 KTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILK---KEVIIAKDEVAHTLTESR-----VLKNTRHPFLTSLKYS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  500 FaganwgsKTAGSSMFSYSGAVSTEIpeqdnnlestYLYIQMEYCprtlrqvfesynhFDKDFAWHLIRQIVEGLAHIHG 579
Cdd:cd05593   84 F-------QTKDRLCFVMEYVNGGEL----------FFHLSRERV-------------FSEDRTRFYGAEIVSALDYLHS 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  580 QGIIHRDFTPNNIFFDARNDIKIGDFGLAKflklEQLDQDGGFSTdvagsgvdstgQAGTYFYTAPEIEQDwPKIDEKAD 659
Cdd:cd05593  134 GKIVYRDLKLENLMLDKDGHIKITDFGLCK----EGITDAATMKT-----------FCGTPEYLAPEVLED-NDYGRAVD 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  660 MYSLGVVFFELW---HPFGTamERHVILTNLKLKGELplkwvnEFP-----EQASLLRRLMSPSPSDR-----PSATELL 726
Cdd:cd05593  198 WWGLGVVMYEMMcgrLPFYN--QDHEKLFELILMEDI------KFPrtlsaDAKSLLSGLLIKDPNKRlgggpDDAKEIM 269

                 ....
gi 30694992  727 KHAF 730
Cdd:cd05593  270 RHSF 273
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
424-730 1.15e-09

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


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 60.88  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIrlkDKEipvnsrivrevATLSRLQHQhvvryyQAWFE----TGVVDP 499
Cdd:cd05609    1 DFETIKLISNGAYGAVYLVRHRETRQRFAMKKI---NKQ-----------NLILRNQIQ------QVFVErdilTFAENP 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  500 FAganwgsktagSSMFsysGAVSTEipeqdnnlesTYLYIQMEYCP----RTLrqvFESYNHFDKDFAWHLIRQIVEGLA 575
Cdd:cd05609   61 FV----------VSMY---CSFETK----------RHLCMVMEYVEggdcATL---LKNIGPLPVDMARMYFAETVLALE 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  576 HIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKfLKLEQLdqdggfSTDVAGSGVDSTGQ-------AGTYFYTAPEI- 647
Cdd:cd05609  115 YLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSK-IGLMSL------TTNLYEGHIEKDTRefldkqvCGTPEYIAPEVi 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  648 -EQDWPKideKADMYSLGVVFFELWH---PF-GTAMER---HVILTNLKLKGE---LPlkwvnefPEQASLLRRLMSPSP 716
Cdd:cd05609  188 lRQGYGK---PVDWWAMGIILYEFLVgcvPFfGDTPEElfgQVISDEIEWPEGddaLP-------DDAQDLITRLLQQNP 257
                        330
                 ....*....|....*..
gi 30694992  717 SDR---PSATELLKHAF 730
Cdd:cd05609  258 LERlgtGGAEEVKQHPF 274
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
429-728 1.22e-09

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


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 60.41  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLG-----QGGFGHVVLCKNKldgrqyAVKKiRLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQA--WFETgvVDPFA 501
Cdd:cd13995    5 RNIGsdfipRGAFGKVYLAQDT------KTKK-RMACKLIPVEQFKPSDVEIQACFRHENIAELYGAllWEET--VHLFM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 GANWGsktagssmfsysGAVsteipeqdnnLEstylyiQMEYCPrTLRQvFEsynhfdkdFAWhLIRQIVEGLAHIHGQG 581
Cdd:cd13995   76 EAGEG------------GSV----------LE------KLESCG-PMRE-FE--------IIW-VTKHVLKGLDFLHSKN 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIgDFGLAKflkleQLDQDGGFSTDVagsgvdstgqAGTYFYTAPEIeqdwpkI-----DE 656
Cdd:cd13995  117 IIHHDIKPSNIVFMSTKAVLV-DFGLSV-----QMTEDVYVPKDL----------RGTEIYMSPEV------IlcrghNT 174
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30694992  657 KADMYSLGVVFFELWH---PFGTAMERHVILTNLKL--KGELPLKWVNE--FPEQASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd13995  175 KADIYSLGATIIHMQTgspPWVRRYPRSAYPSYLYIihKQAPPLEDIAQdcSPAMRELLEAALERNPNHRSSAAELLKH 253
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
570-730 1.83e-09

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: 60.28  E-value: 1.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  570 IVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLakflkleqldqdggfSTDVAGSgvDSTGQAGTYFYTAPE-IE 648
Cdd:cd06619  104 VVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGV---------------STQLVNS--IAKTYVGTNAYMAPErIS 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  649 QDWPKIdeKADMYSLGVVFFEL---WHPFGTAMERHVILTNLKL-----KGELPLKWVNEFPEQ-ASLLRRLMSPSPSDR 719
Cdd:cd06619  167 GEQYGI--HSDVWSLGISFMELalgRFPYPQIQKNQGSLMPLQLlqcivDEDPPVLPVGQFSEKfVHFITQCMRKQPKER 244
                        170
                 ....*....|.
gi 30694992  720 PSATELLKHAF 730
Cdd:cd06619  245 PAPENLMDHPF 255
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
547-670 1.86e-09

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: 59.80  E-value: 1.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  547 TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARND---IKIGDFGLAKflkleqldqdggfS 623
Cdd:cd14155   74 NLEQLLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDENgytAVVGDFGLAE-------------K 140
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 30694992  624 TDVAGSGVDSTGQAGTYFYTAPEIEQDWPkIDEKADMYSLGVVFFEL 670
Cdd:cd14155  141 IPDYSDGKEKLAVVGSPYWMAPEVLRGEP-YNEKADVFSYGIILCEI 186
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
425-730 2.00e-09

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: 59.78  E-value: 2.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKeipVNSRIVREVATLSRLQHQHVVRyyqawFETGVVDPfagan 504
Cdd:cd14662    2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLK---IDENVQREIINHRSLRHPNIIR-----FKEVVLTP----- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysgavsteipeqdnnlesTYLYIQMEYCPRTlrQVFE---SYNHFDKDFAWHLIRQIVEGLAHIHGQG 581
Cdd:cd14662   69 ------------------------------THLAIVMEYAAGG--ELFEricNAGRFSEDEARYFFQQLISGVSYCHSMQ 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDAR--NDIKIGDFGLAKflkleqldqdggfsTDVAGSGVDSTgqAGTYFYTAPEIEQDWPKIDEKAD 659
Cdd:cd14662  117 ICHRDLKLENTLLDGSpaPRLKICDFGYSK--------------SSVLHSQPKST--VGTPAYIAPEVLSRKEYDGKVAD 180
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30694992  660 MYSLGVVFFELW---HPFGTAME----RHVILTNLKLKGELPlKWVNEFPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14662  181 VWSCGVTLYVMLvgaYPFEDPDDpknfRKTIQRIMSVQYKIP-DYVRVSQDCRHLLSRIFVANPAKRITIPEIKNHPW 257
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
424-712 2.08e-09

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: 60.45  E-value: 2.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVK-----KIRLKDKE-IPVNSRIVREVATLSRLQHQHVVRYYqawFETG-- 495
Cdd:cd14223    1 DFSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldkkRIKMKQGEtLALNERIMLSLVSTGDCPFIVCMSYA---FHTPdk 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  496 ---VVDPFAGANWGSKTAGSSMFSysgavsteipEQDNNLESTylyiqmeycprtlrqvfesynhfdkdfawhlirQIVE 572
Cdd:cd14223   78 lsfILDLMNGGDLHYHLSQHGVFS----------EAEMRFYAA---------------------------------EIIL 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  573 GLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAkflkleqldqdGGFSTDVAGSGVdstgqaGTYFYTAPEIEQDWP 652
Cdd:cd14223  115 GLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLA-----------CDFSKKKPHASV------GTHGYMAPEVLQKGV 177
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30694992  653 KIDEKADMYSLGVVFFELWH---PF---GTAMERHVILTNLKLKGELPLKWVnefPEQASLLRRLM 712
Cdd:cd14223  178 AYDSSADWFSLGCMLFKLLRghsPFrqhKTKDKHEIDRMTLTMAVELPDSFS---PELRSLLEGLL 240
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
428-727 2.11e-09

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: 59.77  E-value: 2.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  428 LKPLGQGGFGHVVLCKNKlDGRQYAVKKIR---LKDKEIpvnsriVREVATLSRLQHQHVVRYYqawfetgvvdpfagan 504
Cdd:cd05059    9 LKELGSGQFGVVHLGKWR-GKIDVAIKMIKegsMSEDDF------IEEAKVMMKLSHPKLVQLY---------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysGAVSTEIPeqdnnlestyLYIQMEY----CPRT-LRQVFESynhFDKDFAWHLIRQIVEGLAHIHG 579
Cdd:cd05059   66 --------------GVCTKQRP----------IFIVTEYmangCLLNyLRERRGK---FQTEQLLEMCKDVCEAMEYLES 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  580 QGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLkleqLDQdggfstdvagsgvDSTGQAGTYF---YTAPEIeQDWPKIDE 656
Cdd:cd05059  119 NGFIHRDLAARNCLVGEQNVVKVSDFGLARYV----LDD-------------EYTSSVGTKFpvkWSPPEV-FMYSKFSS 180
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30694992  657 KADMYSLGVVFFELWHPFGTAMERhviLTNLKLKGELPLKWVNEFPEQAS-----LLRRLMSPSPSDRPSATELLK 727
Cdd:cd05059  181 KSDVWSFGVLMWEVFSEGKMPYER---FSNSEVVEHISQGYRLYRPHLAPtevytIMYSCWHEKPEERPTFKILLS 253
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
431-725 2.45e-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: 59.83  E-value: 2.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEipvnsriVREVATLSRLQHQHVVRYYqawfetgvvdpfaganwgskta 510
Cdd:cd13991   14 IGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFR-------AEELMACAGLTSPRVVPLY---------------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  511 gssmfsysGAVSteipeqdnnlESTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTP 589
Cdd:cd13991   65 --------GAVR----------EGPWVNIFMDLKEGgSLGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKA 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  590 NNIFFDAR-NDIKIGDFGLAKFLkleqldQDGGFSTDVAGSGVdstgQAGTYFYTAPEIEQDWPkIDEKADMYSLGVVFF 668
Cdd:cd13991  127 DNVLLSSDgSDAFLCDFGHAECL------DPDGLGKSLFTGDY----IPGTETHMAPEVVLGKP-CDAKVDVWSSCCMML 195
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30694992  669 ELW---HPFgTAMERHVILtnLKLKGELPLKWvnEFPEQ-----ASLLRRLMSPSPSDRPSATEL 725
Cdd:cd13991  196 HMLngcHPW-TQYYSGPLC--LKIANEPPPLR--EIPPScapltAQAIQAGLRKEPVHRASAAEL 255
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
431-670 2.46e-09

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


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 59.58  E-value: 2.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEipVNSRIVREVATLSRLQHQHVVRYyqawfeTGVVdpfaganwgskta 510
Cdd:cd14221    1 LGKGCFGQAIKVTHRETGEVMVMKELIRFDEE--TQRTFLKEVKVMRCLEHPNVLKF------IGVL------------- 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  511 gssmfsysgavsteipEQDNNLESTYLYIQmeycPRTLRQVFESynhFDKDFAWH----LIRQIVEGLAHIHGQGIIHRD 586
Cdd:cd14221   60 ----------------YKDKRLNFITEYIK----GGTLRGIIKS---MDSHYPWSqrvsFAKDIASGMAYLHSMNIIHRD 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  587 FTPNNIFFDARNDIKIGDFGLAKfLKLEQLDQDGGFSTDVAGSGVDSTGQAGTYFYTAPEIEQDwPKIDEKADMYSLGVV 666
Cdd:cd14221  117 LNSHNCLVRENKSVVVADFGLAR-LMVDEKTQPEGLRSLKKPDRKKRYTVVGNPYWMAPEMING-RSYDEKVDVFSFGIV 194

                 ....
gi 30694992  667 FFEL 670
Cdd:cd14221  195 LCEI 198
RWD_DRWD_ELF-like cd11605
RWD, DRWD, and ELF domain family; The family includes the RWD, double-RWD (DRWD), and ELF ...
41-141 2.66e-09

RWD, DRWD, and ELF domain family; The family includes the RWD, double-RWD (DRWD), and ELF domains. They belong to the ubiquitin-conjugating (UBC) superfamily that represents a structural domain with an alpha-beta(4)-alpha(3) core fold. The RWD domain (named after three major RWD-containing proteins: RING finger, WD-repeat-containing proteins and DEXD-like helicases) mediates protein-protein interactions in a variety of pathways in eukaryotes. The DRWD domain is responsible for substrate binding. It is involved in interactions with other kinetochore proteins. The ELF (N-terminal E2-like fold) domain is found in all Fanconi anemia group L protein (FANCL) homologs. It is required to promote efficient DNA damage-induced FANCD2 (Fanconi anemia group D2 protein) monoubiquitination in vertebrate cells.


Pssm-ID: 467641  Cd Length: 94  Bit Score: 55.27  E-value: 2.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   41 ALSAIFQEDCKVVSDSrSPPQIAIKLRPYSkdmgyEDTDISAMLIVRCLPGY-PYKCPKLQITPEQGLTTADAEKLLSLL 119
Cdd:cd11605    1 ALESIYGDELEVLSDD-SPLRFSIRLSPEE-----EEDDPPLELEFTLPPGYpPEEPPLITLRSPKLSSAERLSLLKLEL 74
                         90       100
                 ....*....|....*....|..
gi 30694992  120 EDQANSNarEGRVMIFNLVEAA 141
Cdd:cd11605   75 EEAAEEN--LGEPMLFDLVEAL 94
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
425-610 2.83e-09

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: 59.39  E-value: 2.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKkIRLKDKEipvNSRIVREVATLSRLQHQH---VVRYYqawfetgvvdpfa 501
Cdd:cd14016    2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIK-IEKKDSK---HPQLEYEAKVYKLLQGGPgipRLYWF------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 ganwgsktaGSsmfsysgavsteipEQDNNlestylYIQMEYCPRTLRQVFESYNhfdKDFAWH----LIRQIVEGLAHI 577
Cdd:cd14016   65 ---------GQ--------------EGDYN------VMVMDLLGPSLEDLFNKCG---RKFSLKtvlmLADQMISRLEYL 112
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 30694992  578 HGQGIIHRDFTPNNIFF---DARNDIKIGDFGLAKF 610
Cdd:cd14016  113 HSKGYIHRDIKPENFLMglgKNSNKVYLIDFGLAKK 148
RWD_RWDD3 cd23819
RWD domain of RWD domain-containing protein 3 (RWDD3) and related proteins; RWDD3, also called ...
37-143 3.01e-09

RWD domain of RWD domain-containing protein 3 (RWDD3) and related proteins; RWDD3, also called RWD domain-containing sumoylation enhancer (RSUME), acts as an enhancer of SUMO conjugation and has no effect on ubiquitination. It increases protein sumoylation (a dynamic ubiquitin-like post translational modification) of several proteins including HIF1alpha and I-kappa-B, through direct interaction with UBC9. Its RWD domain is required for the sumoylation enhancement activity.


Pssm-ID: 467655  Cd Length: 106  Bit Score: 55.79  E-value: 3.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   37 EEITALSAIFQED--CKVVSDSRSPPQIAIKLRPySKDMGYEDTDISAMLIVRclPGYPYKCPKLQITPEQgLTTADAEK 114
Cdd:cd23819    1 DELSVLQAIFCGPgeFEVLSSSETSDGVSFKIQI-SVEGFDEDIVLKLTFHLS--PNYPSSLPDISVSSEQ-LTRAQCND 76
                         90       100
                 ....*....|....*....|....*....
gi 30694992  115 LLSLLEDQANSNAreGRVMIFNLVEAAQE 143
Cdd:cd23819   77 LQDSLLEYANSLL--GEPMVLELVLWLQE 103
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
421-730 3.16e-09

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 59.65  E-value: 3.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  421 YLNDFEELkplGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEipVNSRIVREVATLSRLQHQHVVRYYQAWfetgvvdpf 500
Cdd:cd06657   21 YLDNFIKI---GEGSTGIVCIATVKSSGKLVAVKKMDLRKQQ--RRELLFNEVVIMRDYQHENVVEMYNSY--------- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  501 aganwgsktagssmfsysgavsteipeqdnnLESTYLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQ 580
Cdd:cd06657   87 -------------------------------LVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLKALSVLHAQ 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFDARNDIKIGDFglakflkleqldqdgGFSTDVAGSGVDSTGQAGTYFYTAPEIEQDWPKIDEkADM 660
Cdd:cd06657  136 GVIHRDIKSDSILLTHDGRVKLSDF---------------GFCAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPE-VDI 199
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30694992  661 YSLGVVFFELWHPFGTAMERHVILTNLKLKGELPLKWVNEF---PEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd06657  200 WSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPKLKNLHkvsPSLKGFLDRLLVRDPAQRATAAELLKHPF 272
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
431-670 3.91e-09

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


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 59.16  E-value: 3.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRL---KDKEIPVNsrivrEVATLSRLQHQHVVRYYQAWfetgvvdpfaganwgs 507
Cdd:cd14190   12 LGGGKFGKVHTCTEKRTGLKLAAKVINKqnsKDKEMVLL-----EIQVMNQLNHRNLIQLYEAI---------------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 ktagssmfsysgavstEIPEQdnnlestyLYIQMEYCP--RTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHR 585
Cdd:cd14190   71 ----------------ETPNE--------IVLFMEYVEggELFERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHL 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  586 DFTPNNIFFDARND--IKIGDFGLAKFLKLEQldqdggfstdvagsgvDSTGQAGTYFYTAPEIeQDWPKIDEKADMYSL 663
Cdd:cd14190  127 DLKPENILCVNRTGhqVKIIDFGLARRYNPRE----------------KLKVNFGTPEFLSPEV-VNYDQVSFPTDMWSM 189

                 ....*..
gi 30694992  664 GVVFFEL 670
Cdd:cd14190  190 GVITYML 196
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
542-730 4.13e-09

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


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 59.26  E-value: 4.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  542 EYCPRTLRQVFesynhFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFF--DARN--DIKIGDFGLAKflkleQLD 617
Cdd:cd14177   84 ELLDRILRQKF-----FSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYmdDSANadSIRICDFGFAK-----QLR 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  618 QDGGFSTDvagsgvdstgQAGTYFYTAPEI--EQDWpkiDEKADMYSLGVVFFEL---WHPFGTA---MERHVILT---- 685
Cdd:cd14177  154 GENGLLLT----------PCYTANFVAPEVlmRQGY---DAACDIWSLGVLLYTMlagYTPFANGpndTPEEILLRigsg 220
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 30694992  686 NLKLKGElplKWVNEFPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14177  221 KFSLSGG---NWDTVSDAAKDLLSHMLHVDPHQRYTAEQVLKHSW 262
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
423-730 4.69e-09

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


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 59.50  E-value: 4.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDK-------EIpvnsRIVREVATLSRLQHQHVVRYYQaWFEtg 495
Cdd:cd14134   12 NRYKILRLLGEGTFGKVLECWDRKRKRYVAVKIIRNVEKyreaakiEI----DVLETLAEKDPNGKSHCVQLRD-WFD-- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  496 vvdpfaganwgsktagssmfsYSGavsteipeqdnnlestYLYIQMEYCPRTLRQVFESYNH--FDKDFAWHLIRQIVEG 573
Cdd:cd14134   85 ---------------------YRG----------------HMCIVFELLGPSLYDFLKKNNYgpFPLEHVQHIAKQLLEA 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  574 LAHIHGQGIIHRDFTPNNIFFD-------------------ARNDIKIGDFGLAKFlklEQLDQdggfstdvagSGVDST 634
Cdd:cd14134  128 VAFLHDLKLTHTDLKPENILLVdsdyvkvynpkkkrqirvpKSTDIKLIDFGSATF---DDEYH----------SSIVST 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  635 GQagtyfYTAPEI--EQDWpkiDEKADMYSLGVVFFELW-------------H---------PFGTAM-ERHVILTNLKL 689
Cdd:cd14134  195 RH-----YRAPEVilGLGW---SYPCDVWSIGCILVELYtgellfqthdnleHlammerilgPLPKRMiRRAKKGAKYFY 266
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30694992  690 KGELPLKWVN---------------------EFPEQAS---LLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14134  267 FYHGRLDWPEgsssgrsikrvckplkrlmllVDPEHRLlfdLIRKMLEYDPSKRITAKEALKHPF 331
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
429-728 5.71e-09

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: 58.50  E-value: 5.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKLDGRQYAVKKIRlKDKEIPVNSRIVREVATLSRLQHQHVVRYyqawfetgvvdpfaganwgsk 508
Cdd:cd14184    7 KVIGDGNFAVVKECVERSTGKEFALKIID-KAKCCGKEHLIENEVSILRRVKHPNIIML--------------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  509 tagssmfsysgavsteIPEQDNNLEstyLYIQMEYCP--RTLRQVFESYNHFDKDfAWHLIRQIVEGLAHIHGQGIIHRD 586
Cdd:cd14184   65 ----------------IEEMDTPAE---LYLVMELVKggDLFDAITSSTKYTERD-ASAMVYNLASALKYLHGLCIVHRD 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  587 FTPNNI----FFDARNDIKIGDFGLAKFLkleqldqDGGFSTdvagsgvdstgQAGTYFYTAPEIeqdwpkIDE-----K 657
Cdd:cd14184  125 IKPENLlvceYPDGTKSLKLGDFGLATVV-------EGPLYT-----------VCGTPTYVAPEI------IAEtgyglK 180
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30694992  658 ADMYSLGVVFFEL---WHPFGTAMERHVILTNLKLKGELPLK---WVNEFPEQASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14184  181 VDIWAAGVITYILlcgFPPFRSENNLQEDLFDQILLGKLEFPspyWDNITDSAKELISHMLQVNVEARYTAEQILSH 257
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
468-730 6.07e-09

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: 58.48  E-value: 6.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  468 RIVREVATLSRLQHQHVVRYYQAWfetgvvdpfaganwgsktaGSSMFSYSGAV-STEIpeQDNNLESTYLYIQMEYCPR 546
Cdd:cd14033   46 RFSEEVEMLKGLQHPNIVRFYDSW-------------------KSTVRGHKCIIlVTEL--MTSGTLKTYLKRFREMKLK 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  547 TLRQvfesynhfdkdfaWHliRQIVEGLAHIHGQG--IIHRDFTPNNIFFDA-RNDIKIGDFGLAKFLKleqldqdGGFS 623
Cdd:cd14033  105 LLQR-------------WS--RQILKGLHFLHSRCppILHRDLKCDNIFITGpTGSVKIGDLGLATLKR-------ASFA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  624 TDVagsgvdstgqAGTYFYTAPEIEQDwpKIDEKADMYSLGVVFFELW---HPFGTAMERHVILTNLKlKGELPLKWVN- 699
Cdd:cd14033  163 KSV----------IGTPEFMAPEMYEE--KYDEAVDVYAFGMCILEMAtseYPYSECQNAAQIYRKVT-SGIKPDSFYKv 229
                        250       260       270
                 ....*....|....*....|....*....|.
gi 30694992  700 EFPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14033  230 KVPELKEIIEGCIRTDKDERFTIQDLLEHRF 260
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
568-670 6.29e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 59.47  E-value: 6.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   568 RQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleQLDQdggfSTDVAgsgvDSTGQAGTYFYTAPEI 647
Cdd:PHA03207  192 RRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAAC-----KLDA----HPDTP----QCYGWSGTLETNSPEL 258
                          90       100
                  ....*....|....*....|...
gi 30694992   648 EQDWPKIdEKADMYSLGVVFFEL 670
Cdd:PHA03207  259 LALDPYC-AKTDIWSAGLVLFEM 280
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
425-609 6.99e-09

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: 58.04  E-value: 6.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRL-KDKEIpvnsrIVREVATLSRLQ-HQHVVRYYqawfetgvvdpfag 502
Cdd:cd14017    2 WKVVKKIGGGGFGEIYKVRDVVDGEEVAMKVESKsQPKQV-----LKMEVAVLKKLQgKPHFCRLI-------------- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgskTAGSSmfsysgavsteipeqdnnleSTYLYIQMEYCPRTLRQVFESYN--HFDKDFAWHLIRQIVEGLAHIHGQ 580
Cdd:cd14017   63 ------GCGRT--------------------ERYNYIVMTLLGPNLAELRRSQPrgKFSVSTTLRLGIQILKAIEDIHEV 116
                        170       180       190
                 ....*....|....*....|....*....|....
gi 30694992  581 GIIHRDFTPNNI-----FFDARNdIKIGDFGLAK 609
Cdd:cd14017  117 GFLHRDVKPSNFaigrgPSDERT-VYILDFGLAR 149
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
422-741 8.06e-09

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


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 58.85  E-value: 8.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIR----LKDKEIPVNsriVREVATLSRLQHQHVVRYYQAWFETgvV 497
Cdd:cd05615    9 LTDFNFLMVLGKGSFGKVMLAERKGSDELYAIKILKkdvvIQDDDVECT---MVEKRVLALQDKPPFLTQLHSCFQT--V 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  498 DpfaganwgsktagssmfsysgavsteipeqdnnlestYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAH 576
Cdd:cd05615   84 D-------------------------------------RLYFVMEYVNGgDLMYHIQQVGKFKEPQAVFYAAEISVGLFF 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  577 IHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEqldqdggfstdvagsGVDSTGQAGTYFYTAPEIEQDWPkIDE 656
Cdd:cd05615  127 LHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMVE---------------GVTTRTFCGTPDYIAPEIIAYQP-YGR 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  657 KADMYSLGVVFFELWH---PFGTAMERHVILTNLKLKGELPlKWVNEfpEQASLLRRLMSPSPSDR-----PSATELLKH 728
Cdd:cd05615  191 SVDWWAYGVLLYEMLAgqpPFDGEDEDELFQSIMEHNVSYP-KSLSK--EAVSICKGLMTKHPAKRlgcgpEGERDIREH 267
                        330
                 ....*....|...
gi 30694992  729 AFPPRMESELLDN 741
Cdd:cd05615  268 AFFRRIDWDKLEN 280
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
424-740 8.74e-09

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


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 58.47  E-value: 8.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIR----LKDKEIP---VNSRIVREVATLSRLQHQHvvryyqAWFETgv 496
Cdd:cd05616    1 DFNFLMVLGKGSFGKVMLAERKGTDELYAVKILKkdvvIQDDDVEctmVEKRVLALSGKPPFLTQLH------SCFQT-- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  497 vdpfaganwgsktagssmfsysgavsteipeqdnnleSTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLA 575
Cdd:cd05616   73 -------------------------------------MDRLYFVMEYVNGgDLMYHIQQVGRFKEPHAVFYAAEIAIGLF 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  576 HIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleqldqdggfstDVAGSGVDSTGQAGTYFYTAPEIEQDWPkID 655
Cdd:cd05616  116 FLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCK---------------ENIWDGVTTKTFCGTPDYIAPEIIAYQP-YG 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  656 EKADMYSLGVVFFELW--HP----------FGTAMERHVILTNLKLKgelplkwvnefpEQASLLRRLMSPSPSDR---- 719
Cdd:cd05616  180 KSVDWWAFGVLLYEMLagQApfegededelFQSIMEHNVAYPKSMSK------------EAVAICKGLMTKHPGKRlgcg 247
                        330       340
                 ....*....|....*....|..
gi 30694992  720 PSATELLK-HAFPPRMESELLD 740
Cdd:cd05616  248 PEGERDIKeHAFFRYIDWEKLE 269
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
422-730 1.03e-08

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


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 57.71  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEEL-KPLGQGGFGHVVLCKNKLDGRQYA---VKKIRLKDKEIPVN-SRIVREVATLSRLQHQHVVRYYQAwFE--T 494
Cdd:cd14195    3 VEDHYEMgEELGSGQFAIVRKCREKGTGKEYAakfIKKRRLSSSRRGVSrEEIEREVNILREIQHPNIITLHDI-FEnkT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  495 GVVDPFaganwgSKTAGSSMFSYsgavsteIPEQDNnlestylyiqmeycprtlrqvfesynhFDKDFAWHLIRQIVEGL 574
Cdd:cd14195   82 DVVLIL------ELVSGGELFDF-------LAEKES---------------------------LTEEEATQFLKQILDGV 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  575 AHIHGQGIIHRDFTPNNIFFDARN----DIKIGDFGLAKFLKleqldqdggfstdvagSGVDSTGQAGTYFYTAPEIEQD 650
Cdd:cd14195  122 HYLHSKRIAHFDLKPENIMLLDKNvpnpRIKLIDFGIAHKIE----------------AGNEFKNIFGTPEFVAPEIVNY 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  651 WPkIDEKADMYSLGVVFFELW---HPFgTAMERHVILTNLK-LKGELPLKWVNEFPEQAS-LLRRLMSPSPSDRPSATEL 725
Cdd:cd14195  186 EP-LGLEADMWSIGVITYILLsgaSPF-LGETKQETLTNISaVNYDFDEEYFSNTSELAKdFIRRLLVKDPKKRMTIAQS 263

                 ....*
gi 30694992  726 LKHAF 730
Cdd:cd14195  264 LEHSW 268
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
429-725 1.21e-08

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: 57.36  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKL-DGRQYAVKKIRLKDKEIPVNSR-IVREVATLSRLQHQHVVRYYqawfetGVvdpfaganwg 506
Cdd:cd05060    1 KELGHGNFGSVRKGVYLMkSGKEVEVAVKTLKQEHEKAGKKeFLREASVMAQLDHPCIVRLI------GV---------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  507 skTAGSSMFsysgavsteipeqdnnlestylyIQMEYCPR-TLRQVFESYNHF-DKDFAwHLIRQIVEGLAHIHGQGIIH 584
Cdd:cd05060   65 --CKGEPLM-----------------------LVMELAPLgPLLKYLKKRREIpVSDLK-ELAHQVAMGMAYLESKHFVH 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  585 RDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqdggfstdvAGSGVDSTGQAGTY---FYtAPE-IeqDWPKIDEKADM 660
Cdd:cd05060  119 RDLAARNVLLVNRHQAKISDFGMSRALG--------------AGSDYYRATTAGRWplkWY-APEcI--NYGKFSSKSDV 181
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  661 YSLGVVFFELW----HPFGtAMERHVILTNLKLKGELPLKwvNEFPEQA-SLLRRLMSPSPSDRPSATEL 725
Cdd:cd05060  182 WSYGVTLWEAFsygaKPYG-EMKGPEVIAMLESGERLPRP--EECPQEIySIMLSCWKYRPEDRPTFSEL 248
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
431-671 1.30e-08

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: 57.67  E-value: 1.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVL--CKNKL---DGRQYAVKKIrlkdKEIPVNSR--IVREVATLSRLQHQHVVRYYQAWFETgvvDPFAGA 503
Cdd:cd05092   13 LGEGAFGKVFLaeCHNLLpeqDKMLVAVKAL----KEATESARqdFQREAELLTVLQHQHIVRFYGVCTEG---EPLIMV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 NWGSKTAGSSMFSYSGAVSTEIPEQDNNlestylyiqMEYCPRTLRQVFesynhfdkdfawHLIRQIVEGLAHIHGQGII 583
Cdd:cd05092   86 FEYMRHGDLNRFLRSHGPDAKILDGGEG---------QAPGQLTLGQML------------QIASQIASGMVYLASLHFV 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  584 HRDFTPNNIFFDARNDIKIGDFGLAKFLkleqldqdggFSTDVAGSGvdstGQAGTYFYTAPEIEQDWPKIDEKADMYSL 663
Cdd:cd05092  145 HRDLATRNCLVGQGLVVKIGDFGMSRDI----------YSTDYYRVG----GRTMLPIRWMPPESILYRKFTTESDIWSF 210

                 ....*...
gi 30694992  664 GVVFFELW 671
Cdd:cd05092  211 GVVLWEIF 218
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
425-621 1.49e-08

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


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 57.42  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVV--LCKNKLDGRQYAVKKIRLKDKEIPVNSR-IVREVATLSRLQHQHVVRYYqawfetgvvdpfa 501
Cdd:cd05057    9 LEKGKVLGSGAFGTVYkgVWIPEGEKVKIPVAIKVLREETGPKANEeILDEAYVMASVDHPHLVRLL------------- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 GANWGSKTAGSSMFSYSGAVSTEIPEQDNNLESTYLyiqMEYCprtlrqvfesynhfdkdfawhliRQIVEGLAHIHGQG 581
Cdd:cd05057   76 GICLSSQVQLITQLMPLGCLLDYVRNHRDNIGSQLL---LNWC-----------------------VQIAKGMSYLEEKR 129
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGLAKFL--KLEQLDQDGG 621
Cdd:cd05057  130 LVHRDLAARNVLVKTPNHVKITDFGLAKLLdvDEKEYHAEGG 171
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
412-674 1.59e-08

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 57.17  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   412 PNASLPS-SRYLNDFEELKPLG--QGGFGHVVLCKNKLDGRQYAVKKIRLKD-KEIPVNsrivreVATLSRlQHQHVVRY 487
Cdd:PHA03390    2 MDKSLSElVQFLKNCEIVKKLKliDGKFGKVSVLKHKPTQKLFVQKIIKAKNfNAIEPM------VHQLMK-DNPNFIKL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   488 YqawfetgvvdpfaganwgsktagssmFSYsgavsteipeqdNNLESTYL---YIQmeyCPrTLRQVFESYNHFDKDFAW 564
Cdd:PHA03390   75 Y--------------------------YSV------------TTLKGHVLimdYIK---DG-DLFDLLKKEGKLSEAEVK 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   565 HLIRQIVEGLAHIHGQGIIHRDFTPNNI-FFDARNDIKIGDFGLAKFLKLEQLdQDggfstdvagsgvdstgqaGTYFYT 643
Cdd:PHA03390  113 KIIRQLVEALNDLHKHNIIHNDIKLENVlYDRAKDRIYLCDYGLCKIIGTPSC-YD------------------GTLDYF 173
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 30694992   644 APEieqdwpKI-----DEKADMYSLGVVFFELW---HPF 674
Cdd:PHA03390  174 SPE------KIkghnyDVSFDWWAVGVLTYELLtgkHPF 206
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
429-728 1.61e-08

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


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 57.31  E-value: 1.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKLDGRQYAVKKIRlKDKEIPVNSRIVREVATLSRLQHQHVVRYyqawfetgvvdpfaganwgsk 508
Cdd:cd14183   12 RTIGDGNFAVVKECVERSTGREYALKIIN-KSKCRGKEHMIQNEVSILRRVKHPNIVLL--------------------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  509 tagssmfsysgavsteIPEQDNNLEstyLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDF 587
Cdd:cd14183   70 ----------------IEEMDMPTE---LYLVMELVKGgDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDI 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  588 TPNNIFF----DARNDIKIGDFGLAKFLkleqldqDGGFSTdvagsgvdstgQAGTYFYTAPEIEQDwPKIDEKADMYSL 663
Cdd:cd14183  131 KPENLLVyehqDGSKSLKLGDFGLATVV-------DGPLYT-----------VCGTPTYVAPEIIAE-TGYGLKVDIWAA 191
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30694992  664 GVVFFEL---WHPFGTAMERHVILTNLKLKGEL--PLK-WVNEFPEQASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14183  192 GVITYILlcgFPPFRGSGDDQEVLFDQILMGQVdfPSPyWDNVSDSAKELITMMLQVDVDQRYSALQVLEH 262
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
558-728 1.78e-08

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: 57.35  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  558 FDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARND---IKIGDFGLAKflkleQLDQDGGFSTDVAgsgvdst 634
Cdd:cd14170   98 FTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPnaiLKLTDFGFAK-----ETTSHNSLTTPCY------- 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  635 gqagTYFYTAPEIEQDwPKIDEKADMYSLGVVFFELWHPFGTAMERHVILTNLKLKGELPL--------KWVNEFPEQAS 706
Cdd:cd14170  166 ----TPYYVAPEVLGP-EKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKTRIRMgqyefpnpEWSEVSEEVKM 240
                        170       180
                 ....*....|....*....|..
gi 30694992  707 LLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14170  241 LIRNLLKTEPTQRMTITEFMNH 262
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
557-728 1.83e-08

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: 57.47  E-value: 1.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  557 HFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARND---IKIGDFGLAKflkleqLDQdggfstdvagsGVDS 633
Cdd:cd14171  105 HFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEdapIKLCDFGFAK------VDQ-----------GDLM 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  634 TGQAgTYFYTAPEI--------EQDWPKI--------DEKADMYSLGVVFFEL---WHPFGTAMERHVILTNLKLK---G 691
Cdd:cd14171  168 TPQF-TPYYVAPQVleaqrrhrKERSGIPtsptpytyDKSCDMWSLGVIIYIMlcgYPPFYSEHPSRTITKDMKRKimtG 246
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 30694992  692 ELplkwvnEFPEQ---------ASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14171  247 SY------EFPEEewsqisemaKDIVRKLLCVDPEERMTIEEVLHH 286
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
431-727 1.88e-08

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: 57.02  E-value: 1.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVlcKNKLDGRQYAVKKIRLK-DKEIPVNSRIVREVATL-SRLQHQHVVRYyqawfeTGVVdpfaganwgsk 508
Cdd:cd14061    2 IGVGGFGKVY--RGIWRGEEVAVKAARQDpDEDISVTLENVRQEARLfWMLRHPNIIAL------RGVC----------- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  509 tagssmfsysgavsteipeqdnnLESTYLYIQMEYCPR-TLRQVFESYN---HFDKDFAwhliRQIVEGLAHIHGQG--- 581
Cdd:cd14061   63 -----------------------LQPPNLCLVMEYARGgALNRVLAGRKippHVLVDWA----IQIARGMNYLHNEApvp 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFD--------ARNDIKIGDFGLAKFL-KLEQLDQdggfstdvagsgvdstgqAGTYFYTAPE-IEQDw 651
Cdd:cd14061  116 IIHRDLKSSNILILeaienedlENKTLKITDFGLAREWhKTTRMSA------------------AGTYAWMAPEvIKSS- 176
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  652 pKIDEKADMYSLGVVFFELwhpfgtamerhviltnlkLKGELPLKWV-------------------NEFPEQ-ASLLRRL 711
Cdd:cd14061  177 -TFSKASDVWSYGVLLWEL------------------LTGEVPYKGIdglavaygvavnkltlpipSTCPEPfAQLMKDC 237
                        330
                 ....*....|....*.
gi 30694992  712 MSPSPSDRPSATELLK 727
Cdd:cd14061  238 WQPDPHDRPSFADILK 253
lanthi_synth_IV NF038150
class IV lanthionine synthetase LanL; Several classes of lanthionine bridge-producing ...
537-751 1.94e-08

class IV lanthionine synthetase LanL; Several classes of lanthionine bridge-producing peptide-modifying enzymes (lanthionine synthases) have been defined. LanC enzymes are class I, LanM are class II, LanKC are class III, and LanL are class IV. Members of this family are the class IV enzyme, active in the maturation of class IV lanthipeptides, a large fraction of which act as lantibiotics.


Pssm-ID: 468386 [Multi-domain]  Cd Length: 853  Bit Score: 58.74  E-value: 1.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   537 LYIQMEYCP-RTLRQ------VFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAK 609
Cdd:NF038150  269 LFLAQEEVPgVTLRRwvaerlRYRGDGGPPRADALALARRLVDLVAAVHARGLVLRDLTPNNVMVTPDGELRLIDLELAA 348
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   610 flkleqldqdggfstdVAGSGVdstGQAGTYFYTAPE-IEQDWPKIDEKADMYSLG-VVFFELW---------HPFGTAM 678
Cdd:NF038150  349 ----------------RPGDLV---TRVGTPGYSAPEqLAGAPPAAPPTADLYSLGaTLFFLATgldpvllddEPAARPV 409
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   679 ERHV--ILTNLKLKGELPlkwvnefPEQASLLRRLMSPSPSDRPSATELLKH--------------AFPPRMESELLDNI 742
Cdd:NF038150  410 NERLalWLLAAALPGPAP-------RALAPLILGLMADDPARRWDLARARAAlagpappaaarlppAAPDRLLVDGLDHL 482

                  ....*....
gi 30694992   743 LRIMQTSED 751
Cdd:NF038150  483 VATMTPDDD 491
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
429-727 2.16e-08

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 56.90  E-value: 2.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKldGRQYAVKKIRLKDKEIPVNSRivrEVATLSRLQHQHVVRYYqawfetgvvdpfaganwgsk 508
Cdd:cd14056    1 KTIGKGRYGEVWLGKYR--GEKVAVKIFSSRDEDSWFRET---EIYQTVMLRHENILGFI-------------------- 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  509 taGSSMFSYSGavsteipeqdnnleSTYLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQ-------- 580
Cdd:cd14056   56 --AADIKSTGS--------------WTQLWLITEYHEHGSLYDYLQRNTLDTEEALRLAYSAASGLAHLHTEivgtqgkp 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFDARNDIKIGDFGLAkfLKleqldqdggFSTDVAGSGVDSTGQAGTYFYTAPEIeqdwpkIDEK--- 657
Cdd:cd14056  120 AIAHRDLKSKNILVKRDGTCCIADLGLA--VR---------YDSDTNTIDIPPNPRVGTKRYMAPEV------LDDSinp 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  658 --------ADMYSLGVV--------------------FFELWHPFGTAMERHVILTNLKLKGELPLKWVN--EFPEQASL 707
Cdd:cd14056  183 ksfesfkmADIYSFGLVlweiarrceiggiaeeyqlpYFGMVPSDPSFEEMRKVVCVEKLRPPIPNRWKSdpVLRSMVKL 262
                        330       340
                 ....*....|....*....|
gi 30694992  708 LRRLMSPSPSDRPSATELLK 727
Cdd:cd14056  263 MQECWSENPHARLTALRVKK 282
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
434-670 2.98e-08

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: 56.57  E-value: 2.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  434 GGFGHVvlCKNKLDGRQYAVKKIRLKDKEIPVNSRivrEVATLSRLQHQHVVRYYQAwfetgvvdpfaganwgsktagss 513
Cdd:cd14053    6 GRFGAV--WKAQYLNRLVAVKIFPLQEKQSWLTER---EIYSLPGMKHENILQFIGA----------------------- 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  514 mfsysgavstEIPEQDNNLEstyLYIQMEYCPR-TLRQVFESYnhfdkDFAW----HLIRQIVEGLAHIH------GQG- 581
Cdd:cd14053   58 ----------EKHGESLEAE---YWLITEFHERgSLCDYLKGN-----VISWnelcKIAESMARGLAYLHedipatNGGh 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 ---IIHRDFTPNNIFFdaRNDIK--IGDFGLA-KFlkleqlDQDGGFStdvagsgvDSTGQAGTYFYTAPEIEQDWPKID 655
Cdd:cd14053  120 kpsIAHRDFKSKNVLL--KSDLTacIADFGLAlKF------EPGKSCG--------DTHGQVGTRRYMAPEVLEGAINFT 183
                        250
                 ....*....|....*....
gi 30694992  656 EKA----DMYSLGVVFFEL 670
Cdd:cd14053  184 RDAflriDMYAMGLVLWEL 202
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
533-728 3.61e-08

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


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 56.95  E-value: 3.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  533 ESTYLYIQM----EYCPRTLRQVFesynhFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFF--DARN--DIKIGD 604
Cdd:cd14176   86 KYVYVVTELmkggELLDKILRQKF-----FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdESGNpeSIRICD 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  605 FGLAKFLKLEqldqDGGFSTDVAgsgvdstgqagTYFYTAPEI--EQDWpkiDEKADMYSLGVVFFEL---WHPFGTAME 679
Cdd:cd14176  161 FGFAKQLRAE----NGLLMTPCY-----------TANFVAPEVleRQGY---DAACDIWSLGVLLYTMltgYTPFANGPD 222
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 30694992  680 R--HVILTNLKlKGELPLK---WVNEFPEQASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14176  223 DtpEEILARIG-SGKFSLSggyWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRH 275
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
533-730 3.66e-08

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: 56.56  E-value: 3.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  533 ESTYLYIQMEY------CPRTLRQvfesyNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFF-DARND---IKI 602
Cdd:cd14178   68 DGKFVYLVMELmrggelLDRILRQ-----KCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYmDESGNpesIRI 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  603 GDFGLAKFLKleqldqdggfstdvAGSGVDSTgQAGTYFYTAPEI--EQDWpkiDEKADMYSLGVVFFEL---WHPFGTA 677
Cdd:cd14178  143 CDFGFAKQLR--------------AENGLLMT-PCYTANFVAPEVlkRQGY---DAACDIWSLGILLYTMlagFTPFANG 204
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 30694992  678 MER--HVILTNLKlKGELPL---KWVNEFPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14178  205 PDDtpEEILARIG-SGKYALsggNWDSISDAAKDIVSKMLHVDPHQRLTAPQVLRHPW 261
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
429-668 3.72e-08

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


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 56.06  E-value: 3.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEipvNSRIVREVATLSRLQHQHVVRYYQAWFETGVVdpfaganwgsk 508
Cdd:cd14108    8 KEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKK---KTSARRELALLAELDHKSIVRFHDAFEKRRVV----------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  509 tagssmfsysgAVSTEIPEQDnnlestyLYIQMEYCPRTLRQVFESYnhfdkdfawhlIRQIVEGLAHIHGQGIIHRDFT 588
Cdd:cd14108   74 -----------IIVTELCHEE-------LLERITKRPTVCESEVRSY-----------MRQLLEGIEYLHQNDVLHLDLK 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  589 PNNIFF-DARND-IKIGDFGLAKFLKleqldqdggfstdvagSGVDSTGQAGTYFYTAPEIEQDWPkIDEKADMYSLGVV 666
Cdd:cd14108  125 PENLLMaDQKTDqVRICDFGNAQELT----------------PNEPQYCKYGTPEFVAPEIVNQSP-VSKVTDIWPVGVI 187

                 ..
gi 30694992  667 FF 668
Cdd:cd14108  188 AY 189
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
431-728 4.38e-08

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: 56.02  E-value: 4.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRLK--DKEIpvnsrIVREVATLSRLQHQHVVRYYQAWfetgvvdpfaganwgsk 508
Cdd:cd14104    8 LGRGQFGIVHRCVETSSKKTYMAKFVKVKgaDQVL-----VKKEISILNIARHRNILRLHESF----------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  509 tagssmfsysgavstEIPEQdnnLESTYLYIqmeycprTLRQVFESYN----HFDKDFAWHLIRQIVEGLAHIHGQGIIH 584
Cdd:cd14104   66 ---------------ESHEE---LVMIFEFI-------SGVDIFERITtarfELNEREIVSYVRQVCEALEFLHSKNIGH 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  585 RDFTPNNIFFDAR--NDIKIGDFGLAKFLKleqldqdggfstdvagSGVDSTGQAGTYFYTAPEIEQDwPKIDEKADMYS 662
Cdd:cd14104  121 FDIRPENIIYCTRrgSYIKIIEFGQSRQLK----------------PGDKFRLQYTSAEFYAPEVHQH-ESVSTATDMWS 183
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  663 LGVVFFELW---HPFGTAMERHVILTNLKLKGELPLKWVNEFPEQA-SLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14104  184 LGCLVYVLLsgiNPFEAETNQQTIENIRNAEYAFDDEAFKNISIEAlDFVDRLLVKERKSRMTAQEALNH 253
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
558-740 4.41e-08

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: 56.35  E-value: 4.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  558 FDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleqldqDGGFstdvagSGVDSTGQA 637
Cdd:cd05591   93 FDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCK---------EGIL------NGKTTTTFC 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  638 GTYFYTAPEIEQDWPkIDEKADMYSLGVVFFELWH---PFGTAMERHVILTNLKLKGELPLkWVNEfpEQASLLRRLMSP 714
Cdd:cd05591  158 GTPDYIAPEILQELE-YGPSVDWWALGVLMYEMMAgqpPFEADNEDDLFESILHDDVLYPV-WLSK--EAVSILKAFMTK 233
                        170       180       190
                 ....*....|....*....|....*....|...
gi 30694992  715 SPSDRPSATE-------LLKHAFPPRMESELLD 740
Cdd:cd05591  234 NPAKRLGCVAsqggedaIRQHPFFREIDWEALE 266
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
533-721 4.60e-08

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 56.08  E-value: 4.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  533 ESTYLYIQMEYCPR-TLRQVFESYNHFdKDFAWHL----IRQIVEGLAHIHGQG--IIHRDFTPNNIFFDARNDIKIGDF 605
Cdd:cd14026   68 EPEFLGIVTEYMTNgSLNELLHEKDIY-PDVAWPLrlriLYEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADF 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  606 GLAKFLKLeQLDQdggfstdvaGSGVDSTGQAGTYFYTAPEIEQDWPK--IDEKADMYSLGVVFFELW---HPFGTAMER 680
Cdd:cd14026  147 GLSKWRQL-SISQ---------SRSSKSAPEGGTIIYMPPEEYEPSQKrrASVKHDIYSYAIIMWEVLsrkIPFEEVTNP 216
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 30694992  681 HVILTNLkLKGELPLkwVNE------FPEQASLLRRLMS---PSPSDRPS 721
Cdd:cd14026  217 LQIMYSV-SQGHRPD--TGEdslpvdIPHRATLINLIESgwaQNPDERPS 263
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
536-670 4.78e-08

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


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 55.74  E-value: 4.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  536 YLYIQMEYCP-RTLRQ-VFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDaRNDIKIGDFGLakfLKL 613
Cdd:cd14152   70 HLAIITSFCKgRTLYSfVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGL---FGI 145
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30694992  614 EQLDQDGGFSTDVAGSgvdstgqAGTYFYTAPEI--------EQDWPKIDEKADMYSLGVVFFEL 670
Cdd:cd14152  146 SGVVQEGRRENELKLP-------HDWLCYLAPEIvremtpgkDEDCLPFSKAADVYAFGTIWYEL 203
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
433-727 4.94e-08

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: 55.69  E-value: 4.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  433 QGGFGHVVLCKNKLDGRQYAVKKIRLKDKEipvNSRIVREVATLSRLQHQHVVRYYQAWfetgvvdpfaganwgsktags 512
Cdd:cd14110   13 RGRFSVVRQCEEKRSGQMLAAKIIPYKPED---KQLVLREYQVLRRLSHPRIAQLHSAY--------------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  513 smfsysgavsteipeqdnnLESTYLYIQMEYC--PRTLRQVFE--SYNHFD-KDFAWhlirQIVEGLAHIHGQGIIHRDF 587
Cdd:cd14110   69 -------------------LSPRHLVLIEELCsgPELLYNLAErnSYSEAEvTDYLW----QILSAVDYLHSRRILHLDL 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  588 TPNNIFFDARNDIKIGDFGLAKFlkleqLDQDGGFSTDVAGSGVDStgqagtyfyTAPEIEQDWPKIDEkADMYSLGVVF 667
Cdd:cd14110  126 RSENMIITEKNLLKIVDLGNAQP-----FNQGKVLMTDKKGDYVET---------MAPELLEGQGAGPQ-TDIWAIGVTA 190
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30694992  668 FELW---HPFGTAMERHVILTNLKLKGELPLKWVNEFPEQASLLRRLMSPSPSDRPSATELLK 727
Cdd:cd14110  191 FIMLsadYPVSSDLNWERDRNIRKGKVQLSRCYAGLSGGAVNFLKSTLCAKPWGRPTASECLQ 253
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
425-730 5.20e-08

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: 56.56  E-value: 5.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDkeipvnsrivrevaTLSRLQHQHVVRYYQAWFEtgvvdpfAGAN 504
Cdd:cd05626    3 FVKIKTLGIGAFGEVCLACKVDTHALYAMKTLRKKD--------------VLNRNQVAHVKAERDILAE-------ADNE 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 WGSKtagssmFSYSgavsteIPEQDNnlestyLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGII 583
Cdd:cd05626   62 WVVK------LYYS------FQDKDN------LYFVMDYIPGgDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFI 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  584 HRDFTPNNIFFDARNDIKIGDFGLAK----------FLKLEQLDQDGGFSTDV--------AGSGVDSTGQ--------- 636
Cdd:cd05626  124 HRDIKPDNILIDLDGHIKLTDFGLCTgfrwthnskyYQKGSHIRQDSMEPSDLwddvsncrCGDRLKTLEQratkqhqrc 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  637 -----AGTYFYTAPEI--EQDWPKIdekADMYSLGVVFFELW---HPF--GTAMERHVILTNLKLKGELPLKwVNEFPEQ 704
Cdd:cd05626  204 lahslVGTPNYIAPEVllRKGYTQL---CDWWSVGVILFEMLvgqPPFlaPTPTETQLKVINWENTLHIPPQ-VKLSPEA 279
                        330       340
                 ....*....|....*....|....*...
gi 30694992  705 ASLLRRLMSPSPS--DRPSATELLKHAF 730
Cdd:cd05626  280 VDLITKLCCSAEErlGRNGADDIKAHPF 307
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
569-722 6.19e-08

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


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 55.36  E-value: 6.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  569 QIVEGLAHIHGQGIIHRDFTPNNIF---FDARN--DIKIGDFGLAKflkleQLDQDGGFstdvagsgvdstGQAGTYFYT 643
Cdd:cd14067  122 QIAAGLAYLHKKNIIFCDLKSDNILvwsLDVQEhiNIKLSDYGISR-----QSFHEGAL------------GVEGTPGYQ 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  644 APEIEqdwPKI--DEKADMYSLGVVFFELWHPFGTAMERHVILTNLKL-KGELPL----KWVNEFPEQAsLLRRLMSPSP 716
Cdd:cd14067  185 APEIR---PRIvyDEKVDMFSYGMVLYELLSGQRPSLGHHQLQIAKKLsKGIRPVlgqpEEVQFFRLQA-LMMECWDTKP 260

                 ....*.
gi 30694992  717 SDRPSA 722
Cdd:cd14067  261 EKRPLA 266
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
537-779 6.47e-08

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


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 56.09  E-value: 6.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  537 LYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKflklEQ 615
Cdd:cd05619   81 LFFVMEYLNGgDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCK----EN 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  616 LDQDGGFSTdvagsgvdstgQAGTYFYTAPEIEQDwPKIDEKADMYSLGVVFFELW---HPFGTAMERHvILTNLKLKGE 692
Cdd:cd05619  157 MLGDAKTST-----------FCGTPDYIAPEILLG-QKYNTSVDWWSFGVLLYEMLigqSPFHGQDEEE-LFQSIRMDNP 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  693 LPLKWVNEfpEQASLLRRLMSPSPSDRPSAT-ELLKHAFPPRMESELLDNilRIMQTSEDSSVYDRVVSVIFDEEVLEMK 771
Cdd:cd05619  224 FYPRWLEK--EAKDILVKLFVREPERRLGVRgDIRQHPFFREINWEALEE--REIEPPFKPKVKSPFDCSNFDKEFLNEK 299

                 ....*...
gi 30694992  772 SHQSSRSR 779
Cdd:cd05619  300 PRLSFADR 307
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
569-730 6.97e-08

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: 55.72  E-value: 6.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  569 QIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleqldqdggfsTDVAGSGVDSTGqAGTYFYTAPEIE 648
Cdd:cd05620  104 EIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCK--------------ENVFGDNRASTF-CGTPDYIAPEIL 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  649 QDWpKIDEKADMYSLGVVFFELW---HPFGTAMERHvILTNLKLKGELPLKWVNEfpEQASLLRRLMSPSPSDRPSATEL 725
Cdd:cd05620  169 QGL-KYTFSVDWWSFGVLLYEMLigqSPFHGDDEDE-LFESIRVDTPHYPRWITK--ESKDILEKLFERDPTRRLGVVGN 244

                 ....*.
gi 30694992  726 LK-HAF 730
Cdd:cd05620  245 IRgHPF 250
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
569-670 7.29e-08

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: 55.11  E-value: 7.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  569 QIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQldqdggfstdvagsgvDSTGQAGTYF---YTAP 645
Cdd:cd05068  112 QVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARVIKVED----------------EYEAREGAKFpikWTAP 175
                         90       100
                 ....*....|....*....|....*
gi 30694992  646 EiEQDWPKIDEKADMYSLGVVFFEL 670
Cdd:cd05068  176 E-AANYNRFSIKSDVWSFGILLTEI 199
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
431-670 7.51e-08

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: 55.58  E-value: 7.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGhvVLCKNKLDGRQYAVKK-IRLKDKEIP-VNSRIVREVATLSRLQHQHVVRYYQawfetgvvdpfaganwgsk 508
Cdd:cd14158   23 LGEGGFG--VVFKGYINDKNVAVKKlAAMVDISTEdLTKQFEQEIQVMAKCQHENLVELLG------------------- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  509 tagssmFSYSGAvsteipeqdnnlestYLYIQMEYCPR-TLRQVFESYNHfDKDFAWHLIRQIVEGLA----HIHGQGII 583
Cdd:cd14158   82 ------YSCDGP---------------QLCLVYTYMPNgSLLDRLACLND-TPPLSWHMRCKIAQGTAnginYLHENNHI 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  584 HRDFTPNNIFFDARNDIKIGDFGLAKflkleqldQDGGFSTDVAGSGVdstgqAGTYFYTAPEIEQDwpKIDEKADMYSL 663
Cdd:cd14158  140 HRDIKSANILLDETFVPKISDFGLAR--------ASEKFSQTIMTERI-----VGTTAYMAPEALRG--EITPKSDIFSF 204

                 ....*..
gi 30694992  664 GVVFFEL 670
Cdd:cd14158  205 GVVLLEI 211
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
565-670 9.18e-08

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: 54.80  E-value: 9.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  565 HLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGlakFLKLEQLdqdggfstdVAGSGVdstgqaGTYFYTA 644
Cdd:cd13975  106 QIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLG---FCKPEAM---------MSGSIV------GTPIHMA 167
                         90       100
                 ....*....|....*....|....*.
gi 30694992  645 PEIEQDwpKIDEKADMYSLGVVFFEL 670
Cdd:cd13975  168 PELFSG--KYDNSVDVYAFGILFWYL 191
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
448-725 9.57e-08

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


Pssm-ID: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 54.91  E-value: 9.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  448 GRQYAVKKIRLKDKEIPVNSR----IVREVatlsrlQHQHVVRYYQAwfetgVVDPfaganwgsktagssmfsysgavst 523
Cdd:cd14042   30 GNLVAIKKVNKKRIDLTREVLkelkHMRDL------QHDNLTRFIGA-----CVDP------------------------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  524 eipeqdNNLestylYIQMEYCPR-TLRQVFESYN-HFDKDFAWHLIRQIVEGLAHIHGQGII-HRDFTPNNIFFDARNDI 600
Cdd:cd14042   75 ------PNI-----CILTEYCPKgSLQDILENEDiKLDWMFRYSLIHDIVKGMHYLHDSEIKsHGNLKSSNCVVDSRFVL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  601 KIGDFGLAKFLKLEQLDQDGgfstdvagsgvdstgQAGTY--FYTAPE---IEQDWPKIDEKADMYSLGVVFFEL----- 670
Cdd:cd14042  144 KITDFGLHSFRSGQEPPDDS---------------HAYYAklLWTAPEllrDPNPPPPGTQKGDVYSFGIILQEIatrqg 208
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30694992  671 -WHPFGTAMERHVILTNLKLKGELP-----LKWVNEFPEQASLLRRLMSPSPSDRPSATEL 725
Cdd:cd14042  209 pFYEEGPDLSPKEIIKKKVRNGEKPpfrpsLDELECPDEVLSLMQRCWAEDPEERPDFSTL 269
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
431-668 1.05e-07

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


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 54.73  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVK---KIRLKDKEipvNSRIVREVATLSRLQHQHVVRYYQawfetgvvdpfaganwgs 507
Cdd:cd14082   11 LGSGQFGIVYGGKHRKTGRDVAIKvidKLRFPTKQ---ESQLRNEVAILQQLSHPGVVNLEC------------------ 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 ktagssMFsysgavstEIPEQdnnlestyLYIQMEYCPRTLRQVFESYNH--FDKDFAWHLIRQIVEGLAHIHGQGIIHR 585
Cdd:cd14082   70 ------MF--------ETPER--------VFVVMEKLHGDMLEMILSSEKgrLPERITKFLVTQILVALRYLHSKNIVHC 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  586 DFTPNNIFFDARND---IKIGDFGLAKFLKLEQldqdggFSTDVagsgvdstgqAGTYFYTAPEIEQDWPkIDEKADMYS 662
Cdd:cd14082  128 DLKPENVLLASAEPfpqVKLCDFGFARIIGEKS------FRRSV----------VGTPAYLAPEVLRNKG-YNRSLDMWS 190

                 ....*.
gi 30694992  663 LGVVFF 668
Cdd:cd14082  191 VGVIIY 196
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
425-730 1.09e-07

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: 55.12  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKeiPVNSRIVREVATLSRLQHQHVVRYYqawfetgvvdpfagan 504
Cdd:cd06655   21 YTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQ--PKKELIINEILVMKELKNPNIVNFL---------------- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysgavsteipeqDNNLESTYLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIH 584
Cdd:cd06655   83 ------------------------DSFLVGDELFVVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIH 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  585 RDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQdggfstdvagsgvdsTGQAGTYFYTAPEIEQDwPKIDEKADMYSLG 664
Cdd:cd06655  139 RDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSKR---------------STMVGTPYWMAPEVVTR-KAYGPKVDIWSLG 202
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30694992  665 VVFFELWH---PF---GTAMERHVILTNLKLKGELPLKWVNEFPEqasLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd06655  203 IMAIEMVEgepPYlneNPLRALYLIATNGTPELQNPEKLSPIFRD---FLNRCLEMDVEKRGSAKELLQHPF 271
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
558-730 1.13e-07

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: 55.27  E-value: 1.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  558 FDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKfLKLEQLDQDGGFstdvagsgvdstgqA 637
Cdd:cd05585   91 FDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCK-LNMKDDDKTNTF--------------C 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  638 GTYFYTAPEI--EQDWPKIdekADMYSLGVVFFELWH---PF----GTAMERHvILTNlklkgelPLKWVNEFPEQA-SL 707
Cdd:cd05585  156 GTPEYLAPELllGHGYTKA---VDWWTLGVLLYEMLTglpPFydenTNEMYRK-ILQE-------PLRFPDGFDRDAkDL 224
                        170       180
                 ....*....|....*....|....*.
gi 30694992  708 LRRLMSPSPSDR---PSATELLKHAF 730
Cdd:cd05585  225 LIGLLNRDPTKRlgyNGAQEIKNHPF 250
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
431-670 1.17e-07

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: 54.83  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVlcKNKLDGRQYAVKKIRlKDKEIP---VNSRIVREVATLSRLQHQHVVRyyqawfetgvvdpFAGanwgs 507
Cdd:cd14159    1 IGEGGFGCVY--QAVMRNTEYAVKRLK-EDSELDwsvVKNSFLTEVEKLSRFRHPNIVD-------------LAG----- 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 ktagssmfsysgavsteipeqdnnlestYLYIQMEYCprtLRQVF------ESYNHFDKDF---AWHLIRQIVEGLA--- 575
Cdd:cd14159   60 ----------------------------YSAQQGNYC---LIYVYlpngslEDRLHCQVSCpclSWSQRLHVLLGTArai 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  576 ---HIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEqldQDGGFSTDVAGSgvdSTGQaGTYFYTAPEIEQDwP 652
Cdd:cd14159  109 qylHSDSPSLIHGDVKSSNILLDAALNPKLGDFGLARFSRRP---KQPGMSSTLART---QTVR-GTLAYLPEEYVKT-G 180
                        250
                 ....*....|....*...
gi 30694992  653 KIDEKADMYSLGVVFFEL 670
Cdd:cd14159  181 TLSVEIDVYSFGVVLLEL 198
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
541-725 1.28e-07

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


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 54.19  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  541 MEYCPR-TLRQVFESYN-HFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFF-----DARNDIKIGDFGLAKFlkl 613
Cdd:cd14068   64 MELAPKgSLDALLQQDNaSLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIAQY--- 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  614 eqldqdggfstdVAGSGVDSTgqAGTYFYTAPEIEQDWPKIDEKADMYSLGVVFFELWhpfgTAMERhvILTNLKLKGEL 693
Cdd:cd14068  141 ------------CCRMGIKTS--EGTPGFRAPEVARGNVIYNQQADVYSFGLLLYDIL----TCGER--IVEGLKFPNEF 200
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 30694992  694 -----------PLKWVN--EFPEQASLLRRLMSPSPSDRPSATEL 725
Cdd:cd14068  201 delaiqgklpdPVKEYGcaPWPGVEALIKDCLKENPQCRPTSAQV 245
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
431-670 1.52e-07

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: 54.24  E-value: 1.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRL---KDKEipvnsRIVREVATLSRLQHQHVVRyyqawfetgVVDPFAGAnwGS 507
Cdd:cd14191   10 LGSGKFGQVFRLVEKKTKKVWAGKFFKAysaKEKE-----NIRQEISIMNCLHHPKLVQ---------CVDAFEEK--AN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 KTAGSSMFSySGAVSTEIPEQDNNLestylyiqmeycprTLRQVFEsynhfdkdfawhLIRQIVEGLAHIHGQGIIHRDF 587
Cdd:cd14191   74 IVMVLEMVS-GGELFERIIDEDFEL--------------TERECIK------------YMRQISEGVEYIHKQGIVHLDL 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  588 TPNNIFFDAR--NDIKIGDFGLAKflkleQLDQDGGFSTdvagsgvdstgQAGTYFYTAPEIeQDWPKIDEKADMYSLGV 665
Cdd:cd14191  127 KPENIMCVNKtgTKIKLIDFGLAR-----RLENAGSLKV-----------LFGTPEFVAPEV-INYEPIGYATDMWSIGV 189

                 ....*
gi 30694992  666 VFFEL 670
Cdd:cd14191  190 ICYIL 194
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
426-728 1.54e-07

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: 54.05  E-value: 1.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  426 EELKPLGQGGFGHVvlcKNKLDGRQYAVKkIRlkdkeiPVNSRIVREVATLSRLQHQHVVRYYQAWfetgvvdpfaganw 505
Cdd:cd14109   10 EDEKRAAQGAPFHV---TERSTGRNFLAQ-LR------YGDPFLMREVDIHNSLDHPNIVQMHDAY-------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  506 gsKTAGSSMFSYSGAVSTEIPEQDNNLESTylyiqmEYCPRTLRQVFesynhfdkdfawhlIRQIVEGLAHIHGQGIIHR 585
Cdd:cd14109   66 --DDEKLAVTVIDNLASTIELVRDNLLPGK------DYYTERQVAVF--------------VRQLLLALKHMHDLGIAHL 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  586 DFTPNNIFFdARNDIKIGDFGLAKFLkleqldQDGGFSTDVAGSGVdstgqagtyfYTAPEIEQDWPkIDEKADMYSLGV 665
Cdd:cd14109  124 DLRPEDILL-QDDKLKLADFGQSRRL------LRGKLTTLIYGSPE----------FVSPEIVNSYP-VTLATDMWSVGV 185
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30694992  666 VFFELW---HPFGTAMERHViLTNLK-----LKGELplkWVNEFPEQASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14109  186 LTYVLLggiSPFLGDNDRET-LTNVRsgkwsFDSSP---LGNISDDARDFIKKLLVYIPESRLTVDEALNH 252
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
565-670 2.03e-07

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


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 54.27  E-value: 2.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  565 HLIRQIVEGLAHIH-------GQG----IIHRDFTPNNIFFdaRNDIK--IGDFGLAkfLKLEQLDQDGgfstdvagsgv 631
Cdd:cd14140   96 HIAETMARGLSYLHedvprckGEGhkpaIAHRDFKSKNVLL--KNDLTavLADFGLA--VRFEPGKPPG----------- 160
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 30694992  632 DSTGQAGTYFYTAPEIEQDWPKIDEKA----DMYSLGVVFFEL 670
Cdd:cd14140  161 DTHGQVGTRRYMAPEVLEGAINFQRDSflriDMYAMGLVLWEL 203
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
428-670 2.36e-07

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: 53.94  E-value: 2.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  428 LKPLGQGGFGHVVLCKNKLDGRQY----AVKKIRLK---DKEIPVNSRIVREVATLSRLQHQHVVRYYQawfetgvvdpF 500
Cdd:cd14001    4 MKKLGYGTGVNVYLMKRSPRGGSSrspwAVKKINSKcdkGQRSLYQERLKEEAKILKSLNHPNIVGFRA----------F 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  501 AGANWGSktagssmfsysgavsteipeqdnnlestyLYIQMEYCPRTLRQVFESYNHFDKD---------FAWHLIRqiv 571
Cdd:cd14001   74 TKSEDGS-----------------------------LCLAMEYGGKSLNDLIEERYEAGLGpfpaatilkVALSIAR--- 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  572 eGLAHIHGQG-IIHRDFTPNNIFFdaRND---IKIGDFGLAKflkleQLDQDGGFSTDVAGSGVdstgqaGTYFYTAPEI 647
Cdd:cd14001  122 -ALEYLHNEKkILHGDIKSGNVLI--KGDfesVKLCDFGVSL-----PLTENLEVDSDPKAQYV------GTEPWKAKEA 187
                        250       260
                 ....*....|....*....|...
gi 30694992  648 EQDWPKIDEKADMYSLGVVFFEL 670
Cdd:cd14001  188 LEEGGVITDKADIFAYGLVLWEM 210
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
569-670 2.47e-07

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: 53.44  E-value: 2.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  569 QIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqDGGFstdvagsgvdsTGQAGTYF---YTAP 645
Cdd:cd05034  100 QIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLIE------DDEY-----------TAREGAKFpikWTAP 162
                         90       100
                 ....*....|....*....|....*
gi 30694992  646 EIEQDwPKIDEKADMYSLGVVFFEL 670
Cdd:cd05034  163 EAALY-GRFTIKSDVWSFGILLYEI 186
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
423-670 2.61e-07

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: 54.28  E-value: 2.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  423 NDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEiPVNSRIVREVATLSRLQHQHVVRYYQAWFEtgvvdpfag 502
Cdd:cd06649    5 DDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEIKP-AIRNQIIRELQVLHECNSPYIVGFYGAFYS--------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgsktagssmfsySGAVSTEIPEQDNNlestylyiqmeycprTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQ-G 581
Cdd:cd06649   75 ---------------DGEISICMEHMDGG---------------SLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKhQ 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGlakflkleqldqdggfstdVAGSGVDSTGQA--GTYFYTAPEIEQDwPKIDEKAD 659
Cdd:cd06649  125 IMHRDVKPSNILVNSRGEIKLCDFG-------------------VSGQLIDSMANSfvGTRSYMSPERLQG-THYSVQSD 184
                        250
                 ....*....|.
gi 30694992  660 MYSLGVVFFEL 670
Cdd:cd06649  185 IWSMGLSLVEL 195
PRK12421 PRK12421
ATP phosphoribosyltransferase regulatory subunit; Provisional
977-1088 2.90e-07

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 237098  Cd Length: 392  Bit Score: 54.21  E-value: 2.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   977 RQLLQELKLPEAVVNRLQTVAsRFCGDADqALPRLRGAL-RADRPTRKALDELSNLLTYLRVWRIEEHVHIDVlmppTE- 1054
Cdd:PRK12421  199 AEVCQNLGVGSDLRRMFYALA-RLNGGLE-ALDRALSVLaLQDAAIRQALDELKTLAAHLKNRWPELPVSIDL----AEl 272
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 30694992  1055 ---SYHRNLFFQVFLtkenssgtSNDGVLLAVGGRYD 1088
Cdd:PRK12421  273 rgyHYHTGLVFAAYI--------PGRGQALARGGRYD 301
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
424-670 3.01e-07

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: 53.21  E-value: 3.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKlDGRQYAVKKIRLKDKeiPVNSRIVREVATLSRLQHQHVVRYYqawfetGVVdpfaga 503
Cdd:cd05148    7 EFTLERKLGSGYFGEVWEGLWK-NRVRVAIKILKSDDL--LKQQDFQKEVQALKRLRHKHLISLF------AVC------ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgskTAGSSMFsysgaVSTEIPEQDNNLEstYLYIQMEYCPRTLRQVfesynhfdkDFAWhlirQIVEGLAHIHGQGII 583
Cdd:cd05148   72 -----SVGEPVY-----IITELMEKGSLLA--FLRSPEGQVLPVASLI---------DMAC----QVAEGMAYLEEQNSI 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  584 HRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqDGGFSTDvagsgvdstGQAGTYFYTAPEiEQDWPKIDEKADMYSL 663
Cdd:cd05148  127 HRDLAARNILVGEDLVCKVADFGLARLIK------EDVYLSS---------DKKIPYKWTAPE-AASHGTFSTKSDVWSF 190

                 ....*..
gi 30694992  664 GVVFFEL 670
Cdd:cd05148  191 GILLYEM 197
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
565-670 3.20e-07

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


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 53.51  E-value: 3.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  565 HLIRQIVEGLAHIHGQ----------GIIHRDFTPNNIFFDARNDIKIGDFGLAkfLKLEqldqdggfstdVAGSGVDST 634
Cdd:cd14141   96 HIAQTMARGLAYLHEDipglkdghkpAIAHRDIKSKNVLLKNNLTACIADFGLA--LKFE-----------AGKSAGDTH 162
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 30694992  635 GQAGTYFYTAPEIEQDWPKIDEKA----DMYSLGVVFFEL 670
Cdd:cd14141  163 GQVGTRRYMAPEVLEGAINFQRDAflriDMYAMGLVLWEL 202
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
568-725 3.27e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 54.23  E-value: 3.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   568 RQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAkflkleqldqdgGFSTDVAGSgvDSTGQAGTYFYTAPEI 647
Cdd:PHA03212  189 RSVLRAIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGAA------------CFPVDINAN--KYYGWAGTIATNAPEL 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   648 EQDWPkIDEKADMYSLGVVFFELWHPFGTAMERHVILTN----------LKLKGELPlkwvNEFPEQA-SLLRRLM---- 712
Cdd:PHA03212  255 LARDP-YGPAVDIWSAGIVLFEMATCHDSLFEKDGLDGDcdsdrqikliIRRSGTHP----NEFPIDAqANLDEIYigla 329
                         170
                  ....*....|....*.
gi 30694992   713 ---SPSPSDRPSATEL 725
Cdd:PHA03212  330 kksSRKPGSRPLWTNL 345
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
569-670 4.06e-07

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


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 53.55  E-value: 4.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  569 QIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleqldqDGGFstdvagSGVDSTGQAGTYFYTAPEIE 648
Cdd:cd05587  105 EIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCK---------EGIF------GGKTTRTFCGTPDYIAPEII 169
                         90       100
                 ....*....|....*....|..
gi 30694992  649 QDWPkIDEKADMYSLGVVFFEL 670
Cdd:cd05587  170 AYQP-YGKSVDWWAYGVLLYEM 190
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
565-676 4.76e-07

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: 52.70  E-value: 4.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  565 HLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDaRNDIKIGDFGLAKFLKLEQldqdggfstdvAGSGVDSTG-QAGTYFYT 643
Cdd:cd14153  101 QIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFTISGVLQ-----------AGRREDKLRiQSGWLCHL 168
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 30694992  644 APEI--------EQDWPKIDEKADMYSLGVVFFEL----WhPFGT 676
Cdd:cd14153  169 APEIirqlspetEEDKLPFSKHSDVFAFGTIWYELhareW-PFKT 212
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
564-670 4.94e-07

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 52.76  E-value: 4.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  564 WHLIRQIVEGLAHIH----GQG-----IIHRDFTPNNIFFDARNDIKIGDFGLAkfLKLE-QLDQDggfstDVAGSgvds 633
Cdd:cd14055  101 CKMAGSLARGLAHLHsdrtPCGrpkipIAHRDLKSSNILVKNDGTCVLADFGLA--LRLDpSLSVD-----ELANS---- 169
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 30694992  634 tGQAGTYFYTAPEIEQDwpKID-------EKADMYSLGVVFFEL 670
Cdd:cd14055  170 -GQVGTARYMAPEALES--RVNledlesfKQIDVYSMALVLWEM 210
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
566-730 5.15e-07

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


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 52.96  E-value: 5.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  566 LIRQIVEGLAHIHGQ-GIIHRDFTPNNIFFDARN-DIKIGDFGLAKFLkleqldqDGGFSTDVagsgvdSTGQagtyfYT 643
Cdd:cd14136  124 IARQVLQGLDYLHTKcGIIHTDIKPENVLLCISKiEVKIADLGNACWT-------DKHFTEDI------QTRQ-----YR 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  644 APE--IEQDWpkiDEKADMYSLGVVFFE------LWHPFGT------------------AMERHVILTNLKL------KG 691
Cdd:cd14136  186 SPEviLGAGY---GTPADIWSTACMAFElatgdyLFDPHSGedysrdedhlaliiellgRIPRSIILSGKYSreffnrKG 262
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 30694992  692 EL---------PLKWV----NEFPEQ-----ASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14136  263 ELrhisklkpwPLEDVlvekYKWSKEeakefASFLLPMLEYDPEKRATAAQCLQHPW 319
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
431-727 5.31e-07

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


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 52.30  E-value: 5.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVlcKNKLDGRQYAVKKIRLK-DKEIPVNSRIVREVATL-SRLQHQHVVRYyqawfeTGVVdpfaganwgsk 508
Cdd:cd14148    2 IGVGGFGKVY--KGLWRGEEVAVKAARQDpDEDIAVTAENVRQEARLfWMLQHPNIIAL------RGVC----------- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  509 tagssmfsysgavsteipeqdnnLESTYLYIQMEYCPR-TLRQVFESynhfdKDFAWHLIR----QIVEGLAHIHGQG-- 581
Cdd:cd14148   63 -----------------------LNPPHLCLVMEYARGgALNRALAG-----KKVPPHVLVnwavQIARGMNYLHNEAiv 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 -IIHRDFTPNNIFF--DARND------IKIGDFGLAKflkleqldqDGGFSTDVAGsgvdstgqAGTYFYTAPEIEQdWP 652
Cdd:cd14148  115 pIIHRDLKSSNILIlePIENDdlsgktLKITDFGLAR---------EWHKTTKMSA--------AGTYAWMAPEVIR-LS 176
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  653 KIDEKADMYSLGVVFFELWH-------------PFGTAMERhviLTnlklkgeLPLKwvNEFPEQ-ASLLRRLMSPSPSD 718
Cdd:cd14148  177 LFSKSSDVWSFGVLLWELLTgevpyreidalavAYGVAMNK---LT-------LPIP--STCPEPfARLLEECWDPDPHG 244

                 ....*....
gi 30694992  719 RPSATELLK 727
Cdd:cd14148  245 RPDFGSILK 253
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
569-726 5.78e-07

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


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 52.35  E-value: 5.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  569 QIVEGLAHIHGQGI---IHRDFTPNNIFF-------DARNDI-KIGDFGLAKflkleqldqDGGFSTDVAGsgvdstgqA 637
Cdd:cd14145  112 QIARGMNYLHCEAIvpvIHRDLKSSNILIlekvengDLSNKIlKITDFGLAR---------EWHRTTKMSA--------A 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  638 GTYFYTAPEIEQDwPKIDEKADMYSLGVVFFELWH---PF----GTAMERHVILTNLKLKgeLPlkwvNEFPEQ-ASLLR 709
Cdd:cd14145  175 GTYAWMAPEVIRS-SMFSKGSDVWSYGVLLWELLTgevPFrgidGLAVAYGVAMNKLSLP--IP----STCPEPfARLME 247
                        170
                 ....*....|....*..
gi 30694992  710 RLMSPSPSDRPSATELL 726
Cdd:cd14145  248 DCWNPDPHSRPPFTNIL 264
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
565-725 6.41e-07

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: 52.42  E-value: 6.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  565 HLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKleqldqdggfstdvagsGVDSTGQAGTYF--- 641
Cdd:cd05052  108 YMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMT-----------------GDTYTAHAGAKFpik 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  642 YTAPEiEQDWPKIDEKADMYSLGVVFFELwHPFGTAMERHVILTNL--KLKGELPLKWVNEFPEQA-SLLRRLMSPSPSD 718
Cdd:cd05052  171 WTAPE-SLAYNKFSIKSDVWAFGVLLWEI-ATYGMSPYPGIDLSQVyeLLEKGYRMERPEGCPPKVyELMRACWQWNPSD 248

                 ....*..
gi 30694992  719 RPSATEL 725
Cdd:cd05052  249 RPSFAEI 255
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
425-730 6.63e-07

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: 52.42  E-value: 6.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKeiPVNSRIVREVATLSRLQHQHVVRYYqawfetgvvdpfagan 504
Cdd:cd06654   22 YTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQ--PKKELIINEILVMRENKNPNIVNYL---------------- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysgavsteipeqDNNLESTYLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIH 584
Cdd:cd06654   84 ------------------------DSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIH 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  585 RDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQdggfstdvagsgvdsTGQAGTYFYTAPEIEQDwPKIDEKADMYSLG 664
Cdd:cd06654  140 RDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR---------------STMVGTPYWMAPEVVTR-KAYGPKVDIWSLG 203
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30694992  665 VVFFELWH---PF---GTAMERHVILTNLKLKGELPLKWVNEFPEqasLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd06654  204 IMAIEMIEgepPYlneNPLRALYLIATNGTPELQNPEKLSAIFRD---FLNRCLEMDVEKRGSAKELLQHQF 272
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
431-670 7.27e-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: 52.25  E-value: 7.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNsrIVREVATLSRLQHQHVVRYyqawfeTGVVdpfaganwgskta 510
Cdd:cd14222    1 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKT--FLTEVKVMRSLDHPNVLKF------IGVL------------- 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  511 gssmfsysgavsteipEQDNNLESTYLYIQMEycprTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPN 590
Cdd:cd14222   60 ----------------YKDKRLNLLTEFIEGG----TLKDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSH 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  591 NIFFDARNDIKIGDFGLAKFLKLEQL--DQDGGFSTDVAGSGVDSTGQ---AGTYFYTAPEIeQDWPKIDEKADMYSLGV 665
Cdd:cd14222  120 NCLIKLDKTVVVADFGLSRLIVEEKKkpPPDKPTTKKRTLRKNDRKKRytvVGNPYWMAPEM-LNGKSYDEKVDIFSFGI 198

                 ....*
gi 30694992  666 VFFEL 670
Cdd:cd14222  199 VLCEI 203
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
573-727 1.24e-06

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: 51.16  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  573 GLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleqlDQDGGFstdVAGSGVDSTgqagTYFYTAPEiEQDWP 652
Cdd:cd05085  106 GMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSR-------QEDDGV---YSSSGLKQI----PIKWTAPE-ALNYG 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  653 KIDEKADMYSLGVVffeLWHPFGTAMERHVILTNLKLKGELPLKWVNEFPEQA-----SLLRRLMSPSPSDRPSATELLK 727
Cdd:cd05085  171 RYSSESDVWSFGIL---LWETFSLGVCPYPGMTNQQAREQVEKGYRMSAPQRCpediyKIMQRCWDYNPENRPKFSELQK 247
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
425-607 1.52e-06

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: 51.97  E-value: 1.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEIPVNSRIVR-EVATLSRLQHQHVVRYYqawfetgvvdpfaga 503
Cdd:cd05625    3 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKaERDILAEADNEWVVRLY--------------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 nwgsktagssmFSYSgavsteipEQDNnlestyLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGI 582
Cdd:cd05625   68 -----------YSFQ--------DKDN------LYFVMDYIPGgDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGF 122
                        170       180
                 ....*....|....*....|....*
gi 30694992  583 IHRDFTPNNIFFDARNDIKIGDFGL 607
Cdd:cd05625  123 IHRDIKPDNILIDRDGHIKLTDFGL 147
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
539-610 1.54e-06

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 50.29  E-value: 1.54e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30694992    539 IQMEYCP-RTLRQVFESYNHfdkdfawHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARnDIKIGDFGLAKF 610
Cdd:TIGR03724   74 IVMEYIEgKPLKDVIEENGD-------ELAREIGRLVGKLHKAGIVHGDLTTSNIIVRDD-KVYLIDFGLGKY 138
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
403-670 1.55e-06

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


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 51.20  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  403 WEPPSDScepnaslpssrylndFEELKPLGQGGFGHVVLCKNKlDGRQYAVKKirLKDKEIPVNSrIVREVATLSRLQHQ 482
Cdd:cd05072    2 WEIPRES---------------IKLVKKLGAGQFGEVWMGYYN-NSTKVAVKT--LKPGTMSVQA-FLEEANLMKTLQHD 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  483 HVVRYYqawfetgvvdpfaganwgsktagssmfsysGAVSTEIPeqdnnlestyLYIQMEYCPRTLRQVFESYNHFDKDF 562
Cdd:cd05072   63 KLVRLY------------------------------AVVTKEEP----------IYIITEYMAKGSLLDFLKSDEGGKVL 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  563 AWHLI---RQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLdqdggfstdvagsgvdsTGQAGT 639
Cdd:cd05072  103 LPKLIdfsAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEY-----------------TAREGA 165
                        250       260       270
                 ....*....|....*....|....*....|....
gi 30694992  640 YF---YTAPEiEQDWPKIDEKADMYSLGVVFFEL 670
Cdd:cd05072  166 KFpikWTAPE-AINFGSFTIKSDVWSFGILLYEI 198
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
442-670 1.55e-06

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


Pssm-ID: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 51.01  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  442 CKNKLDGRQYAVKKIrlKDKEIPVNSRIVREVATLSRLQHQHVVRyyqawfetgvvdpFAGAnwgsktagssmfsysgav 521
Cdd:cd14045   24 QTGIYDGRTVAIKKI--AKKSFTLSKRIRKEVKQVRELDHPNLCK-------------FIGG------------------ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  522 STEIPEqdnnlestyLYIQMEYCPR-TLRQVFESYN-HFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARND 599
Cdd:cd14045   71 CIEVPN---------VAIITEYCPKgSLNDVLLNEDiPLNWGFRFSFATDIARGMAYLHQHKIYHGRLKSSNCVIDDRWV 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30694992  600 IKIGDFGLAKFLKleqldQDGgfstdvaGSGVDSTGQAGTYFYTAPEIEQ--DWpKIDEKADMYSLGVVFFEL 670
Cdd:cd14045  142 CKIADYGLTTYRK-----EDG-------SENASGYQQRLMQVYLPPENHSntDT-EPTQATDVYSYAIILLEI 201
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
429-727 1.94e-06

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


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 51.12  E-value: 1.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVLC-KNKLDGR----QYAVKKirLKDKEIPVNSR-IVREVATLSRLQHQHVVRYYQAWFETGVvdPFAG 502
Cdd:cd05045    6 KTLGEGEFGKVVKAtAFRLKGRagytTVAVKM--LKENASSSELRdLLSEFNLLKQVNHPHVIKLYGACSQDGP--LLLI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 ANWGSKTAGSSMFSYSGAVSTEIPEQDNNLESTYLYIQMEYcPRTLRQVFEsynhfdkdFAWhlirQIVEGLAHIHGQGI 582
Cdd:cd05045   82 VEYAKYGSLRSFLRESRKVGPSYLGSDGNRNSSYLDNPDER-ALTMGDLIS--------FAW----QISRGMQYLAEMKL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  583 IHRDFTPNNIFFDARNDIKIGDFGLAKflklEQLDQDggfstdvagSGVDSTGQAGTYFYTAPEIEQDwPKIDEKADMYS 662
Cdd:cd05045  149 VHRDLAARNVLVAEGRKMKISDFGLSR----DVYEED---------SYVKRSKGRIPVKWMAIESLFD-HIYTTQSDVWS 214
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  663 LGVVFFEL----WHPF-GTAMERhviLTNLKLKGELPLKWVNEFPEQASLLRRLMSPSPSDRPSATELLK 727
Cdd:cd05045  215 FGVLLWEIvtlgGNPYpGIAPER---LFNLLKTGYRMERPENCSEEMYNLMLTCWKQEPDKRPTFADISK 281
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
425-730 2.04e-06

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: 51.26  E-value: 2.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKeiPVNSRIVREVATLSRLQHQHVVRYYqawfetgvvdpfagan 504
Cdd:cd06656   21 YTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQ--PKKELIINEILVMRENKNPNIVNYL---------------- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 wgsktagssmfsysgavsteipeqDNNLESTYLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIH 584
Cdd:cd06656   83 ------------------------DSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIH 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  585 RDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQdggfstdvagsgvdsTGQAGTYFYTAPEIEQDwPKIDEKADMYSLG 664
Cdd:cd06656  139 RDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR---------------STMVGTPYWMAPEVVTR-KAYGPKVDIWSLG 202
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30694992  665 VVFFELWH---PF---GTAMERHVILTNLKLKGELPLKWVNEFPEqasLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd06656  203 IMAIEMVEgepPYlneNPLRALYLIATNGTPELQNPERLSAVFRD---FLNRCLEMDVDRRGSAKELLQHPF 271
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
431-728 2.32e-06

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


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 50.81  E-value: 2.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVlcKNKLDGRQYAVKKIRLK-DKEIPVNSRIVREVATL-SRLQHQHVVRYYQAWFETG---VVDPFAGANW 505
Cdd:cd14146    2 IGVGGFGKVY--RATWKGQEVAVKAARQDpDEDIKATAESVRQEAKLfSMLRHPNIIKLEGVCLEEPnlcLVMEFARGGT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  506 GSKTAGSSMFSYSGAVSTEIPeqdnnlestylyiqmeycPRTLrqvfesynhfdkdFAWHLirQIVEGLAHIHGQG---I 582
Cdd:cd14146   80 LNRALAAANAAPGPRRARRIP------------------PHIL-------------VNWAV--QIARGMLYLHEEAvvpI 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  583 IHRDFTPNNIFF--------DARNDIKIGDFGLAKflkleQLDQDGGFSTdvagsgvdstgqAGTYFYTAPEIEQDwPKI 654
Cdd:cd14146  127 LHRDLKSSNILLlekiehddICNKTLKITDFGLAR-----EWHRTTKMSA------------AGTYAWMAPEVIKS-SLF 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  655 DEKADMYSLGVVFFELWH---PF----GTAMERHVILTNLKLKgeLPlkwvNEFPEQ-ASLLRRLMSPSPSDRPSATELL 726
Cdd:cd14146  189 SKGSDIWSYGVLLWELLTgevPYrgidGLAVAYGVAVNKLTLP--IP----STCPEPfAKLMKECWEQDPHIRPSFALIL 262

                 ..
gi 30694992  727 KH 728
Cdd:cd14146  263 EQ 264
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
431-670 2.43e-06

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: 51.10  E-value: 2.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRLKdkeiPVNSRIVR-EVATLSRLQ-------HQHVVRYYqawfetgvvDPFag 502
Cdd:cd14212    7 LGQGTFGQVVKCQDLKTNKLVAVKVLKNK----PAYFRQAMlEIAILTLLNtkydpedKHHIVRLL---------DHF-- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgsktagssMFSYSGAVSTEipeqdnnLESTYLYiQMeycprtLRQVfeSYNHFDKDFAWHLIRQIVEGLAHIHGQGI 582
Cdd:cd14212   72 -----------MHHGHLCIVFE-------LLGVNLY-EL------LKQN--QFRGLSLQLIRKFLQQLLDALSVLKDARI 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  583 IHRDFTPNNIFFDARN--DIKIGDFGLAKFlkleqldqdggfstdvAGSGVDSTGQagTYFYTAPEIEQDWPkIDEKADM 660
Cdd:cd14212  125 IHCDLKPENILLVNLDspEIKLIDFGSACF----------------ENYTLYTYIQ--SRFYRSPEVLLGLP-YSTAIDM 185
                        250
                 ....*....|
gi 30694992  661 YSLGVVFFEL 670
Cdd:cd14212  186 WSLGCIAAEL 195
PLN03225 PLN03225
Serine/threonine-protein kinase SNT7; Provisional
422-730 2.58e-06

Serine/threonine-protein kinase SNT7; Provisional


Pssm-ID: 215638 [Multi-domain]  Cd Length: 566  Bit Score: 51.72  E-value: 2.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   422 LNDFEELKPLGQGGFGHV----VLCKNKLDGRQYAVKKIR-LKDKEIPVNSRIVREVATlsrlqhqhVVRYYQAWFETGV 496
Cdd:PLN03225  131 KDDFVLGKKLGEGAFGVVykasLVNKQSKKEGKYVLKKATeYGAVEIWMNERVRRACPN--------SCADFVYGFLEPV 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   497 VDPFAGANW------GSKTAGSSMfsysgaVSTEIPEqdnNLEsTYLYIQMEYCPRTLRQvfesynhfDKDFAWHLIRQI 570
Cdd:PLN03225  203 SSKKEDEYWlvwryeGESTLADLM------QSKEFPY---NVE-PYLLGKVQDLPKGLER--------ENKIIQTIMRQI 264
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   571 VEGLAHIHGQGIIHRDFTPNNIFFD-ARNDIKIGDFGLAKFLKLEQLDQDGGFSTDVAgsgvdstgqagtyfYTAPE--- 646
Cdd:PLN03225  265 LFALDGLHSTGIVHRDVKPQNIIFSeGSGSFKIIDLGAAADLRVGINYIPKEFLLDPR--------------YAAPEqyi 330
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   647 IEQDWPK------------------IDEKADMYSLGVVFFELWHPfGTAMERHVILTNLKLK--GELPLKWVNEFPEQAS 706
Cdd:PLN03225  331 MSTQTPSapsapvatalspvlwqlnLPDRFDIYSAGLIFLQMAFP-NLRSDSNLIQFNRQLKrnDYDLVAWRKLVEPRAS 409
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 30694992   707 -------------------LLRRLMSPSPSDRPSATELLKHAF 730
Cdd:PLN03225  410 pdlrrgfevldldggagweLLKSMMRFKGRQRISAKAALAHPY 452
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
429-671 3.96e-06

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: 50.04  E-value: 3.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVL--CKNKLDGRQYAVKKIR-LKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAWFETgvvDPFAGANW 505
Cdd:cd05093   11 RELGEGAFGKVFLaeCYNLCPEQDKILVAVKtLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEG---DPLIMVFE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  506 GSKTAGSSMFSYS-GAVSTEIPEQDNNLESTYlyiqmeycPRTLrqvfesynhfdkdfawHLIRQIVEGLAHIHGQGIIH 584
Cdd:cd05093   88 YMKHGDLNKFLRAhGPDAVLMAEGNRPAELTQ--------SQML----------------HIAQQIAAGMVYLASQHFVH 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  585 RDFTPNNIFFDARNDIKIGDFGLAKFLkleqldqdggFSTDVAGSGvdstGQAGTYFYTAPEIEQDWPKIDEKADMYSLG 664
Cdd:cd05093  144 RDLATRNCLVGENLLVKIGDFGMSRDV----------YSTDYYRVG----GHTMLPIRWMPPESIMYRKFTTESDVWSLG 209

                 ....*..
gi 30694992  665 VVFFELW 671
Cdd:cd05093  210 VVLWEIF 216
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
568-728 4.00e-06

Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. This subfamily is composed of NRBP1, also called MLF1-adaptor molecule (MADM), and MADML. NRBP1 was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking. MADML (for MADM-Like) has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. The NRBP1-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270886 [Multi-domain]  Cd Length: 256  Bit Score: 49.84  E-value: 4.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  568 RQIVEGLAHIHG--QGIIHRDFTPNNIFFDARNDIKIGDFglakflkleqldqdggfSTDVAGSGVDSTGQA-GTYFYTA 644
Cdd:cd13984  110 TQILSALSYLHScdPPIIHGNLTCDTIFIQHNGLIKIGSV-----------------APDAIHNHVKTCREEhRNLHFFA 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  645 PEIEQDwPKIDEKADMYSLGVVFFELwhpfgTAMERHVILTNLKLKGELPLKWVN--EFPEQASLLRRLMSPSPSDRPSA 722
Cdd:cd13984  173 PEYGYL-EDVTTAVDIYSFGMCALEM-----AALEIQSNGEKVSANEEAIIRAIFslEDPLQKDFIRKCLSVAPQDRPSA 246

                 ....*.
gi 30694992  723 TELLKH 728
Cdd:cd13984  247 RDLLFH 252
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
431-730 4.04e-06

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: 50.08  E-value: 4.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVlckNKLDGRQYA-VKKIRLKDKEIPV--NSRIVREVATLSRLQHQHVVRYYQAWfetgvvdpfaganwGS 507
Cdd:cd14032    9 LGRGSFKTVY---KGLDTETWVeVAWCELQDRKLTKveRQRFKEEAEMLKGLQHPNIVRFYDFW--------------ES 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 KTAGSSMFsysgAVSTEIpeQDNNLESTYLYIQMEYCPRTLRqvfesynhfdkdfAWhlIRQIVEGLAHIHGQG--IIHR 585
Cdd:cd14032   72 CAKGKRCI----VLVTEL--MTSGTLKTYLKRFKVMKPKVLR-------------SW--CRQILKGLLFLHTRTppIIHR 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  586 DFTPNNIFFDA-RNDIKIGDFGLAKFlkleqldQDGGFSTDVagsgvdstgqAGTYFYTAPEIEQDwpKIDEKADMYSLG 664
Cdd:cd14032  131 DLKCDNIFITGpTGSVKIGDLGLATL-------KRASFAKSV----------IGTPEFMAPEMYEE--HYDESVDVYAFG 191
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  665 VVFFELW---HPFGTAMERHVILTNLKLkGELPLKWVN-EFPEQASLLRRLMSPSPSDRPSATELLKHAF 730
Cdd:cd14032  192 MCMLEMAtseYPYSECQNAAQIYRKVTC-GIKPASFEKvTDPEIKEIIGECICKNKEERYEIKDLLSHAF 260
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
425-670 4.47e-06

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


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 50.14  E-value: 4.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIrlkdKEIPVNSRIVR-EVATLSRLQHQ-----HVVRYYQAwfetgvvd 498
Cdd:cd14211    1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKIL----KNHPSYARQGQiEVSILSRLSQEnadefNFVRAYEC-------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  499 pFAGANwgsKTAgssmfsysgaVSTEIPEQdnNLestYLYI-QMEYCPRTLRQVFEsynhfdkdfawhLIRQIVEGLAHI 577
Cdd:cd14211   69 -FQHKN---HTC----------LVFEMLEQ--NL---YDFLkQNKFSPLPLKYIRP------------ILQQVLTALLKL 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  578 HGQGIIHRDFTPNNIFF----DARNDIKIGDFGLAKFlkleqldqdggFSTDVAGSGVDSTgqagtyFYTAPEIEQDWPk 653
Cdd:cd14211  118 KSLGLIHADLKPENIMLvdpvRQPYRVKVIDFGSASH-----------VSKAVCSTYLQSR------YYRAPEIILGLP- 179
                        250
                 ....*....|....*..
gi 30694992  654 IDEKADMYSLGVVFFEL 670
Cdd:cd14211  180 FCEAIDMWSLGCVIAEL 196
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
538-610 4.55e-06

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: 48.03  E-value: 4.55e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30694992  538 YIQMEYCP-RTLRQVFESYNHFDKdfawhLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDaRNDIKIGDFGLAKF 610
Cdd:COG3642   32 DLVMEYIEgETLADLLEEGELPPE-----LLRELGRLLARLHRAGIVHGDLTTSNILVD-DGGVYLIDFGLARY 99
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
582-725 4.71e-06

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 49.80  E-value: 4.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGLAKFlkleqldqdGGFSTDvagSGVDSTGQAGTYFYTAPE--IEQDWPkIDEKAD 659
Cdd:cd14025  115 LLHLDLKPANILLDAHYHVKISDFGLAKW---------NGLSHS---HDLSRDGLRGTIAYLPPErfKEKNRC-PDTKHD 181
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30694992  660 MYSLGVVFFELW---HPF-GTAMERHVILTNLK-LKGELPL---KWVNEFPEQASLLRRLMSPSPSDRPSATEL 725
Cdd:cd14025  182 VYSFAIVIWGILtqkKPFaGENNILHIMVKVVKgHRPSLSPiprQRPSECQQMICLMKRCWDQDPRKRPTFQDI 255
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
570-726 4.74e-06

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: 49.56  E-value: 4.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  570 IVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLdqdggfstdvagsgvdsTGQAGTYF---YTAPE 646
Cdd:cd05112  109 VCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDDQY-----------------TSSTGTKFpvkWSSPE 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  647 IEQdWPKIDEKADMYSLGVVFFELWHPFGTAMERHvilTNLKLKGELPLKWVNEFPEQAS-----LLRRLMSPSPSDRPS 721
Cdd:cd05112  172 VFS-FSRYSSKSDVWSFGVLMWEVFSEGKIPYENR---SNSEVVEDINAGFRLYKPRLASthvyeIMNHCWKERPEDRPS 247

                 ....*
gi 30694992  722 ATELL 726
Cdd:cd05112  248 FSLLL 252
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
569-724 5.07e-06

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: 49.47  E-value: 5.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  569 QIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAkflkleqldqdggfsTDVAGSgvdSTGQAGTYFYTAPEIe 648
Cdd:cd05576  121 EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRW---------------SEVEDS---CDSDAIENMYCAPEV- 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  649 QDWPKIDEKADMYSLGVVFFELW--------HPFGtaMERHVILtnlklkgELPlKWVNEfpEQASLLRRLMSPSPSDRP 720
Cdd:cd05576  182 GGISEETEACDWWSLGALLFELLtgkalvecHPAG--INTHTTL-------NIP-EWVSE--EARSLLQQLLQFNPTERL 249

                 ....
gi 30694992  721 SATE 724
Cdd:cd05576  250 GAGV 253
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
564-728 5.60e-06

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


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 49.71  E-value: 5.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  564 WHLIRQIVEGLahiHGQGIIHRDFTPNNIFFDAR-NDIKIGDFGLAKFLKLEqldqdggfsTDVAgsgvdsTGQAGTYFY 642
Cdd:cd13974  138 FYDVVRVVEAL---HKKNIVHRDLKLGNMVLNKRtRKITITNFCLGKHLVSE---------DDLL------KDQRGSPAY 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  643 TAPEIEQDWPKIDEKADMYSLGVVFFELWH---PFGTAMERHVIltnLKLKGElplkwvnEF---------PEQASLLRR 710
Cdd:cd13974  200 ISPDVLSGKPYLGKPSDMWALGVVLFTMLYgqfPFYDSIPQELF---RKIKAA-------EYtipedgrvsENTVCLIRK 269
                        170
                 ....*....|....*...
gi 30694992  711 LMSPSPSDRPSATELLKH 728
Cdd:cd13974  270 LLVLNPQKRLTASEVLDS 287
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
573-721 5.89e-06

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: 49.16  E-value: 5.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  573 GLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleqLDQDGGFStdvagsgvdSTG--QAGTYFYTAPEiEQD 650
Cdd:cd05084  107 GMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSR------EEEDGVYA---------ATGgmKQIPVKWTAPE-ALN 170
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30694992  651 WPKIDEKADMYSLGVVffeLWHPFGTAMERHVILTNLKLKGELPLKWVNEFPEQA-----SLLRRLMSPSPSDRPS 721
Cdd:cd05084  171 YGRYSSESDVWSFGIL---LWETFSLGAVPYANLSNQQTREAVEQGVRLPCPENCpdevyRLMEQCWEYDPRKRPS 243
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
417-670 6.02e-06

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: 50.03  E-value: 6.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  417 PSSRYLNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRlkdKEIPVNSRIVREVAtlsrlQHQHVvryyqawFETGV 496
Cdd:cd05618   14 SSSLGLQDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVK---KELVNDDEDIDWVQ-----TEKHV-------FEQAS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  497 VDPFaganwgsktagssMFSYSGAVSTEipeqdnnlesTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLA 575
Cdd:cd05618   79 NHPF-------------LVGLHSCFQTE----------SRLFFVIEYVNGgDLMFHMQRQRKLPEEHARFYSAEISLALN 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  576 HIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleqldqdggfstDVAGSGVDSTGQAGTYFYTAPEIEQDwPKID 655
Cdd:cd05618  136 YLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCK---------------EGLRPGDTTSTFCGTPNYIAPEILRG-EDYG 199
                        250
                 ....*....|....*
gi 30694992  656 EKADMYSLGVVFFEL 670
Cdd:cd05618  200 FSVDWWALGVLMFEM 214
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
429-671 6.51e-06

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: 49.62  E-value: 6.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVVL--CKN---KLDGRQYAVKKirLKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAwfeTGVVDPFAGA 503
Cdd:cd05094   11 RELGEGAFGKVFLaeCYNlspTKDKMLVAVKT--LKDPTLAARKDFQREAELLTNLQHDHIVKFYGV---CGDGDPLIMV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  504 NWGSKTAGSSMFsysgaVSTEIPEQdnnlestylYIQMEYCPRtlrqvfESYNHFDKDFAWHLIRQIVEGLAHIHGQGII 583
Cdd:cd05094   86 FEYMKHGDLNKF-----LRAHGPDA---------MILVDGQPR------QAKGELGLSQMLHIATQIASGMVYLASQHFV 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  584 HRDFTPNNIFFDARNDIKIGDFGLAKFLkleqldqdggFSTDVAGSGvdstGQAGTYFYTAPEIEQDWPKIDEKADMYSL 663
Cdd:cd05094  146 HRDLATRNCLVGANLLVKIGDFGMSRDV----------YSTDYYRVG----GHTMLPIRWMPPESIMYRKFTTESDVWSF 211

                 ....*...
gi 30694992  664 GVVFFELW 671
Cdd:cd05094  212 GVILWEIF 219
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
428-721 7.12e-06

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: 49.11  E-value: 7.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  428 LKPLGQGGFGHVVLCKNKlDGRQYAVKKIRLKDKEIpvnSRIVREVATLSRLQHQHVVRYYqawfetgvvdpfaganwgs 507
Cdd:cd05067   12 VERLGAGQFGEVWMGYYN-GHTKVAIKSLKQGSMSP---DAFLAEANLMKQLQHQRLVRLY------------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 ktagssmfsysgAVSTEIPeqdnnlestyLYIQMEYCPRTLRQVFESYNHFDKDFAWHLI---RQIVEGLAHIHGQGIIH 584
Cdd:cd05067   69 ------------AVVTQEP----------IYIITEYMENGSLVDFLKTPSGIKLTINKLLdmaAQIAEGMAFIEERNYIH 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  585 RDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLdqdggfstdvagsgvdsTGQAGTYF---YTAPEiEQDWPKIDEKADMY 661
Cdd:cd05067  127 RDLRAANILVSDTLSCKIADFGLARLIEDNEY-----------------TAREGAKFpikWTAPE-AINYGTFTIKSDVW 188
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30694992  662 SLGVVFFELWH----PFgTAMERHVILTNLKLKGELPLKwvNEFPEQA-SLLRRLMSPSPSDRPS 721
Cdd:cd05067  189 SFGILLTEIVThgriPY-PGMTNPEVIQNLERGYRMPRP--DNCPEELyQLMRLCWKERPEDRPT 250
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
570-670 7.51e-06

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: 49.36  E-value: 7.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  570 IVEGLAHIHGQ--------GIIHRDFTPNNIFFDARNDIKIGDFGLAkflkleqLDQDGGFST-DVAgsgvdSTGQAGTY 640
Cdd:cd14143  101 IASGLAHLHMEivgtqgkpAIAHRDLKSKNILVKKNGTCCIADLGLA-------VRHDSATDTiDIA-----PNHRVGTK 168
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 30694992  641 FYTAPEIEQDWPKID-----EKADMYSLGVVFFEL 670
Cdd:cd14143  169 RYMAPEVLDDTINMKhfesfKRADIYALGLVFWEI 203
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
425-730 9.55e-06

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 49.22  E-value: 9.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKirLKDKEI----PVNSRIV--REVATLSRLQHQHVVRYYqAWFETG--- 495
Cdd:cd05589    1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKA--LKKGDIiardEVESLMCekRIFETVNSARHPFLVNLF-ACFQTPehv 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  496 --VVDPFAGanwgsktaGSSMFSYSGAVSTEipeqdnnlestylyiqmeycPRTlrqVFESynhfdkdfawhliRQIVEG 573
Cdd:cd05589   78 cfVMEYAAG--------GDLMMHIHEDVFSE--------------------PRA---VFYA-------------ACVVLG 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  574 LAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleqldQDGGFStdvagsgvDSTGQ-AGTYFYTAPEIEQDwP 652
Cdd:cd05589  114 LQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK--------EGMGFG--------DRTSTfCGTPEFLAPEVLTD-T 176
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  653 KIDEKADMYSLGVVFFELwhpfgtamerhviltnlkLKGELPL----------KWVNE---FP-----EQASLLRRLMSP 714
Cdd:cd05589  177 SYTRAVDWWGLGVLIYEM------------------LVGESPFpgddeeevfdSIVNDevrYPrflstEAISIMRRLLRK 238
                        330       340
                 ....*....|....*....|.
gi 30694992  715 SPSDRPSATE-----LLKHAF 730
Cdd:cd05589  239 NPERRLGASErdaedVKKQPF 259
PRK14879 PRK14879
Kae1-associated kinase Bud32;
539-610 1.30e-05

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 47.59  E-value: 1.30e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30694992   539 IQMEYCP-RTLRQVFESYNHFDKDFAWHLIRQIveglAHIHGQGIIHRDFTPNN-IFFDarNDIKIGDFGLAKF 610
Cdd:PRK14879   76 IVMEYIEgEPLKDLINSNGMEELELSREIGRLV----GKLHSAGIIHGDLTTSNmILSG--GKIYLIDFGLAEF 143
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
537-671 1.37e-05

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 48.32  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  537 LYIQMEYCPR--TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLE 614
Cdd:cd05114   74 IYIVTEFMENgcLLNYLRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDD 153
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 30694992  615 QLdqdggfstdvagsgVDSTGQAGTYFYTAPEIeQDWPKIDEKADMYSLGVVFFELW 671
Cdd:cd05114  154 QY--------------TSSSGAKFPVKWSPPEV-FNYSKFSSKSDVWSFGVLMWEVF 195
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
563-728 1.43e-05

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 47.81  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  563 AWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKigdfglakfLKLEQLDQdggfSTDVAGSGVDSTGQAGTYFY 642
Cdd:cd13976   86 AARLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEERTK---------LRLESLED----AVILEGEDDSLSDKHGCPAY 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  643 TAPEIEQDWPKIDEK-ADMYSLGVVFFELW---HPFGTAmeRHVILTNLKLKGELPLkwvnefPEQAS-----LLRRLMS 713
Cdd:cd13976  153 VSPEILNSGATYSGKaADVWSLGVILYTMLvgrYPFHDS--EPASLFAKIRRGQFAI------PETLSprarcLIRSLLR 224
                        170
                 ....*....|....*
gi 30694992  714 PSPSDRPSATELLKH 728
Cdd:cd13976  225 REPSERLTAEDILLH 239
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
422-675 1.58e-05

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: 48.05  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEELKPLGQGGFGHVVLCKNKldGRQYAVKKIrlkdKEIPVNSRIVREVATLSRLQHQHVVRYYQAWFEtgvvdpfa 501
Cdd:cd05082    5 MKELKLLQTIGKGEFGDVMLGDYR--GNKVAVKCI----KNDATAQAFLAEASVMTQLRHSNLVQLLGVIVE-------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 ganwgsktagssmfsysgavsteipeqdnnlESTYLYIQMEYCPR-TLRQVFESYNH--FDKDFAWHLIRQIVEGLAHIH 578
Cdd:cd05082   71 -------------------------------EKGGLYIVTEYMAKgSLVDYLRSRGRsvLGGDCLLKFSLDVCEAMEYLE 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  579 GQGIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleqldqdggfstdvAGSGVDSTGQAGTYfYTAPEIEQDwPKIDEKA 658
Cdd:cd05082  120 GNNFVHRDLAARNVLVSEDNVAKVSDFGLTK-----------------EASSTQDTGKLPVK-WTAPEALRE-KKFSTKS 180
                        250
                 ....*....|....*..
gi 30694992  659 DMYSLGVVFFELWhPFG 675
Cdd:cd05082  181 DVWSFGILLWEIY-SFG 196
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
569-728 1.63e-05

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 47.99  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  569 QIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLdqdggfstdvagsgvdsTGQAGTYF---YTAP 645
Cdd:cd14203   99 QIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEY-----------------TARQGAKFpikWTAP 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  646 EIEQdWPKIDEKADMYSLGvvffelwhpfgtamerhVILTNLKLKGELPLKWVN--EFPEQASLLRRLMSPsPSDRPSAT 723
Cdd:cd14203  162 EAAL-YGRFTIKSDVWSFG-----------------ILLTELVTKGRVPYPGMNnrEVLEQVERGYRMPCP-PGCPESLH 222

                 ....*
gi 30694992  724 ELLKH 728
Cdd:cd14203  223 ELMCQ 227
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
568-730 1.71e-05

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: 48.12  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  568 RQIVEGLAHIHGQG--IIHRDFTPNNIFFDA-RNDIKIGDFGLAKFlkleqldQDGGFSTDVagsgvdstgqAGTYFYTA 644
Cdd:cd14030  135 RQILKGLQFLHTRTppIIHRDLKCDNIFITGpTGSVKIGDLGLATL-------KRASFAKSV----------IGTPEFMA 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  645 PEIEQDwpKIDEKADMYSLGVVFFELW---HPFGTAMERHVILTNLKlKGELPLKWVN-EFPEQASLLRRLMSPSPSDRP 720
Cdd:cd14030  198 PEMYEE--KYDESVDVYAFGMCMLEMAtseYPYSECQNAAQIYRRVT-SGVKPASFDKvAIPEVKEIIEGCIRQNKDERY 274
                        170
                 ....*....|
gi 30694992  721 SATELLKHAF 730
Cdd:cd14030  275 AIKDLLNHAF 284
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
421-725 1.80e-05

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: 47.95  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  421 YLNDFEEL---KPLGQGGFGHVVlcKNKLDGRQYAVKKIRLKdkeipVNSR-IVREVATLSRLQHQHVVRYYQAWFETGv 496
Cdd:cd05083    1 WLLNLQKLtlgEIIGEGEFGAVL--QGEYMGQKVAVKNIKCD-----VTAQaFLEETAVMTKLQHKNLVRLLGVILHNG- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  497 vdpfaganwgsktagssmfsysgavsteipeqdnnlestyLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLI--RQIVEG 573
Cdd:cd05083   73 ----------------------------------------LYIVMELMSKgNLVNFLRSRGRALVPVIQLLQfsLDVAEG 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  574 LAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleqldqdggfstdVAGSGVDSTGQAGTyfYTAPEIEQDWpK 653
Cdd:cd05083  113 MEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAK----------------VGSMGVDNSRLPVK--WTAPEALKNK-K 173
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30694992  654 IDEKADMYSLGVVffeLWHPFGTAMERHVILTNLKLKGELPLKWVNEFPEQA-----SLLRRLMSPSPSDRPSATEL 725
Cdd:cd05083  174 FSSKSDVWSYGVL---LWEVFSYGRAPYPKMSVKEVKEAVEKGYRMEPPEGCppdvySIMTSCWEAEPGKRPSFKKL 247
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
431-727 1.89e-05

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: 47.90  E-value: 1.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNKLDGRQYAVKKIRLKDKEipvnSRIVREVATLSRLQHQHVVRYYQAWFETGVVDPfaganwgskta 510
Cdd:cd14156    1 IGSGFFSKVYKVTHGATGKVMVVKIYKNDVDQ----HKIVREISLLQKLSHPNIVRYLGICVKDEKLHP----------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  511 gssMFSY-SGAVSTEIpeqdnnlestylyIQMEYCPRTLRQVFEsynhfdkdfawhLIRQIVEGLAHIHGQGIIHRDFTP 589
Cdd:cd14156   66 ---ILEYvSGGCLEEL-------------LAREELPLSWREKVE------------LACDISRGMVYLHSKNIYHRDLNS 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  590 NNIFFDARNDIK---IGDFGLAKFL-KLEQLDQDGGFSTdvagsgvdstgqAGTYFYTAPEIEQDWPkIDEKADMYSLGV 665
Cdd:cd14156  118 KNCLIRVTPRGReavVTDFGLAREVgEMPANDPERKLSL------------VGSAFWMAPEMLRGEP-YDRKVDVFSFGI 184
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30694992  666 VFFELWHPFGTAMERHVILTNLKLKGELPLKWVNEFPEQA-SLLRRLMSPSPSDRPSATELLK 727
Cdd:cd14156  185 VLCEILARIPADPEVLPRTGDFGLDVQAFKEMVPGCPEPFlDLAASCCRMDAFKRPSFAELLD 247
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
424-720 2.02e-05

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: 47.72  E-value: 2.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELK---PLGQGGFGHVVlcKNKLDGRQYAVKKIRLK-DKEIPVNSRIVREVATL-SRLQHQHVVRYYQAWFETG--- 495
Cdd:cd14147    1 SFQELRleeVIGIGGFGKVY--RGSWRGELVAVKAARQDpDEDISVTAESVRQEARLfAMLAHPNIIALKAVCLEEPnlc 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  496 -VVDPFAGANWGSKTAGSsmfsysgavstEIPeqdnnlestylyiqmeycPRTLrqvfesynhfdkdFAWHLirQIVEGL 574
Cdd:cd14147   79 lVMEYAAGGPLSRALAGR-----------RVP------------------PHVL-------------VNWAV--QIARGM 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  575 AHIHGQGI---IHRDFTPNNIF--FDARND------IKIGDFGLAK-FLKLEQLDQdggfstdvagsgvdstgqAGTYFY 642
Cdd:cd14147  115 HYLHCEALvpvIHRDLKSNNILllQPIENDdmehktLKITDFGLAReWHKTTQMSA------------------AGTYAW 176
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30694992  643 TAPEIEQDwPKIDEKADMYSLGVVFFELwhpfgtamerhviltnlkLKGELPLKWVNEFPEQASL-LRRLMSPSPSDRP 720
Cdd:cd14147  177 MAPEVIKA-STFSKGSDVWSFGVLLWEL------------------LTGEVPYRGIDCLAVAYGVaVNKLTLPIPSTCP 236
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
535-670 2.07e-05

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: 47.86  E-value: 2.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  535 TYLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHG-----QG---IIHRDFTPNNIFFDARNDIKIGDFG 606
Cdd:cd14144   66 TQLYLITDYHENGSLYDFLRGNTLDTQSMLKLAYSAACGLAHLHTeifgtQGkpaIAHRDIKSKNILVKKNGTCCIADLG 145
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  607 LA-KFLkleqldqdggfsTDVAGSGVDSTGQAGTYFYTAPEI--EQDWPKIDE---KADMYSLGVVFFEL 670
Cdd:cd14144  146 LAvKFI------------SETNEVDLPPNTRVGTKRYMAPEVldESLNRNHFDaykMADMYSFGLVLWEI 203
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
422-670 2.51e-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: 48.09  E-value: 2.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  422 LNDFEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIRlkdKEIPVNSRIVREVATlsrlqHQHVvryyqawFETGVVDPFa 501
Cdd:cd05617   14 LQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVK---KELVHDDEDIDWVQT-----EKHV-------FEQASSNPF- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  502 ganwgsktagssMFSYSGAVSTEipeqdnnlesTYLYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQ 580
Cdd:cd05617   78 ------------LVGLHSCFQTT----------SRLFLVIEYVNGgDLMFHMQRQRKLPEEHARFYAAEICIALNFLHER 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  581 GIIHRDFTPNNIFFDARNDIKIGDFGLAKflkleqldqdggfstDVAGSGVDSTGQAGTYFYTAPEIEQDwPKIDEKADM 660
Cdd:cd05617  136 GIIYRDLKLDNVLLDADGHIKLTDYGMCK---------------EGLGPGDTTSTFCGTPNYIAPEILRG-EEYGFSVDW 199
                        250
                 ....*....|
gi 30694992  661 YSLGVVFFEL 670
Cdd:cd05617  200 WALGVLMFEM 209
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
405-670 2.98e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 48.15  E-value: 2.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   405 PPSDSCEPNASLP---SSRYLNDFEELKPLGQGGFGHVVLC------------KNKLDGRQYAVKKIRLKDKEIPVNSRI 469
Cdd:PHA03210  127 PDAAGPVPLAQAKlkhDDEFLAHFRVIDDLPAGAFGKIFICalrasteeaearRGVNSTNQGKPKCERLIAKRVKAGSRA 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   470 V----REVATLSRLQHQHVVRYyqawfetgvvdpfaganwgsktagssmfsysgavsTEIPEQDNNlesTYLYIQmeycp 545
Cdd:PHA03210  207 AiqleNEILALGRLNHENILKI-----------------------------------EEILRSEAN---TYMITQ----- 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   546 rtlRQVFESYNH-FDKDFAWH----------LIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLE 614
Cdd:PHA03210  244 ---KYDFDLYSFmYDEAFDWKdrpllkqtraIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLGDFGTAMPFEKE 320
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 30694992   615 QLDQDGGFstdvagsgvdstgqAGTYFYTAPEI-EQDwpKIDEKADMYSLGVVFFEL 670
Cdd:PHA03210  321 REAFDYGW--------------VGTVATNSPEIlAGD--GYCEITDIWSCGLILLDM 361
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
553-728 3.45e-05

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 46.96  E-value: 3.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  553 ESYNHFDKDF-----------------AWHLIRQIVEGLAHIHgqgiihrdftpnniffdaRNDIKIGDFGLAKF----- 610
Cdd:cd14023   59 KAYVFFEKDFgdmhsyvrsckrlreeeAARLFKQIVSAVAHCH------------------QSAIVLGDLKLRKFvfsde 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  611 ----LKLEQLDqdggfSTDVAGSGVDS-TGQAGTYFYTAPEIEQDWPKIDEK-ADMYSLGVVFFELW---HPFGTAmERH 681
Cdd:cd14023  121 ertqLRLESLE-----DTHIMKGEDDAlSDKHGCPAYVSPEILNTTGTYSGKsADVWSLGVMLYTLLvgrYPFHDS-DPS 194
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 30694992  682 VILTNLKlKGELPLkwvnefPEQAS-----LLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14023  195 ALFSKIR-RGQFCI------PDHVSpkarcLIRSLLRREPSERLTAPEILLH 239
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
560-728 3.48e-05

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


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 46.95  E-value: 3.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  560 KDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIgdfglakflKLEQLDQdggfSTDVAGSGVDSTGQAGT 639
Cdd:cd14022   83 EEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEERTRV---------KLESLED----AYILRGHDDSLSDKHGC 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  640 YFYTAPEIEQDWPKIDEK-ADMYSLGVVFFELW---HPFGTaMERHVILTNLKlKGELPLKWVNEfPEQASLLRRLMSPS 715
Cdd:cd14022  150 PAYVSPEILNTSGSYSGKaADVWSLGVMLYTMLvgrYPFHD-IEPSSLFSKIR-RGQFNIPETLS-PKAKCLIRSILRRE 226
                        170
                 ....*....|...
gi 30694992  716 PSDRPSATELLKH 728
Cdd:cd14022  227 PSERLTSQEILDH 239
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
431-725 4.01e-05

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


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 46.65  E-value: 4.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHV---VLCKNKLDGRQYAVKKIRlKDKEIPVNSRIVREVATLSRLQHQHVVRYyqawfeTGVVdpfaganwgs 507
Cdd:cd05056   14 IGEGQFGDVyqgVYMSPENEKIAVAVKTCK-NCTSPSVREKFLQEAYIMRQFDHPHIVKL------IGVI---------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 ktagssmfsysgavsTEIPeqdnnlestyLYIQMEYCPR-TLRQVFESYnhfdKDFAWHLI-----RQIVEGLAHIHGQG 581
Cdd:cd05056   77 ---------------TENP----------VWIVMELAPLgELRSYLQVN----KYSLDLASlilyaYQLSTALAYLESKR 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  582 IIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLDQdggfstdvagsgvDSTGQAGTYfYTAPEiEQDWPKIDEKADMY 661
Cdd:cd05056  128 FVHRDIAARNVLVSSPDCVKLGDFGLSRYMEDESYYK-------------ASKGKLPIK-WMAPE-SINFRRFTSASDVW 192
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30694992  662 SLGVVFFELW----HPFGTAMERHVIltnLKL-KGELPLKWVNEFPEQASLLRRLMSPSPSDRPSATEL 725
Cdd:cd05056  193 MFGVCMWEILmlgvKPFQGVKNNDVI---GRIeNGERLPMPPNCPPTLYSLMTKCWAYDPSKRPRFTEL 258
Kinase-like pfam14531
Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. ...
537-719 4.47e-05

Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. These proteins have a typical bilobed protein kinase fold, but lack catalytic actvity.


Pssm-ID: 405254 [Multi-domain]  Cd Length: 288  Bit Score: 46.72  E-value: 4.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992    537 LYIQMEYCPRTLRQVFESYNHFDKDFAWH----LIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFglakflk 612
Cdd:pfam14531  116 LYPAMSVDLQLLGEVLLSHSSTHKSLVHHarlqLTLQLIRLAANLQHYGLVHGQFTVDNFFLDQRGGVFLGGF------- 188
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992    613 lEQLDQDG----GFSTDVAGSGVDSTGQAGTYFYTAPEieqdwpKIDEKADMYSLGVVFFELWH---PFGTAMErhvilt 685
Cdd:pfam14531  189 -EHLVRDGtkvvASEVPRGFAPPELLGSRGGYTMKNTT------LMTHAFDAWQLGLVIYWIWCldlPNTLDAE------ 255
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 30694992    686 nlKLKGELPLKWVNEFPEQ-ASLLRRLMSPSPSDR 719
Cdd:pfam14531  256 --EGGIEWKFRLCKNIPEPvRALLKGFLNYSQEDR 288
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
431-670 4.56e-05

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: 46.97  E-value: 4.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVLCKNK--LDGRQYAVKKIrlkdKEIPVNSRIVREVATLSRLQHQHVVRYYQAWFETGVVDPFAGANWGSK 508
Cdd:cd07868   25 VGRGTYGHVYKAKRKdgKDDKDYALKQI----EGTGISMSACREIALLRELKHPNVISLQKVFLSHADRKVWLLFDYAEH 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  509 TAGSSMFSYSGAVSTEIPEQdnnlestylyiqmeyCPRTLRQvfesynhfdkdfawHLIRQIVEGLAHIHGQGIIHRDFT 588
Cdd:cd07868  101 DLWHIIKFHRASKANKKPVQ---------------LPRGMVK--------------SLLYQILDGIHYLHANWVLHRDLK 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  589 PNNIFF----DARNDIKIGDFGLAKFLK--LEQLdqdggfstdvagsgVDSTGQAGTYFYTAPEIEQDWPKIDEKADMYS 662
Cdd:cd07868  152 PANILVmgegPERGRVKIADMGFARLFNspLKPL--------------ADLDPVVVTFWYRAPELLLGARHYTKAIDIWA 217

                 ....*...
gi 30694992  663 LGVVFFEL 670
Cdd:cd07868  218 IGCIFAEL 225
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
428-671 5.68e-05

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: 46.41  E-value: 5.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  428 LKPLGQGGFGHVVLCKNKldgRQYAVKKIRLKDKEIPvNSRIVREVATLSRLQHQHVVRYYqawfetgvvdpfaganwgs 507
Cdd:cd05113    9 LKELGTGQFGVVKYGKWR---GQYDVAIKMIKEGSMS-EDEFIEEAKVMMNLSHEKLVQLY------------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  508 ktagssmfsysGAVSTEIPeqdnnlestyLYIQMEYCPR--TLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHR 585
Cdd:cd05113   66 -----------GVCTKQRP----------IFIITEYMANgcLLNYLREMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHR 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  586 DFTPNNIFFDARNDIKIGDFGLAKFLkleqLDQdggfstdvagsgvDSTGQAGTYF---YTAPEIEQdWPKIDEKADMYS 662
Cdd:cd05113  125 DLAARNCLVNDQGVVKVSDFGLSRYV----LDD-------------EYTSSVGSKFpvrWSPPEVLM-YSKFSSKSDVWA 186

                 ....*....
gi 30694992  663 LGVVFFELW 671
Cdd:cd05113  187 FGVLMWEVY 195
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
569-670 5.76e-05

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 46.17  E-value: 5.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  569 QIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLkleqldQDGGFstdvagsgvdsTGQAGTYF---YTAP 645
Cdd:cd05073  115 QIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVI------EDNEY-----------TAREGAKFpikWTAP 177
                         90       100
                 ....*....|....*....|....*
gi 30694992  646 EiEQDWPKIDEKADMYSLGVVFFEL 670
Cdd:cd05073  178 E-AINFGSFTIKSDVWSFGILLMEI 201
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
568-671 6.11e-05

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: 46.45  E-value: 6.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  568 RQIVEGLAHIHGQGIIHRDFTPNNIFFDA-RNDIKIGDFGLAKFLkleqldqdggfstdvagSGVDSTGQAGTYFYTAPE 646
Cdd:cd14135  112 QQLFLALKHLKKCNILHADIKPDNILVNEkKNTLKLCDFGSASDI-----------------GENEITPYLVSRFYRAPE 174
                         90       100
                 ....*....|....*....|....*
gi 30694992  647 IEQDWPkIDEKADMYSLGVVFFELW 671
Cdd:cd14135  175 IILGLP-YDYPIDMWSVGCTLYELY 198
RWD_IMPACT cd23821
RWD domain of protein IMPACT and related proteins; IMPACT, also imprinted and ancient gene ...
37-145 7.17e-05

RWD domain of protein IMPACT and related proteins; IMPACT, also imprinted and ancient gene protein homolog, acts as a translational regulator that ensures constant high levels of translation upon a variety of stress conditions, such as amino acid starvation, UV-C irradiation, proteasome inhibitor treatment, and glucose deprivation. It plays a role as a negative regulator of EIF2AK4/GCN2 kinase activity. It impairs GCN1-mediated EIF2AK4/GCN2 activation, and hence EIF2AK4/GCN2-mediated eIF-2-alpha phosphorylation and subsequent down-regulation of protein synthesis. IMPACT may be required to regulate translation in specific neuronal cells under amino acid starvation conditions by preventing GCN2 activation and therefore ATF4 synthesis. Through its inhibitory action on EIF2AK4/GCN2, IMPACT plays a role in differentiation of neuronal cells by stimulating neurite outgrowth.


Pssm-ID: 467657  Cd Length: 101  Bit Score: 42.99  E-value: 7.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   37 EEITALSAIFQEDCKVVSDSRSPPQIAIKLRpyskdmgyEDTDISAMLIVRCLPGYPYKC-PKLQITPEQgLTTADAEKL 115
Cdd:cd23821    2 EEIEALEAIYGEDFVVIDESARSFVIRIELD--------GPHLPPLVLRVHLPPDYPSHSpPIFELSAPW-LSGEERSEL 72
                         90       100       110
                 ....*....|....*....|....*....|
gi 30694992  116 LSLLEDQANSNAreGRVMIFNLVEAAQEFL 145
Cdd:cd23821   73 CAELDEIWEENA--GEPVLFQWVEWLREYL 100
HGTP_anticodon2 pfam12745
Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on ...
1135-1233 8.09e-05

Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on Gcn2 proteins which bind tRNA to down regulate translation in certain stress situations.


Pssm-ID: 432758  Cd Length: 259  Bit Score: 45.67  E-value: 8.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   1135 VLVCSRGGGGLLVQRMELVAELWEKSIKAEFVPTPDPSLTEQYEYANEHEIKCLVIITESGVAQNQIEF-VKVRHLELKK 1213
Cdd:pfam12745    8 VLVASFDASILRTTGVEILQELWAHGISADLAVDASYSPEDLVSRARDDGVSWIVIIKQQNKSSDSKYKpLKVKNLLRKE 87
                           90       100
                   ....*....|....*....|
gi 30694992   1214 EKVVGREELVKFLLDAMAVQ 1233
Cdd:pfam12745   88 DVDLDSDELVSWLRGEIRER 107
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
566-670 8.16e-05

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: 46.01  E-value: 8.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  566 LIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLkleQLDQDGGFSTdvagsgvdsTGQAGTYFYTAP 645
Cdd:cd05066  111 MLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVL---EDDPEAAYTT---------RGGKIPIRWTAP 178
                         90       100
                 ....*....|....*....|....*
gi 30694992  646 EIEQdWPKIDEKADMYSLGVVFFEL 670
Cdd:cd05066  179 EAIA-YRKFTSASDVWSYGIVMWEV 202
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
424-621 8.53e-05

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


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 46.17  E-value: 8.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVLCKNKLDGRQ----YAVKKIRlKDKEIPVNSRIVREVATLSRLQHQHVVRYYQAWFETGV--- 496
Cdd:cd05108    8 EFKKIKVLGSGAFGTVYKGLWIPEGEKvkipVAIKELR-EATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVqli 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  497 --VDPFaganwgsktagssmfsysGAVSTEIPEQDNNLESTYLyiqMEYCPrtlrqvfesynhfdkdfawhlirQIVEGL 574
Cdd:cd05108   87 tqLMPF------------------GCLLDYVREHKDNIGSQYL---LNWCV-----------------------QIAKGM 122
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 30694992  575 AHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLD--QDGG 621
Cdd:cd05108  123 NYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEyhAEGG 171
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
569-730 1.00e-04

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 45.83  E-value: 1.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  569 QIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLdqdggfstdvagsgvdsTGQAGTYF---YTAP 645
Cdd:cd05070  113 QVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEY-----------------TARQGAKFpikWTAP 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  646 EIEQdWPKIDEKADMYSLGvvffelwhpfgtamerhVILTNLKLKGELPLKWVNEFPEQASLLRRLMSPSPSDRP-SATE 724
Cdd:cd05070  176 EAAL-YGRFTIKSDVWSFG-----------------ILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPiSLHE 237

                 ....*.
gi 30694992  725 LLKHAF 730
Cdd:cd05070  238 LMIHCW 243
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
424-621 1.03e-04

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 45.79  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  424 DFEELKPLGQGGFGHVVlcknkldgrqyavKKIRLKDKE---IPVNSRIVREvaTLSRLQHQHVVRyyQAWFETGVVDPF 500
Cdd:cd05109    8 ELKKVKVLGSGAFGTVY-------------KGIWIPDGEnvkIPVAIKVLRE--NTSPKANKEILD--EAYVMAGVGSPY 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  501 AganwgSKTAGSSMFSYSGAVSTEIP---------EQDNNLESTYLyiqMEYCprtlrqvfesynhfdkdfawhliRQIV 571
Cdd:cd05109   71 V-----CRLLGICLTSTVQLVTQLMPygclldyvrENKDRIGSQDL---LNWC-----------------------VQIA 119
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 30694992  572 EGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEQLD--QDGG 621
Cdd:cd05109  120 KGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEyhADGG 171
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
428-609 1.14e-04

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: 45.49  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  428 LKPLGQGGFGHVVL-----CKNKLDGRQ-YAVKKIRLK--DKEIpvnSRIVREVATLSRL-QHQHVVRYYqawfetgvvd 498
Cdd:cd05053   17 GKPLGEGAFGQVVKaeavgLDNKPNEVVtVAVKMLKDDatEKDL---SDLVSEMEMMKMIgKHKNIINLL---------- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  499 pfaganwgsktagssmfsysGAVSTEIPeqdnnlestyLYIQMEYCP--------RTLRQVFESYNHFD----------K 560
Cdd:cd05053   84 --------------------GACTQDGP----------LYVVVEYASkgnlreflRARRPPGEEASPDDprvpeeqltqK 133
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 30694992  561 D---FAWhlirQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAK 609
Cdd:cd05053  134 DlvsFAY----QVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLAR 181
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
566-670 1.16e-04

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: 45.35  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  566 LIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLkleQLDQDGGFSTdvagsgvdsTGQAGTYFYTAP 645
Cdd:cd05063  112 MLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVL---EDDPEGTYTT---------SGGKIPIRWTAP 179
                         90       100
                 ....*....|....*....|....*
gi 30694992  646 EiEQDWPKIDEKADMYSLGVVFFEL 670
Cdd:cd05063  180 E-AIAYRKFTSASDVWSFGIVMWEV 203
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
565-671 1.29e-04

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


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 45.31  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  565 HLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARND-IKIGDFGLAkflkLEQLDQDGGFstdvagsgVDSTGqagtyfYT 643
Cdd:cd14020  114 HCARDVLEALAFLHHEGYVHADLKPRNILWSAEDEcFKLIDFGLS----FKEGNQDVKY--------IQTDG------YR 175
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 30694992  644 APEIE----------QDWPKIDEKADMYSLGVVFFELW 671
Cdd:cd14020  176 APEAElqnclaqaglQSETECTSAVDLWSLGIVLLEMF 213
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
538-728 1.71e-04

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


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 45.02  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  538 YIQMEYCprTLRQVFE---SYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDAR---NDIKIGDFGLAKFl 611
Cdd:cd14088   75 FIFLELA--TGREVFDwilDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNRlknSKIVISDFHLAKL- 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  612 kleqldqDGGFSTDvagsgvdstgQAGTYFYTAPEI--EQDWPKideKADMYSLGVVFFELWH---PFGTAMERHVILTN 686
Cdd:cd14088  152 -------ENGLIKE----------PCGTPEYLAPEVvgRQRYGR---PVDCWAIGVIMYILLSgnpPFYDEAEEDDYENH 211
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 30694992  687 LK------LKGELPLK---WVNEFPEQASLLRRLMSPSPSDRPSATELLKH 728
Cdd:cd14088  212 DKnlfrkiLAGDYEFDspyWDDISQAAKDLVTRLMEVEQDQRITAEEAISH 262
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
429-669 2.03e-04

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: 44.57  E-value: 2.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  429 KPLGQGGFGHVV--LCKNKLDGRQYAVKKIRLKDKEIPVNSRIVREVATLSRLQHQHVVRyyqawfetgvvdpfaganwg 506
Cdd:cd05116    1 GELGSGNFGTVKkgYYQMKKVVKTVAVKILKNEANDPALKDELLREANVMQQLDNPYIVR-------------------- 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  507 sktagssMFSYSGAvsteipeqdnnlESTYLYIQM-EYCPrtLRQVFESYNHFDKDFAWHLIRQIVEGLAHIHGQGIIHR 585
Cdd:cd05116   61 -------MIGICEA------------ESWMLVMEMaELGP--LNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHR 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  586 DFTPNNIFFDARNDIKIGDFGLAKFLkleqldqdggfSTDVAGSGVDSTGQAGTYFYtAPEIeQDWPKIDEKADMYSLGV 665
Cdd:cd05116  120 DLAARNVLLVTQHYAKISDFGLSKAL-----------RADENYYKAQTHGKWPVKWY-APEC-MNYYKFSSKSDVWSFGV 186

                 ....
gi 30694992  666 VFFE 669
Cdd:cd05116  187 LMWE 190
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
569-670 2.05e-04

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 45.10  E-value: 2.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  569 QIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKflklEQLdQDGgfstdvagsgvDSTGQ-AGTYFYTAPEI 647
Cdd:cd05588  104 EISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCK----EGL-RPG-----------DTTSTfCGTPNYIAPEI 167
                         90       100
                 ....*....|....*....|....*
gi 30694992  648 --EQDWpkiDEKADMYSLGVVFFEL 670
Cdd:cd05588  168 lrGEDY---GFSVDWWALGVLMFEM 189
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
431-609 3.02e-04

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: 44.38  E-value: 3.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  431 LGQGGFGHVVL--CKN---KLDGRQYAVKKirLKDKEIPVNSR-IVREVATLSRLQHQHVVRYYqawfetGVVdpFAGAN 504
Cdd:cd05049   13 LGEGAFGKVFLgeCYNlepEQDKMLVAVKT--LKDASSPDARKdFEREAELLTNLQHENIVKFY------GVC--TEGDP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  505 WgsktagSSMFSY--SGAVSTEIPEQDNNLEstyLYIQMEYCPRTLRQVfesynhfdkdFAWHLIRQIVEGLAHIHGQGI 582
Cdd:cd05049   83 L------LMVFEYmeHGDLNKFLRSHGPDAA---FLASEDSAPGELTLS----------QLLHIAVQIASGMVYLASQHF 143
                        170       180
                 ....*....|....*....|....*..
gi 30694992  583 IHRDFTPNNIFFDARNDIKIGDFGLAK 609
Cdd:cd05049  144 VHRDLATRNCLVGTNLVVKIGDFGMSR 170
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
425-679 3.43e-04

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: 44.25  E-value: 3.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  425 FEELKPLGQGGFGHVVLCKNKLDGRQYAVKKIrlkdKEIPVNSRIVR-EVATLSRLQHQHV-----VRYYQAwfetgvvd 498
Cdd:cd14229    2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKIL----KNHPSYARQGQiEVGILARLSNENAdefnfVRAYEC-------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  499 pfaganwgsktagssmFSYSGAVSTEIPEQDNNLestYLYI-QMEYCPRTLRQVFEsynhfdkdfawhLIRQIVEGLAHI 577
Cdd:cd14229   70 ----------------FQHRNHTCLVFEMLEQNL---YDFLkQNKFSPLPLKVIRP------------ILQQVATALKKL 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  578 HGQGIIHRDFTPNNIFF--DARND--IKIGDFGLAKFLkleqldqdggfSTDVAGSGVDSTgqagtyFYTAPEIEQDWPk 653
Cdd:cd14229  119 KSLGLIHADLKPENIMLvdPVRQPyrVKVIDFGSASHV-----------SKTVCSTYLQSR------YYRAPEIILGLP- 180
                        250       260
                 ....*....|....*....|....*....
gi 30694992  654 IDEKADMYSLGVVFFEL---WHPFGTAME 679
Cdd:cd14229  181 FCEAIDMWSLGCVIAELflgWPLYPGALE 209
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
428-609 3.69e-04

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: 43.90  E-value: 3.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  428 LKPLGQGGFG-----HVVLCKNKLDGRQYAVKKIRlKDKEIPVNSRIVREVATLSRLQHQHVVRYyqawfeTGVVdpfag 502
Cdd:cd05048   10 LEELGEGAFGkvykgELLGPSSEESAISVAIKTLK-ENASPKTQQDFRREAELMSDLQHPNIVCL------LGVC----- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  503 anwgSKTAGSSM-FSYsgavsteIPEQDN----NLESTYLYIQMEYCPRTLRQVFESynhfdKDFAwHLIRQIVEGLAHI 577
Cdd:cd05048   78 ----TKEQPQCMlFEY-------MAHGDLheflVRHSPHSDVGVSSDDDGTASSLDQ-----SDFL-HIAIQIAAGMEYL 140
                        170       180       190
                 ....*....|....*....|....*....|..
gi 30694992  578 HGQGIIHRDFTPNNIFFDARNDIKIGDFGLAK 609
Cdd:cd05048  141 SSHHYVHRDLAARNCLVGDGLTVKISDFGLSR 172
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
534-670 3.71e-04

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


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 43.97  E-value: 3.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  534 STYLYIQMEYCPRTLRQVFESYNHFDKDFAWHLIRQIVEGLAHIH-----GQG---IIHRDFTPNNIFFDARNDIKIGDF 605
Cdd:cd14142   75 CTQLWLITHYHENGSLYDYLQRTTLDHQEMLRLALSAASGLVHLHteifgTQGkpaIAHRDLKSKNILVKSNGQCCIADL 154
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  606 GLAKFLKLEQLDQDGGFSTDVagsgvdstgqaGTYFYTAPEIEQDWPKID-----EKADMYSLGVVFFEL 670
Cdd:cd14142  155 GLAVTHSQETNQLDVGNNPRV-----------GTKRYMAPEVLDETINTDcfesyKRVDIYAFGLVLWEV 213
HGTP_anticodon pfam03129
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ...
1135-1228 4.25e-04

Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases it is probably the anticodon binding domain.


Pssm-ID: 460819 [Multi-domain]  Cd Length: 94  Bit Score: 40.65  E-value: 4.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   1135 VLVCSRGGGGLLVQRMELVAELWEKSIKAEFVPTpDPSLTEQYEYANEHEIKCLVIITESGVAQNQiefVKVRHLELKKE 1214
Cdd:pfam03129    4 VIPLGEKAEELEEYAQKLAEELRAAGIRVELDDR-NESIGKKFRRADLIGIPFALVVGEKELEEGT---VTVRRRDTGEQ 79
                           90
                   ....*....|....
gi 30694992   1215 KVVGREELVKFLLD 1228
Cdd:pfam03129   80 ETVSLDELVEKLKE 93
PLN03224 PLN03224
probable serine/threonine protein kinase; Provisional
566-608 5.02e-04

probable serine/threonine protein kinase; Provisional


Pssm-ID: 178763 [Multi-domain]  Cd Length: 507  Bit Score: 44.29  E-value: 5.02e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 30694992   566 LIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLA 608
Cdd:PLN03224  314 VMRQVLTGLRKLHRIGIVHRDIKPENLLVTVDGQVKIIDFGAA 356
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
537-750 7.34e-04

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


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 43.08  E-value: 7.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  537 LYIQMEYCPR-TLRQVFESYNHFDKDFAWHLIR----------------QIVEGLAHIHGQGIIHRDFTPNNIFFDARND 599
Cdd:cd05101  105 LYVIVEYASKgNLREYLRARRPPGMEYSYDINRvpeeqmtfkdlvsctyQLARGMEYLASQKCIHRDLAARNVLVTENNV 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  600 IKIGDFGLAKflkleqldqdggfstDVagSGVD----STGQAGTYFYTAPEIEQDwPKIDEKADMYSLGVVFFELW---- 671
Cdd:cd05101  185 MKIADFGLAR---------------DI--NNIDyykkTTNGRLPVKWMAPEALFD-RVYTHQSDVWSFGVLMWEIFtlgg 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  672 HPF-GTAMERHVILTNLKLKGELPLKWVNEFpeqASLLRRLMSPSPSDRPSATELLkhafpprmesELLDNILRIMQTSE 750
Cdd:cd05101  247 SPYpGIPVEELFKLLKEGHRMDKPANCTNEL---YMMMRDCWHAVPSQRPTFKQLV----------EDLDRILTLTTNEE 313
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
569-621 7.40e-04

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 43.13  E-value: 7.40e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 30694992  569 QIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLK--LEQLDQDGG 621
Cdd:cd05110  117 QIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLLEgdEKEYNADGG 171
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
407-670 7.61e-04

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 43.43  E-value: 7.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   407 SDSCEPNASLPSSRYlNDFEELKPLGQGGFGHVVLCKNKldGRQYAVKKIRLKDKeipvnSRIVREVATLSRLQHQHVVR 486
Cdd:PTZ00426   15 SDSTKEPKRKNKMKY-EDFNFIRTLGTGSFGRVILATYK--NEDFPPVAIKRFEK-----SKIIKQKQVDHVFSERKILN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   487 YyqawfetgVVDPFAGANWGSKTagssmfsysgavsteipeqdnnlESTYLYIQMEYCPRTLRQVFESYN-HFDKDFAWH 565
Cdd:PTZ00426   87 Y--------INHPFCVNLYGSFK-----------------------DESYLYLVLEFVIGGEFFTFLRRNkRFPNDVGCF 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992   566 LIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLKLEqldqdggfstdvagsgvdSTGQAGTYFYTAP 645
Cdd:PTZ00426  136 YAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVVDTR------------------TYTLCGTPEYIAP 197
                         250       260
                  ....*....|....*....|....*
gi 30694992   646 EIEQDWPKiDEKADMYSLGVVFFEL 670
Cdd:PTZ00426  198 EILLNVGH-GKAADWWTLGIFIYEI 221
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
565-610 1.06e-03

bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 43.34  E-value: 1.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 30694992   565 HLIRQIVEGLAHIHGQGIIHRDFTPNNIFFDaRNDIKIGDFGLAKF 610
Cdd:PRK09605  432 ELVRKVGEIVAKLHKAGIVHGDLTTSNFIVR-DDRLYLIDFGLGKY 476
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
566-670 1.09e-03

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: 42.55  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694992  566 LIRQIVEGLAHIHGQGIIHRDFTPNNIFFDARNDIKIGDFGLAKFLkleqldQDGgfSTDVAGSGvdSTGQAGTYFYTAP 645
Cdd:cd05065  111 MLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFL------EDD--TSDPTYTS--SLGGKIPIRWTAP 180
                         90       100
                 ....*....|....*....|....*
gi 30694992  646 EIEQdWPKIDEKADMYSLGVVFFEL 670
Cdd:cd05065  181 EAIA-YRKFTSASDVWSYGIVMWEV 204
 
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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