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Conserved domains on  [gi|63054755|ref|NP_595991|]
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eIF2 alpha kinase Gcn2 [Schizosaccharomyces pombe]

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 ...
549-917 3.98e-143

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: 440.27  E-value: 3.98e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  549 VSRYETDFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENSRILREVMTLSRLHHEHVVRYYTAWVETEAnd 628
Cdd:cd14046    1 FSRYLTDFEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIKLRSESKNNSRILREVMLLSRLNHQHVVRYYQAWIERAN-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  629 tvteiissdseslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkegssdkdssie 708
Cdd:cd14046      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  709 eassvktqenglnatLYIQMEYCEKLSLQDIIRDKI--PVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNV 786
Cdd:cd14046   79 ---------------LYIQMEYCEKSTLRDLIDSGLfqDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNV 143
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  787 KLGDFGLATENEN-----YQDNNDKWKNRQSADEDLTTGVGTALYVAPELLSRRnGVRYDAKVDMYSLGIILFEMCMTFS 861
Cdd:cd14046  144 KIGDFGLATSNKLnvelaTQDINKSTSAALGSSGDLTGNVGTALYVAPEVQSGT-KSTYNEKVDMYSLGIIFFEMCYPFS 222
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  862 TSMERIRIIDTIRSPSISFPSTFPFSRASHEFKVIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd14046  223 TGMERVQILTALRSVSIEFPPDFDDNKHSKQAKLIRWLLNHDPAKRPSAQELLKSE 278
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
241-508 1.46e-95

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: 308.52  E-value: 1.46e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  241 ISHSNLSTLTLVKPESKEISLQDCVFLlrtvrISTPYWSTEDGKREIQELEYELESLKVIRHDLLASIYEYQLERETRGY 320
Cdd:cd14012    1 SSESPSGTFYLVYEVVLDNSKKPGKFL-----TSQEYFKTSNGKKQIQLLEKELESLKKLRHPNLVSYLAFSIERRGRSD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  321 GWRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHRTFAKLMDFGFTR 400
Cdd:cd14012   76 GWKVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAGTGIVKLTDYSLGK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  401 TLRDMNAshpfninSQSITNILPEGLYPPEVSESSFaAASRKTDIWCFGLLVLQMLCGAHVLNKFSSLKLIMthVIPLLP 480
Cdd:cd14012  156 TLLDMCS-------RGSLDEFKQTYWLPPELAQGSK-SPTRKTDVWDLGLLFLQMLFGLDVLEKYTSPNPVL--VSLDLS 225
                        250       260
                 ....*....|....*....|....*...
gi 63054755  481 GSYQDLVRRCLMRDSRKRPSAIDLLSSH 508
Cdd:cd14012  226 ASLQDFLSKCLSLDPKKRPTALELLPHE 253
HGTP_anticodon2 pfam12745
Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on ...
1326-1575 6.23e-81

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: 267.16  E-value: 6.23e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   1326 WAPRRVDVLVTSIGKDSI-LEKCSLLQELWALNIQADIVLRGASSLEEIVTHYRSEGINWVLVVRQKN---TQMEHSVKA 1401
Cdd:pfam12745    1 WKPRRCDVLVASFDASILrTTGVEILQELWAHGISADLAVDASYSPEDLVSRARDDGVSWIVIIKQQNkssDSKYKPLKV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   1402 RNILKNEDDEIRFDEVGMWLLGEINER-KRNESMLQSKRILDSAQQDVAKFVDTSQSN----------LDVQLISLKdVN 1470
Cdd:pfam12745   81 KNLLRKEDVDLDSDELVSWLRGEIRERdQREGTALSPKSLRAPSQPEDDGSSQDGPLFsvdirqkvvvVLNDATRSK-KS 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   1471 DRKYKWKHKQNAMNKVYDLVQSAIresseDAIALAVDCDSEAMEKLRSTTTLDEESWKRLIESCPASQREYMQRLQKKLV 1550
Cdd:pfam12745  160 NKRNKWEQEDDAQNAAASLVKSLL-----NGPIAAIDTRDEVLDMISITSLSDPDEWRKVIQSVPTSPRSYATNIYNLLS 234
                          250       260
                   ....*....|....*....|....*
gi 63054755   1551 TLAEQDKKRVWICSFRTNEIYLYGL 1575
Cdd:pfam12745  235 KEASKGTKWAILYNFRTGKCCYYDL 259
RWD_GCN2 cd23823
RWD domain of eIF-2-alpha kinase GCN2 and related proteins; GCN2 (EC 2.7.11.1), also called ...
11-128 9.86e-35

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: 128.88  E-value: 9.86e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   11 KEIQENEIEALKAIFMDDFEELkvRNAWNVTNGHVYCIHLCS-RSANSKSIAKLDLCIELGRSYPYVKPVIKLQNGENVL 89
Cdd:cd23823    1 EEEQEEELEALQSIYGDDFEDL--SSKKAVWSPPEFRIRLRPqEGESEENHVSVDLHVKFPPTYPDVPPEIELENVKGLS 78
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 63054755   90 NSQIRFLLDKLDTKAKDLLGEEMIFELASIVQDYLNDWQ 128
Cdd:cd23823   79 DEQLEELLKELEELAKELLGEEMIFELAEAVQEFLEEHN 117
PLN02972 super family cl33611
Histidyl-tRNA synthetase
990-1425 1.04e-29

Histidyl-tRNA synthetase


The actual alignment was detected with superfamily member PLN02972:

Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 128.08  E-value: 1.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   990 VRDH----VVKVFRRHGAKERESHILFPKSS---QYDKDQASV-SLLDKNGTLLQLPYDTVLPYARNVARNAVEEEKTYL 1061
Cdd:PLN02972  343 IREKafsiITSVFKRHGATALDTPVFELRETlmgKYGEDSKLIyDLADQGGELCSLRYDLTVPFARYVAMNGITSFKRYQ 422
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  1062 ISDVF-REAKGGGRPKAIKEISFDITTNSDNLDwYDAETIKALDEVLTEIpSLTESCILINHADILSSILDYLQVSKDKR 1140
Cdd:PLN02972  423 IAKVYrRDNPSKGRYREFYQCDFDIAGVYEPMG-PDFEIIKVLTELLDEL-DIGTYEVKLNHRKLLDGMLEICGVPPEKF 500
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  1141 RMATHILGQINQRlTLSQVRNQLRIESLVPSTTLDDLSLF-DFRENYEEGASKLRKIFGKEMPQKM-RTALNYMERVVKL 1218
Cdd:PLN02972  501 RTICSSIDKLDKQ-SFEQVKKEMVEEKGLSNETADKIGNFvKERGPPLELLSKLRQEGSEFLGNASsRAALDELEIMFKA 579
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  1219 LRALKISHQLYFMPLCVYNFEFYDgGLMFQAINLAEKSELICAGGRYDKLVRFFdpplmrTARKKHVVGICFALEKlVFS 1298
Cdd:PLN02972  580 LEKSKAIGKIVFDLSLARGLDYYT-GVIYEAVFKGAQVGSIAAGGRYDNLVGMF------SGKQVPAVGVSLGIER-VFA 651
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  1299 MLRYirfHNSKQSSKHSPSPTlksvgpwaprrvDVLVTSIGKDSILEKCSLLQELWALNIQADIVLrgASSLEEIVTHYR 1378
Cdd:PLN02972  652 IMEQ---QEEEKSQVIRPTET------------EVLVSIIGDDKLALAAELVSELWNAGIKAEYKV--STRKAKHLKRAK 714
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 63054755  1379 SEGINWVLVVRQKNTQmEHSVKARNILKNEDDEIRFDEVGMWLLGEI 1425
Cdd:PLN02972  715 ESGIPWMVLVGEKELS-KGFVKLKNLEAGVEEEVDRTCFVQELKAEL 760
 
Name Accession Description Interval E-value
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
549-917 3.98e-143

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: 440.27  E-value: 3.98e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  549 VSRYETDFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENSRILREVMTLSRLHHEHVVRYYTAWVETEAnd 628
Cdd:cd14046    1 FSRYLTDFEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIKLRSESKNNSRILREVMLLSRLNHQHVVRYYQAWIERAN-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  629 tvteiissdseslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkegssdkdssie 708
Cdd:cd14046      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  709 eassvktqenglnatLYIQMEYCEKLSLQDIIRDKI--PVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNV 786
Cdd:cd14046   79 ---------------LYIQMEYCEKSTLRDLIDSGLfqDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNV 143
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  787 KLGDFGLATENEN-----YQDNNDKWKNRQSADEDLTTGVGTALYVAPELLSRRnGVRYDAKVDMYSLGIILFEMCMTFS 861
Cdd:cd14046  144 KIGDFGLATSNKLnvelaTQDINKSTSAALGSSGDLTGNVGTALYVAPEVQSGT-KSTYNEKVDMYSLGIIFFEMCYPFS 222
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  862 TSMERIRIIDTIRSPSISFPSTFPFSRASHEFKVIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd14046  223 TGMERVQILTALRSVSIEFPPDFDDNKHSKQAKLIRWLLNHDPAKRPSAQELLKSE 278
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
241-508 1.46e-95

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: 308.52  E-value: 1.46e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  241 ISHSNLSTLTLVKPESKEISLQDCVFLlrtvrISTPYWSTEDGKREIQELEYELESLKVIRHDLLASIYEYQLERETRGY 320
Cdd:cd14012    1 SSESPSGTFYLVYEVVLDNSKKPGKFL-----TSQEYFKTSNGKKQIQLLEKELESLKKLRHPNLVSYLAFSIERRGRSD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  321 GWRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHRTFAKLMDFGFTR 400
Cdd:cd14012   76 GWKVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAGTGIVKLTDYSLGK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  401 TLRDMNAshpfninSQSITNILPEGLYPPEVSESSFaAASRKTDIWCFGLLVLQMLCGAHVLNKFSSLKLIMthVIPLLP 480
Cdd:cd14012  156 TLLDMCS-------RGSLDEFKQTYWLPPELAQGSK-SPTRKTDVWDLGLLFLQMLFGLDVLEKYTSPNPVL--VSLDLS 225
                        250       260
                 ....*....|....*....|....*...
gi 63054755  481 GSYQDLVRRCLMRDSRKRPSAIDLLSSH 508
Cdd:cd14012  226 ASLQDFLSKCLSLDPKKRPTALELLPHE 253
HGTP_anticodon2 pfam12745
Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on ...
1326-1575 6.23e-81

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: 267.16  E-value: 6.23e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   1326 WAPRRVDVLVTSIGKDSI-LEKCSLLQELWALNIQADIVLRGASSLEEIVTHYRSEGINWVLVVRQKN---TQMEHSVKA 1401
Cdd:pfam12745    1 WKPRRCDVLVASFDASILrTTGVEILQELWAHGISADLAVDASYSPEDLVSRARDDGVSWIVIIKQQNkssDSKYKPLKV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   1402 RNILKNEDDEIRFDEVGMWLLGEINER-KRNESMLQSKRILDSAQQDVAKFVDTSQSN----------LDVQLISLKdVN 1470
Cdd:pfam12745   81 KNLLRKEDVDLDSDELVSWLRGEIRERdQREGTALSPKSLRAPSQPEDDGSSQDGPLFsvdirqkvvvVLNDATRSK-KS 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   1471 DRKYKWKHKQNAMNKVYDLVQSAIresseDAIALAVDCDSEAMEKLRSTTTLDEESWKRLIESCPASQREYMQRLQKKLV 1550
Cdd:pfam12745  160 NKRNKWEQEDDAQNAAASLVKSLL-----NGPIAAIDTRDEVLDMISITSLSDPDEWRKVIQSVPTSPRSYATNIYNLLS 234
                          250       260
                   ....*....|....*....|....*
gi 63054755   1551 TLAEQDKKRVWICSFRTNEIYLYGL 1575
Cdd:pfam12745  235 KEASKGTKWAILYNFRTGKCCYYDL 259
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
556-915 1.86e-67

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 228.18  E-value: 1.86e-67
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755     556 FEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENSRILREVMTLSRLHHEHVVRYYtawveteandtvteiis 635
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLY----------------- 63
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755     636 sdseslsqslnmavdfrqssslpadklsslDIHFEDDYnssadeedpeasdisfqysntsdkegssdkdssieeassvkt 715
Cdd:smart00220   64 ------------------------------DVFEDEDK------------------------------------------ 71
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755     716 qenglnatLYIQMEYCEKLSLQDIIRDK--IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGL 793
Cdd:smart00220   72 --------LYLVMEYCEGGDLFDLLKKRgrLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGL 143
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755     794 ATENENyqdnndkwknrqsaDEDLTTGVGTALYVAPELLSRRngvRYDAKVDMYSLGIILFEMCM---TFSTSMERIRII 870
Cdd:smart00220  144 ARQLDP--------------GEKLTTFVGTPEYMAPEVLLGK---GYGKAVDIWSLGVILYELLTgkpPFPGDDQLLELF 206
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|....*.
gi 63054755     871 DTIRSPSISFPStfPFSRASHEFK-VIHCLLQHDPTKRPSSQELLE 915
Cdd:smart00220  207 KKIGKPKPPFPP--PEWDISPEAKdLIRKLLVKDPEKRLTAEEALQ 250
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
556-915 6.38e-43

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 164.80  E-value: 6.38e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  556 FEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLV--LLSDDKENSRILREVMTLSRLHHEHVVRYYtawveteandtvtei 633
Cdd:COG0515    9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRpeLAADPEARERFRREARALARLNHPNIVRVY--------------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  634 issdseslsqslnmavdfrqssslpadklssldihfedDYnssaDEEDPeasdisfqysntsdkegssdkdssieeassv 713
Cdd:COG0515   74 --------------------------------------DV----GEEDG------------------------------- 80
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  714 ktqenglnaTLYIQMEYCEKLSLQDIIRDK--IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDF 791
Cdd:COG0515   81 ---------RPYLVMEYVEGESLADLLRRRgpLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDF 151
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  792 GLAtenenyqdnndkwknRQSADEDLT---TGVGTALYVAPELLSrrnGVRYDAKVDMYSLGIILFEMC-----MTFSTS 863
Cdd:COG0515  152 GIA---------------RALGGATLTqtgTVVGTPGYMAPEQAR---GEPVDPRSDVYSLGVTLYELLtgrppFDGDSP 213
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 63054755  864 MERIRIIdtIRSPSISFPSTFPfsRASHEF-KVIHCLLQHDPTKRPSS-QELLE 915
Cdd:COG0515  214 AELLRAH--LREPPPPPSELRP--DLPPALdAIVLRALAKDPEERYQSaAELAA 263
RWD_GCN2 cd23823
RWD domain of eIF-2-alpha kinase GCN2 and related proteins; GCN2 (EC 2.7.11.1), also called ...
11-128 9.86e-35

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: 128.88  E-value: 9.86e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   11 KEIQENEIEALKAIFMDDFEELkvRNAWNVTNGHVYCIHLCS-RSANSKSIAKLDLCIELGRSYPYVKPVIKLQNGENVL 89
Cdd:cd23823    1 EEEQEEELEALQSIYGDDFEDL--SSKKAVWSPPEFRIRLRPqEGESEENHVSVDLHVKFPPTYPDVPPEIELENVKGLS 78
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 63054755   90 NSQIRFLLDKLDTKAKDLLGEEMIFELASIVQDYLNDWQ 128
Cdd:cd23823   79 DEQLEELLKELEELAKELLGEEMIFELAEAVQEFLEEHN 117
Pkinase pfam00069
Protein kinase domain;
556-916 5.61e-30

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 119.27  E-value: 5.61e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755    556 FEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLS-DDKENSRILREVMTLSRLHHEHVVRYYTAwveteandtvteii 634
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKiKKKKDKNILREIKILKKLNHPNIVRLYDA-------------- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755    635 ssdseslsqslnmavdfrqssslpadklssldihFEDDYNssadeedpeasdisfqysntsdkegssdkdssieeassvk 714
Cdd:pfam00069   67 ----------------------------------FEDKDN---------------------------------------- 72
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755    715 tqenglnatLYIQMEYCEKLSLQDIIRDKIPVDE--MWRLFRQILEALAYihsrgmmhrdlkpgnifldenrnvklgdfg 792
Cdd:pfam00069   73 ---------LYLVLEYVEGGSLFDLLSEKGAFSEreAKFIMKQILEGLES------------------------------ 113
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755    793 latenenyqdnndkwknrqsaDEDLTTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMcMT------FSTSMER 866
Cdd:pfam00069  114 ---------------------GSSLTTFVGTPWYMAPEVLGGNP---YGPKVDVWSLGCILYEL-LTgkppfpGINGNEI 168
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 63054755    867 IRIIDTIRSPSISFPSTFpfsraSHEFK-VIHCLLQHDPTKRPSSQELLES 916
Cdd:pfam00069  169 YELIIDQPYAFPELPSNL-----SEEAKdLLKKLLKKDPSKRLTATQALQH 214
PLN02972 PLN02972
Histidyl-tRNA synthetase
990-1425 1.04e-29

Histidyl-tRNA synthetase


Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 128.08  E-value: 1.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   990 VRDH----VVKVFRRHGAKERESHILFPKSS---QYDKDQASV-SLLDKNGTLLQLPYDTVLPYARNVARNAVEEEKTYL 1061
Cdd:PLN02972  343 IREKafsiITSVFKRHGATALDTPVFELRETlmgKYGEDSKLIyDLADQGGELCSLRYDLTVPFARYVAMNGITSFKRYQ 422
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  1062 ISDVF-REAKGGGRPKAIKEISFDITTNSDNLDwYDAETIKALDEVLTEIpSLTESCILINHADILSSILDYLQVSKDKR 1140
Cdd:PLN02972  423 IAKVYrRDNPSKGRYREFYQCDFDIAGVYEPMG-PDFEIIKVLTELLDEL-DIGTYEVKLNHRKLLDGMLEICGVPPEKF 500
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  1141 RMATHILGQINQRlTLSQVRNQLRIESLVPSTTLDDLSLF-DFRENYEEGASKLRKIFGKEMPQKM-RTALNYMERVVKL 1218
Cdd:PLN02972  501 RTICSSIDKLDKQ-SFEQVKKEMVEEKGLSNETADKIGNFvKERGPPLELLSKLRQEGSEFLGNASsRAALDELEIMFKA 579
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  1219 LRALKISHQLYFMPLCVYNFEFYDgGLMFQAINLAEKSELICAGGRYDKLVRFFdpplmrTARKKHVVGICFALEKlVFS 1298
Cdd:PLN02972  580 LEKSKAIGKIVFDLSLARGLDYYT-GVIYEAVFKGAQVGSIAAGGRYDNLVGMF------SGKQVPAVGVSLGIER-VFA 651
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  1299 MLRYirfHNSKQSSKHSPSPTlksvgpwaprrvDVLVTSIGKDSILEKCSLLQELWALNIQADIVLrgASSLEEIVTHYR 1378
Cdd:PLN02972  652 IMEQ---QEEEKSQVIRPTET------------EVLVSIIGDDKLALAAELVSELWNAGIKAEYKV--STRKAKHLKRAK 714
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 63054755  1379 SEGINWVLVVRQKNTQmEHSVKARNILKNEDDEIRFDEVGMWLLGEI 1425
Cdd:PLN02972  715 ESGIPWMVLVGEKELS-KGFVKLKNLEAGVEEEVDRTCFVQELKAEL 760
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
12-124 1.59e-24

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: 99.71  E-value: 1.59e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755     12 EIQENEIEALKAIFMDDFEELKvRNAWNvTNGHVYCIHLCSRSANSKSIAKLDLCIELGRSYPYVKPVIKLQNGENVLNS 91
Cdd:pfam05773    1 EEQEEELEALESIYPDEFEVIS-DSPYE-SLEIEIKLSLDSDESDSSHLPPLVLKFTLPEDYPDEPPKISLSSPWNLSDE 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 63054755     92 QIRFLLDKLDTKAKDLLGEEMIFELASIVQDYL 124
Cdd:pfam05773   79 QVLSLLEELEELAEENLGEVMIFELIEWLQENL 111
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
716-856 3.32e-24

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 109.11  E-value: 3.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   716 QENGLNatlYIQMEYCEKLSLQDIIRD--KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGL 793
Cdd:NF033483   77 EDGGIP---YIVMEYVDGRTLKDYIREhgPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGI 153
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755   794 AtenenyqdnndkwknRQSADEDLT-TG--VGTALYVAPElLSRrnGVRYDAKVDMYSLGIILFEM 856
Cdd:NF033483  154 A---------------RALSSTTMTqTNsvLGTVHYLSPE-QAR--GGTVDARSDIYSLGIVLYEM 201
RWD smart00591
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily ...
17-127 1.94e-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: 96.27  E-value: 1.94e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755      17 EIEALKAIFMDDFEELKVRNawnvtNGHVYCIHLCSRSANS-KSIAKLDLCIELGRSYPYVKPVIKLQNGENVLNSQIRF 95
Cdd:smart00591    1 ELEALESIYPEDFEVIDEDA-----RIPEITIKLSPSSDEGeDQYVSLTLQVKLPENYPDEAPPISLLNSEGLSDEQLAE 75
                            90       100       110
                    ....*....|....*....|....*....|..
gi 63054755      96 LLDKLDTKAKDLLGEEMIFELASIVQDYLNDW 127
Cdd:smart00591   76 LLKKLEEIAEENLGEVMIFELVEKLQEFLSEF 107
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
724-917 4.76e-23

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 104.71  E-value: 4.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   724 LYIQMEYCEKLSLQDIIR----DKIPVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEn 797
Cdd:PTZ00267  140 LLLIMEYGSGGDLNKQIKqrlkEHLPFQEyeVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQ- 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   798 enYQDnndkwknrqSADEDLTTG-VGTALYVAPELLSRRngvRYDAKVDMYSLGIILFEMcMTFSTSMERIRIIDTIRSP 876
Cdd:PTZ00267  219 --YSD---------SVSLDVASSfCGTPYYLAPELWERK---RYSKKADMWSLGVILYEL-LTLHRPFKGPSQREIMQQV 283
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 63054755   877 SISFPSTFPFSRASHEFKVIHCLLQHDPTKRPSSQELLESE 917
Cdd:PTZ00267  284 LYGKYDPFPCPVSSGMKALLDPLLSKNPALRPTTQQLLHTE 324
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
293-505 2.51e-21

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 95.29  E-value: 2.51e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755     293 ELESLKVIRHDLLASIYEYQLEREtrgygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISH 372
Cdd:smart00220   47 EIKILKKLKHPNIVRLYDVFEDED------KLYLVMEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVH 120
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755     373 KSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDmnashPFNINSQSITnilPEglY-PPEV-SESSFaaaSRKTDIWCFGL 450
Cdd:smart00220  121 RDLKPENILLDEDGH---VKLADFGLARQLDP-----GEKLTTFVGT---PE--YmAPEVlLGKGY---GKAVDIWSLGV 184
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63054755     451 LVLQMLCG----AHVLNKFSSLKLIMTHVIPLLPGSY------QDLVRRCLMRDSRKRPSAIDLL 505
Cdd:smart00220  185 ILYELLTGkppfPGDDQLLELFKKIGKPKPPFPPPEWdispeaKDLIRKLLVKDPEKRLTAEEAL 249
HisRS-like_core cd00773
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ...
990-1295 4.00e-21

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: 94.59  E-value: 4.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  990 VRDHVVKVFRRHGAKEreshILFP----------KSSQYDKDQAsVSLLDKNGTLLQLPYDTVLPYARNVARNAVEEE-- 1057
Cdd:cd00773    8 IEDTLREVFERYGYEE----IDTPvfeytelflrKSGDEVSKEM-YRFKDKGGRDLALRPDLTAPVARAVAENLLSLPlp 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755 1058 -KTYLISDVFR-EAKGGGRPKAIKEISFDITTnSDNLDwYDAETIKALDEVLTEIPsLTESCILINHADILSSIldylqv 1135
Cdd:cd00773   83 lKLYYIGPVFRyERPQKGRYREFYQVGVEIIG-SDSPL-ADAEVIALAVEILEALG-LKDFQIKINHRGILDGI------ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755 1136 skdkrrmathilgqinqrltlsqvrnqlrieslvpsttlddLSLFDFRENYEEgasKLRKIFGKEmpqkmrtALNYMERV 1215
Cdd:cd00773  154 -----------------------------------------AGLLEDREEYIE---RLIDKLDKE-------ALAHLEKL 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755 1216 VKLLRALKISHQLYFMPLCVYNFEFYdGGLMFQAI-NLAEKSELICAGGRYDKLVRFFdpplmrTARKKHVVGICFALEK 1294
Cdd:cd00773  183 LDYLEALGVDIKYSIDLSLVRGLDYY-TGIVFEAVaDGLGAQGSIAGGGRYDGLLEEF------GGEDVPAVGFAIGLER 255

                 .
gi 63054755 1295 L 1295
Cdd:cd00773  256 L 256
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
293-505 1.94e-18

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 90.46  E-value: 1.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  293 ELESLKVIRHDLLASIYEYQLEREtrgygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISH 372
Cdd:COG0515   57 EARALARLNHPNIVRVYDVGEEDG------RPYLVMEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVH 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  373 KSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDMNASHPFninsqsitniLPEG--LY-PPEVSESsfAAASRKTDIWCFG 449
Cdd:COG0515  131 RDIKPANILLTPDGR---VKLIDFGIARALGGATLTQTG----------TVVGtpGYmAPEQARG--EPVDPRSDVYSLG 195
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  450 LLVLQMLCGAHVLNKFSSLKLIMTHV----------IPLLPGSYQDLVRRCLMRDSRKRP-SAIDLL 505
Cdd:COG0515  196 VTLYELLTGRPPFDGDSPAELLRAHLrepppppselRPDLPPALDAIVLRALAKDPEERYqSAAELA 262
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
724-914 3.42e-14

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 78.35  E-value: 3.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755    724 LYIQMEYCEKLSLQDIIRDK--IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFL---DENRNVKLGDFGLATENE 798
Cdd:TIGR03903   54 LFAVFEYVPGRTLREVLAADgaLPAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVsqtGVRPHAKVLDFGIGTLLP 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755    799 NYQDNNDKWKNRQsadedlTTGVGTALYVAPELLsrrNGVRYDAKVDMYSLGIILFEmCMTFSTSMERIRIIDTIRSPSI 878
Cdd:TIGR03903  134 GVRDADVATLTRT------TEVLGTPTYCAPEQL---RGEPVTPNSDLYAWGLIFLE-CLTGQRVVQGASVAEILYQQLS 203
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 63054755    879 SFPSTFPFSRASHEF-KVIHCLLQHDPTKRPSSQELL 914
Cdd:TIGR03903  204 PVDVSLPPWIAGHPLgQVLRKALNKDPRQRAASAPAL 240
hisZ_biosyn_reg TIGR00443
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ...
990-1272 4.48e-14

ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA synthetase, found in Bacillus subtilis, Synechocystis sp., Aquifex aeolicus, and others, are in fact a regulatory subunit of ATP phosphoribosyltransferase, and usually encoded by a gene adjacent to that encoding the catalytic subunit. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273081 [Multi-domain]  Cd Length: 313  Bit Score: 74.96  E-value: 4.48e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755    990 VRDHVVKVFRRHGAKEreshILFPKSSQYDKDQASVS--------LLDKNGTLLQLPYDTVLPYARNVA---RNAVEEEK 1058
Cdd:TIGR00443   14 IERQLQDVFRSWGYQE----IITPTLEYLDTLSAGSGilnedlfkLFDQLGRVLGLRPDMTAPIARLVStrlRDRPLPLR 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   1059 TYLISDVFR-EAKGGGRPKAIK----EISFDITTNSDnldwydAETIKALDEVLTEIpSLTESCILINHADILSSILDYL 1133
Cdd:TIGR00443   90 LCYAGNVFRtNESGGGRSREFTqagvELIGAGGPAAD------AEVIALLIEALKAL-GLKDFKIELGHVGLVRALLEEA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   1134 QVSKDKRRMATHILGQinqrltlsqvRNQLRIESLVPSTTLDD------LSLFDFRENYEEGASKLRKIFGKEmpqKMRT 1207
Cdd:TIGR00443  163 GLPEEAREALREALAR----------KDLVALEELVAELGLSPevrerlLALPRLRGDGEEVLEEARALAGSE---TAEA 229
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755   1208 ALNYMERVVKLLRALKISHQLYFmPLC-VYNFEFYDGgLMFQAInLAEKSELICAGGRYDKLVRFF 1272
Cdd:TIGR00443  230 ALDELEAVLELLEARGVEEYISL-DLGlVRGYHYYTG-LIFEGY-APGLGAPLAGGGRYDELLGRF 292
HisZ COG3705
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
1096-1272 6.04e-10

ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];


Pssm-ID: 442919 [Multi-domain]  Cd Length: 312  Bit Score: 62.50  E-value: 6.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755 1096 DAETIKALDEVLTEIpSLTESCILINHADILSSILDYLQVSKDKRRMATHILGQinqrltlsqvRNQLRIESLVPSTTLD 1175
Cdd:COG3705  124 DAEVIALALEALKAA-GLEDFTLDLGHVGLFRALLEALGLSEEQREELRRALAR----------KDAVELEELLAELGLS 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755 1176 D------LSLFDFRENyEEGASKLRKIFGKEmpqKMRTALNYMERVVKLLRALKISHQLYFMPLCVYNFEFYDGgLMFQA 1249
Cdd:COG3705  193 EelaealLALPELYGG-EEVLARARALLLDA---AIRAALDELEALAEALAARGPDVRLTFDLSELRGYDYYTG-IVFEA 267
                        170       180
                 ....*....|....*....|...
gi 63054755 1250 InLAEKSELICAGGRYDKLVRFF 1272
Cdd:COG3705  268 Y-APGVGDPLARGGRYDGLLAAF 289
tRNA-synt_His pfam13393
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ...
1096-1272 1.15e-06

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: 52.20  E-value: 1.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   1096 DAETIKALDEVL--TEIPSLTescILINHADILSSILDYLQVSKDKRRMATHILgqinQRLTLSQVRNQLRiESLVPSTT 1173
Cdd:pfam13393  127 DAEIISLLLEALaaAGVPGVT---LDLGHVGLVRALLEAAGLSEALEEALRAAL----QRKDAAELAELAA-EAGLPPAL 198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   1174 LDDLSLFDFRENYEEGASKLRKIFGKemPQKMRTALNYMERVVKLLRALKISHQLYFMPLCVYNFEFYDGgLMFQAInLA 1253
Cdd:pfam13393  199 RRALLALPDLYGGPEVLDEARAALPG--LPALQEALDELEALAALLEALGDGVRLTFDLAELRGYEYYTG-IVFAAY-AP 274
                          170
                   ....*....|....*....
gi 63054755   1254 EKSELICAGGRYDKLVRFF 1272
Cdd:pfam13393  275 GVGEPLARGGRYDDLGAAF 293
Pkinase pfam00069
Protein kinase domain;
293-507 4.24e-06

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 49.55  E-value: 4.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755    293 ELESLKVIRHDLLASIYEYqLERETRgygwrLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAelhrlgish 372
Cdd:pfam00069   48 EIKILKKLNHPNIVRLYDA-FEDKDN-----LYLVLEYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLE--------- 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755    373 KSLHLDNVVlfhsGHRTFAklmdfgftrtlrdmnashpfninsqsitnilpeglyPPEVSESSfaAASRKTDIWCFGLLV 452
Cdd:pfam00069  113 SGSSLTTFV----GTPWYM------------------------------------APEVLGGN--PYGPKVDVWSLGCIL 150
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63054755    453 LQMLCG----AHVLNKFSSLKLIMTHVIPLLPGSY-----QDLVRRCLMRDSRKRPSAIDLLSS 507
Cdd:pfam00069  151 YELLTGkppfPGINGNEIYELIIDQPYAFPELPSNlseeaKDLLKKLLKKDPSKRLTATQALQH 214
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
284-458 4.89e-05

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 47.51  E-value: 4.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   284 KREI------QELEYELESLKVIRHDLLASIYE-YQLERetrgygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSN 356
Cdd:PTZ00263   53 KREIlkmkqvQHVAQEKSILMELSHPFIVNMMCsFQDEN-------RVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHA 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   357 NILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDmnasHPFNINSQsitnilPEGLyPPEVSESSf 436
Cdd:PTZ00263  126 ELVLAFEYLHSKDIIYRDLKPENLLLDNKGH---VKVTDFGFAKKVPD----RTFTLCGT------PEYL-APEVIQSK- 190
                         170       180
                  ....*....|....*....|..
gi 63054755   437 aAASRKTDIWCFGLLVLQMLCG 458
Cdd:PTZ00263  191 -GHGKAVDWWTMGVLLYEFIAG 211
 
Name Accession Description Interval E-value
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
549-917 3.98e-143

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: 440.27  E-value: 3.98e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  549 VSRYETDFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENSRILREVMTLSRLHHEHVVRYYTAWVETEAnd 628
Cdd:cd14046    1 FSRYLTDFEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIKLRSESKNNSRILREVMLLSRLNHQHVVRYYQAWIERAN-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  629 tvteiissdseslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkegssdkdssie 708
Cdd:cd14046      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  709 eassvktqenglnatLYIQMEYCEKLSLQDIIRDKI--PVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNV 786
Cdd:cd14046   79 ---------------LYIQMEYCEKSTLRDLIDSGLfqDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNV 143
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  787 KLGDFGLATENEN-----YQDNNDKWKNRQSADEDLTTGVGTALYVAPELLSRRnGVRYDAKVDMYSLGIILFEMCMTFS 861
Cdd:cd14046  144 KIGDFGLATSNKLnvelaTQDINKSTSAALGSSGDLTGNVGTALYVAPEVQSGT-KSTYNEKVDMYSLGIIFFEMCYPFS 222
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  862 TSMERIRIIDTIRSPSISFPSTFPFSRASHEFKVIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd14046  223 TGMERVQILTALRSVSIEFPPDFDDNKHSKQAKLIRWLLNHDPAKRPSAQELLKSE 278
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
241-508 1.46e-95

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: 308.52  E-value: 1.46e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  241 ISHSNLSTLTLVKPESKEISLQDCVFLlrtvrISTPYWSTEDGKREIQELEYELESLKVIRHDLLASIYEYQLERETRGY 320
Cdd:cd14012    1 SSESPSGTFYLVYEVVLDNSKKPGKFL-----TSQEYFKTSNGKKQIQLLEKELESLKKLRHPNLVSYLAFSIERRGRSD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  321 GWRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHRTFAKLMDFGFTR 400
Cdd:cd14012   76 GWKVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAGTGIVKLTDYSLGK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  401 TLRDMNAshpfninSQSITNILPEGLYPPEVSESSFaAASRKTDIWCFGLLVLQMLCGAHVLNKFSSLKLIMthVIPLLP 480
Cdd:cd14012  156 TLLDMCS-------RGSLDEFKQTYWLPPELAQGSK-SPTRKTDVWDLGLLFLQMLFGLDVLEKYTSPNPVL--VSLDLS 225
                        250       260
                 ....*....|....*....|....*...
gi 63054755  481 GSYQDLVRRCLMRDSRKRPSAIDLLSSH 508
Cdd:cd14012  226 ASLQDFLSKCLSLDPKKRPTALELLPHE 253
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
550-917 1.51e-84

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: 278.02  E-value: 1.51e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  550 SRYETDFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENSRILREVMTLSRLHHEHVVRYYTAWVETEandt 629
Cdd:cd13996    2 SRYLNDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSASEKVLREVKALAKLNHPNIVRYYTAWVEEP---- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  630 vteiissdseslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkegssdkdssiee 709
Cdd:cd13996      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  710 assvktqenglnaTLYIQMEYCEKLSLQDIIRD-----KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDEN- 783
Cdd:cd13996   78 -------------PLYIQMELCEGGTLRDWIDRrnsssKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDd 144
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  784 RNVKLGDFGLATENENYQDNNDKWKNRQS-ADEDLTTGVGTALYVAPELLSrrnGVRYDAKVDMYSLGIILFEMCMTFST 862
Cdd:cd13996  145 LQVKIGDFGLATSIGNQKRELNNLNNNNNgNTSNNSVGIGTPLYASPEQLD---GENYNEKADIYSLGIILFEMLHPFKT 221
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  863 SMERIRIIDTIRspSISFPSTFpfsRASH--EFKVIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd13996  222 AMERSTILTDLR--NGILPESF---KAKHpkEADLIQSLLSKNPEERPSAEQLLRSL 273
HGTP_anticodon2 pfam12745
Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on ...
1326-1575 6.23e-81

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: 267.16  E-value: 6.23e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   1326 WAPRRVDVLVTSIGKDSI-LEKCSLLQELWALNIQADIVLRGASSLEEIVTHYRSEGINWVLVVRQKN---TQMEHSVKA 1401
Cdd:pfam12745    1 WKPRRCDVLVASFDASILrTTGVEILQELWAHGISADLAVDASYSPEDLVSRARDDGVSWIVIIKQQNkssDSKYKPLKV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   1402 RNILKNEDDEIRFDEVGMWLLGEINER-KRNESMLQSKRILDSAQQDVAKFVDTSQSN----------LDVQLISLKdVN 1470
Cdd:pfam12745   81 KNLLRKEDVDLDSDELVSWLRGEIRERdQREGTALSPKSLRAPSQPEDDGSSQDGPLFsvdirqkvvvVLNDATRSK-KS 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   1471 DRKYKWKHKQNAMNKVYDLVQSAIresseDAIALAVDCDSEAMEKLRSTTTLDEESWKRLIESCPASQREYMQRLQKKLV 1550
Cdd:pfam12745  160 NKRNKWEQEDDAQNAAASLVKSLL-----NGPIAAIDTRDEVLDMISITSLSDPDEWRKVIQSVPTSPRSYATNIYNLLS 234
                          250       260
                   ....*....|....*....|....*
gi 63054755   1551 TLAEQDKKRVWICSFRTNEIYLYGL 1575
Cdd:pfam12745  235 KEASKGTKWAILYNFRTGKCCYYDL 259
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
556-915 1.86e-67

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 228.18  E-value: 1.86e-67
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755     556 FEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENSRILREVMTLSRLHHEHVVRYYtawveteandtvteiis 635
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLY----------------- 63
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755     636 sdseslsqslnmavdfrqssslpadklsslDIHFEDDYnssadeedpeasdisfqysntsdkegssdkdssieeassvkt 715
Cdd:smart00220   64 ------------------------------DVFEDEDK------------------------------------------ 71
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755     716 qenglnatLYIQMEYCEKLSLQDIIRDK--IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGL 793
Cdd:smart00220   72 --------LYLVMEYCEGGDLFDLLKKRgrLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGL 143
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755     794 ATENENyqdnndkwknrqsaDEDLTTGVGTALYVAPELLSRRngvRYDAKVDMYSLGIILFEMCM---TFSTSMERIRII 870
Cdd:smart00220  144 ARQLDP--------------GEKLTTFVGTPEYMAPEVLLGK---GYGKAVDIWSLGVILYELLTgkpPFPGDDQLLELF 206
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|....*.
gi 63054755     871 DTIRSPSISFPStfPFSRASHEFK-VIHCLLQHDPTKRPSSQELLE 915
Cdd:smart00220  207 KKIGKPKPPFPP--PEWDISPEAKdLIRKLLVKDPEKRLTAEEALQ 250
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
550-917 1.46e-58

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: 203.89  E-value: 1.46e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  550 SRYETDFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENSR-ILREVMTLSRLHHEHVVRYYTAWVETeand 628
Cdd:cd14049    2 SRYLNEFEEIARLGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMkVLREVKVLAGLQHPNIVGYHTAWMEH---- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  629 tvteiissdseslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkegssdkdssie 708
Cdd:cd14049      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  709 eassvktqengLNATLYIQMEYCEkLSLQDIIRDK--------------IPVDEMW--RLFRQILEALAYIHSRGMMHRD 772
Cdd:cd14049   78 -----------VQLMLYIQMQLCE-LSLWDWIVERnkrpceeefksapyTPVDVDVttKILQQLLEGVTYIHSMGIVHRD 145
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  773 LKPGNIFLD-ENRNVKLGDFGLATENEnYQDNNDKWKNRQSADEDLTTGVGTALYVAPELLsrrNGVRYDAKVDMYSLGI 851
Cdd:cd14049  146 LKPRNIFLHgSDIHVRIGDFGLACPDI-LQDGNDSTTMSRLNGLTHTSGVGTCLYAAPEQL---EGSHYDFKSDMYSIGV 221
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  852 ILFEMCMTFSTSMERIRIIDTIRSPsiSFPSTFPfSRASHEFKVIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd14049  222 ILLELFQPFGTEMERAEVLTQLRNG--QIPKSLC-KRWPVQAKYIKLLTSTEPSERPSASQLLESE 284
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
550-917 2.28e-58

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: 203.18  E-value: 2.28e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  550 SRYETDFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENSRILREVMTLSRLHHEHVVRYYTAWveteandt 629
Cdd:cd14048    2 SRFLTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLPNNELAREKVLREVRALAKLDHPGIVRYFNAW-------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  630 vteiissdseslsqslnmavdfrqssslpadklssldihfeddynssaDEEDPEasdisfqysntsdkegssdkdssiee 709
Cdd:cd14048   74 ------------------------------------------------LERPPE-------------------------- 79
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  710 assvKTQENGLNATLYIQMEYCEKLSLQDIIRDKIPVDE-----MWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENR 784
Cdd:cd14048   80 ----GWQEKMDEVYLYIQMQLCRKENLKDWMNRRCTMESrelfvCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDD 155
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  785 NVKLGDFGLATEnenyQDNNDKWKNRQS---ADEDLTTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMCMTFS 861
Cdd:cd14048  156 VVKVGDFGLVTA----MDQGEPEQTVLTpmpAYAKHTGQVGTRLYMSPEQIHGNQ---YSEKVDIFALGLILFELIYSFS 228
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  862 TSMERIRIIDTIRspSISFPSTFpFSRASHEFKVIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd14048  229 TQMERIRTLTDVR--KLKFPALF-TNKYPEERDMVQQMLSPSPSERPEAHEVIEHA 281
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
555-919 7.28e-54

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: 189.21  E-value: 7.28e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  555 DFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLS-DDKENSRILREVMTLSRLHHEHVVRYYTAWVEteandtvtei 633
Cdd:cd08215    1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNmSEKEREEALNEVKLLSKLKHPNIVKYYESFEE---------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  634 issdseslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkegssdkdssieeassv 713
Cdd:cd08215      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  714 ktqenglNATLYIQMEYCEKLSLQDIIRDK------IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVK 787
Cdd:cd08215   71 -------NGKLCIVMEYADGGDLAQKIKKQkkkgqpFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVK 143
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  788 LGDFGLAtenenyqdnndkwKNRQSADEDLTTGVGTALYVAPELLSRRngvRYDAKVDMYSLGIILFEMCM---TF-STS 863
Cdd:cd08215  144 LGDFGIS-------------KVLESTTDLAKTVVGTPYYLSPELCENK---PYNYKSDIWALGCVLYELCTlkhPFeANN 207
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  864 MERI--RIIDTIRSPsisFPSTFpfsraSHEFK-VIHCLLQHDPTKRPSSQELLESEAI 919
Cdd:cd08215  208 LPALvyKIVKGQYPP---IPSQY-----SSELRdLVNSMLQKDPEKRPSANEILSSPFI 258
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
555-919 2.05e-52

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: 185.44  E-value: 2.05e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  555 DFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLS-DDKENSRILREVMTLSRLHHEHVVRYYtawveteandtvtei 633
Cdd:cd08217    1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKmSEKEKQQLVSEVNILRELKHPNIVRYY--------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  634 issdseslsqslnmavdfrqssslpaDKlssldIHfeddynssadeedpeasdisfqysntsDKEgssdkdssieeassv 713
Cdd:cd08217   66 --------------------------DR-----IV---------------------------DRA--------------- 72
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  714 ktqenglNATLYIQMEYCEKLSLQDII------RDKIPVDEMWRLFRQILEALAYIHSRG-----MMHRDLKPGNIFLDE 782
Cdd:cd08217   73 -------NTTLYIVMEYCEGGDLAQLIkkckkeNQYIPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFLDS 145
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  783 NRNVKLGDFGLAtenenyqdnndkwKNRQSADEDLTTGVGTALYVAPELLSRRngvRYDAKVDMYSLGIILFEMCM---- 858
Cdd:cd08217  146 DNNVKLGDFGLA-------------RVLSHDSSFAKTYVGTPYYMSPELLNEQ---SYDEKSDIWSLGCLIYELCAlhpp 209
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054755  859 -TFSTSMERIRIIDTIRSPSIsfPSTFpfsraSHE-FKVIHCLLQHDPTKRPSSQELLESEAI 919
Cdd:cd08217  210 fQAANQLELAKKIKEGKFPRI--PSRY-----SSElNEVIKSMLNVDPDKRPSVEELLQLPLI 265
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
549-914 4.55e-51

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: 181.54  E-value: 4.55e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  549 VSRYETDFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLlsddkENSRILREVMTLSRLHHEHVVRYYTAWVETeand 628
Cdd:cd14047    1 DERFRQDFKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVKL-----NNEKAEREVKALAKLDHPNIVRYNGCWDGF---- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  629 tvteiissdseslsqslnmavdfrqssslpadklssldihfedDYNSSADEEDPEASDISFqysntsdkegssdkdssie 708
Cdd:cd14047   72 -------------------------------------------DYDPETSSSNSSRSKTKC------------------- 89
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  709 eassvktqenglnatLYIQMEYCEKLSLQDII--RDKIPVDEM--WRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENR 784
Cdd:cd14047   90 ---------------LFIQMEFCEKGTLESWIekRNGEKLDKVlaLEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTG 154
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  785 NVKLGDFGLATENENYqdnNDKWKNRqsadedlttgvGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMCMTFSTSM 864
Cdd:cd14047  155 KVKIGDFGLVTSLKND---GKRTKSK-----------GTLSYMSPEQISSQD---YGKEVDIYALGLILFELLHVCDSAF 217
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 63054755  865 ERIRIIDTIRSPSIS--FPSTFPFsrashEFKVIHCLLQHDPTKRPSSQELL 914
Cdd:cd14047  218 EKSKFWTDLRNGILPdiFDKRYKI-----EKTIIKKMLSKKPEDRPNASEIL 264
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
562-917 3.27e-50

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: 177.08  E-value: 3.27e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  562 LGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENSRILREVMTLSRLHHEHVVRYYtAWVETEANdtvteiissdsesl 641
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLLEELLREIEILKKLNHPNIVKLY-DVFETENF-------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  642 sqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkegssdkdssieeassvktqengln 721
Cdd:cd00180      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  722 atLYIQMEYCEKLSLQDIIRDK---IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENE 798
Cdd:cd00180   66 --LYLVMEYCEGGSLKDLLKENkgpLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLD 143
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  799 NYQDNNDKwknrqsadedlTTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEmcmtfstsMERIRiidtirspsi 878
Cdd:cd00180  144 SDDSLLKT-----------TGGTTPPYYAPPELLGGRY---YGPKVDIWSLGVILYE--------LEELK---------- 191
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 63054755  879 sfpstfpfsrashefKVIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd00180  192 ---------------DLIRRMLQYDPKKRPSAKELLEHL 215
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
559-915 3.12e-48

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: 173.16  E-value: 3.12e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  559 LEFLGRGGFGEVVKVKNRIDGRFYAVKKLV--LLSDDKENSRILREVMTLSRLHHEHVVRYYtawveteandtvteiiss 636
Cdd:cd14014    5 VRLLGRGGMGEVYRARDTLLGRPVAIKVLRpeLAEDEEFRERFLREARALARLSHPNIVRVY------------------ 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  637 dseslsqslnmavdfrqssslpadklsslDIHFEDDynssadeedpeasdisfqysntsdkegssdkdssieeassvktq 716
Cdd:cd14014   67 -----------------------------DVGEDDG-------------------------------------------- 73
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  717 englnaTLYIQMEYCEKLSLQDIIRDK--IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLA 794
Cdd:cd14014   74 ------RPYIVMEYVEGGSLADLLRERgpLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIA 147
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  795 tenenyqdnndkwknRQSADEDLTTG---VGTALYVAPELLSrrnGVRYDAKVDMYSLGIILFEMCM-----TFSTSME- 865
Cdd:cd14014  148 ---------------RALGDSGLTQTgsvLGTPAYMAPEQAR---GGPVDPRSDIYSLGVVLYELLTgrppfDGDSPAAv 209
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 63054755  866 -RIRIIDTIRSPSISFPSTFPFSRAshefkVIHCLLQHDPTKRPSS-QELLE 915
Cdd:cd14014  210 lAKHLQEAPPPPSPLNPDVPPALDA-----IILRALAKDPEERPQSaAELLA 256
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
555-917 3.76e-46

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


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 167.27  E-value: 3.76e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  555 DFEELEFLGRGGFGEVVKVKNRIDGRFYAVK---KLVLLSDDKEnsRILREVMTLSRLHHEHVVRYYtawveteandtvt 631
Cdd:cd05117    1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKiidKKKLKSEDEE--MLRREIEILKRLDHPNIVKLY------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  632 eiissdseslsqslnmavDFrqssslpadklssldihFEDDYNssadeedpeasdisfqysntsdkegssdkdssieeas 711
Cdd:cd05117   66 ------------------EV-----------------FEDDKN------------------------------------- 73
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  712 svktqenglnatLYIQMEYCEKLSLQDII--RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFL---DENRNV 786
Cdd:cd05117   74 ------------LYLVMELCTGGELFDRIvkKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPI 141
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  787 KLGDFGLATENENyqdnndkwknrqsaDEDLTTGVGTALYVAPELLSRRngvRYDAKVDMYSLGIILFEM---CMTFSTS 863
Cdd:cd05117  142 KIIDFGLAKIFEE--------------GEKLKTVCGTPYYVAPEVLKGK---GYGKKCDIWSLGVILYILlcgYPPFYGE 204
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 63054755  864 MERiRIIDTIRSPSISFPStFPFSRASHEFK-VIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd05117  205 TEQ-ELFEKILKGKYSFDS-PEWKNVSEEAKdLIKRLLVVDPKKRLTAAEALNHP 257
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
555-915 2.67e-44

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: 161.60  E-value: 2.67e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  555 DFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENSrILREVMTLSRLHHEHVVRYYTAwveteandtvteii 634
Cdd:cd05122    1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKES-ILNEIAILKKCKHPNIVKYYGS-------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  635 ssdseslsqslnmavdfrqssslpadklssldiHFEDDYnssadeedpeasdisfqysntsdkegssdkdssieeassvk 714
Cdd:cd05122   66 ---------------------------------YLKKDE----------------------------------------- 71
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  715 tqenglnatLYIQMEYCEKLSLQDIIRDKI-PVDEMWRLF--RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDF 791
Cdd:cd05122   72 ---------LWIVMEFCSGGSLKDLLKNTNkTLTEQQIAYvcKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDF 142
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  792 GLATENENYQDNNdkwknrqsadedltTGVGTALYVAPELLsrrNGVRYDAKVDMYSLGIILFEMC-----MTFSTSMER 866
Cdd:cd05122  143 GLSAQLSDGKTRN--------------TFVGTPYWMAPEVI---QGKPYGFKADIWSLGITAIEMAegkppYSELPPMKA 205
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 63054755  867 IRIIDTirSPSISFPSTfpfSRASHEFK--VIHClLQHDPTKRPSSQELLE 915
Cdd:cd05122  206 LFLIAT--NGPPGLRNP---KKWSKEFKdfLKKC-LQKDPEKRPTAEQLLK 250
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
556-915 6.38e-43

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 164.80  E-value: 6.38e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  556 FEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLV--LLSDDKENSRILREVMTLSRLHHEHVVRYYtawveteandtvtei 633
Cdd:COG0515    9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRpeLAADPEARERFRREARALARLNHPNIVRVY--------------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  634 issdseslsqslnmavdfrqssslpadklssldihfedDYnssaDEEDPeasdisfqysntsdkegssdkdssieeassv 713
Cdd:COG0515   74 --------------------------------------DV----GEEDG------------------------------- 80
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  714 ktqenglnaTLYIQMEYCEKLSLQDIIRDK--IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDF 791
Cdd:COG0515   81 ---------RPYLVMEYVEGESLADLLRRRgpLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDF 151
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  792 GLAtenenyqdnndkwknRQSADEDLT---TGVGTALYVAPELLSrrnGVRYDAKVDMYSLGIILFEMC-----MTFSTS 863
Cdd:COG0515  152 GIA---------------RALGGATLTqtgTVVGTPGYMAPEQAR---GEPVDPRSDVYSLGVTLYELLtgrppFDGDSP 213
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 63054755  864 MERIRIIdtIRSPSISFPSTFPfsRASHEF-KVIHCLLQHDPTKRPSS-QELLE 915
Cdd:COG0515  214 AELLRAH--LREPPPPPSELRP--DLPPALdAIVLRALAKDPEERYQSaAELAA 263
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
555-914 1.04e-41

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: 154.08  E-value: 1.04e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  555 DFEELEFLGRGGFGEVVKVKNRIDGRFYAVKK-LVLLSDDKENSRILREVMTLSRL-HHEHVVRYYTAWveteandtvte 632
Cdd:cd13997    1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVKKsKKPFRGPKERARALREVEAHAALgQHPNIVRYYSSW----------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  633 iissdseslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkegssdkdssieeass 712
Cdd:cd13997      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  713 vktQENGlnaTLYIQMEYCEKLSLQDIIR-----DKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVK 787
Cdd:cd13997   70 ---EEGG---HLYIQMELCENGSLQDALEelspiSKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCK 143
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  788 LGDFGLATENENYQDNNDkwknrqsadedlttgvGTALYVAPELLSrrNGVRYDAKVDMYSLGIILFEMcmtfSTSMERI 867
Cdd:cd13997  144 IGDFGLATRLETSGDVEE----------------GDSRYLAPELLN--ENYTHLPKADIFSLGVTVYEA----ATGEPLP 201
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 63054755  868 RIIDTIRSPSISFPSTFPFSRASHEFK-VIHCLLQHDPTKRPSSQELL 914
Cdd:cd13997  202 RNGQQWQQLRQGKLPLPPGLVLSQELTrLLKVMLDPDPTRRPTADQLL 249
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
555-917 9.68e-41

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: 151.52  E-value: 9.68e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  555 DFEELEFLGRGGFGEVVKVKNRIDGRFYAVK---KLVLlsDDKENSRILREVMTLSRLHHEHVVRYYtawveteandtvt 631
Cdd:cd14003    1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKiidKSKL--KEEIEEKIKREIEIMKLLNHPNIIKLY------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  632 EIISsdseslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysnTSDKegssdkdssieeas 711
Cdd:cd14003   66 EVIE----------------------------------------------------------TENK-------------- 73
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  712 svktqenglnatLYIQMEYCEKLSLQDII--RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLG 789
Cdd:cd14003   74 ------------IYLVMEYASGGELFDYIvnNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKII 141
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  790 DFGLATENENyqdnndkwknrqsaDEDLTTGVGTALYVAPELLSRRNgvrYDA-KVDMYSLGIILFEM---CMTFS-TSM 864
Cdd:cd14003  142 DFGLSNEFRG--------------GSLLKTFCGTPAYAAPEVLLGRK---YDGpKADVWSLGVILYAMltgYLPFDdDND 204
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 63054755  865 ERIRiiDTIRSPSISFPSTFpfsraSHEFK-VIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd14003  205 SKLF--RKILKGKYPIPSHL-----SPDARdLIRRMLVVDPSKRITIEEILNHP 251
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
560-915 1.71e-40

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: 150.75  E-value: 1.71e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  560 EFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENSR-ILREVMTLSRLHHEHVVRYYtaWVETEANdtvteiissds 638
Cdd:cd06606    6 ELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELEaLEREIRILSSLKHPNIVRYL--GTERTEN----------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  639 eslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkegssdkdssieeassvktqen 718
Cdd:cd06606      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  719 glnaTLYIQMEYCEKLSLQDIIRDKIPVDE-MWRLF-RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAte 796
Cdd:cd06606   73 ----TLNIFLEYVPGGSLASLLKKFGKLPEpVVRKYtRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCA-- 146
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  797 nenyqdnndKWKNRQSADEDLTTGVGTALYVAPELLsrrNGVRYDAKVDMYSLGIILFEMCMT------FSTSMERI-RI 869
Cdd:cd06606  147 ---------KRLAEIATGEGTKSLRGTPYWMAPEVI---RGEGYGRAADIWSLGCTVIEMATGkppwseLGNPVAALfKI 214
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 63054755  870 IDTIRSPSIsfPSTFpfsraSHEFK--VIHClLQHDPTKRPSSQELLE 915
Cdd:cd06606  215 GSSGEPPPI--PEHL-----SEEAKdfLRKC-LQRDPKKRPTADELLQ 254
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
555-915 3.07e-40

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: 149.93  E-value: 3.07e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  555 DFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLV--LLSDDKENSRILREVMTLSRLHHEHVVRYYTawveteandtvte 632
Cdd:cd14007    1 DFEIGKPLGKGKFGNVYLAREKKSGFIVALKVISksQLQKSGLEHQLRREIEIQSHLRHPNILRLYG------------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  633 iissdseslsqslnmavdfrqssslpadklssldiHFEDDYNssadeedpeasdisfqysntsdkegssdkdssieeass 712
Cdd:cd14007   68 -----------------------------------YFEDKKR-------------------------------------- 74
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  713 vktqenglnatLYIQMEYCEKLSLQDIIRDKIPVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGD 790
Cdd:cd14007   75 -----------IYLILEYAPNGELYKELKKQKRFDEkeAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLAD 143
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  791 FGLATENENyqdnndkwKNRQsadedltTGVGTALYVAPELLsrrNGVRYDAKVDMYSLGIILFEMCMTFS--TSMERIR 868
Cdd:cd14007  144 FGWSVHAPS--------NRRK-------TFCGTLDYLPPEMV---EGKEYDYKVDIWSLGVLCYELLVGKPpfESKSHQE 205
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 63054755  869 IIDTIRSPSISFPSTFpfsraSHEFK-VIHCLLQHDPTKRPSSQELLE 915
Cdd:cd14007  206 TYKRIQNVDIKFPSSV-----SPEAKdLISKLLQKDPSKRLSLEQVLN 248
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
560-917 4.42e-40

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: 149.63  E-value: 4.42e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  560 EFLGRGGFGEVVKVKNRIDGRFYAVK--KLVLLSDDKENSRILREVMTLSRLHHEHVVRYYTawveteandtvteiissd 637
Cdd:cd14099    7 KFLGKGGFAKCYEVTDMSTGKVYAGKvvPKSSLTKPKQREKLKSEIKIHRSLKHPNIVKFHD------------------ 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  638 seslsqslnmavdfrqssslpadklssldiHFEDDYNssadeedpeasdisfqysntsdkegssdkdssieeassvktqe 717
Cdd:cd14099   69 ------------------------------CFEDEEN------------------------------------------- 75
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  718 nglnatLYIQMEYCEKLSLQDII--RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAT 795
Cdd:cd14099   76 ------VYILLELCSNGSLMELLkrRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAA 149
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  796 ENEnyqdnndkwknrqSADEDLTTGVGTALYVAPELLSRRNGvrYDAKVDMYSLGIILFEM--------CMTFSTSMERI 867
Cdd:cd14099  150 RLE-------------YDGERKKTLCGTPNYIAPEVLEKKKG--HSFEVDIWSLGVILYTLlvgkppfeTSDVKETYKRI 214
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 63054755  868 RIIDtirspsISFPSTFPFSRASHEFkvIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd14099  215 KKNE------YSFPSHLSISDEAKDL--IRSMLQPDPTKRPSLDEILSHP 256
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
562-915 1.95e-37

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: 141.52  E-value: 1.95e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  562 LGRGGFGEVVKVKNRidGRFYAVKKLVLLSDDKENSR-ILREVMTLSRLHHEHVVRYYtawveteandtvteiissdses 640
Cdd:cd13999    1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDNDELLKeFRREVSILSKLRHPNIVQFI---------------------- 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  641 lsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkeGSSDKDSsieeassvktqengl 720
Cdd:cd13999   57 ----------------------------------------------------------GACLSPP--------------- 63
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  721 naTLYIQMEYCEKLSLQDIIRDK---IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEn 797
Cdd:cd13999   64 --PLCIVTEYMPGGSLYDLLHKKkipLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRI- 140
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  798 ENYQDNNdkwknrqsadedLTTGVGTALYVAPELLsrrNGVRYDAKVDMYSLGIILFEMC--------MTFSTSMERIRI 869
Cdd:cd13999  141 KNSTTEK------------MTGVVGTPRWMAPEVL---RGEPYTEKADVYSFGIVLWELLtgevpfkeLSPIQIAAAVVQ 205
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 63054755  870 IDTIRSPSISFPSTFpfsrasheFKVIHCLLQHDPTKRPSSQELLE 915
Cdd:cd13999  206 KGLRPPIPPDCPPEL--------SKLIKRCWNEDPEKRPSFSEIVK 243
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
556-916 1.31e-36

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: 139.65  E-value: 1.31e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  556 FEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENsrILREVMTLSRLHHEHVVRYYtawveteandtvteiis 635
Cdd:cd06614    2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQNKEL--IINEILIMKECKHPNIVDYY----------------- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  636 sdseslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkegssdkDSSIeeassvkt 715
Cdd:cd06614   63 --------------------------------------------------------------------DSYL-------- 66
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  716 qengLNATLYIQMEYCEKLSLQDIIR---DKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFG 792
Cdd:cd06614   67 ----VGDELWVVMEYMDGGSLTDIITqnpVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFG 142
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  793 LATenenyQDNNDKwKNRqsadedlTTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMC------MTFStSMER 866
Cdd:cd06614  143 FAA-----QLTKEK-SKR-------NSVVGTPYWMAPEVIKRKD---YGPKVDIWSLGIMCIEMAegeppyLEEP-PLRA 205
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 63054755  867 IRIIDTIRSPSISFPSTFpfsraSHEFK-VIHCLLQHDPTKRPSSQELLES 916
Cdd:cd06614  206 LFLITTKGIPPLKNPEKW-----SPEFKdFLNKCLVKDPEKRPSAEELLQH 251
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
555-919 2.89e-36

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: 138.70  E-value: 2.89e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  555 DFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLS-DDKENSRILREVMTLSRLHHEHVVRYYTAWVEteandtvtei 633
Cdd:cd08529    1 DFEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRmSRKMREEAIDEARVLSKLNSPYVIKYYDSFVD---------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  634 issdseslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkegssdkdssieeassv 713
Cdd:cd08529      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  714 ktqenglNATLYIQMEYCEKLSLQDIIRDK----IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLG 789
Cdd:cd08529   71 -------KGKLNIVMEYAENGDLHSLIKSQrgrpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIG 143
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  790 DFGLAtenENYQDNNDKWKnrqsadedltTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMCM---TFSTSMER 866
Cdd:cd08529  144 DLGVA---KILSDTTNFAQ----------TIVGTPYYLSPELCEDKP---YNEKSDVWALGCVLYELCTgkhPFEAQNQG 207
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 63054755  867 IRIIDTIRSPSISFPStfPFSRASheFKVIHCLLQHDPTKRPSSQELLESEAI 919
Cdd:cd08529  208 ALILKIVRGKYPPISA--SYSQDL--SQLIDSCLTKDYRQRPDTTELLRNPSL 256
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
555-919 7.47e-36

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: 137.72  E-value: 7.47e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  555 DFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENSRILREVMTLSRLHHEHVVRYYTAWveteandtvteii 634
Cdd:cd06623    2 DLERVKVLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAF------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  635 ssdseslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsDKEGSsdkdssieeassvk 714
Cdd:cd06623   69 -------------------------------------------------------------YKEGE-------------- 73
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  715 tqenglnatLYIQMEYCEKLSLQDIIRD--KIPVDEMWRLFRQILEALAYIHS-RGMMHRDLKPGNIFLDENRNVKLGDF 791
Cdd:cd06623   74 ---------ISIVLEYMDGGSLADLLKKvgKIPEPVLAYIARQILKGLDYLHTkRHIIHRDIKPSNLLINSKGEVKIADF 144
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  792 GLATENENYQDNNDKWknrqsadedlttgVGTALYVAPEllsRRNGVRYDAKVDMYSLGIILFEMCM-----TFSTSMER 866
Cdd:cd06623  145 GISKVLENTLDQCNTF-------------VGTVTYMSPE---RIQGESYSYAADIWSLGLTLLECALgkfpfLPPGQPSF 208
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  867 IRIIDTI-RSPSISFPSTfpfsRASHEFK--VIHClLQHDPTKRPSSQELLESEAI 919
Cdd:cd06623  209 FELMQAIcDGPPPSLPAE----EFSPEFRdfISAC-LQKDPKKRPSAAELLQHPFI 259
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
555-919 7.56e-35

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: 134.44  E-value: 7.56e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  555 DFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLS-DDKENSRILREVMTLSRLHHEHVVRYYTAwveteandtvtei 633
Cdd:cd08530    1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSlSQKEREDSVNEIRLLASVNHPNIIRYKEA------------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  634 issdseslsqslnmavdfrqssslpadklsSLDIHfeddynssadeedpeasdisfqysntsdkegssdkdssieeassv 713
Cdd:cd08530   68 ------------------------------FLDGN--------------------------------------------- 72
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  714 ktqenglnaTLYIQMEYC------EKLSLQDIIRDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVK 787
Cdd:cd08530   73 ---------RLCIVMEYApfgdlsKLISKRKKKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVK 143
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  788 LGDFGLAtenenyqdnndKWKNRQSAdedlTTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMcMTFSTSME-- 865
Cdd:cd08530  144 IGDLGIS-----------KVLKKNLA----KTQIGTPLYAAPEVWKGRP---YDYKSDIWSLGCLLYEM-ATFRPPFEar 204
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  866 -----RIRIIDTiRSPSIsfPSTFpfsraSHEF-KVIHCLLQHDPTKRPSSQELLESEAI 919
Cdd:cd08530  205 tmqelRYKVCRG-KFPPI--PPVY-----SQDLqQIIRSLLQVNPKKRPSCDKLLQSPAV 256
RWD_GCN2 cd23823
RWD domain of eIF-2-alpha kinase GCN2 and related proteins; GCN2 (EC 2.7.11.1), also called ...
11-128 9.86e-35

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: 128.88  E-value: 9.86e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   11 KEIQENEIEALKAIFMDDFEELkvRNAWNVTNGHVYCIHLCS-RSANSKSIAKLDLCIELGRSYPYVKPVIKLQNGENVL 89
Cdd:cd23823    1 EEEQEEELEALQSIYGDDFEDL--SSKKAVWSPPEFRIRLRPqEGESEENHVSVDLHVKFPPTYPDVPPEIELENVKGLS 78
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 63054755   90 NSQIRFLLDKLDTKAKDLLGEEMIFELASIVQDYLNDWQ 128
Cdd:cd23823   79 DEQLEELLKELEELAKELLGEEMIFELAEAVQEFLEEHN 117
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
721-915 3.33e-34

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: 132.87  E-value: 3.33e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  721 NATLYIQMEYCEKLSLQDIIRDKIP---VDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAT 795
Cdd:cd06610   71 GDELWLVMPLLSGGSLLDIMKSSYPrggLDEaiIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSA 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  796 ENENYQDNNDKWKNrqsadedltTGVGTALYVAPELLSRRNGvrYDAKVDMYSLGIILFEMCM---TFSTSMERIRIIDT 872
Cdd:cd06610  151 SLATGGDRTRKVRK---------TFVGTPCWMAPEVMEQVRG--YDFKADIWSFGITAIELATgaaPYSKYPPMKVLMLT 219
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 63054755  873 IRSPSISFPSTFPFSRASHEFK--VIHClLQHDPTKRPSSQELLE 915
Cdd:cd06610  220 LQNDPPSLETGADYKKYSKSFRkmISLC-LQKDPSKRPTAEELLK 263
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
562-917 9.25e-34

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 131.52  E-value: 9.25e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  562 LGRGGFGEVVKVKNRIDGRFYAVK---------KLVLLSDDKE----NSRILREVMTLSRLHHEHVVRYYtawveteand 628
Cdd:cd14008    1 LGRGSFGKVKLALDTETGQLYAIKifnksrlrkRREGKNDRGKiknaLDDVRREIAIMKKLDHPNIVRLY---------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  629 tvtEIIssdseslsqslnmavdfrqssslpadklssldihfeddynssadeEDPEasdisfqysntsdkegsSDKdssie 708
Cdd:cd14008   71 ---EVI---------------------------------------------DDPE-----------------SDK----- 80
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  709 eassvktqenglnatLYIQMEYCEKLSLQDIIRDK----IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENR 784
Cdd:cd14008   81 ---------------LYLVLEYCEGGPVMELDSGDrvppLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADG 145
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  785 NVKLGDFGLATENENyqdnndkwknrqsADEDLTTGVGTALYVAPELLSRRNGvRYDAK-VDMYSLGIILFemCMTF--- 860
Cdd:cd14008  146 TVKISDFGVSEMFED-------------GNDTLQKTAGTPAFLAPELCDGDSK-TYSGKaADIWALGVTLY--CLVFgrl 209
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054755  861 ----STSMErirIIDTIRSPSISfpstFPFSRA-SHEFK-VIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd14008  210 pfngDNILE---LYEAIQNQNDE----FPIPPElSPELKdLLRRMLEKDPEKRITLKEIKEHP 265
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
721-917 1.94e-33

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: 130.77  E-value: 1.94e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  721 NATLYIQMEYCEKLSLQDIIRDKIPVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtene 798
Cdd:cd14080   74 GSKVFIFMEYAEHGDLLEYIQKRGALSEsqARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFA---- 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  799 nyqdnndKWKNRQSADEDLTTGVGTALYVAPELLSrrnGVRYDAKV-DMYSLGIILFEM---CMTFSTS----MERIRII 870
Cdd:cd14080  150 -------RLCPDDDGDVLSKTFCGSAAYAAPEILQ---GIPYDPKKyDIWSLGVILYIMlcgSMPFDDSnikkMLKDQQN 219
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 63054755  871 DTIRspsisFPSTfpFSRASHEFK-VIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd14080  220 RKVR-----FPSS--VKKLSPECKdLIDQLLEPDPTKRATIEEILNHP 260
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
556-914 3.60e-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: 129.35  E-value: 3.60e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  556 FEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLV-LLSDDKENSRILREVMTLSRLH-HEHVVRYYTAWVETEandtvtei 633
Cdd:cd14050    3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRsRFRGEKDRKRKLEEVERHEKLGeHPNCVRFIKAWEEKG-------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  634 issdseslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkegssdkdssieeassv 713
Cdd:cd14050      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  714 ktqenglnaTLYIQMEYCEKlSLQDIIR--DKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDF 791
Cdd:cd14050   75 ---------ILYIQTELCDT-SLQQYCEetHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDF 144
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  792 GLATEnenyQDNNDKwknrQSADEdlttgvGTALYVAPELLsrrNGvRYDAKVDMYSLGIILFEMcmtfSTSMERIRIID 871
Cdd:cd14050  145 GLVVE----LDKEDI----HDAQE------GDPRYMAPELL---QG-SFTKAADIFSLGITILEL----ACNLELPSGGD 202
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 63054755  872 T---IRSPSIsfPSTFpFSRASHEFK-VIHCLLQHDPTKRPSSQELL 914
Cdd:cd14050  203 GwhqLRQGYL--PEEF-TAGLSPELRsIIKLMMDPDPERRPTAEDLL 246
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
724-919 3.07e-32

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: 127.42  E-value: 3.07e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDKIPVDE-MWRLF-RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATenenyq 801
Cdd:cd06626   74 VYIFMEYCQEGTLEELLRHGRILDEaVIRVYtLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAV------ 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  802 dnndKWKNRQS--ADEDLTTGVGTALYVAPELLSRRNGVRYDAKVDMYSLGIILFEMCmtfstsmeririidTIRSP--- 876
Cdd:cd06626  148 ----KLKNNTTtmAPGEVNSLVGTPAYMAPEVITGNKGEGHGRAADIWSLGCVVLEMA--------------TGKRPwse 209
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 63054755  877 -----SISF----------PSTFPFSRASHEFkVIHClLQHDPTKRPSSQELLESEAI 919
Cdd:cd06626  210 ldnewAIMYhvgmghkppiPDSLQLSPEGKDF-LSRC-LESDPKKRPTASELLDHPFI 265
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
555-919 6.16e-32

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: 126.59  E-value: 6.16e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  555 DFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENSRILREVMTLSRLHHEHVVRYYtawveteandtvteii 634
Cdd:cd06609    2 LFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEEAEDEIEDIQQEIQFLSQCDSPYITKYY---------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  635 ssdseslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkeGSSDKDSsieeassvk 714
Cdd:cd06609   66 ----------------------------------------------------------------GSFLKGS--------- 72
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  715 tqenglnaTLYIQMEYCEKLSLQDIIRdKIPVDEMWRLF--RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFG 792
Cdd:cd06609   73 --------KLWIIMEYCGGGSVLDLLK-PGPLDETYIAFilREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFG 143
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  793 LATENENYQDNNDkwknrqsadedltTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMCM---TFST--SMERI 867
Cdd:cd06609  144 VSGQLTSTMSKRN-------------TFVGTPFWMAPEVIKQSG---YDEKADIWSLGITAIELAKgepPLSDlhPMRVL 207
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 63054755  868 RIIDTIRSPSISFPStfpFSRASHEFkvIHCLLQHDPTKRPSSQELLESEAI 919
Cdd:cd06609  208 FLIPKNNPPSLEGNK---FSKPFKDF--VELCLNKDPKERPSAKELLKHKFI 254
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
560-915 2.56e-31

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: 124.44  E-value: 2.56e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  560 EFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKEN----SRILREVMTLSRLHHEHVVRYYtawveteandtvteiis 635
Cdd:cd06632    6 QLLGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDDKKSresvKQLEQEIALLSKLRHPNIVQYY----------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  636 sdseslsqslnmavdfrqssslpadklssldihfeddynSSADEEDPeasdisfqysntsdkegssdkdssieeassvkt 715
Cdd:cd06632   69 ---------------------------------------GTEREEDN--------------------------------- 76
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  716 qenglnatLYIQMEYCEKLSLQDIIRDKIPVDE-MWRLF-RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGL 793
Cdd:cd06632   77 --------LYIFLEYVPGGSIHKLLQRYGAFEEpVIRLYtRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGM 148
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  794 AtenenyqdnndkwknRQSADEDLTTGV-GTALYVAPELLSRRNGvRYDAKVDMYSLGIILFEMCMT---FStSMERIRI 869
Cdd:cd06632  149 A---------------KHVEAFSFAKSFkGSPYWMAPEVIMQKNS-GYGLAVDIWSLGCTVLEMATGkppWS-QYEGVAA 211
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 63054755  870 IDTIRS----PSIsfPSTfpFSRASHEFkvIHCLLQHDPTKRPSSQELLE 915
Cdd:cd06632  212 IFKIGNsgelPPI--PDH--LSPDAKDF--IRLCLQRDPEDRPTASQLLE 255
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
728-917 2.81e-31

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: 124.34  E-value: 2.81e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  728 MEYCEKLSLQDIIR--DKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenENYQDNND 805
Cdd:cd13994   77 MEYCPGGDLFTLIEkaDSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTA---EVFGMPAE 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  806 KwknrQSADEDlttG-VGTALYVAPELLSrrnGVRYDAK-VDMYSLGIILFEM----------CMTFSTSMERIRI-IDT 872
Cdd:cd13994  154 K----ESPMSA---GlCGSEPYMAPEVFT---SGSYDGRaVDVWSCGIVLFALftgrfpwrsaKKSDSAYKAYEKSgDFT 223
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 63054755  873 IRSPSISFPSTFpfsraSHEFKVIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd13994  224 NGPYEPIENLLP-----SECRRLIYRMLHPDPEKRITIDEALNDP 263
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
555-914 3.20e-31

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: 123.95  E-value: 3.20e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  555 DFEELEFLGRGGFGEVVKVKNRIDGRFYAVKkLVLLSDDKENSRILREVMTLSRLHHEHVVRYYTAWVeteandtvteii 634
Cdd:cd06613    1 DYELIQRIGSGTYGDVYKARNIATGELAAVK-VIKLEPGDDFEIIQQEISMLKECRHPNIVAYFGSYL------------ 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  635 ssdseslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkegSSDKdssieeassvk 714
Cdd:cd06613   68 -----------------------------------------------------------------RRDK----------- 71
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  715 tqenglnatLYIQMEYCEKLSLQDIIRDKIPVDEMWRLF--RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFG 792
Cdd:cd06613   72 ---------LWIVMEYCGGGSLQDIYQVTGPLSELQIAYvcRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFG 142
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  793 LATENENyqdnndKWKNRQSAdedlttgVGTALYVAPELLSRRNGVRYDAKVDMYSLGIILFEMC-----MTFSTSMERI 867
Cdd:cd06613  143 VSAQLTA------TIAKRKSF-------IGTPYWMAPEVAAVERKGGYDGKCDIWALGITAIELAelqppMFDLHPMRAL 209
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 63054755  868 RIIdtirsPSISFPStfP-------FSRASHEFkvIHCLLQHDPTKRPSSQELL 914
Cdd:cd06613  210 FLI-----PKSNFDP--PklkdkekWSPDFHDF--IKKCLTKNPKKRPTATKLL 254
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
562-910 3.34e-31

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: 123.78  E-value: 3.34e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  562 LGRGGFGEVVKVKNRIDGRFYAVKKLV--LLSDDKENSRILREVMTLSRLHHEHVVR-YYtawveteandtvteiissds 638
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKVLRkkEIIKRKEVEHTLNERNILERVNHPFIVKlHY-------------------- 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  639 eslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdiSFQysntsdkegssdkdssieeassvkTQEN 718
Cdd:cd05123   61 -------------------------------------------------AFQ------------------------TEEK 67
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  719 glnatLYIQMEYCEKLSLQDIIRD--KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATE 796
Cdd:cd05123   68 -----LYLVLDYVPGGELFSHLSKegRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKE 142
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  797 NEnyqdnndkwknrqSADEDLTTGVGTALYVAPELLsrrNGVRYDAKVDMYSLGIILFEMCMTFS--TSMERIRIIDTIR 874
Cdd:cd05123  143 LS-------------SDGDRTYTFCGTPEYLAPEVL---LGKGYGKAVDWWSLGVLLYEMLTGKPpfYAENRKEIYEKIL 206
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 63054755  875 SPSISFPSTFpfsraSHEFK-VIHCLLQHDPTKRPSS 910
Cdd:cd05123  207 KSPLKFPEYV-----SPEAKsLISGLLQKDPTKRLGS 238
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
553-919 8.16e-31

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: 122.76  E-value: 8.16e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  553 ETDFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLvllSDDKENSRILREVMTLSRLHHEHVVRYYtawveteandtvte 632
Cdd:cd06612    2 EEVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVV---PVEEDLQEIIKEISILKQCDSPYIVKYY-------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  633 iissdseslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkeGSSDKDSsieeass 712
Cdd:cd06612   65 ------------------------------------------------------------------GSYFKNT------- 71
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  713 vktqenglnaTLYIQMEYCEKLSLQDIIR---DKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLG 789
Cdd:cd06612   72 ----------DLWIVMEYCGAGSVSDIMKitnKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLA 141
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  790 DFGLATEnenYQDNNDKWKnrqsadedltTGVGTALYVAPELLSRrngVRYDAKVDMYSLGIILFEMCMTFST-----SM 864
Cdd:cd06612  142 DFGVSGQ---LTDTMAKRN----------TVIGTPFWMAPEVIQE---IGYNNKADIWSLGITAIEMAEGKPPysdihPM 205
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  865 ERIRIIDTIRSPSISFPSTFpfsraSHEFK--VIHCLLQhDPTKRPSSQELLESEAI 919
Cdd:cd06612  206 RAIFMIPNKPPPTLSDPEKW-----SPEFNdfVKKCLVK-DPEERPSAIQLLQHPFI 256
Pkinase pfam00069
Protein kinase domain;
556-916 5.61e-30

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 119.27  E-value: 5.61e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755    556 FEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLS-DDKENSRILREVMTLSRLHHEHVVRYYTAwveteandtvteii 634
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKiKKKKDKNILREIKILKKLNHPNIVRLYDA-------------- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755    635 ssdseslsqslnmavdfrqssslpadklssldihFEDDYNssadeedpeasdisfqysntsdkegssdkdssieeassvk 714
Cdd:pfam00069   67 ----------------------------------FEDKDN---------------------------------------- 72
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755    715 tqenglnatLYIQMEYCEKLSLQDIIRDKIPVDE--MWRLFRQILEALAYihsrgmmhrdlkpgnifldenrnvklgdfg 792
Cdd:pfam00069   73 ---------LYLVLEYVEGGSLFDLLSEKGAFSEreAKFIMKQILEGLES------------------------------ 113
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755    793 latenenyqdnndkwknrqsaDEDLTTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMcMT------FSTSMER 866
Cdd:pfam00069  114 ---------------------GSSLTTFVGTPWYMAPEVLGGNP---YGPKVDVWSLGCILYEL-LTgkppfpGINGNEI 168
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 63054755    867 IRIIDTIRSPSISFPSTFpfsraSHEFK-VIHCLLQHDPTKRPSSQELLES 916
Cdd:pfam00069  169 YELIIDQPYAFPELPSNL-----SEEAKdLLKKLLKKDPSKRLTATQALQH 214
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
721-915 6.66e-30

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: 121.10  E-value: 6.66e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  721 NATLYIQMEYCEKlSLQDII--RDKIPVDE------MWrlfrQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFG 792
Cdd:cd07830   70 NDELYFVFEYMEG-NLYQLMkdRKGKPFSEsvirsiIY----QILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFG 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  793 LATENENyqdnndkwknrqsaDEDLTTGVGTALYVAPELLSRRNgvRYDAKVDMYSLGIILFEMCMT---F--STSMERI 867
Cdd:cd07830  145 LAREIRS--------------RPPYTDYVSTRWYRAPEILLRST--SYSSPVDIWALGCIMAELYTLrplFpgSSEIDQL 208
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 63054755  868 -RIIDTIRSPS---------------ISFPSTFP------FSRASHEF-KVIHCLLQHDPTKRPSSQELLE 915
Cdd:cd07830  209 yKICSVLGTPTkqdwpegyklasklgFRFPQFAPtslhqlIPNASPEAiDLIKDMLRWDPKKRPTASQALQ 279
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
556-919 7.01e-30

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: 120.66  E-value: 7.01e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  556 FEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENSRILREVMTLSRLHH---EHVVRYYTAWVeteaNDTvte 632
Cdd:cd06917    3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNLDTDDDDVSDIQKEVALLSQLKLgqpKNIIKYYGSYL----KGP--- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  633 iissdseslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkegssdkdssieeass 712
Cdd:cd06917      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  713 vktqenglnaTLYIQMEYCEKLSLQDIIRDKiPVDEMW--RLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGD 790
Cdd:cd06917   76 ----------SLWIIMDYCEGGSIRTLMRAG-PIAERYiaVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCD 144
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  791 FGLATEnenYQDNNDKwknRQsadedltTGVGTALYVAPELLsrRNGVRYDAKVDMYSLGIILFEMC-----MTFSTSME 865
Cdd:cd06917  145 FGVAAS---LNQNSSK---RS-------TFVGTPYWMAPEVI--TEGKYYDTKADIWSLGITTYEMAtgnppYSDVDALR 209
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 63054755  866 RIRIIDTIRSPSISFPStfpFSRASHEFkVIHClLQHDPTKRPSSQELLESEAI 919
Cdd:cd06917  210 AVMLIPKSKPPRLEGNG---YSPLLKEF-VAAC-LDEEPKDRLSADELLKSKWI 258
PLN02972 PLN02972
Histidyl-tRNA synthetase
990-1425 1.04e-29

Histidyl-tRNA synthetase


Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 128.08  E-value: 1.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   990 VRDH----VVKVFRRHGAKERESHILFPKSS---QYDKDQASV-SLLDKNGTLLQLPYDTVLPYARNVARNAVEEEKTYL 1061
Cdd:PLN02972  343 IREKafsiITSVFKRHGATALDTPVFELRETlmgKYGEDSKLIyDLADQGGELCSLRYDLTVPFARYVAMNGITSFKRYQ 422
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  1062 ISDVF-REAKGGGRPKAIKEISFDITTNSDNLDwYDAETIKALDEVLTEIpSLTESCILINHADILSSILDYLQVSKDKR 1140
Cdd:PLN02972  423 IAKVYrRDNPSKGRYREFYQCDFDIAGVYEPMG-PDFEIIKVLTELLDEL-DIGTYEVKLNHRKLLDGMLEICGVPPEKF 500
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  1141 RMATHILGQINQRlTLSQVRNQLRIESLVPSTTLDDLSLF-DFRENYEEGASKLRKIFGKEMPQKM-RTALNYMERVVKL 1218
Cdd:PLN02972  501 RTICSSIDKLDKQ-SFEQVKKEMVEEKGLSNETADKIGNFvKERGPPLELLSKLRQEGSEFLGNASsRAALDELEIMFKA 579
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  1219 LRALKISHQLYFMPLCVYNFEFYDgGLMFQAINLAEKSELICAGGRYDKLVRFFdpplmrTARKKHVVGICFALEKlVFS 1298
Cdd:PLN02972  580 LEKSKAIGKIVFDLSLARGLDYYT-GVIYEAVFKGAQVGSIAAGGRYDNLVGMF------SGKQVPAVGVSLGIER-VFA 651
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  1299 MLRYirfHNSKQSSKHSPSPTlksvgpwaprrvDVLVTSIGKDSILEKCSLLQELWALNIQADIVLrgASSLEEIVTHYR 1378
Cdd:PLN02972  652 IMEQ---QEEEKSQVIRPTET------------EVLVSIIGDDKLALAAELVSELWNAGIKAEYKV--STRKAKHLKRAK 714
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 63054755  1379 SEGINWVLVVRQKNTQmEHSVKARNILKNEDDEIRFDEVGMWLLGEI 1425
Cdd:PLN02972  715 ESGIPWMVLVGEKELS-KGFVKLKNLEAGVEEEVDRTCFVQELKAEL 760
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
556-915 2.00e-29

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: 119.51  E-value: 2.00e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  556 FEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLlsdDKENSRI----LREVMTLSRLHHEHVVRYYtawveteandtvt 631
Cdd:cd07829    1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRL---DNEEEGIpstaLREISLLKELKHPNIVKLL------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  632 eiissdseslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkegssdkdssieeas 711
Cdd:cd07829      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  712 SVKTQENglnaTLYIQMEYCEKlSLQDIIRD---KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKL 788
Cdd:cd07829   65 DVIHTEN----KLYLVFEYCDQ-DLKKYLDKrpgPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKL 139
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  789 GDFGLAtenenyqdnndkwKNRQSADEDLTTGVGTALYVAPELL--SRrngvRYDAKVDMYSLGIILFEMCMT---FSTS 863
Cdd:cd07829  140 ADFGLA-------------RAFGIPLRTYTHEVVTLWYRAPEILlgSK----HYSTAVDIWSVGCIFAELITGkplFPGD 202
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  864 MER---IRIIDTIRSPSIS----------FPSTFP----------FSRASHE-FKVIHCLLQHDPTKRPSSQELLE 915
Cdd:cd07829  203 SEIdqlFKIFQILGTPTEEswpgvtklpdYKPTFPkwpkndlekvLPRLDPEgIDLLSKMLQYNPAKRISAKEALK 278
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
555-917 4.75e-29

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: 117.96  E-value: 4.75e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  555 DFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLV---LLSDDKENSRILREVMTLSRLHHEHVVRyytawveteandtvt 631
Cdd:cd14098    1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVkrkVAGNDKNLQLFQREINILKSLEHPGIVR--------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  632 eiissdseslsqslnmavdfrqssslpadklssLDIHFEDDynssadeedpeasdisfqysntsdkegssdkdssieeas 711
Cdd:cd14098   66 ---------------------------------LIDWYEDD--------------------------------------- 73
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  712 svktqenglnATLYIQMEYCEKLSLQDIIRD--KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFL--DENRNVK 787
Cdd:cd14098   74 ----------QHIYLVMEYVEGGDLMDFIMAwgAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILItqDDPVIVK 143
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  788 LGDFGLAtenenyqdnndkwkNRQSADEDLTTGVGTALYVAPELLSRRNGVR---YDAKVDMYSLGIILFEMcMT----F 860
Cdd:cd14098  144 ISDFGLA--------------KVIHTGTFLVTFCGTMAYLAPEILMSKEQNLqggYSNLVDMWSVGCLVYVM-LTgalpF 208
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  861 STSmERIRIIDTIRSPSISFPSTFPFSRASHEFKVIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd14098  209 DGS-SQLPVEKRIRKGRYTQPPLVDFNISEEAIDFILRLLDVDPEKRMTAAQALDHP 264
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
556-915 5.18e-29

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: 119.55  E-value: 5.18e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  556 FEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENS-RILREVMTLSRLHHEHVVRyytawveteandtVTEII 634
Cdd:cd07834    2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISNVFDDLIDAkRILREIKILRHLKHENIIG-------------LLDIL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  635 ssdseslsqslnmavdfrqsssLPADKLSsldihFEDdynssadeedpeasdisfqysntsdkegssdkdssieeassvk 714
Cdd:cd07834   69 ----------------------RPPSPEE-----FND------------------------------------------- 78
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  715 tqenglnatLYIQMEYCEkLSLQDIIRDKIPVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFG 792
Cdd:cd07834   79 ---------VYIVTELME-TDLHKVIKSPQPLTDdhIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFG 148
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  793 LATENENyqdnndkwknrQSADEDLTTGVGTALYVAPELLSrrNGVRYDAKVDMYSLGIILFEM-CMT--F--STSMERI 867
Cdd:cd07834  149 LARGVDP-----------DEDKGFLTEYVVTRWYRAPELLL--SSKKYTKAIDIWSVGCIFAELlTRKplFpgRDYIDQL 215
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63054755  868 -RIIDTIRSPSISF----------------------PSTFPFSRASHEFkvIHCL---LQHDPTKRPSSQELLE 915
Cdd:cd07834  216 nLIVEVLGTPSEEDlkfissekarnylkslpkkpkkPLSEVFPGASPEA--IDLLekmLVFNPKKRITADEALA 287
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
560-915 8.19e-29

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 116.94  E-value: 8.19e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  560 EFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKEN-SRILREVMTLSRLHHEHVVRYYTawveteandtvteiissds 638
Cdd:cd06627    6 DLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDlKSVMGEIDLLKKLNHPNIVKYIG------------------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  639 eslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkegssdkdssieeasSVKTQEn 718
Cdd:cd06627   67 -------------------------------------------------------------------------SVKTKD- 72
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  719 glnaTLYIQMEYCEKLSLQDIIRD--KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATe 796
Cdd:cd06627   73 ----SLYIILEYVENGSLASIIKKfgKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVAT- 147
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  797 nenyqdnndkwkNRQSADEDLTTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMCMTFSTSMER------IRII 870
Cdd:cd06627  148 ------------KLNEVEKDENSVVGTPYWMAPEVIEMSG---VTTASDIWSVGCTVIELLTGNPPYYDLqpmaalFRIV 212
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 63054755  871 DTIRSPsisFPSTfpfsrASHEFK--VIHClLQHDPTKRPSSQELLE 915
Cdd:cd06627  213 QDDHPP---LPEN-----ISPELRdfLLQC-FQKDPTLRPSAKELLK 250
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
724-911 3.25e-28

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: 115.78  E-value: 3.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDKIPVDE-MWRL-FRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEN-ENY 800
Cdd:cd05579   68 LYLVMEYLPGGDLYSLLENVGALDEdVARIyIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVGlVRR 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  801 QDNNDKWKNRQSADEDLTTG-VGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEM---CMTF--STSMErirIIDTIR 874
Cdd:cd05579  148 QIKLSIQKKSNGAPEKEDRRiVGTPDYLAPEILLGQG---HGKTVDWWSLGVILYEFlvgIPPFhaETPEE---IFQNIL 221
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 63054755  875 SPSISFPSTFPFSRASHEFkvIHCLLQHDPTKRPSSQ 911
Cdd:cd05579  222 NGKIEWPEDPEVSDEAKDL--ISKLLTPDPEKRLGAK 256
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
555-856 5.60e-28

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: 114.68  E-value: 5.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  555 DFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVL--LSDDKENSRILREVMTLSRLHHEHVVRYYTAWVEteandtvte 632
Cdd:cd08224    1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIfeMMDAKARQDCLKEIDLLQQLNHPNIIKYLASFIE--------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  633 iissdseslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkegssdkdssieeass 712
Cdd:cd08224      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  713 vktqenglNATLYIQMEYCEKLSLQDIIR----DKIPVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNV 786
Cdd:cd08224   72 --------NNELNIVLELADAGDLSRLIKhfkkQKRLIPErtIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVV 143
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054755  787 KLGDFGLAtenenyqdnndkwknRQSADEDLTTG--VGTALYVAPELLsRRNGvrYDAKVDMYSLGIILFEM 856
Cdd:cd08224  144 KLGDLGLG---------------RFFSSKTTAAHslVGTPYYMSPERI-REQG--YDFKSDIWSLGCLLYEM 197
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
555-915 1.79e-27

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: 113.59  E-value: 1.79e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  555 DFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENSRILREVMTLSRLHHEHVVRYYTAwveteandtvteii 634
Cdd:cd06605    2 DLEYLGELGEGNGGVVSKVRHRPSGQIMAVKVIRLEIDEALQKQILRELDVLHKCNSPYIVGFYGA-------------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  635 ssdseslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisFQYsntsdkegssdkdssieeassvk 714
Cdd:cd06605   68 ------------------------------------------------------FYS----------------------- 70
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  715 tqenglNATLYIQMEYCEKLSLQDIIR--DKIPVDEMWRLFRQILEALAYIHS-RGMMHRDLKPGNIFLDENRNVKLGDF 791
Cdd:cd06605   71 ------EGDISICMEYMDGGSLDKILKevGRIPERILGKIAVAVVKGLIYLHEkHKIIHRDVKPSNILVNSRGQVKLCDF 144
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  792 GLATenenyQDNNDKWKnrqsadedltTGVGTALYVAPEllsRRNGVRYDAKVDMYSLGIILFEMCM-----TFSTSMER 866
Cdd:cd06605  145 GVSG-----QLVDSLAK----------TFVGTRSYMAPE---RISGGKYTVKSDIWSLGLSLVELATgrfpyPPPNAKPS 206
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 63054755  867 IRIID----TIRSPSISFPSTfPFSRASHEFkVIHClLQHDPTKRPSSQELLE 915
Cdd:cd06605  207 MMIFEllsyIVDEPPPLLPSG-KFSPDFQDF-VSQC-LQKDPTERPSYKELME 256
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
724-915 2.84e-27

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: 112.48  E-value: 2.84e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDII--RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQ 801
Cdd:cd14078   76 IFMVLEYCPGGELFDYIvaKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKPKGGM 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  802 DNNdkwknrqsadedLTTGVGTALYVAPELLSrrnGVRY-DAKVDMYSLGIILFEMCMTF-----STSMERIRiidTIRS 875
Cdd:cd14078  156 DHH------------LETCCGSPAYAAPELIQ---GKPYiGSEADVWSMGVLLYALLCGFlpfddDNVMALYR---KIQS 217
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 63054755  876 PSISFPSTfpFSRASheFKVIHCLLQHDPTKRPSSQELLE 915
Cdd:cd14078  218 GKYEEPEW--LSPSS--KLLLDQMLQVDPKKRITVKELLN 253
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
724-912 2.96e-27

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: 112.38  E-value: 2.96e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDKIPVDE-MWRLF-RQILEALAYIHSRGMMHRDLKPGNIFLDENRNV--KLGDFGLAtenen 799
Cdd:cd14121   70 IYLIMEYCSGGDLSRFIRSRRTLPEsTVRRFlQQLASALQFLREHNISHMDLKPQNLLLSSRYNPvlKLADFGFA----- 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  800 yqdnndkwkNRQSADEDLTTGVGTALYVAPELLSRRngvRYDAKVDMYSLGIILFEmCM---------TFSTSMERIRii 870
Cdd:cd14121  145 ---------QHLKPNDEAHSLRGSPLYMAPEMILKK---KYDARVDLWSVGVILYE-CLfgrapfasrSFEELEEKIR-- 209
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 63054755  871 dtiRSPSISFPSTFPFSRASHEfkVIHCLLQHDPTKRPSSQE 912
Cdd:cd14121  210 ---SSKPIEIPTRPELSADCRD--LLLRLLQRDPDRRISFEE 246
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
555-919 3.28e-27

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


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 113.08  E-value: 3.28e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  555 DFEELEFLGRGGFGEVVKVKNRIDGRFYAVK---KLVLLSDDKENSrILREVMTLSRLHHEHVVR-YYTawveteandtv 630
Cdd:cd05581    2 DFKFGKPLGEGSYSTVVLAKEKETGKEYAIKvldKRHIIKEKKVKY-VTIEKEVLSRLAHPGIVKlYYT----------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  631 teiissdseslsqslnmavdfrqssslpadklssldihFEDDYNssadeedpeasdisfqysntsdkegssdkdssieea 710
Cdd:cd05581   70 --------------------------------------FQDESK------------------------------------ 75
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  711 ssvktqenglnatLYIQMEYCEKLSLQDIIRDKIPVDEMWRLF--RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKL 788
Cdd:cd05581   76 -------------LYFVLEYAPNGDLLEYIRKYGSLDEKCTRFytAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKI 142
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  789 GDFGLA----TENENYQDNNDKWKNRQSADEDLTTGVGTALYVAPELLSRRngvRYDAKVDMYSLGIILFEMcMT----F 860
Cdd:cd05581  143 TDFGTAkvlgPDSSPESTKGDADSQIAYNQARAASFVGTAEYVSPELLNEK---PAGKSSDLWALGCIIYQM-LTgkppF 218
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  861 STSMErIRIIDTIRSPSISFPSTFPfsRASHEFkvIHCLLQHDPTKRPSSQELLESEAI 919
Cdd:cd05581  219 RGSNE-YLTFQKIVKLEYEFPENFP--PDAKDL--IQKLLVLDPSKRLGVNENGGYDEL 272
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
724-915 3.70e-27

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: 112.42  E-value: 3.70e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRD--KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDEN----RNVKLGDFGLATEn 797
Cdd:cd14095   73 LYLVMELVKGGDLFDAITSstKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHedgsKSLKLADFGLATE- 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  798 enyqdnndkwknrqsADEDLTTGVGTALYVAPELLSrRNGvrYDAKVDMYSLGIILFEMCMTF----STSMERIRIIDTI 873
Cdd:cd14095  152 ---------------VKEPLFTVCGTPTYVAPEILA-ETG--YGLKVDIWAAGVITYILLCGFppfrSPDRDQEELFDLI 213
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 63054755  874 RSPSISFPSTF--PFSRASHEfkVIHCLLQHDPTKRPSSQELLE 915
Cdd:cd14095  214 LAGEFEFLSPYwdNISDSAKD--LISRMLVVDPEKRYSAGQVLD 255
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
556-917 5.23e-27

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: 112.66  E-value: 5.23e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  556 FEELEFLGRGGFGEVVKVKNRIDGRFYAVKKlVLLSDDKENSRI--LREVMTLSRLHHEHVVRYYtawveteandtvtEI 633
Cdd:cd07840    1 YEKIAQIGEGTYGQVYKARNKKTGELVALKK-IRMENEKEGFPItaIREIKLLQKLDHPNVVRLK-------------EI 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  634 ISsdseslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqySNTSDKEGSSdkdssieeassv 713
Cdd:cd07840   67 VT--------------------------------------------------------SKGSAKYKGS------------ 78
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  714 ktqenglnatLYIQMEYCEKlSLQDIIRD---KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGD 790
Cdd:cd07840   79 ----------IYMVFEYMDH-DLTGLLDNpevKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLAD 147
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  791 FGLATenenyqdnndKWKNRQSAdeDLTTGVGTALYVAPELL--SRrngvRYDAKVDMYSLGIILFEM-----CMTFSTS 863
Cdd:cd07840  148 FGLAR----------PYTKENNA--DYTNRVITLWYRPPELLlgAT----RYGPEVDMWSVGCILAELftgkpIFQGKTE 211
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63054755  864 MERI-RIIDTIRSPSI-SFP--STFPF-----------SRASHEFK---------VIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd07840  212 LEQLeKIFELCGSPTEeNWPgvSDLPWfenlkpkkpykRRLREVFKnvidpsaldLLDKLLTLDPKKRISADQALQHE 289
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
723-856 3.05e-26

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 109.73  E-value: 3.05e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  723 TLYIQMEYCEKLSLQDIIRDK--IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENeny 800
Cdd:cd14069   74 FQYLFLEYASGGELFDKIEPDvgMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATVF--- 150
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  801 qdnndKWKNRQSAdedLTTGVGTALYVAPELLSRRngvRYDA-KVDMYSLGIILFEM 856
Cdd:cd14069  151 -----RYKGKERL---LNKMCGTLPYVAPELLAKK---KYRAePVDVWSCGIVLFAM 196
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
724-915 8.94e-26

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: 110.34  E-value: 8.94e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKlSLQDIIRDKIPVDEMWR-LFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLA---TENEN 799
Cdd:cd07852   84 IYLVFEYMET-DLHAVIRANILEDIHKQyIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLArslSQLEE 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  800 YQDNNdkwknrqsadeDLTTGVGTALYVAPELL--SRrngvRYDAKVDMYSLGIILFEM-----CMTFSTSMERI-RI-- 869
Cdd:cd07852  163 DDENP-----------VLTDYVATRWYRAPEILlgST----RYTKGVDMWSVGCILGEMllgkpLFPGTSTLNQLeKIie 227
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  870 ---------IDTIRSP-------SISFPSTFP----FSRASHE-FKVIHCLLQHDPTKRPSSQELLE 915
Cdd:cd07852  228 vigrpsaedIESIQSPfaatmleSLPPSRPKSldelFPKASPDaLDLLKKLLVFNPNKRLTAEEALR 294
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
556-914 1.25e-25

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: 108.56  E-value: 1.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  556 FEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLvLLSDDKENSR--ILREVMTLSRLHHEHVVRYYTAwveteandtvtei 633
Cdd:cd07833    3 YEVLGVVGEGAYGVVLKCRNKATGEIVAIKKF-KESEDDEDVKktALREVKVLRQLRHENIVNLKEA------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  634 issdseslsqslnmavdFRqssslpadklssldihfeddynssadeedpeasdisfqysntsdkegSSDKdssieeassv 713
Cdd:cd07833   69 -----------------FR-----------------------------------------------RKGR---------- 74
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  714 ktqenglnatLYIQMEYCEKLSLQDIIRDK--IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDF 791
Cdd:cd07833   75 ----------LYLVFEYVERTLLELLEASPggLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDF 144
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  792 GLATEnenyqdnndkwkNRQSADEDLTTGVGTALYVAPELLSrrNGVRYDAKVDMYSLGIILFEMCM------------- 858
Cdd:cd07833  145 GFARA------------LTARPASPLTDYVATRWYRAPELLV--GDTNYGKPVDVWAIGCIMAELLDgeplfpgdsdidq 210
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  859 -----------------TFSTSmERIRiidTIRSPSISFPST----FPFSRASHEFKVIHCLLQHDPTKRPSSQELL 914
Cdd:cd07833  211 lyliqkclgplppshqeLFSSN-PRFA---GVAFPEPSQPESlerrYPGKVSSPALDFLKACLRMDPKERLTCDELL 283
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
723-915 1.57e-25

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: 107.34  E-value: 1.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  723 TLYIQMEyceklsLQDIIRD--KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAteneny 800
Cdd:cd14002   79 TEYAQGE------LFQILEDdgTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFA------ 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  801 qdnndkwKNRQSADEDLTTGVGTALYVAPELLSRRngvRYDAKVDMYSLGIILFEMCM---TFSTS--MERIRIIdtIRS 875
Cdd:cd14002  147 -------RAMSCNTLVLTSIKGTPLYMAPELVQEQ---PYDHTADLWSLGCILYELFVgqpPFYTNsiYQLVQMI--VKD 214
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 63054755  876 PsISFPSTFpfsraSHEFK-VIHCLLQHDPTKRPSSQELLE 915
Cdd:cd14002  215 P-VKWPSNM-----SPEFKsFLQGLLNKDPSKRLSWPDLLE 249
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
721-916 1.81e-25

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: 107.51  E-value: 1.81e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  721 NATLYIQMEYCEKLSLQDIIR---DKIPVDEM--WRLFrQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAt 795
Cdd:cd08221   71 GESLFIEMEYCNGGNLHDKIAqqkNQLFPEEVvlWYLY-QIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGIS- 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  796 enenyqdnndkwKNRQSADEDLTTGVGTALYVAPELLsrrNGVRYDAKVDMYSLGIILFE---MCMTFSTSmERIRIIDT 872
Cdd:cd08221  149 ------------KVLDSESSMAESIVGTPYYMSPELV---QGVKYNFKSDIWAVGCVLYElltLKRTFDAT-NPLRLAVK 212
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 63054755  873 IRSPSISFPSTfpfsRASHEF-KVIHCLLQHDPTKRPSSQELLES 916
Cdd:cd08221  213 IVQGEYEDIDE----QYSEEIiQLVHDCLHQDPEDRPTAEELLER 253
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
726-915 3.74e-25

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: 107.03  E-value: 3.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  726 IQMEYCEKlSLQDIIRDKIP----VDEMWRLFRQILEALAYIH--SRGMMHRDLKPGNIFLDENRNVKLGDFGLATeNEN 799
Cdd:cd13985   79 LLMEYCPG-SLVDILEKSPPsplsEEEVLRIFYQICQAVGHLHsqSPPIIHRDIKIENILFSNTGRFKLCDFGSAT-TEH 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  800 YQDNndKWKNRQSADEDLTTGVgTALYVAPELLSRRNGVRYDAKVDMYSLGIILFEMC---MTFSTSmERIRIID-TIRS 875
Cdd:cd13985  157 YPLE--RAEEVNIIEEEIQKNT-TPMYRAPEMIDLYSKKPIGEKADIWALGCLLYKLCffkLPFDES-SKLAIVAgKYSI 232
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 63054755  876 PsisfpstfPFSRASHEFKV-IHCLLQHDPTKRPSSQELLE 915
Cdd:cd13985  233 P--------EQPRYSPELHDlIRHMLTPDPAERPDIFQVIN 265
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
556-907 4.39e-25

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: 106.32  E-value: 4.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  556 FEELEFLGRGGFGEVVKVKNRIDGRFYAVK--KLVLLSDDKENSRILREVMTLSRLHHEHVVRYYtawveteandtvtEI 633
Cdd:cd14073    3 YELLETLGKGTYGKVKLAIERATGREVAIKsiKKDKIEDEQDMVRIRREIEIMSSLNHPHIIRIY-------------EV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  634 issdseslsqslnmavdfrqssslpadklssldihFEddynssadeedpeasdisfqysntsdkegSSDKdssieeassv 713
Cdd:cd14073   70 -----------------------------------FE-----------------------------NKDK---------- 75
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  714 ktqenglnatLYIQMEYCEKLSLQDII--RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDF 791
Cdd:cd14073   76 ----------IVIVMEYASGGELYDYIseRRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADF 145
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  792 GLATeneNYQDNNdkwknrqsadeDLTTGVGTALYVAPELLsrrNGVRYDA-KVDMYSLGIILFEM---CMTFSTSMERI 867
Cdd:cd14073  146 GLSN---LYSKDK-----------LLQTFCGSPLYASPEIV---NGTPYQGpEVDCWSLGVLLYTLvygTMPFDGSDFKR 208
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 63054755  868 RIidtirsPSISFPSTFPFSRASHEFKVIHCLLQHDPTKR 907
Cdd:cd14073  209 LV------KQISSGDYREPTQPSDASGLIRWMLTVNPKRR 242
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
724-917 6.41e-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: 105.56  E-value: 6.41e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRD--KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQ 801
Cdd:cd14663   75 IFFVMELVTGGELFSKIAKngRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSALSEQFR 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  802 DnndkwknrqsaDEDLTTGVGTALYVAPELLSRRNgvrYD-AKVDMYSLGIILFEM---CMTFSTS--MERIRIIDTIRS 875
Cdd:cd14663  155 Q-----------DGLLHTTCGTPNYVAPEVLARRG---YDgAKADIWSCGVILFVLlagYLPFDDEnlMALYRKIMKGEF 220
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 63054755  876 PsisFPSTFPFSRAShefkVIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd14663  221 E---YPRWFSPGAKS----LIKRILDPNPSTRITVEQIMASP 255
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
724-913 6.60e-25

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: 105.38  E-value: 6.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDII--RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRN---VKLGDFGLAtene 798
Cdd:cd14009   67 IYLVLEYCAGGDLSQYIrkRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDdpvLKIADFGFA---- 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  799 nyqdnndkwknRQSADEDLT-TGVGTALYVAPELLSRRngvRYDAKVDMYSLGIILFEMC-----MTFSTSMERIRIIDT 872
Cdd:cd14009  143 -----------RSLQPASMAeTLCGSPLYMAPEILQFQ---KYDAKADLWSVGAILFEMLvgkppFRGSNHVQLLRNIER 208
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 63054755  873 IRSPsISFPSTFPFSRasHEFKVIHCLLQHDPTKRPSSQEL 913
Cdd:cd14009  209 SDAV-IPFPIAAQLSP--DCKDLLRRLLRRDPAERISFEEF 246
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
724-917 7.98e-25

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: 105.84  E-value: 7.98e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIR--DKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLA---TEN- 797
Cdd:cd14010   69 LWLVVEYCTGGDLETLLRqdGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLArreGEIl 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  798 -ENYQDNNDKWKNRQSADEdlTTGVGTALYVAPELLSrrnGVRYDAKVDMYSLGIILFEMCMT----FSTSMEriRIIDT 872
Cdd:cd14010  149 kELFGQFSDEGNVNKVSKK--QAKRGTPYYMAPELFQ---GGVHSFASDLWALGCVLYEMFTGkppfVAESFT--ELVEK 221
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 63054755  873 IRSPSISFPSTFPFSRASHEFK-VIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd14010  222 ILNEDPPPPPPKVSSKPSPDFKsLLKGLLEKDPAKRLSWDELVKHP 267
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
559-916 1.01e-24

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: 105.84  E-value: 1.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  559 LEFLGRGGFGEVVKVKNRIDGRFYAVKKlVLLSDDKENSRILREVMTLSRLHHEHVVRYYtawveteandtvteiissds 638
Cdd:cd13986    5 QRLLGEGGFSFVYLVEDLSTGRLYALKK-ILCHSKEDVKEAMREIENYRLFNHPNILRLL-------------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  639 eslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkegssdkdssieeASSVKTQEN 718
Cdd:cd13986   64 -----------------------------------------------------------------------DSQIVKEAG 72
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  719 GlNATLYIQMEYCEKLSLQDIIR------DKIPVDEMWRLFRQILEALAYIHS---RGMMHRDLKPGNIFLDENRNVKLG 789
Cdd:cd13986   73 G-KKEVYLLLPYYKRGSLQDEIErrlvkgTFFPEDRILHIFLGICRGLKAMHEpelVPYAHRDIKPGNVLLSEDDEPILM 151
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  790 DFGLATENENyqdnndKWKNRQSADE--DLTTGVGTALYVAPELLSRRNGVRYDAKVDMYSLGIILFEMcMTFSTSMERI 867
Cdd:cd13986  152 DLGSMNPARI------EIEGRREALAlqDWAAEHCTMPYRAPELFDVKSHCTIDEKTDIWSLGCTLYAL-MYGESPFERI 224
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 63054755  868 RIIDT-----IRSPSISFPSTFPFSRASHEFkvIHCLLQHDPTKRPSSQELLES 916
Cdd:cd13986  225 FQKGDslalaVLSGNYSFPDNSRYSEELHQL--VKSMLVVNPAERPSIDDLLSR 276
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
724-856 1.08e-24

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: 105.03  E-value: 1.08e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDK--IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATenenYQ 801
Cdd:cd14081   76 LYLVLEYVSGGELFDYLVKKgrLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMAS----LQ 151
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  802 DNNDKwknrqsadedLTTGVGTALYVAPELLSrrnGVRYD-AKVDMYSLGIILFEM 856
Cdd:cd14081  152 PEGSL----------LETSCGSPHYACPEVIK---GEKYDgRKADIWSCGVILYAL 194
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
12-124 1.59e-24

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: 99.71  E-value: 1.59e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755     12 EIQENEIEALKAIFMDDFEELKvRNAWNvTNGHVYCIHLCSRSANSKSIAKLDLCIELGRSYPYVKPVIKLQNGENVLNS 91
Cdd:pfam05773    1 EEQEEELEALESIYPDEFEVIS-DSPYE-SLEIEIKLSLDSDESDSSHLPPLVLKFTLPEDYPDEPPKISLSSPWNLSDE 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 63054755     92 QIRFLLDKLDTKAKDLLGEEMIFELASIVQDYL 124
Cdd:pfam05773   79 QVLSLLEELEELAEENLGEVMIFELIEWLQENL 111
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
280-505 2.54e-24

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: 104.14  E-value: 2.54e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  280 TEDGKREIQELEYELESLKVIRHDLLASIYEYQLERETrgygwrLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNIL 359
Cdd:cd06606   36 SGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENT------LNIFLEYVPGGSLASLLKKFGKLPEPVVRKYTRQIL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  360 EGLAELHRLGISHKSLHLDNVVLFHSGhrtFAKLMDFGFTRTLRDMNASHPFNINSQSItnilpegLY-PPEVSESSfaA 438
Cdd:cd06606  110 EGLEYLHSNGIVHRDIKGANILVDSDG---VVKLADFGCAKRLAEIATGEGTKSLRGTP-------YWmAPEVIRGE--G 177
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  439 ASRKTDIWCFGLLVLQMLCGAHVLNKFSSLKLIMTHV-----IPLLPGSY----QDLVRRCLMRDSRKRPSAIDLL 505
Cdd:cd06606  178 YGRAADIWSLGCTVIEMATGKPPWSELGNPVAALFKIgssgePPPIPEHLseeaKDFLRKCLQRDPKKRPTADELL 253
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
720-914 2.58e-24

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: 104.35  E-value: 2.58e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  720 LNATLYIQMEYCEKLSLQDIIRDKIPV----DEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENR-NVKLGDFGLA 794
Cdd:cd13993   76 TEVAIYIVLEYCPNGDLFEAITENRIYvgktELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEgTVKLCDFGLA 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  795 TenenyqdnNDKWknrqSADedltTGVGTALYVAPELLSRRNGVR--YD-AKVDMYSLGIILFEmcMTFSTsmeririiD 871
Cdd:cd13993  156 T--------TEKI----SMD----FGVGSEFYMAPECFDEVGRSLkgYPcAAGDIWSLGIILLN--LTFGR--------N 209
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 63054755  872 TIRSPSISFPSTFPFSRAS-HEFKVI-------HCLL----QHDPTKRPSSQELL 914
Cdd:cd13993  210 PWKIASESDPIFYDYYLNSpNLFDVIlpmsddfYNLLrqifTVNPNNRILLPELQ 264
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
716-856 3.32e-24

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 109.11  E-value: 3.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   716 QENGLNatlYIQMEYCEKLSLQDIIRD--KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGL 793
Cdd:NF033483   77 EDGGIP---YIVMEYVDGRTLKDYIREhgPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGI 153
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755   794 AtenenyqdnndkwknRQSADEDLT-TG--VGTALYVAPElLSRrnGVRYDAKVDMYSLGIILFEM 856
Cdd:NF033483  154 A---------------RALSSTTMTqTNsvLGTVHYLSPE-QAR--GGTVDARSDIYSLGIVLYEM 201
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
545-914 7.34e-24

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: 103.99  E-value: 7.34e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  545 YRKSVSRYEtdfeELEFLGRGGFGEVVKVKNRIDGRFYAVKKlVLLSDDKENSRI--LREVMTLSRLHHEHVVRYytawv 622
Cdd:cd07865    7 FCDEVSKYE----KLAKIGQGTFGEVFKARHRKTGQIVALKK-VLMENEKEGFPItaLREIKILQLLKHENVVNL----- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  623 eteandtvteiissdseslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkegssd 702
Cdd:cd07865      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  703 kdssIEEASSVKTQENGLNATLYIQMEYCEK-----LSLQDIirdKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGN 777
Cdd:cd07865   77 ----IEICRTKATPYNRYKGSIYLVFEFCEHdlaglLSNKNV---KFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAAN 149
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  778 IFLDENRNVKLGDFGLA---TENENYQDNndKWKNRqsadedlttgVGTALYVAPE-LLSRRNgvrYDAKVDMYSLGIIL 853
Cdd:cd07865  150 ILITKDGVLKLADFGLArafSLAKNSQPN--RYTNR----------VVTLWYRPPElLLGERD---YGPPIDMWGAGCIM 214
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  854 FEM-----CMTFSTSMERIRIIDTIRSpSISfPSTFP---------------------------FSRASHEFKVIHCLLQ 901
Cdd:cd07865  215 AEMwtrspIMQGNTEQHQLTLISQLCG-SIT-PEVWPgvdklelfkkmelpqgqkrkvkerlkpYVKDPYALDLIDKLLV 292
                        410
                 ....*....|...
gi 63054755  902 HDPTKRPSSQELL 914
Cdd:cd07865  293 LDPAKRIDADTAL 305
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
729-917 9.13e-24

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 102.82  E-value: 9.13e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  729 EYCEKLSLQDIIRDKIPVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENEnyqdnndk 806
Cdd:cd14093   89 ELCRKGELFDYLTEVVTLSEkkTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRLD-------- 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  807 wknrqsADEDLTTGVGTALYVAPELLSRR---NGVRYDAKVDMYSLGIILFEMCMTFSTSMERIRII--DTIRSPSISFP 881
Cdd:cd14093  161 ------EGEKLRELCGTPGYLAPEVLKCSmydNAPGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVmlRNIMEGKYEFG 234
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 63054755  882 STfPFSRASHEFK-VIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd14093  235 SP-EWDDISDTAKdLISKLLVVDPKKRLTAEEALEHP 270
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
284-507 1.63e-23

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: 100.42  E-value: 1.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  284 KREIQELEYELESLKVIRHDLLASIYEYQLEREtrgygwRLYVLQEYSPKFTLFSLLQT-VLTLDVETVRAFSNNILEGL 362
Cdd:cd00180   32 KKLLEELLREIEILKKLNHPNIVKLYDVFETEN------FLYLVMEYCEGGSLKDLLKEnKGPLSEEEALSILRQLLSAL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  363 AELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDmnashpFNINSQSITNILPEGLYPPEVSESSfaAASRK 442
Cdd:cd00180  106 EYLHSNGIIHRDLKPENILLDSDGT---VKLADFGLAKDLDS------DDSLLKTTGGTTPPYYAPPELLGGR--YYGPK 174
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63054755  443 TDIWCFGLLVLQMlcgahvlnkfsslklimthvipllpGSYQDLVRRCLMRDSRKRPSAIDLLSS 507
Cdd:cd00180  175 VDIWSLGVILYEL-------------------------EELKDLIRRMLQYDPKKRPSAKELLEH 214
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
721-913 1.77e-23

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: 101.47  E-value: 1.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  721 NATLYIQMEYCEKLSLQDIIRDK-IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLD-ENRNVKLGDFGLATENE 798
Cdd:cd14164   73 NGRLYIVMEAAATDLLQKIQEVHhIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSaDDRKIKIADFGFARFVE 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  799 NYQDNNdkwknrqsadedlTTGVGTALYVAPELLSrrnGVRYDA-KVDMYSLGIILFEM---CMTF-STSMERIRiidtI 873
Cdd:cd14164  153 DYPELS-------------TTFCGSRAYTPPEVIL---GTPYDPkKYDVWSLGVVLYVMvtgTMPFdETNVRRLR----L 212
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 63054755  874 RSPSISFPSTFPFSRASHEFkvIHCLLQHDPTKRPSSQEL 913
Cdd:cd14164  213 QQRGVLYPSGVALEEPCRAL--IRTLLQFNPSTRPSIQQV 250
RWD smart00591
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily ...
17-127 1.94e-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: 96.27  E-value: 1.94e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755      17 EIEALKAIFMDDFEELKVRNawnvtNGHVYCIHLCSRSANS-KSIAKLDLCIELGRSYPYVKPVIKLQNGENVLNSQIRF 95
Cdd:smart00591    1 ELEALESIYPEDFEVIDEDA-----RIPEITIKLSPSSDEGeDQYVSLTLQVKLPENYPDEAPPISLLNSEGLSDEQLAE 75
                            90       100       110
                    ....*....|....*....|....*....|..
gi 63054755      96 LLDKLDTKAKDLLGEEMIFELASIVQDYLNDW 127
Cdd:smart00591   76 LLKKLEEIAEENLGEVMIFELVEKLQEFLSEF 107
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
554-907 2.13e-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: 102.27  E-value: 2.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  554 TDFEELEFLGRGGFGEVVKVKNRIDGRFYAVK-----KLVLLsddKENSRILREVMTLSRLHHEHVVRYYTAwveteand 628
Cdd:cd05580    1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKilkkaKIIKL---KQVEHVLNEKRILSEVRHPFIVNLLGS-------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  629 tvteiissdseslsqslnmavdfrqssslpadklssldihFEDDYNssadeedpeasdisfqysntsdkegssdkdssie 708
Cdd:cd05580   70 ----------------------------------------FQDDRN---------------------------------- 75
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  709 eassvktqenglnatLYIQMEYCEKLSLQDIIR--DKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNV 786
Cdd:cd05580   76 ---------------LYMVMEYVPGGELFSLLRrsGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHI 140
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  787 KLGDFGLA--TENENYqdnndkwknrqsadedltTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMCMTFST-- 862
Cdd:cd05580  141 KITDFGFAkrVKDRTY------------------TLCGTPEYLAPEIILSKG---HGKAVDWWALGILIYEMLAGYPPff 199
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 63054755  863 SMERIRIIDTIRSPSISFPStfPFSRASHEfkVIHCLLQHDPTKR 907
Cdd:cd05580  200 DENPMKIYEKILEGKIRFPS--FFDPDAKD--LIKRLLVVDLTKR 240
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
556-928 2.31e-23

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: 102.12  E-value: 2.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  556 FEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENSRILREVMTLSRLHHEHVVRYYTAWVEteandtvteiis 635
Cdd:cd06621    3 IVELSSLGEGAGGSVTKCRLRNTKTIFALKTITTDPNPDVQKQILRELEINKSCASPYIVKYYGAFLD------------ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  636 sdseslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkegssDKDSSIeeassvkt 715
Cdd:cd06621   71 ------------------------------------------------------------------EQDSSI-------- 76
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  716 qenglnatlYIQMEYCEKLSLQDIIRD------KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLG 789
Cdd:cd06621   77 ---------GIAMEYCEGGSLDSIYKKvkkkggRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLC 147
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  790 DFGLATENENYQDnndkwknrqsadedlTTGVGTALYVAPEllsRRNGVRYDAKVDMYSLGIILFEM---CMTFSTS--- 863
Cdd:cd06621  148 DFGVSGELVNSLA---------------GTFTGTSYYMAPE---RIQGGPYSITSDVWSLGLTLLEVaqnRFPFPPEgep 209
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  864 ----MERIRIIDTIRSPS-ISFPST-FPFSRASHEFkvIHCLLQHDPTKRPSSQELLE------SEAIPPKVgEEFI 928
Cdd:cd06621  210 plgpIELLSYIVNMPNPElKDEPENgIKWSESFKDF--IEKCLEKDGTRRPGPWQMLAhpwikaQEKKKVNM-AKFV 283
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
726-915 2.51e-23

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: 101.30  E-value: 2.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  726 IQMEYCEKLSLQDIIRDKIPVDE-MWRLF-RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQDN 803
Cdd:cd06629   85 IFLEYVPGGSIGSCLRKYGKFEEdLVRFFtRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKKSDDIYGN 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  804 NDKwknrqsadedlTTGVGTALYVAPELLSrRNGVRYDAKVDMYSLGIILFEMCMTFS--TSMERIRI---IDTIRS-PS 877
Cdd:cd06629  165 NGA-----------TSMQGSVFWMAPEVIH-SQGQGYSAKVDIWSLGCVVLEMLAGRRpwSDDEAIAAmfkLGNKRSaPP 232
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 63054755  878 IsfPSTFPFSRASHEFKVIHCLLqhDPTKRPSSQELLE 915
Cdd:cd06629  233 V--PEDVNLSPEALDFLNACFAI--DPRDRPTAAELLS 266
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
691-908 4.35e-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: 4.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  691 YSNTSDKEGSSDKDSS----IEEASSVKTQENGLNAT-----------LYIQMEYCEKLSLQDII------RDKIPVDEM 749
Cdd:cd08528   36 MTNPAFGRTEQERDKSvgdiISEVNIIKEQLRHPNIVryyktflendrLYIVMELIEGAPLGEHFsslkekNEHFTEDRI 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  750 WRLFRQILEALAYIH-SRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenenyqdnndkwKNRQSADEDLTTGVGTALYVA 828
Cdd:cd08528  116 WNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDKVTITDFGLA-------------KQKGPESSKMTSVVGTILYSC 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  829 PELLSRRNgvrYDAKVDMYSLGIILFEMCMT----FSTSMERI--RIIDTIRSPsisfpstFPFSRASHEFK-VIHCLLQ 901
Cdd:cd08528  183 PEIVQNEP---YGEKADIWALGCILYQMCTLqppfYSTNMLTLatKIVEAEYEP-------LPEGMYSDDITfVIRSCLT 252

                 ....*..
gi 63054755  902 HDPTKRP 908
Cdd:cd08528  253 PDPEARP 259
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
724-917 4.76e-23

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 104.71  E-value: 4.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   724 LYIQMEYCEKLSLQDIIR----DKIPVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEn 797
Cdd:PTZ00267  140 LLLIMEYGSGGDLNKQIKqrlkEHLPFQEyeVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQ- 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   798 enYQDnndkwknrqSADEDLTTG-VGTALYVAPELLSRRngvRYDAKVDMYSLGIILFEMcMTFSTSMERIRIIDTIRSP 876
Cdd:PTZ00267  219 --YSD---------SVSLDVASSfCGTPYYLAPELWERK---RYSKKADMWSLGVILYEL-LTLHRPFKGPSQREIMQQV 283
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 63054755   877 SISFPSTFPFSRASHEFKVIHCLLQHDPTKRPSSQELLESE 917
Cdd:PTZ00267  284 LYGKYDPFPCPVSSGMKALLDPLLSKNPALRPTTQQLLHTE 324
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
725-916 5.22e-23

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: 100.55  E-value: 5.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  725 YIQMEYCEKLSLQDIIRD--KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFL---DENRNVKLGDFGLAtenen 799
Cdd:cd14084   87 YIVLELMEGGELFDRVVSnkRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLssqEEECLIKITDFGLS----- 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  800 yqdnndkwKNRQSaDEDLTTGVGTALYVAPELLSRRNGVRYDAKVDMYSLGIILFeMCMT----FSTSMERIRIIDTIRS 875
Cdd:cd14084  162 --------KILGE-TSLMKTLCGTPTYLAPEVLRSFGTEGYTRAVDCWSLGVILF-ICLSgyppFSEEYTQMSLKEQILS 231
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 63054755  876 PSISFPSTFPFSRASHEFKVIHCLLQHDPTKRPSSQELLES 916
Cdd:cd14084  232 GKYTFIPKAWKNVSEEAKDLVKKMLVVDPSRRPSIEEALEH 272
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
556-915 5.26e-23

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: 100.00  E-value: 5.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  556 FEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLlsDDKENSRILREVMTLSRL----HHEHVVRyytawveteandtvt 631
Cdd:cd05118    1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKN--DFRHPKAALREIKLLKHLndveGHPNIVK--------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  632 eiissdseslsqslnmavdfrqssslpadklssLDIHFEDdynssadeedpeasdisfqysntsdkEGSSDkdssieeas 711
Cdd:cd05118   64 ---------------------------------LLDVFEH--------------------------RGGNH--------- 75
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  712 svktqenglnatLYIQMEYCEkLSLQDIIRD---KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLD-ENRNVK 787
Cdd:cd05118   76 ------------LCLVFELMG-MNLYELIKDyprGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINlELGQLK 142
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  788 LGDFGLAtenenyqdnndkwknRQSADEDLTTGVGTALYVAPELLSrrNGVRYDAKVDMYSLGIILFEMCMTF-----ST 862
Cdd:cd05118  143 LADFGLA---------------RSFTSPPYTPYVATRWYRAPEVLL--GAKPYGSSIDIWSLGCILAELLTGRplfpgDS 205
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 63054755  863 SMERI-RIIDTIRSPsisfpstfpfsrashEFK-VIHCLLQHDPTKRPSSQELLE 915
Cdd:cd05118  206 EVDQLaKIVRLLGTP---------------EALdLLSKMLKYDPAKRITASQALA 245
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
723-919 9.00e-23

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: 99.45  E-value: 9.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  723 TLYIQMEYCEKlSLQDII---RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenen 799
Cdd:cd06607   75 TAWLVMEYCLG-SASDIVevhKKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSA----- 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  800 yqdnndkwknrqSADEDLTTGVGTALYVAPELLSRRNGVRYDAKVDMYSLGII----------LFEMcmtfsTSMERIRI 869
Cdd:cd06607  149 ------------SLVCPANSFVGTPYWMAPEVILAMDEGQYDGKVDVWSLGITcielaerkppLFNM-----NAMSALYH 211
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 63054755  870 IDTIRSPSIsfpSTFPFSRASHEFkVIHClLQHDPTKRPSSQELLESEAI 919
Cdd:cd06607  212 IAQNDSPTL---SSGEWSDDFRNF-VDSC-LQKIPQDRPSAEDLLKHPFV 256
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
725-856 1.63e-22

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 98.91  E-value: 1.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  725 YIQMEYCEKLSLQDIIRDK--IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQD 802
Cdd:cd14162   76 YIIMELAENGDLLDYIRKNgaLPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARGVMKTKD 155
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 63054755  803 NndKWKNRQsadedltTGVGTALYVAPELLsrrNGVRYDAKV-DMYSLGIILFEM 856
Cdd:cd14162  156 G--KPKLSE-------TYCGSYAYASPEIL---RGIPYDPFLsDIWSMGVVLYTM 198
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
257-505 1.99e-22

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 98.53  E-value: 1.99e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  257 KEISLQDcvfllrtvriSTPywstedgkREIQELEYELESLKVIRHDLLASIYEYQLEREtrgygwRLYVLQEYSPKFTL 336
Cdd:cd06626   31 KEIRFQD----------NDP--------KTIKEIADEMKVLEGLDHPNLVRYYGVEVHRE------EVYIFMEYCQEGTL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  337 FSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGhrtFAKLMDFGFTRTLRDMNASHPF-NINS 415
Cdd:cd06626   87 EELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNG---LIKLGDFGSAVKLKNNTTTMAPgEVNS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  416 QSITnilPEGLYPPEVSESSFAAASRKTDIWCFGLLVLQMLCGAHVLNKFSSLKLIMTHV----IPLLPGSYQ------D 485
Cdd:cd06626  164 LVGT---PAYMAPEVITGNKGEGHGRAADIWSLGCVVLEMATGKRPWSELDNEWAIMYHVgmghKPPIPDSLQlspegkD 240
                        250       260
                 ....*....|....*....|
gi 63054755  486 LVRRCLMRDSRKRPSAIDLL 505
Cdd:cd06626  241 FLSRCLESDPKKRPTASELL 260
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
759-907 2.11e-22

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: 98.48  E-value: 2.11e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  759 ALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATenenyqdnndKWKnrqsADEDLTTGVGTALYVAPELLSRRNgv 838
Cdd:cd05578  112 ALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIAT----------KLT----DGTLATSTSGTKPYMAPEVFMRAG-- 175
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63054755  839 rYDAKVDMYSLGIILFEMCMT-----FSTSMERIRIIDTIRSPSISFPSTFPFSRAShefkVIHCLLQHDPTKR 907
Cdd:cd05578  176 -YSFAVDWWSLGVTAYEMLRGkrpyeIHSRTSIEEIRAKFETASVLYPAGWSEEAID----LINKLLERDPQKR 244
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
754-914 2.18e-22

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: 98.51  E-value: 2.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  754 RQILEALAYIHSRGMMHRDLKPGNIFLDENRN---VKLGDFGLATENENyqdnndkwknrqsaDEDLTTGVGTALYVAPE 830
Cdd:cd14089  107 RQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPnaiLKLTDFGFAKETTT--------------KKSLQTPCYTPYYVAPE 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  831 LLSRRngvRYDAKVDMYSLGIILFEM-C----------MTFSTSMERiriidTIRSPSISFPSTfPFSRASHEFK-VIHC 898
Cdd:cd14089  173 VLGPE---KYDKSCDMWSLGVIMYILlCgyppfysnhgLAISPGMKK-----RIRNGQYEFPNP-EWSNVSEEAKdLIRG 243
                        170
                 ....*....|....*.
gi 63054755  899 LLQHDPTKRPSSQELL 914
Cdd:cd14089  244 LLKTDPSERLTIEEVM 259
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
555-915 3.02e-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: 98.63  E-value: 3.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  555 DFEELEFLGRGGFGEVVKVKNRIDGRFYAVK---KLVLLSDDKENSriLREVMTLSRL-HHEHVVRYYTAWVEteandtv 630
Cdd:cd14051    1 EFHEVEKIGSGEFGSVYKCINRLDGCVYAIKkskKPVAGSVDEQNA--LNEVYAHAVLgKHPHVVRYYSAWAE------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  631 teiissdseslsqslnmavdfrqssslpadklssldihfeDDYnssadeedpeasdisfqysntsdkegssdkdssieea 710
Cdd:cd14051   72 ----------------------------------------DDH------------------------------------- 74
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  711 ssvktqenglnatLYIQMEYCEKLSLQDIIRD------KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENR 784
Cdd:cd14051   75 -------------MIIQNEYCNGGSLADAISEnekageRFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISRTP 141
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  785 NVklgdFGLATENENYQDNNDKWKNRQS----ADEDLTTGV-------GTALYVAPELLsrRNGVRYDAKVDMYSLGIIL 853
Cdd:cd14051  142 NP----VSSEEEEEDFEGEEDNPESNEVtykiGDLGHVTSIsnpqveeGDCRFLANEIL--QENYSHLPKADIFALALTV 215
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63054755  854 FEMC-----MTFSTSMERIRiidtirspSISFPstfPFSRASHEF-KVIHCLLQHDPTKRPSSQELLE 915
Cdd:cd14051  216 YEAAgggplPKNGDEWHEIR--------QGNLP---PLPQCSPEFnELLRSMIHPDPEKRPSAAALLQ 272
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
724-907 3.52e-22

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: 98.07  E-value: 3.52e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDKIPVDEMWRLF--RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATenenyq 801
Cdd:cd05572   68 LYMLMEYCLGGELWTILRDRGLFDEYTARFytACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAK------ 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  802 dnndKWKNRQSAdedlTTGVGTALYVAPELLSrrnGVRYDAKVDMYSLGIILFE-MCMT--FSTS-------MERI-RII 870
Cdd:cd05572  142 ----KLGSGRKT----WTFCGTPEYVAPEIIL---NKGYDFSVDYWSLGILLYElLTGRppFGGDdedpmkiYNIIlKGI 210
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 63054755  871 DTIRSPSIsfpstfpFSRASHefKVIHCLLQHDPTKR 907
Cdd:cd05572  211 DKIEFPKY-------IDKNAK--NLIKQLLRRNPEER 238
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
723-951 4.11e-22

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: 98.96  E-value: 4.11e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  723 TLYIQMEYCEKlSLQDIIR-DKIPVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenen 799
Cdd:cd06633   95 TAWLVMEYCLG-SASDLLEvHKKPLQEveIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSA----- 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  800 yqdnndkwknrqSADEDLTTGVGTALYVAPELLSRRNGVRYDAKVDMYSLGIILFEMC-----MTFSTSMERIRIIDTIR 874
Cdd:cd06633  169 ------------SIASPANSFVGTPYWMAPEVILAMDEGQYDGKVDIWSLGITCIELAerkppLFNMNAMSALYHIAQND 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  875 SPSI-SFPSTFPFSRAshefkVIHClLQHDPTKRPSSQELLESEAI----PPKVGEEFIQ---EGLRLLSNPNtpyYLKL 946
Cdd:cd06633  237 SPTLqSNEWTDSFRGF-----VDYC-LQKIPQERPSSAELLRHDFVrrerPPRVLIDLIQrtkDAVRELDNLQ---YRKM 307

                 ....*
gi 63054755  947 LKVLF 951
Cdd:cd06633  308 KKILF 312
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
723-917 5.31e-22

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: 97.31  E-value: 5.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  723 TLYIQMEYCEKLSLQDI--IRDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATenenY 800
Cdd:cd14189   75 NIYIFLELCSRKSLAHIwkARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAA----R 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  801 QDNNDKWKNrqsadedltTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFE-MCMT--FSTS--MERIRIIDTIRs 875
Cdd:cd14189  151 LEPPEQRKK---------TICGTPNYLAPEVLLRQG---HGPESDVWSLGCVMYTlLCGNppFETLdlKETYRCIKQVK- 217
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 63054755  876 psisfpSTFPFSRASHEFKVIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd14189  218 ------YTLPASLSLPARHLLAGILKRNPGDRLTLDQILEHE 253
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
725-917 6.53e-22

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: 97.20  E-value: 6.53e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  725 YIQMEYCEKLSLQDIIRDKIPVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAT--ENENY 800
Cdd:cd14070   79 YLVMELCPGGNLMHRIYDKKRLEEreARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNcaGILGY 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  801 QDnndkwknrqsadeDLTTGVGTALYVAPELLSRRngvRYDAKVDMYSLGIILFEMCM-TFSTSMERIRIIDTIRSPSIS 879
Cdd:cd14070  159 SD-------------PFSTQCGSPAYAAPELLARK---KYGPKVDVWSIGVNMYAMLTgTLPFTVEPFSLRALHQKMVDK 222
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 63054755  880 FPSTFPFSRASHEFKVIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd14070  223 EMNPLPTDLSPGAISFLRSLLEPDPLKRPNIKQALANR 260
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
726-913 7.06e-22

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: 96.95  E-value: 7.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  726 IQMEYCEKLSLQDIIRDKIPVDEMW--RLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenenyqdn 803
Cdd:cd14161   79 IVMEYASRGDLYDYISERQRLSELEarHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLS--------- 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  804 ndkwkNRQSADEDLTTGVGTALYVAPELLsrrNGVRYDA-KVDMYSLGIILFEM---CMTFSTSMERIrIIDTIRSPSIS 879
Cdd:cd14161  150 -----NLYNQDKFLQTYCGSPLYASPEIV---NGRPYIGpEVDSWSLGVLLYILvhgTMPFDGHDYKI-LVKQISSGAYR 220
                        170       180       190
                 ....*....|....*....|....*....|....
gi 63054755  880 FPstfpfSRASHEFKVIHCLLQHDPTKRPSSQEL 913
Cdd:cd14161  221 EP-----TKPSDACGLIRWLLMVNPERRATLEDV 249
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
559-915 7.84e-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: 96.85  E-value: 7.84e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755     559 LEFLGRGGFGEVVK--VKNRIDGRFY--AVKKLVLLSDDKENSRILREVMTLSRLHHEHVVRYYTAwveteandtVTEii 634
Cdd:smart00221    4 GKKLGEGAFGEVYKgtLKGKGDGKEVevAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGV---------CTE-- 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755     635 ssdseslsqslnmavdfrqssslpadklssldihfeddynssadeEDPeasdisfqysntsdkegssdkdssieeassvk 714
Cdd:smart00221   73 ---------------------------------------------EEP-------------------------------- 75
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755     715 tqenglnatLYIQMEYCEKLSLQDIIRDK----IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGD 790
Cdd:smart00221   76 ---------LMIVMEYMPGGDLLDYLRKNrpkeLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISD 146
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755     791 FGLAtenenyqdnndkwknRQSADEDLTTGVGTALYV---APELLSRRngvRYDAKVDMYSLGIILFEMC---------M 858
Cdd:smart00221  147 FGLS---------------RDLYDDDYYKVKGGKLPIrwmAPESLKEG---KFTSKSDVWSFGVLLWEIFtlgeepypgM 208
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755     859 TFSTSMERIRIIDTIRSPSiSFPSTFpfsrasheFKVIHCLLQHDPTKRPSSQELLE 915
Cdd:smart00221  209 SNAEVLEYLKKGYRLPKPP-NCPPEL--------YKLMLQCWAEDPEDRPTFSELVE 256
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
555-915 7.95e-22

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: 97.37  E-value: 7.95e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  555 DFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKEnsRILREVMTLSRL-HHEHVVRYYTAWveteandtvtei 633
Cdd:cd06608    7 IFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEE--EIKLEINILRKFsNHPNIATFYGAF------------ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  634 issdseslsqslnmavdFRQSSSLPADKLssldihfeddynssadeedpeasdisfqysntsdkegssdkdssieeassv 713
Cdd:cd06608   73 -----------------IKKDPPGGDDQL--------------------------------------------------- 84
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  714 ktqenglnatlYIQMEYCEKLSLQDIIRDKI----PVDEMW--RLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVK 787
Cdd:cd06608   85 -----------WLVMEYCGGGSVTDLVKGLRkkgkRLKEEWiaYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVK 153
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  788 LGDFGLatenenyqdnndkwknrqSADEDLT-----TGVGTALYVAPELLS--RRNGVRYDAKVDMYSLGIILFEMCMT- 859
Cdd:cd06608  154 LVDFGV------------------SAQLDSTlgrrnTFIGTPYWMAPEVIAcdQQPDASYDARCDVWSLGITAIELADGk 215
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  860 --FStSMERIRIIDTI-RSPSISFPSTFPFSRASHEFkVIHCLLQhDPTKRPSSQELLE 915
Cdd:cd06608  216 ppLC-DMHPMRALFKIpRNPPPTLKSPEKWSKEFNDF-ISECLIK-NYEQRPFTEELLE 271
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
721-919 8.76e-22

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: 96.42  E-value: 8.76e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  721 NATLYIQMEYCEKLSLQDIIRDK----IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAte 796
Cdd:cd08218   71 NGNLYIVMDYCDGGDLYKRINAQrgvlFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIA-- 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  797 nenyqdnndkwKNRQSADEDLTTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMCM---TFSTSMERIRIIDTI 873
Cdd:cd08218  149 -----------RVLNSTVELARTCIGTPYYLSPEICENKP---YNNKSDIWALGCVLYEMCTlkhAFEAGNMKNLVLKII 214
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 63054755  874 RSpsiSFPSTFPfsRASHEFK-VIHCLLQHDPTKRPSSQELLESEAI 919
Cdd:cd08218  215 RG---SYPPVPS--RYSYDLRsLVSQLFKRNPRDRPSINSILEKPFI 256
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
555-907 8.89e-22

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: 98.90  E-value: 8.89e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  555 DFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKL----VLLSDDKENSRILREVMTLSrlHHEHVVR-YYTawveteandt 629
Cdd:cd05573    2 DFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILrksdMLKREQIAHVRAERDILADA--DSPWIVRlHYA---------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  630 vteiissdseslsqslnmavdfrqssslpadklssldihFEDDYNssadeedpeasdisfqysntsdkegssdkdssiee 709
Cdd:cd05573   70 ---------------------------------------FQDEDH----------------------------------- 75
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  710 assvktqenglnatLYIQMEYC---EKLSLQdIIRDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNV 786
Cdd:cd05573   76 --------------LYLVMEYMpggDLMNLL-IKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHI 140
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  787 KLGDFGLAT-----------ENENYQDNNDKWKNRQSADEDL-----TTGVGTALYVAPELLSrrnGVRYDAKVDMYSLG 850
Cdd:cd05573  141 KLADFGLCTkmnksgdresyLNDSVNTLFQDNVLARRRPHKQrrvraYSAVGTPDYIAPEVLR---GTGYGPECDWWSLG 217
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054755  851 IILFEMCMTF-----STSME-RIRIIDTIRspSISFPSTfpfSRASHEFKVIHCLLQHDPTKR 907
Cdd:cd05573  218 VILYEMLYGFppfysDSLVEtYSKIMNWKE--SLVFPDD---PDVSPEAIDLIRRLLCDPEDR 275
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
559-915 1.07e-21

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 96.45  E-value: 1.07e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755     559 LEFLGRGGFGEVVK--VKNRIDGRFY--AVKKLVLLSDDKENSRILREVMTLSRLHHEHVVRYYTAwveteandtvteii 634
Cdd:smart00219    4 GKKLGEGAFGEVYKgkLKGKGGKKKVevAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGV-------------- 69
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755     635 ssdseslsqslnmavdfrqssslpadklssldihfeddynssADEEDPeasdisfqysntsdkegssdkdssieeassvk 714
Cdd:smart00219   70 ------------------------------------------CTEEEP-------------------------------- 75
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755     715 tqenglnatLYIQMEYCEKLSLQDIIRD---KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDF 791
Cdd:smart00219   76 ---------LYIVMEYMEGGDLLSYLRKnrpKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDF 146
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755     792 GLAtenenyqdnndkwknRQSADEDLTTGVGTALYV---APELLSRRngvRYDAKVDMYSLGIILFEMC---------MT 859
Cdd:smart00219  147 GLS---------------RDLYDDDYYRKRGGKLPIrwmAPESLKEG---KFTSKSDVWSFGVLLWEIFtlgeqpypgMS 208
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 63054755     860 FSTSMERIRIIDTIRSPsisfpstfpfSRASHEFKVI--HClLQHDPTKRPSSQELLE 915
Cdd:smart00219  209 NEEVLEYLKNGYRLPQP----------PNCPPELYDLmlQC-WAEDPEDRPTFSELVE 255
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
726-914 1.29e-21

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: 96.34  E-value: 1.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  726 IQMEYCEKLSLQDIIRD------KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRnVKLGDFGLAtenen 799
Cdd:cd08222   79 IVTEYCEGGDLDDKISEykksgtTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNNV-IKVGDFGIS----- 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  800 yqdnndkwkNRQSADEDL-TTGVGTALYVAPELLsrrNGVRYDAKVDMYSLGIILFEMC-----MTFSTSMERIRIIDTI 873
Cdd:cd08222  153 ---------RILMGTSDLaTTFTGTPYYMSPEVL---KHEGYNSKSDIWSLGCILYEMCclkhaFDGQNLLSVMYKIVEG 220
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 63054755  874 RSPSIsfPSTFPfsraSHEFKVIHCLLQHDPTKRPSSQELL 914
Cdd:cd08222  221 ETPSL--PDKYS----KELNAIYSRMLNKDPALRPSAAEIL 255
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
721-917 1.64e-21

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: 96.16  E-value: 1.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  721 NATLYIQMEYCEKLSLQDI--IRDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENE 798
Cdd:cd14187   79 NDFVYVVLELCRRRSLLELhkRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVE 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  799 nYQDNNDKwknrqsadedltTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMCM---TFSTSMERIRIIdTIRS 875
Cdd:cd14187  159 -YDGERKK------------TLCGTPNYIAPEVLSKKG---HSFEVDIWSIGCIMYTLLVgkpPFETSCLKETYL-RIKK 221
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 63054755  876 PSISFPSTF-PFSRAshefkVIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd14187  222 NEYSIPKHInPVAAS-----LIQKMLQTDPTARPTINELLNDE 259
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
293-505 2.51e-21

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 95.29  E-value: 2.51e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755     293 ELESLKVIRHDLLASIYEYQLEREtrgygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISH 372
Cdd:smart00220   47 EIKILKKLKHPNIVRLYDVFEDED------KLYLVMEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVH 120
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755     373 KSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDmnashPFNINSQSITnilPEglY-PPEV-SESSFaaaSRKTDIWCFGL 450
Cdd:smart00220  121 RDLKPENILLDEDGH---VKLADFGLARQLDP-----GEKLTTFVGT---PE--YmAPEVlLGKGY---GKAVDIWSLGV 184
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63054755     451 LVLQMLCG----AHVLNKFSSLKLIMTHVIPLLPGSY------QDLVRRCLMRDSRKRPSAIDLL 505
Cdd:smart00220  185 ILYELLTGkppfPGDDQLLELFKKIGKPKPPFPPPEWdispeaKDLIRKLLVKDPEKRLTAEEAL 249
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
724-914 2.82e-21

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: 95.86  E-value: 2.82e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKlSLQDIIRDK---IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENy 800
Cdd:cd07832   75 FVLVFEYMLS-SLSEVLRDEerpLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLFSE- 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  801 qdnndkwknrqSADEDLTTGVGTALYVAPELL--SRrngvRYDAKVDMYSLGIILFEMCMT---FS--TSMERI-RIIDT 872
Cdd:cd07832  153 -----------EDPRLYSHQVATRWYRAPELLygSR----KYDEGVDLWAVGCIFAELLNGsplFPgeNDIEQLaIVLRT 217
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63054755  873 IRSPS---------------ISFP--------STFPFSRAShEFKVIHCLLQHDPTKRPSSQELL 914
Cdd:cd07832  218 LGTPNektwpeltslpdynkITFPeskgirleEIFPDCSPE-AIDLLKGLLVYNPKKRLSAEEAL 281
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
724-914 2.87e-21

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 95.04  E-value: 2.87e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDK----IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenen 799
Cdd:cd08219   73 LYIVMEYCDGGDLMQKIKLQrgklFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSA----- 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  800 yqdnndkwKNRQSADEDLTTGVGTALYVAPELLSrrnGVRYDAKVDMYSLGIILFEMCM---TFSTSMERIRIIDTIRSP 876
Cdd:cd08219  148 --------RLLTSPGAYACTYVGTPYYVPPEIWE---NMPYNNKSDIWSLGCILYELCTlkhPFQANSWKNLILKVCQGS 216
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 63054755  877 SISFPSTFpfsraSHEFK-VIHCLLQHDPTKRPSSQELL 914
Cdd:cd08219  217 YKPLPSHY-----SYELRsLIKQMFKRNPRSRPSATTIL 250
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
728-915 3.13e-21

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: 95.03  E-value: 3.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  728 MEYCEKLSLQDII--RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenenyqdnnd 805
Cdd:cd14079   81 MEYVSGGELFDYIvqKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLS----------- 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  806 kwkNRQSADEDLTTGVGTALYVAPELLSrrnGVRYDA-KVDMYSLGIILFEM-CMTFSTSMERI-RIIDTIRSPSISFPS 882
Cdd:cd14079  150 ---NIMRDGEFLKTSCGSPNYAAPEVIS---GKLYAGpEVDVWSCGVILYALlCGSLPFDDEHIpNLFKKIKSGIYTIPS 223
                        170       180       190
                 ....*....|....*....|....*....|...
gi 63054755  883 TfpFSRASHEfkVIHCLLQHDPTKRPSSQELLE 915
Cdd:cd14079  224 H--LSPGARD--LIKRMLVVDPLKRITIPEIRQ 252
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
724-913 3.15e-21

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: 95.02  E-value: 3.15e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKlSLQDIIRD----KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENEN 799
Cdd:cd14119   71 LYMVMEYCVG-GLQEMLDSapdkRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEALDL 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  800 YQDnndkwknrqsaDEDLTTGVGTALYVAPELLsrrNGVRYDA--KVDMYSLGIILFEMCM-TFSTSMERI-RIIDTIRS 875
Cdd:cd14119  150 FAE-----------DDTCTTSQGSPAFQPPEIA---NGQDSFSgfKVDIWSAGVTLYNMTTgKYPFEGDNIyKLFENIGK 215
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 63054755  876 PSISFPSTFPFSRAShefkVIHCLLQHDPTKRPSSQEL 913
Cdd:cd14119  216 GEYTIPDDVDPDLQD----LLRGMLEKDPEKRFTIEQI 249
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
554-856 3.72e-21

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: 96.23  E-value: 3.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  554 TDFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLvLLSDDKENSRI--LREVMTLSRLHHEHVVRyytawveteandtvt 631
Cdd:cd07866    8 RDYEILGKLGEGTFGEVYKARQIKTGRVVALKKI-LMHNEKDGFPItaLREIKILKKLKHPNVVP--------------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  632 eiissdseslsqSLNMAVDfrqssslpadklssldihfeddyNSSADEEDPEASDISFQYSntsdkegssDKD-SSIEEA 710
Cdd:cd07866   72 ------------LIDMAVE-----------------------RPDKSKRKRGSVYMVTPYM---------DHDlSGLLEN 107
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  711 SSVKTQENGLNATLYiqmeyceklslqdiirdkipvdemwrlfrQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGD 790
Cdd:cd07866  108 PSVKLTESQIKCYML-----------------------------QLLEGINYLHENHILHRDIKAANILIDNQGILKIAD 158
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  791 FGLAtenENYQDNNDKWKNRQSA-DEDLTTGVGTALYVAPELLSRRNgvRYDAKVDMYSLGIILFEM 856
Cdd:cd07866  159 FGLA---RPYDGPPPNPKGGGGGgTRKYTNLVVTRWYRPPELLLGER--RYTTAVDIWGIGCVFAEM 220
HisRS-like_core cd00773
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ...
990-1295 4.00e-21

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: 94.59  E-value: 4.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  990 VRDHVVKVFRRHGAKEreshILFP----------KSSQYDKDQAsVSLLDKNGTLLQLPYDTVLPYARNVARNAVEEE-- 1057
Cdd:cd00773    8 IEDTLREVFERYGYEE----IDTPvfeytelflrKSGDEVSKEM-YRFKDKGGRDLALRPDLTAPVARAVAENLLSLPlp 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755 1058 -KTYLISDVFR-EAKGGGRPKAIKEISFDITTnSDNLDwYDAETIKALDEVLTEIPsLTESCILINHADILSSIldylqv 1135
Cdd:cd00773   83 lKLYYIGPVFRyERPQKGRYREFYQVGVEIIG-SDSPL-ADAEVIALAVEILEALG-LKDFQIKINHRGILDGI------ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755 1136 skdkrrmathilgqinqrltlsqvrnqlrieslvpsttlddLSLFDFRENYEEgasKLRKIFGKEmpqkmrtALNYMERV 1215
Cdd:cd00773  154 -----------------------------------------AGLLEDREEYIE---RLIDKLDKE-------ALAHLEKL 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755 1216 VKLLRALKISHQLYFMPLCVYNFEFYdGGLMFQAI-NLAEKSELICAGGRYDKLVRFFdpplmrTARKKHVVGICFALEK 1294
Cdd:cd00773  183 LDYLEALGVDIKYSIDLSLVRGLDYY-TGIVFEAVaDGLGAQGSIAGGGRYDGLLEEF------GGEDVPAVGFAIGLER 255

                 .
gi 63054755 1295 L 1295
Cdd:cd00773  256 L 256
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
555-917 4.03e-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: 95.18  E-value: 4.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  555 DFEELEFLGRGGFGEVVKVKNRID-GRFYAVKKL-VLLSDDKENSRILREVMTLSRLH---HEHVVRYYTAWveteandt 629
Cdd:cd14052    1 RFANVELIGSGEFSQVYKVSERVPtGKVYAVKKLkPNYAGAKDRLRRLEEVSILRELTldgHDNIVQLIDSW-------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  630 vteiissdseslsqslnmavdfrqssslpadklssldihfedDYNSSadeedpeasdisfqysntsdkegssdkdssiee 709
Cdd:cd14052   73 ------------------------------------------EYHGH--------------------------------- 77
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  710 assvktqenglnatLYIQMEYCEKLSLQDIIR---DKIPVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENR 784
Cdd:cd14052   78 --------------LYIQTELCENGSLDVFLSelgLLGRLDEfrVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEG 143
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  785 NVKLGDFGLATenenyqdnndkwknRQSADEDLtTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMCMTFS--- 861
Cdd:cd14052  144 TLKIGDFGMAT--------------VWPLIRGI-EREGDREYIAPEILSEHM---YDKPADIFSLGLILLEAAANVVlpd 205
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054755  862 -------------TSMERIRIID--TIRSPSISFPSTFPFSRASHE--FKVIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd14052  206 ngdawqklrsgdlSDAPRLSSTDlhSASSPSSNPPPDPPNMPILSGslDRVVRWMLSPEPDRRPTADDVLATP 278
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
724-917 4.93e-21

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: 94.33  E-value: 4.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDII--RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENyq 801
Cdd:cd14075   76 LHLVMEYASGGELYTKIstEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAKR-- 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  802 dnndkwknrqsaDEDLTTGVGTALYVAPELLSRRNgvRYDAKVDMYSLGIILFEMC---MTFstsmeRIRIIDTIRSPSI 878
Cdd:cd14075  154 ------------GETLNTFCGSPPYAAPELFKDEH--YIGIYVDIWALGVLLYFMVtgvMPF-----RAETVAKLKKCIL 214
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 63054755  879 SFPSTFP--FSRASHEfkVIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd14075  215 EGTYTIPsyVSEPCQE--LIRGILQPVPSDRYSIDEIKNSE 253
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
725-917 1.00e-20

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: 94.67  E-value: 1.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  725 YIQMEYCEKLSLQDIIRDKIPVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNI-FLDENRN--VKLGDFGLAteneN 799
Cdd:cd14092   75 YLVMELLRGGELLERIRKKKRFTEseASRIMRQLVSAVSFMHSKGVVHRDLKPENLlFTDEDDDaeIKIVDFGFA----R 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  800 YQDNNdkwknrqsadEDLTTGVGTALYVAPELLSRRNGVR-YDAKVDMYSLGIILFEMC------MTFSTSMERIRIIDT 872
Cdd:cd14092  151 LKPEN----------QPLKTPCFTLPYAAPEVLKQALSTQgYDESCDLWSLGVILYTMLsgqvpfQSPSRNESAAEIMKR 220
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 63054755  873 IRSPSISFPSTfPFSRASHEFK-VIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd14092  221 IKSGDFSFDGE-EWKNVSSEAKsLIQGLLTVDPSKRLTMSELRNHP 265
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
724-870 1.07e-20

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: 93.23  E-value: 1.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQD---IIRDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEneny 800
Cdd:cd14062   63 LAIVTQWCEGSSLYKhlhVLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLATV---- 138
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054755  801 qdnndkwKNRQSADEDLTTGVGTALYVAPELLSRRNGVRYDAKVDMYSLGIILFEM---CMTFSTSMERIRII 870
Cdd:cd14062  139 -------KTRWSGSQQFEQPTGSILWMAPEVIRMQDENPYSFQSDVYAFGIVLYELltgQLPYSHINNRDQIL 204
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
724-930 1.19e-20

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


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 94.04  E-value: 1.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRD-KIPVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENEny 800
Cdd:cd06611   77 LWILIEFCDGGALDSIMLElERGLTEpqIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNK-- 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  801 qdnndkwKNRQSADedltTGVGTALYVAPELLSRRN--GVRYDAKVDMYSLGIILFEMCMTF--STSMERIRIIDTIRS- 875
Cdd:cd06611  155 -------STLQKRD----TFIGTPYWMAPEVVACETfkDNPYDYKADIWSLGITLIELAQMEppHHELNPMRVLLKILKs 223
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 63054755  876 --PSISFPSTfpFSRASHEFkVIHClLQHDPTKRPSSQELLE----SEAIPPKVGEEFIQE 930
Cdd:cd06611  224 epPTLDQPSK--WSSSFNDF-LKSC-LVKDPDDRPTAAELLKhpfvSDQSDNKAIKDLLAE 280
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
724-915 1.26e-20

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


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 93.31  E-value: 1.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDII--RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtENENYQ 801
Cdd:cd14165   77 VYIVMELGVQGDLLEFIklRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFS-KRCLRD 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  802 DNNDKWKNRqsadedltTGVGTALYVAPELLsrrNGVRYDAKV-DMYSLGIILFEM-C--MTFSTS----MERIRIIDTI 873
Cdd:cd14165  156 ENGRIVLSK--------TFCGSAAYAAPEVL---QGIPYDPRIyDIWSLGVILYIMvCgsMPYDDSnvkkMLKIQKEHRV 224
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 63054755  874 RspsisfpstFPFSRA-SHEFK-VIHCLLQHDPTKRPSSQELLE 915
Cdd:cd14165  225 R---------FPRSKNlTSECKdLIYRLLQPDVSQRLCIDEVLS 259
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
724-915 1.47e-20

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: 93.94  E-value: 1.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRD---KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENY 800
Cdd:cd06644   84 LWIMIEFCPGGAVDAIMLEldrGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKT 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  801 QDNNDKWknrqsadedlttgVGTALYVAPELL--SRRNGVRYDAKVDMYSLGIILFEMCMTFSTSME--RIRIIDTI--- 873
Cdd:cd06644  164 LQRRDSF-------------IGTPYWMAPEVVmcETMKDTPYDYKADIWSLGITLIEMAQIEPPHHElnPMRVLLKIaks 230
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 63054755  874 RSPSISFPSTFpfsraSHEFK-VIHCLLQHDPTKRPSSQELLE 915
Cdd:cd06644  231 EPPTLSQPSKW-----SMEFRdFLKTALDKHPETRPSAAQLLE 268
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
721-915 1.89e-20

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: 92.80  E-value: 1.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  721 NATLYIQMEYCEKLSLQDIIRDKIPVDE-MWRLF-RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtene 798
Cdd:cd06625   74 EKSLSIFMEYMPGGSVKDEIKAYGALTEnVTRKYtRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGAS---- 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  799 nyqdnndkwKNRQS--ADEDLTTGVGTALYVAPELLsrrNGVRYDAKVDMYSLGIILFEMCMT------FStSMERIRII 870
Cdd:cd06625  150 ---------KRLQTicSSTGMKSVTGTPYWMSPEVI---NGEGYGRKADIWSVGCTVVEMLTTkppwaeFE-PMAAIFKI 216
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 63054755  871 DTiRSPSISFPSTfpFSRASHEFkvIHCLLQHDPTKRPSSQELLE 915
Cdd:cd06625  217 AT-QPTNPQLPPH--VSEDARDF--LSLIFVRNKKQRPSAEELLS 256
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
752-914 2.41e-20

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 96.48  E-value: 2.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   752 LFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenenyqdnndKWKNRQSADEDLTTGVGTALYVAPEL 831
Cdd:PTZ00283  148 LFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFS-----------KMYAATVSDDVGRTFCGTPYYVAPEI 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   832 LSRRNgvrYDAKVDMYSLGIILFEMcMTFSTSMERIRIIDTIRSPSISFPSTFPFSRASHEFKVIHCLLQHDPTKRPSSQ 911
Cdd:PTZ00283  217 WRRKP---YSKKADMFSLGVLLYEL-LTLKRPFDGENMEEVMHKTLAGRYDPLPPSISPEMQEIVTALLSSDPKRRPSSS 292

                  ...
gi 63054755   912 ELL 914
Cdd:PTZ00283  293 KLL 295
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
556-915 2.49e-20

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: 93.11  E-value: 2.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  556 FEELEFLGRGGFGEVVKVKNRIDGRFYAVKKL-VLLSDDKENSRILREVMTLSRL-HHEH--VVRYytawveteandtvt 631
Cdd:cd07838    1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVrVPLSEEGIPLSTIREIALLKQLeSFEHpnVVRL-------------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  632 eiissdseslsqslnmavdfrqssslpadklssLDIhfeddynssadeedpeasdisfqysntsdkegssdkdssieeaS 711
Cdd:cd07838   67 ---------------------------------LDV-------------------------------------------C 70
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  712 SVKTQENGLNatLYIQMEYCEklslQDIIR--DK-----IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENR 784
Cdd:cd07838   71 HGPRTDRELK--LTLVFEHVD----QDLATylDKcpkpgLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDG 144
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  785 NVKLGDFGLAtenenyqdnndKWKNRQSAdedLTTGVGTALYVAPELLSrrnGVRYDAKVDMYSLGIILFEMcmtF---- 860
Cdd:cd07838  145 QVKLADFGLA-----------RIYSFEMA---LTSVVVTLWYRAPEVLL---QSSYATPVDMWSVGCIFAEL---Fnrrp 204
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  861 ----STSMERI-RIIDTIRSPS-------ISFP-STFPFSRASHEFKVIHCL-----------LQHDPTKRPSSQELLE 915
Cdd:cd07838  205 lfrgSSEADQLgKIFDVIGLPSeeewprnSALPrSSFPSYTPRPFKSFVPEIdeegldllkkmLTFNPHKRISAFEALQ 283
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
724-915 2.55e-20

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: 92.51  E-value: 2.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDII-RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATenenyQD 802
Cdd:cd06648   79 LWVVMEFLEGGALTDIVtHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCA-----QV 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  803 NNDKWKNRqsadedltTGVGTALYVAPELLSRrngVRYDAKVDMYSLGIILFEMCMT----FSTS----MERIRiidtir 874
Cdd:cd06648  154 SKEVPRRK--------SLVGTPYWMAPEVISR---LPYGTEVDIWSLGIMVIEMVDGeppyFNEPplqaMKRIR------ 216
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 63054755  875 spsisfPSTFPFSRASHEFKVI------HCLLQhDPTKRPSSQELLE 915
Cdd:cd06648  217 ------DNEPPKLKNLHKVSPRlrsfldRMLVR-DPAQRATAAELLN 256
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
555-917 2.58e-20

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 92.89  E-value: 2.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  555 DFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENSRILREVMTLSRLHHEHVVRYYTAWVeTEANDTVteii 634
Cdd:cd06620    6 DLETLKDLGAGNGGSVSKVLHIPTGTIMAKKVIHIDAKSSVRKQILRELQILHECHSPYIVSFYGAFL-NENNNII---- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  635 ssdseslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkegssdkdssieeassvk 714
Cdd:cd06620      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  715 tqenglnatlyIQMEYCEKLSLQDIIRDK--IPVDEMWRLFRQILEALAYIHSR-GMMHRDLKPGNIFLDENRNVKLGDF 791
Cdd:cd06620   81 -----------ICMEYMDCGSLDKILKKKgpFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKGQIKLCDF 149
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  792 GLATENENyqdnndkwknrQSADedltTGVGTALYVAPEllsRRNGVRYDAKVDMYSLGIILFEMCM-TFSTSMERIR-- 868
Cdd:cd06620  150 GVSGELIN-----------SIAD----TFVGTSTYMSPE---RIQGGKYSVKSDVWSLGLSIIELALgEFPFAGSNDDdd 211
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  869 -------IIDTIR----SPSISFPSTFPFSRASHEFkVIHCLLQhDPTKRPSSQELLESE 917
Cdd:cd06620  212 gyngpmgILDLLQrivnEPPPRLPKDRIFPKDLRDF-VDRCLLK-DPRERPSPQLLLDHD 269
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
556-914 3.29e-20

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: 92.75  E-value: 3.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  556 FEELEFLGRGGFGEVVKVKNRIDGRFYAVKkLVLLSDDKENSRILREVMTLSRLHHEHVVRyytawveteandtvteiis 635
Cdd:cd14166    5 FIFMEVLGSGAFSEVYLVKQRSTGKLYALK-CIKKSPLSRDSSLENEIAVLKRIKHENIVT------------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  636 sdseslsqslnmavdfrqssslpadklssldihFEDDYNSSADeedpeasdisfqysntsdkegssdkdssieeassvkt 715
Cdd:cd14166   65 ---------------------------------LEDIYESTTH------------------------------------- 74
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  716 qenglnatLYIQMEYCEKLSLQDIIRDKIPVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFL---DENRNVKLGD 790
Cdd:cd14166   75 --------YYLVMQLVSGGELFDRILERGVYTEkdASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITD 146
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  791 FGLATENENyqdnndkwknrqsadEDLTTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMCMTFSTSMERI--R 868
Cdd:cd14166  147 FGLSKMEQN---------------GIMSTACGTPGYVAPEVLAQKP---YSKAVDCWSIGVITYILLCGYPPFYEETesR 208
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 63054755  869 IIDTIRSPSISFPSTF--PFSRASHEFkvIHCLLQHDPTKRPSSQELL 914
Cdd:cd14166  209 LFEKIKEGYYEFESPFwdDISESAKDF--IRHLLEKNPSKRYTCEKAL 254
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
556-917 4.66e-20

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: 92.63  E-value: 4.66e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  556 FEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVL--LSDDKE--NSRILREVMTLSRLHHEHVVryytawveteandtvt 631
Cdd:cd07841    2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLgeRKEAKDgiNFTALREIKLLQELKHPNII---------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  632 eiissdseslsqslnmavdfrqssslpadklssldihfeddynssadeedpEASDISFQYSNtsdkegssdkdssieeas 711
Cdd:cd07841   66 ---------------------------------------------------GLLDVFGHKSN------------------ 76
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  712 svktqenglnatLYIQMEYCEKlSLQDIIRDKI----PVDE---MWrlfrQILEALAYIHSRGMMHRDLKPGNIFLDENR 784
Cdd:cd07841   77 ------------INLVFEFMET-DLEKVIKDKSivltPADIksyML----MTLRGLEYLHSNWILHRDLKPNNLLIASDG 139
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  785 NVKLGDFGLAtenenyqdnndkwknRQ--SADEDLTTGVGTALYVAPELLSrrnGVR-YDAKVDMYSLGIILFEMCM--T 859
Cdd:cd07841  140 VLKLADFGLA---------------RSfgSPNRKMTHQVVTRWYRAPELLF---GARhYGVGVDMWSVGCIFAELLLrvP 201
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  860 FSTSMERIRIIDTI----------------RSPSISFPSTFP-------FSRASHE-FKVIHCLLQHDPTKRPSSQELLE 915
Cdd:cd07841  202 FLPGDSDIDQLGKIfealgtpteenwpgvtSLPDYVEFKPFPptplkqiFPAASDDaLDLLQRLLTLNPNKRITARQALE 281

                 ..
gi 63054755  916 SE 917
Cdd:cd07841  282 HP 283
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
735-856 4.88e-20

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: 93.51  E-value: 4.88e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  735 SLQDIIRDKIPVDEMWR-LFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenenyqdnndkwknRQsA 813
Cdd:cd07851  105 DLNNIVKCQKLSDDHIQfLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLA---------------RH-T 168
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 63054755  814 DEDLTTGVGTALYVAPELLsrRNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd07851  169 DDEMTGYVATRWYRAPEIM--LNWMHYNQTVDIWSVGCIMAEL 209
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
724-914 5.57e-20

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: 91.33  E-value: 5.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDK----IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRN-VKLGDFGLATEne 798
Cdd:cd08220   74 LMIVMEYAPGGTLFEYIQQRkgslLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTvVKIGDFGISKI-- 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  799 nyqdnndkwknrQSADEDLTTGVGTALYVAPELLsrrNGVRYDAKVDMYSLGIILFEMCMTfstsmerIRIIDTIRSPSI 878
Cdd:cd08220  152 ------------LSSKSKAYTVVGTPCYISPELC---EGKPYNQKSDIWALGCVLYELASL-------KRAFEAANLPAL 209
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 63054755  879 SFP---STF-PFS-RASHEFK-VIHCLLQHDPTKRPSSQELL 914
Cdd:cd08220  210 VLKimrGTFaPISdRYSEELRhLILSMLHLDPNKRPTLSEIM 251
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
724-914 5.89e-20

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: 91.56  E-value: 5.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCeKLSLQDIIRDKIPVD-------EMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLD-----ENRNVKLGDF 791
Cdd:cd13982   70 LYIALELC-AASLQDLVESPRESKlflrpglEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILIStpnahGNVRAMISDF 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  792 GLATenenyqdnndKWKNRQSADEDLTTGVGTALYVAPELLSRRNGVRYDAKVDMYSLGIILF----EMCMTFSTSMERI 867
Cdd:cd13982  149 GLCK----------KLDVGRSSFSRRSGVAGTSGWIAPEMLSGSTKRRQTRAVDIFSLGCVFYyvlsGGSHPFGDKLERE 218
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 63054755  868 RiidTIRSPSISFPSTfpfSRASHEFKVIHCL----LQHDPTKRPSSQELL 914
Cdd:cd13982  219 A---NILKGKYSLDKL---LSLGEHGPEAQDLiermIDFDPEKRPSAEEVL 263
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
686-915 6.17e-20

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: 91.17  E-value: 6.17e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  686 DISFQYSNTSDKEGSSDKD---SSIEEASSV----KTQENGlnaTLYIQMEYCEKLSLQDIIRDKIPV----DEMWRLFR 754
Cdd:cd08225   32 EIDLTKMPVKEKEASKKEVillAKMKHPNIVtffaSFQENG---RLFIVMEYCDGGDLMKRINRQRGVlfseDQILSWFV 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNV-KLGDFGLAtenenyqdnndkwknRQSAD--EDLTTGVGTALYVAPEL 831
Cdd:cd08225  109 QISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIA---------------RQLNDsmELAYTCVGTPYYLSPEI 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  832 LSRRNgvrYDAKVDMYSLGIILFEMCM---TFSTSMERIRIIDTIRSpsiSFPSTFP-FSRASHefKVIHCLLQHDPTKR 907
Cdd:cd08225  174 CQNRP---YNNKTDIWSLGCVLYELCTlkhPFEGNNLHQLVLKICQG---YFAPISPnFSRDLR--SLISQLFKVSPRDR 245

                 ....*...
gi 63054755  908 PSSQELLE 915
Cdd:cd08225  246 PSITSILK 253
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
723-913 8.35e-20

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: 91.42  E-value: 8.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  723 TLYIQMEYCEKLSLQDIIRDK---IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLA----- 794
Cdd:cd14154   64 KLNLITEYIPGGTLKDVLKDMarpLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLArlive 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  795 --TENENYQDNNDKWKNRQSADEDLTTGVGTALYVAPELLsrrNGVRYDAKVDMYSLGIILFEMC-------------MT 859
Cdd:cd14154  144 erLPSGNMSPSETLRHLKSPDRKKRYTVVGNPYWMAPEML---NGRSYDEKVDIFSFGIVLCEIIgrveadpdylprtKD 220
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 63054755  860 FSTSMERIRIIDTIRSPSISFPSTFpfsrashefkvIHCLLqhDPTKRPSSQEL 913
Cdd:cd14154  221 FGLNVDSFREKFCAGCPPPFFKLAF-----------LCCDL--DPEKRPPFETL 261
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
728-913 1.16e-19

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 90.84  E-value: 1.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  728 MEYCEKLSLQDIIRDK--IPVDEMWRLFRQILEALAYI--HSRGMMHRDLKPGNIFLDENR---NVKLGDFGLA--TENE 798
Cdd:cd13990   84 LEYCDGNDLDFYLKQHksIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSGNvsgEIKITDFGLSkiMDDE 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  799 NYQDNNdkwknrqsadEDLTT-GVGTALYVAPELLSR-RNGVRYDAKVDMYSLGIILFEMCM---TFSTSMERIRII--D 871
Cdd:cd13990  164 SYNSDG----------MELTSqGAGTYWYLPPECFVVgKTPPKISSKVDVWSVGVIFYQMLYgrkPFGHNQSQEAILeeN 233
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 63054755  872 TI-RSPSISFPSTFPFSRASHEFkvIHCLLQHDPTKRPSSQEL 913
Cdd:cd13990  234 TIlKATEVEFPSKPVVSSEAKDF--IRRCLTYRKEDRPDVLQL 274
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
694-919 1.37e-19

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: 90.88  E-value: 1.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  694 TSDKEGSSDKDSSIEEASSVKTQENGLNAT-----------LYIQMEYCEKLSLQDIIRDKiPVDE--MWRLFRQILEAL 760
Cdd:cd06640   36 IIDLEEAEDEIEDIQQEITVLSQCDSPYVTkyygsylkgtkLWIIMEYLGGGSALDLLRAG-PFDEfqIATMLKEILKGL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  761 AYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQDNNDkwknrqsadedltTGVGTALYVAPELLSRRngvRY 840
Cdd:cd06640  115 DYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRN-------------TFVGTPFWMAPEVIQQS---AY 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  841 DAKVDMYSLGIILFEMCM--TFSTSMERIRIIDTIrsPSISFPS-TFPFSRASHEFkvIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd06640  179 DSKADIWSLGITAIELAKgePPNSDMHPMRVLFLI--PKNNPPTlVGDFSKPFKEF--IDACLNKDPSFRPTAKELLKHK 254

                 ..
gi 63054755  918 AI 919
Cdd:cd06640  255 FI 256
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
724-917 1.81e-19

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: 89.69  E-value: 1.81e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRD-KIPVDEMWRLF-RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENEnyq 801
Cdd:cd14188   76 IYILLEYCSRRSMAHILKArKVLTEPEVRYYlRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLE--- 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  802 dnndkwknrqSADEDLTTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMCM---TFSTS--MERIRiidTIRSP 876
Cdd:cd14188  153 ----------PLEHRRRTICGTPNYLSPEVLNKQG---HGCESDIWALGCVMYTMLLgrpPFETTnlKETYR---CIREA 216
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 63054755  877 SISFPSTFpFSRASHefkVIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd14188  217 RYSLPSSL-LAPAKH---LIASMLSKNPEDRPSLDEIIRHD 253
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
723-917 2.09e-19

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: 89.73  E-value: 2.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  723 TLYIQMEYCEKLSLQDIIR--DKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENR---NVKLGDFGLATEn 797
Cdd:cd14012   78 KVYLLTEYAPGGSLSELLDsvGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAgtgIVKLTDYSLGKT- 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  798 enYQDNNdkwkNRQSADEDLTTgvgtaLYVAPELLsrRNGVRYDAKVDMYSLGIILFEMCMTFSTSMERIRIIDTIRSPS 877
Cdd:cd14012  157 --LLDMC----SRGSLDEFKQT-----YWLPPELA--QGSKSPTRKTDVWDLGLLFLQMLFGLDVLEKYTSPNPVLVSLD 223
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 63054755  878 ISFPstfpfsraSHEFkVIHClLQHDPTKRPSSQELLESE 917
Cdd:cd14012  224 LSAS--------LQDF-LSKC-LSLDPKKRPTALELLPHE 253
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
720-859 2.45e-19

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: 89.35  E-value: 2.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  720 LNATLYIQMEYCEKLSLQDIIRDKIPVDE-MWRLF-RQILEALAYIHSRGMMHRDLKPGNIFLDENRN---------VKL 788
Cdd:cd14120   63 TSSSVYLVMEYCNGGDLADYLQAKGTLSEdTIRVFlQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGrkpspndirLKI 142
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054755  789 GDFGLAtenenyqdnndkwknRQSADEDL-TTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEmCMT 859
Cdd:cd14120  143 ADFGFA---------------RFLQDGMMaATLCGSPMYMAPEVIMSLQ---YDAKADLWSIGTIVYQ-CLT 195
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
712-914 2.50e-19

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: 89.42  E-value: 2.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  712 SVKTQENGLNATLYIQMEYCEKLSLQDIIRDK--IPVDE----MWrlFRQILEALAYIHSRGMMHRDLKPGNIFLDENRN 785
Cdd:cd08223   63 SYKESFEGEDGFLYIVMGFCEGGDLYTRLKEQkgVLLEErqvvEW--FVQIAMALQYMHERNILHRDLKTQNIFLTKSNI 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  786 VKLGDFGLATENENYQDNndkwknrqsadedLTTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMCM---TFST 862
Cdd:cd08223  141 IKVGDLGIARVLESSSDM-------------ATTLIGTPYYMSPELFSNKP---YNHKSDVWALGCCVYEMATlkhAFNA 204
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 63054755  863 -SMERI--RIIDTiRSPSIsfpstfPFSRASHEFKVIHCLLQHDPTKRPSSQELL 914
Cdd:cd08223  205 kDMNSLvyKILEG-KLPPM------PKQYSPELGELIKAMLHQDPEKRPSVKRIL 252
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
724-916 3.63e-19

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: 89.34  E-value: 3.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDKiPVDEM--WRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENEnyq 801
Cdd:cd14118   91 LYMVFELVDKGAVMEVPTDN-PLSEEtaRSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFGVSNEFE--- 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  802 dnndkwknrqSADEDLTTGVGTALYVAPELLSrRNGVRYDAK-VDMYSLGIILFemCMTFST----SMERIRIIDTIRSP 876
Cdd:cd14118  167 ----------GDDALLSSTAGTPAFMAPEALS-ESRKKFSGKaLDIWAMGVTLY--CFVFGRcpfeDDHILGLHEKIKTD 233
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 63054755  877 SISFPSTFPFSRASHEfkVIHCLLQHDPTKRPSSQELLES 916
Cdd:cd14118  234 PVVFPDDPVVSEQLKD--LILRMLDKNPSERITLPEIKEH 271
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
725-917 4.80e-19

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: 89.04  E-value: 4.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  725 YIQMEYCEKLSLQDII--RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAteneNYQD 802
Cdd:cd14077   89 YMLFEYVDGGQLLDYIisHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGLS----NLYD 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  803 NNDKwknrqsadedLTTGVGTALYVAPELLsrrNGVRYDA-KVDMYSLGIILFEM---CMTF-STSMERIRiiDTIRSPS 877
Cdd:cd14077  165 PRRL----------LRTFCGSLYFAAPELL---QAQPYTGpEVDVWSFGVVLYVLvcgKVPFdDENMPALH--AKIKKGK 229
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 63054755  878 ISFPSTFpfsraSHEFK-VIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd14077  230 VEYPSYL-----SSECKsLISRMLVVDPKKRATLEQVLNHP 265
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
724-915 5.10e-19

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: 90.16  E-value: 5.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEkLSLQDIIRDKIPV-DEMWRLF-RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATE-NENY 800
Cdd:cd07857   81 LYLYEELME-ADLHQIIRSGQPLtDAHFQSFiYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARGfSENP 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  801 QDNndkwknrqsaDEDLTTGVGTALYVAPE-LLSRRngvRYDAKVDMYSLGIIL-------------------FEMCMTF 860
Cdd:cd07857  160 GEN----------AGFMTEYVATRWYRAPEiMLSFQ---SYTKAIDVWSVGCILaellgrkpvfkgkdyvdqlNQILQVL 226
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  861 STSMERI-------RIIDTIRS----PSISFPSTFPFsrASHE-FKVIHCLLQHDPTKRPSSQELLE 915
Cdd:cd07857  227 GTPDEETlsrigspKAQNYIRSlpniPKKPFESIFPN--ANPLaLDLLEKLLAFDPTKRISVEEALE 291
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
723-914 6.06e-19

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: 88.65  E-value: 6.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  723 TLYIQMEYCEKLSLQDIIRDKIPVDEM--WRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLA---TEN 797
Cdd:cd06631   77 VVSIFMEFVPGGSIASILARFGALEEPvfCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAkrlCIN 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  798 ENYQDNNDKWKNRQsadedlttgvGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMCMTFS--TSMERIRIIDTI-- 873
Cdd:cd06631  157 LSSGSQSQLLKSMR----------GTPYWMAPEVINETG---HGRKSDIWSIGCTVFEMATGKPpwADMNPMAAIFAIgs 223
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 63054755  874 -RSPSISFPSTfpFSRASHEFkvIHCLLQHDPTKRPSSQELL 914
Cdd:cd06631  224 gRKPVPRLPDK--FSPEARDF--VHACLTRDQDERPSAEQLL 261
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
285-506 8.58e-19

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: 88.03  E-value: 8.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  285 REIQELEYELESLKVIRHDLLASIYEYQLEREtrgygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAE 364
Cdd:cd14014   42 EFRERFLREARALARLSHPNIVRVYDVGEDDG------RPYIVMEYVEGGSLADLLRERGPLPPREALRILAQIADALAA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  365 LHRLGIshksLHLD----NVVLFHSGHrtfAKLMDFGFTRTLRDmnashpfNINSQSITNIlpeG--LY-PPEVSESsfA 437
Cdd:cd14014  116 AHRAGI----VHRDikpaNILLTEDGR---VKLTDFGIARALGD-------SGLTQTGSVL---GtpAYmAPEQARG--G 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  438 AASRKTDIWCFGLLVLQMLCGAHVLNKFSSLKLIMTHVI----------PLLPGSYQDLVRRCLMRDSRKRP-SAIDLLS 506
Cdd:cd14014  177 PVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQeappppsplnPDVPPALDAIILRALAKDPEERPqSAAELLA 256
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
725-915 9.37e-19

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: 88.11  E-value: 9.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  725 YIQMEYCEKLSLQDI----IRDKIPVDEMWRLFRQILEALAYIHSRG--MMHRDLKPGNIFLDENRNVKLGDFGLATEne 798
Cdd:cd14037   82 LLLMEYCKGGGVIDLmnqrLQTGLTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSGNYKLCDFGSATT-- 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  799 nyQDNN-DKWKNRQSADEDLTTGVgTALYVAPELLSRRNGVRYDAKVDMYSLGIILFEMCMtFSTSMERIRIIdTIRSPS 877
Cdd:cd14037  160 --KILPpQTKQGVTYVEEDIKKYT-TLQYRAPEMIDLYRGKPITEKSDIWALGCLLYKLCF-YTTPFEESGQL-AILNGN 234
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 63054755  878 ISFPSTFPFSRASHefKVIHCLLQHDPTKRPSSQELLE 915
Cdd:cd14037  235 FTFPDNSRYSKRLH--KLIRYMLEEDPEKRPNIYQVSY 270
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
281-506 1.43e-18

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: 87.49  E-value: 1.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  281 EDGKREIQELEYELESLKVIRHDLLASIYEYQLERETrgygwrLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILE 360
Cdd:cd06631   41 EKAEKEYEKLQEEVDLLKTLKHVNIVGYLGTCLEDNV------VSIFMEFVPGGSIASILARFGALEEPVFCRYTKQILE 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  361 GLAELHRLGISHKSLHLDNVVLFHSGhrtFAKLMDFGFTRTLrdmnashPFNINSQSITNIL------PEGLYPPEVSES 434
Cdd:cd06631  115 GVAYLHNNNVIHRDIKGNNIMLMPNG---VIKLIDFGCAKRL-------CINLSSGSQSQLLksmrgtPYWMAPEVINET 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  435 SFAaasRKTDIWCFGLLVLQMLCG----AHVlNKFSSLKLIMTH--VIPLLPGSY----QDLVRRCLMRDSRKRPSAIDL 504
Cdd:cd06631  185 GHG---RKSDIWSIGCTVFEMATGkppwADM-NPMAAIFAIGSGrkPVPRLPDKFspeaRDFVHACLTRDQDERPSAEQL 260

                 ..
gi 63054755  505 LS 506
Cdd:cd06631  261 LK 262
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
725-913 1.75e-18

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: 86.72  E-value: 1.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  725 YIQMEYCEKLSLQDIIRDKIPVDEM-------WRLfrQILEALAYIHS---RGMMHRDLKPGNIFLDEN-RNVKLGDFGL 793
Cdd:cd14058   62 CLVMEYAEGGSLYNVLHGKEPKPIYtaahamsWAL--QCAKGVAYLHSmkpKALIHRDLKPPNLLLTNGgTVLKICDFGT 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  794 ATENENYQDNNDkwknrqsadedlttgvGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMcmtfstsMERIRIIDTI 873
Cdd:cd14058  140 ACDISTHMTNNK----------------GSAAWMAPEVFEGSK---YSEKCDVFSWGIILWEV-------ITRRKPFDHI 193
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 63054755  874 RSPSisfpstFPFSRASHEFK--------------VIHCLLQHDPTKRPSSQEL 913
Cdd:cd14058  194 GGPA------FRIMWAVHNGErpplikncpkpiesLMTRCWSKDPEKRPSMKEI 241
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
724-919 1.87e-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: 87.22  E-value: 1.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDK--IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIF----LDENR---NVKLGDFGLA 794
Cdd:cd14097   75 MYLVMELCEDGELKELLLRKgfFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILvkssIIDNNdklNIKVTDFGLS 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  795 TEnenyqdnndkwknRQSADED-LTTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMCM---TFSTSMERiRII 870
Cdd:cd14097  155 VQ-------------KYGLGEDmLQETCGTPIYMAPEVISAHG---YSQQCDIWSIGVIMYMLLCgepPFVAKSEE-KLF 217
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 63054755  871 DTIRSPSISFpSTFPFSRASHEFK-VIHCLLQHDPTKRPSSQELLESEAI 919
Cdd:cd14097  218 EEIRKGDLTF-TQSVWQSVSDAAKnVLQQLLKVDPAHRMTASELLDNPWI 266
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
293-505 1.94e-18

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 90.46  E-value: 1.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  293 ELESLKVIRHDLLASIYEYQLEREtrgygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISH 372
Cdd:COG0515   57 EARALARLNHPNIVRVYDVGEEDG------RPYLVMEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVH 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  373 KSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDMNASHPFninsqsitniLPEG--LY-PPEVSESsfAAASRKTDIWCFG 449
Cdd:COG0515  131 RDIKPANILLTPDGR---VKLIDFGIARALGGATLTQTG----------TVVGtpGYmAPEQARG--EPVDPRSDVYSLG 195
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  450 LLVLQMLCGAHVLNKFSSLKLIMTHV----------IPLLPGSYQDLVRRCLMRDSRKRP-SAIDLL 505
Cdd:COG0515  196 VTLYELLTGRPPFDGDSPAELLRAHLrepppppselRPDLPPALDAIVLRALAKDPEERYqSAAELA 262
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
724-914 1.99e-18

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: 87.01  E-value: 1.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDKIPVDEMWRLF--RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEnenyq 801
Cdd:cd06646   81 LWICMEYCGGGSLQDIYHVTGPLSELQIAYvcRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAK----- 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  802 dNNDKWKNRQSAdedlttgVGTALYVAPELLSRRNGVRYDAKVDMYSLGIILFEMC-----MTFSTSMERIRIIDTIRSP 876
Cdd:cd06646  156 -ITATIAKRKSF-------IGTPYWMAPEVAAVEKNGGYNQLCDIWAVGITAIELAelqppMFDLHPMRALFLMSKSNFQ 227
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 63054755  877 SISFPSTFPFSRASHEFkvIHCLLQHDPTKRPSSQELL 914
Cdd:cd06646  228 PPKLKDKTKWSSTFHNF--VKISLTKNPKKRPTAERLL 263
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
723-907 2.18e-18

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: 86.68  E-value: 2.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  723 TLYIQMEYCEKLSLQDII--RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAteneny 800
Cdd:cd14071   73 MLYLVTEYASNGEIFDYLaqHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFS------ 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  801 qdnndkwkNRQSADEDLTTGVGTALYVAPELLSrrnGVRYDA-KVDMYSLGIILFEM-C--MTFSTSMeririIDTIRSP 876
Cdd:cd14071  147 --------NFFKPGELLKTWCGSPPYAAPEVFE---GKEYEGpQLDIWSLGVVLYVLvCgaLPFDGST-----LQTLRDR 210
                        170       180       190
                 ....*....|....*....|....*....|.
gi 63054755  877 SISFPSTFPFSRASHEFKVIHCLLQHDPTKR 907
Cdd:cd14071  211 VLSGRFRIPFFMSTDCEHLIRRMLVLDPSKR 241
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
743-914 2.58e-18

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 88.39  E-value: 2.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   743 KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENyqdnndkwknrqsADEDLTTGvG 822
Cdd:PHA03209  153 PLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQFPVV-------------APAFLGLA-G 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   823 TALYVAPELLSRrngVRYDAKVDMYSLGIILFEMCMTFST----------------SMERIRIIDTIRSPSISFPSTfPF 886
Cdd:PHA03209  219 TVETNAPEVLAR---DKYNSKADIWSAGIVLFEMLAYPSTifedppstpeeyvkscHSHLLKIISTLKVHPEEFPRD-PG 294
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 63054755   887 SRASHEFK---------------------------VIHCLLQHDPTKRPSSQELL 914
Cdd:PHA03209  295 SRLVRGFIeyaslerqpytrypcfqrvnlpidgefLVHKMLTFDAAMRPSAEEIL 349
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
551-919 2.71e-18

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: 87.43  E-value: 2.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  551 RYETDFEELEF---LGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENSRILREVMTLSRLHH-EHVVRYYTAWVetea 626
Cdd:cd06618    9 KYKADLNDLENlgeIGSGTCGQVYKMRHKKTGHVMAVKQMRRSGNKEENKRILMDLDVVLKSHDcPYIVKCYGYFI---- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  627 ndtvteiissdseslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkegssdKDSS 706
Cdd:cd06618   85 ----------------------------------------------------------------------------TDSD 88
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  707 IeeassvktqenglnatlYIQMEY----CEKLSLQdiIRDKIPVDEMWRLFRQILEALAYIHSR-GMMHRDLKPGNIFLD 781
Cdd:cd06618   89 V-----------------FICMELmstcLDKLLKR--IQGPIPEDILGKMTVSIVKALHYLKEKhGVIHRDVKPSNILLD 149
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  782 ENRNVKLGDFGLAtenenyqdnndkwkNRQSADEDLTTGVGTALYVAPELLSRRNGVRYDAKVDMYSLGIILFEM----- 856
Cdd:cd06618  150 ESGNVKLCDFGIS--------------GRLVDSKAKTRSAGCAAYMAPERIDPPDNPKYDIRADVWSLGISLVELatgqf 215
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  857 ----CMTFSTSMERIriidtIRSPSISFPSTFPFSRASHEFkVIHClLQHDPTKRPSSQELLESEAI 919
Cdd:cd06618  216 pyrnCKTEFEVLTKI-----LNEEPPSLPPNEGFSPDFCSF-VDLC-LTKDHRYRPKYRELLQHPFI 275
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
556-857 2.78e-18

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: 86.40  E-value: 2.78e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755    556 FEELEFLGRGGFGEVVK--VKNRIDGRFY--AVKKLVLLSDDKENSRILREVMTLSRLHHEHVVRYYTAwveteandtVT 631
Cdd:pfam07714    1 LTLGEKLGEGAFGEVYKgtLKGEGENTKIkvAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGV---------CT 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755    632 EiissdseslsqslnmavdfrqssslpadklssldihfeddynssadeEDPeasdisfqysntsdkegssdkdssieeas 711
Cdd:pfam07714   72 Q-----------------------------------------------GEP----------------------------- 75
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755    712 svktqenglnatLYIQMEYCEKLSLQDIIRD---KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKL 788
Cdd:pfam07714   76 ------------LYIVTEYMPGGDLLDFLRKhkrKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKI 143
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755    789 GDFGLA---TENENYQDNND-----KWknrqsadedlttgvgtalyVAPELLSRRngvRYDAKVDMYSLGIILFEMC 857
Cdd:pfam07714  144 SDFGLSrdiYDDDYYRKRGGgklpiKW-------------------MAPESLKDG---KFTSKSDVWSFGVLLWEIF 198
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
555-914 3.25e-18

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: 86.50  E-value: 3.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  555 DFEELEFLGRGGFGEVVKVKNRiDGRFYAVKKlVLLSDDKENSR--ILREVMTLSRL-HHEHVVRYYTAwveteandtvt 631
Cdd:cd14131    2 PYEILKQLGKGGSSKVYKVLNP-KKKIYALKR-VDLEGADEQTLqsYKNEIELLKKLkGSDRIIQLYDY----------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  632 eiissdseslsqslnmavdfrqssslpadklsslDIHFEDDYnssadeedpeasdisfqysntsdkegssdkdssieeas 711
Cdd:cd14131   69 ----------------------------------EVTDEDDY-------------------------------------- 76
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  712 svktqenglnatLYIQMEYCEkLSLQDIIRDKI--PVDEMWR--LFRQILEALAYIHSRGMMHRDLKPGNiFLDENRNVK 787
Cdd:cd14131   77 ------------LYMVMECGE-IDLATILKKKRpkPIDPNFIryYWKQMLEAVHTIHEEGIVHSDLKPAN-FLLVKGRLK 142
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  788 LGDFGLATENENYQDNndkwKNRQSAdedlttgVGTALYVAPELL---SRRNGVRYDAKV----DMYSLGIILFEMCM-- 858
Cdd:cd14131  143 LIDFGIAKAIQNDTTS----IVRDSQ-------VGTLNYMSPEAIkdtSASGEGKPKSKIgrpsDVWSLGCILYQMVYgk 211
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054755  859 ----TFSTSMERI-RIIDTirSPSISFPS-TFPFSrasheFKVIHCLLQHDPTKRPSSQELL 914
Cdd:cd14131  212 tpfqHITNPIAKLqAIIDP--NHEIEFPDiPNPDL-----IDVMKRCLQRDPKKRPSIPELL 266
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
559-856 3.27e-18

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: 86.28  E-value: 3.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  559 LEFLGRGGFGEVVKVKNRidGRFYAVKKLVLLSDDKENSRILREVMTLSRLHHEHVVRyytawveteandtvteiissds 638
Cdd:cd13979    8 QEPLGSGGFGSVYKATYK--GETVAVKIVRRRRKNRASRQSFWAELNAARLRHENIVR---------------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  639 eslsqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkegssdkdssIEEASSVKTQEN 718
Cdd:cd13979   64 --------------------------------------------------------------------VLAAETGTDFAS 75
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  719 -GLnatlyIQMEYCEKLSLQDII---RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLA 794
Cdd:cd13979   76 lGL-----IIMEYCGNGTLQQLIyegSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCS 150
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054755  795 TENENYQDnndkwknrqsADEDLTTGVGTALYVAPELLsrrNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd13979  151 VKLGEGNE----------VGTPRSHIGGTYTYRAPELL---KGERVTPKADIYSFGITLWQM 199
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
755-915 3.45e-18

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: 87.09  E-value: 3.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFL---DENRNVKLGDFGLATEnenYQDNNDKWKNRqsadedlttgVGTALYVAPEL 831
Cdd:cd14086  108 QILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIE---VQGDQQAWFGF----------AGTPGYLSPEV 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  832 LSRrngVRYDAKVDMYSLGIILFEMCMTFSTSMER--IRIIDTIRSPSISFPSTfPFSRASHEFK-VIHCLLQHDPTKRP 908
Cdd:cd14086  175 LRK---DPYGKPVDIWACGVILYILLVGYPPFWDEdqHRLYAQIKAGAYDYPSP-EWDTVTPEAKdLINQMLTVNPAKRI 250

                 ....*..
gi 63054755  909 SSQELLE 915
Cdd:cd14086  251 TAAEALK 257
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
736-915 4.12e-18

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: 85.74  E-value: 4.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  736 LQDIIRDKIPVDEMWrlFRQILEALAYIHSRG--MMHRDLKPGNIFLDENRN-VKLGDFGLATEnenyqdnndkwKNRQS 812
Cdd:cd13983   93 LKRFKRLKLKVIKSW--CRQILEGLNYLHTRDppIIHRDLKCDNIFINGNTGeVKIGDLGLATL-----------LRQSF 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  813 AdedlTTGVGTALYVAPELLSRrngvRYDAKVDMYSLGIILFEMcMTFSTS-MERIRIIDTIRSPSISFPstfP--FSRA 889
Cdd:cd13983  160 A----KSVIGTPEFMAPEMYEE----HYDEKVDIYAFGMCLLEM-ATGEYPySECTNAAQIYKKVTSGIK---PesLSKV 227
                        170       180       190
                 ....*....|....*....|....*....|
gi 63054755  890 SH----EFkVIHCLLQhdPTKRPSSQELLE 915
Cdd:cd13983  228 KDpelkDF-IEKCLKP--PDERPSARELLE 254
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
755-916 4.59e-18

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: 86.43  E-value: 4.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEnenyqdnndkwknrQSADEDLTTGVGTALYVAPELLsr 834
Cdd:cd05577  103 EIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVE--------------FKGGKKIKGRVGTHGYMAPEVL-- 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  835 RNGVRYDAKVDMYSLGIILFEMCMTFSTSMERIRIIDT--IRSPSISFPSTFP--FSRASHEFkvIHCLLQHDPTKR--- 907
Cdd:cd05577  167 QKEVAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKeeLKRRTLEMAVEYPdsFSPEARSL--CEGLLQKDPERRlgc 244
                        170
                 ....*....|.
gi 63054755  908 --PSSQELLES 916
Cdd:cd05577  245 rgGSADEVKEH 255
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
724-907 6.39e-18

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 85.61  E-value: 6.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDKIPVDEMW--RLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENEnyq 801
Cdd:cd05611   72 LYLVMEYLNGGDCASLIKTLGGLPEDWakQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGL--- 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  802 dnndkwKNRQSADEdlttgVGTALYVAPELLsrrNGVRYDAKVDMYSLGIILFEMCMTF-----STSMErirIIDTIRSP 876
Cdd:cd05611  149 ------EKRHNKKF-----VGTPDYLAPETI---LGVGDDKMSDWWSLGCVIFEFLFGYppfhaETPDA---VFDNILSR 211
                        170       180       190
                 ....*....|....*....|....*....|..
gi 63054755  877 SISFPStFPFSRASHEFK-VIHCLLQHDPTKR 907
Cdd:cd05611  212 RINWPE-EVKEFCSPEAVdLINRLLCMDPAKR 242
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
724-915 8.30e-18

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: 84.98  E-value: 8.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDKIPVD-EMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQD 802
Cdd:cd06647   79 LWVVMEYLAGGSLTDVVTETCMDEgQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQS 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  803 NNdkwknrqsadedlTTGVGTALYVAPELLSRRngvRYDAKVDMYSLGIILFEMC-----MTFSTSMERIRIIDTIRSPS 877
Cdd:cd06647  159 KR-------------STMVGTPYWMAPEVVTRK---AYGPKVDIWSLGIMAIEMVegeppYLNENPLRALYLIATNGTPE 222
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 63054755  878 ISFPSTfpFSRASHEFkVIHClLQHDPTKRPSSQELLE 915
Cdd:cd06647  223 LQNPEK--LSAIFRDF-LNRC-LEMDVEKRGSAKELLQ 256
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
721-856 9.05e-18

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: 84.77  E-value: 9.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  721 NATLYIQMEYCEKLSLQDII---RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGN-IFLDENRNVKLGDFGLAte 796
Cdd:cd14074   74 QTKLYLILELGDGGDMYDYImkhENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFS-- 151
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 63054755  797 nenyqdnndkwkNRQSADEDLTTGVGTALYVAPELLSrrnGVRYDA-KVDMYSLGIILFEM 856
Cdd:cd14074  152 ------------NKFQPGEKLETSCGSLAYSAPEILL---GDEYDApAVDIWSLGVILYML 197
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
550-915 9.48e-18

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: 85.46  E-value: 9.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  550 SRYETDFEELEFLGRGGFGEVVKVKNRIDGRFYAV---KKLVLLSDDKENSriLREVMTLSRL-HHEHVVRYYTAWVete 625
Cdd:cd14138    1 SRYATEFHELEKIGSGEFGSVFKCVKRLDGCIYAIkrsKKPLAGSVDEQNA--LREVYAHAVLgQHSHVVRYYSAWA--- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  626 andtvteiissdseslsqslnmavdfrqssslpadklssldihfEDDYnssadeedpeasdisfqysntsdkegssdkds 705
Cdd:cd14138   76 --------------------------------------------EDDH-------------------------------- 79
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  706 sieeassvktqenglnatLYIQMEYCEKLSLQDIIRDK------IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIF 779
Cdd:cd14138   80 ------------------MLIQNEYCNGGSLADAISENyrimsyFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIF 141
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  780 L------------------DENRNV-KLGDFGLATENENYQdnndkwknrqsADEdlttgvGTALYVAPELLsrRNGVRY 840
Cdd:cd14138  142 IsrtsipnaaseegdedewASNKVIfKIGDLGHVTRVSSPQ-----------VEE------GDSRFLANEVL--QENYTH 202
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63054755  841 DAKVDMYSLGIILFEMCMT--FSTSMERIRIIDTIRSPSIsfPSTFpfsraSHEF-KVIHCLLQHDPTKRPSSQELLE 915
Cdd:cd14138  203 LPKADIFALALTVVCAAGAepLPTNGDQWHEIRQGKLPRI--PQVL-----SQEFlDLLKVMIHPDPERRPSAVALVK 273
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
282-506 9.51e-18

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: 84.71  E-value: 9.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  282 DGKREIQELEYELESLKVIRHDLLASIYEYQLERETrgygwrLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEG 361
Cdd:cd06625   41 EASKEVKALECEIQLLKNLQHERIVQYYGCLQDEKS------LSIFMEYMPGGSVKDEIKAYGALTENVTRKYTRQILEG 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  362 LAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRdmnashpfNINSQSITNILPEGLY--PPEVSESsfAAA 439
Cdd:cd06625  115 LAYLHSNMIVHRDIKGANILRDSNGN---VKLGDFGASKRLQ--------TICSSTGMKSVTGTPYwmSPEVING--EGY 181
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63054755  440 SRKTDIWCFGLLVLQMLCGAHVLNKFSSL----KLIMTHVIPLLPG----SYQDLVRRCLMRDSRKRPSAIDLLS 506
Cdd:cd06625  182 GRKADIWSVGCTVVEMLTTKPPWAEFEPMaaifKIATQPTNPQLPPhvseDARDFLSLIFVRNKKQRPSAEELLS 256
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
724-914 9.60e-18

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: 85.63  E-value: 9.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEkLSLQDIIRDK------IPVDEMwRLFR-QILEALAYIHSRGMMHRDLKPGNIFLDENRNV-KLGDFGLAt 795
Cdd:cd14137   78 LNLVMEYMP-ETLYRVIRHYsknkqtIPIIYV-KLYSyQLFRGLAYLHSLGICHRDIKPQNLLVDPETGVlKLCDFGSA- 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  796 enenyqdnndKwknRQSADEDLTTGVGTALYVAPELLSrrNGVRYDAKVDMYSLGIILFEMCMTF-----STSMERIR-I 869
Cdd:cd14137  155 ----------K---RLVPGEPNVSYICSRYYRAPELIF--GATDYTTAIDIWSAGCVLAELLLGQplfpgESSVDQLVeI 219
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  870 IDTIRSPSIS-------------FPSTFP------FS-RASHEFK-VIHCLLQHDPTKRPSSQELL 914
Cdd:cd14137  220 IKVLGTPTREqikamnpnytefkFPQIKPhpwekvFPkRTPPDAIdLLSKILVYNPSKRLTALEAL 285
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
724-915 1.04e-17

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: 85.81  E-value: 1.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRD-KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATenenyQD 802
Cdd:cd06659   93 LWVLMEYLQGGALTDIVSQtRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCA-----QI 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  803 NNDKWKNRqsadedltTGVGTALYVAPELLSRrngVRYDAKVDMYSLGIILFEMC----MTFSTS----MERIRiidtiR 874
Cdd:cd06659  168 SKDVPKRK--------SLVGTPYWMAPEVISR---CPYGTEVDIWSLGIMVIEMVdgepPYFSDSpvqaMKRLR-----D 231
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 63054755  875 SPSisfPSTFPFSRASHEFK-VIHCLLQHDPTKRPSSQELLE 915
Cdd:cd06659  232 SPP---PKLKNSHKASPVLRdFLERMLVRDPQERATAQELLD 270
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
556-915 1.37e-17

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: 85.03  E-value: 1.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  556 FEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKE-NSRILREVMTLSRLHHEHVVRYYtawveteandtvteii 634
Cdd:cd07835    1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIRLETEDEGvPSTAIREISLLKELNHPNIVRLL---------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  635 ssdseslsqslnmavdfrqssslpadklsslDIHFEDD--YnssadeedpeasdISFQYsntsdkegssdkdssieeass 712
Cdd:cd07835   65 -------------------------------DVVHSENklY-------------LVFEF--------------------- 79
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  713 vktqengLNATLYIQMEYCEKLSL-QDIIRdkipvdemwRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDF 791
Cdd:cd07835   80 -------LDLDLKKYMDSSPLTGLdPPLIK---------SYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADF 143
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  792 GLA----TENENYqdnndkwknrqsadedlTTGVGTALYVAPELLSrrnGVR-YDAKVDMYSLGIILFEMCMT---FSTS 863
Cdd:cd07835  144 GLArafgVPVRTY-----------------THEVVTLWYRAPEILL---GSKhYSTPVDIWSVGCIFAEMVTRrplFPGD 203
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  864 ME-----RI-RIIDT---IRSPSIS----FPSTFPFSRASHEFKVIHCL-----------LQHDPTKRPSSQELLE 915
Cdd:cd07835  204 SEidqlfRIfRTLGTpdeDVWPGVTslpdYKPTFPKWARQDLSKVVPSLdedgldllsqmLVYDPAKRISAKAALQ 279
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
754-915 1.43e-17

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 86.42  E-value: 1.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   754 RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFG----LAtenenyqdnndkwknrQSADEdLTTGVGTALYVAP 829
Cdd:PLN00034  175 RQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGvsriLA----------------QTMDP-CNSSVGTIAYMSP 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   830 ELLSRR-NGVRYDAKV-DMYSLGIILFEMCM-TFSTSMER----IRIIDTIrspSISFPSTFPFSrASHEFK-VIHCLLQ 901
Cdd:PLN00034  238 ERINTDlNHGAYDGYAgDIWSLGVSILEFYLgRFPFGVGRqgdwASLMCAI---CMSQPPEAPAT-ASREFRhFISCCLQ 313
                         170
                  ....*....|....
gi 63054755   902 HDPTKRPSSQELLE 915
Cdd:PLN00034  314 REPAKRWSAMQLLQ 327
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
723-917 1.63e-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: 85.11  E-value: 1.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  723 TLYIQMEYCEK--LSLQDIIRDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAteneny 800
Cdd:cd07845   82 SIFLVMEYCEQdlASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLA------ 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  801 qdnndkwKNRQSADEDLTTGVGTALYVAPELLSrrnGVR-YDAKVDMYSLGIILFEM-----CMTFSTSMERIR-IIDTI 873
Cdd:cd07845  156 -------RTYGLPAKPMTPKVVTLWYRAPELLL---GCTtYTTAIDMWAVGCILAELlahkpLLPGKSEIEQLDlIIQLL 225
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  874 RSPS---------------ISFPSTfPFSRASHEF--------KVIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd07845  226 GTPNesiwpgfsdlplvgkFTLPKQ-PYNNLKHKFpwlseaglRLLNFLLMYDPKKRATAEEALESS 291
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
726-916 1.64e-17

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: 84.21  E-value: 1.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  726 IQMEY---CEklSLQDIIRDKIPVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENR-NVKLGDFGLATenen 799
Cdd:cd14005   83 LIMERpepCQ--DLFDFITERGALSEnlARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRTgEVKLIDFGCGA---- 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  800 yqdnndkwKNRQSADEDLTtgvGTALYVAPELLSRRngvRYDAK-VDMYSLGIILFEM-CMTFSTSmERIRIIDtirsPS 877
Cdd:cd14005  157 --------LLKDSVYTDFD---GTRVYSPPEWIRHG---RYHGRpATVWSLGILLYDMlCGDIPFE-NDEQILR----GN 217
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 63054755  878 ISFPSTfpFSRASHEFkvIHCLLQHDPTKRPSSQELLES 916
Cdd:cd14005  218 VLFRPR--LSKECCDL--ISRCLQFDPSKRPSLEQILSH 252
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
725-917 2.11e-17

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: 84.58  E-value: 2.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  725 YIQMEYCEKlSLQDIIRDKIP---VDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEnenYQ 801
Cdd:cd07843   82 YMVMEYVEH-DLKSLMETMKQpflQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLARE---YG 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  802 DNNDKwknrqsadedLTTGVGTALYVAPELLsrRNGVRYDAKVDMYSLGIILFEM-------------------CMTFST 862
Cdd:cd07843  158 SPLKP----------YTQLVVTLWYRAPELL--LGAKEYSTAIDMWSVGCIFAELltkkplfpgkseidqlnkiFKLLGT 225
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  863 SMERI----------RIIDTIRSPSISFPSTFPFSRASHE-FKVIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd07843  226 PTEKIwpgfselpgaKKKTFTKYPYNQLRKKFPALSLSDNgFDLLNRLLTYDPAKRISAEDALKHP 291
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
721-915 3.88e-17

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


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 83.07  E-value: 3.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  721 NATLYIQMEYCEKLSLQDIIRD--KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFL----DENRNVKLGDFGLA 794
Cdd:cd14185   70 EKEIYLILEYVRGGDLFDAIIEsvKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhnpDKSTTLKLADFGLA 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  795 tenenyqdnndkwknrQSADEDLTTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMCMTF----STSMERIRII 870
Cdd:cd14185  150 ----------------KYVTGPIFTVCGTPTYVAPEILSEKG---YGLEVDMWAAGVILYILLCGFppfrSPERDQEELF 210
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 63054755  871 DTIRSPSISFPSTFpFSRASHEFK-VIHCLLQHDPTKRPSSQELLE 915
Cdd:cd14185  211 QIIQLGHYEFLPPY-WDNISEAAKdLISRLLVVDPEKRYTAKQVLQ 255
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
724-879 3.89e-17

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: 83.57  E-value: 3.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQD---IIRDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEneny 800
Cdd:cd14151   78 LAIVTQWCEGSSLYHhlhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATV---- 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  801 qdnndkwKNRQSADEDLTTGVGTALYVAPELLSRRNGVRYDAKVDMYSLGIILFEM---CMTFSTSMERIRIIDTIRSPS 877
Cdd:cd14151  154 -------KSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELmtgQLPYSNINNRDQIIFMVGRGY 226

                 ..
gi 63054755  878 IS 879
Cdd:cd14151  227 LS 228
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
726-917 4.06e-17

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 84.43  E-value: 4.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   726 IQMEYCEKlSLQDIIRDKIPVDEMWR--LFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATE--NENYQ 801
Cdd:PTZ00024   97 LVMDIMAS-DLKKVVDRKIRLTESQVkcILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARRygYPPYS 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   802 DNNDKWKNRQSaDEDLTTGVGTALYVAPELLSRRNgvRYDAKVDMYSLGIILFEM-----CMTFSTSMERI-RIIDTIRS 875
Cdd:PTZ00024  176 DTLSKDETMQR-REEMTSKVVTLWYRAPELLMGAE--KYHFAVDMWSVGCIFAELltgkpLFPGENEIDQLgRIFELLGT 252
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054755   876 PS-------ISFPSTFPFSRAS-HEFKVI--HC----------LLQHDPTKRPSSQELLESE 917
Cdd:PTZ00024  253 PNednwpqaKKLPLYTEFTPRKpKDLKTIfpNAsddaidllqsLLKLNPLERISAKEALKHE 314
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
723-951 4.19e-17

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: 83.92  E-value: 4.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  723 TLYIQMEYCEKlSLQDIIR-DKIPVDEM--WRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenen 799
Cdd:cd06634   89 TAWLVMEYCLG-SASDLLEvHKKPLQEVeiAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSA----- 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  800 yqdnndkwknrqSADEDLTTGVGTALYVAPELLSRRNGVRYDAKVDMYSLGIILFEMC-----MTFSTSMERIRIIDTIR 874
Cdd:cd06634  163 ------------SIMAPANSFVGTPYWMAPEVILAMDEGQYDGKVDVWSLGITCIELAerkppLFNMNAMSALYHIAQNE 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  875 SPSIsfpSTFPFSRASHEFkvIHCLLQHDPTKRPSSQELLESEAI----PPKVGEEFIQEGLRLLSNPNTPYYLKLLKVL 950
Cdd:cd06634  231 SPAL---QSGHWSEYFRNF--VDSCLQKIPQDRPTSDVLLKHRFLlrerPPTVIMDLIQRTKDAVRELDNLQYRKMKKIL 305

                 .
gi 63054755  951 F 951
Cdd:cd06634  306 F 306
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
726-873 4.32e-17

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: 83.14  E-value: 4.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  726 IQMEYCEKLSLQ---DIIRDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEnenyqd 802
Cdd:cd14150   72 IITQWCEGSSLYrhlHVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATV------ 145
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 63054755  803 nndkwKNRQSADEDLTTGVGTALYVAPELLSRRNGVRYDAKVDMYSLGIILFEMcMTFSTSMERIRIIDTI 873
Cdd:cd14150  146 -----KTRWSGSQQVEQPSGSILWMAPEVIRMQDTNPYSFQSDVYAYGVVLYEL-MSGTLPYSNINNRDQI 210
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
720-907 4.37e-17

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 83.14  E-value: 4.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  720 LNATLYIQMEYCEKLSLQDIIRDKIPVDE-MWRLF-RQILEALAYIHSRGMMHRDLKPGNIFLD---------ENRNVKL 788
Cdd:cd14202   72 IANSVYLVMEYCNGGDLADYLHTMRTLSEdTIRLFlQQIAGAMKMLHSKGIIHRDLKPQNILLSysggrksnpNNIRIKI 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  789 GDFGLATENENyqdnndkwkNRQSAdedltTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEmCMTF-----STS 863
Cdd:cd14202  152 ADFGFARYLQN---------NMMAA-----TLCGSPMYMAPEVIMSQH---YDAKADLWSIGTIIYQ-CLTGkapfqASS 213
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 63054755  864 MERIRII---DTIRSPSIsfpstfPFSRASHEFKVIHCLLQHDPTKR 907
Cdd:cd14202  214 PQDLRLFyekNKSLSPNI------PRETSSHLRQLLLGLLQRNQKDR 254
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
754-922 4.54e-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: 83.75  E-value: 4.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  754 RQILEALAYIHSRGMMHRDLKPGNIFLDENRN---VKLGDFGLATenenyqdnndkwknrQSADEDLTTG--VGTALYVA 828
Cdd:cd14094  116 RQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAI---------------QLGESGLVAGgrVGTPHFMA 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  829 PELLSRRngvRYDAKVDMYSLGIILFEM---CMTFSTSMERI--RIIDTirspSISFPSTFPFSRASHEFKVIHCLLQHD 903
Cdd:cd14094  181 PEVVKRE---PYGKPVDVWGCGVILFILlsgCLPFYGTKERLfeGIIKG----KYKMNPRQWSHISESAKDLVRRMLMLD 253
                        170
                 ....*....|....*....
gi 63054755  904 PTKRPSSQELLESEAIPPK 922
Cdd:cd14094  254 PAERITVYEALNHPWIKER 272
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
556-915 4.59e-17

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: 83.87  E-value: 4.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  556 FEELEFLGRGGFGEVVKV--KNRIDGRFYAVKKLVllSDDKENSRI----LREVMTLSRLHHEHVVryytawveteandT 629
Cdd:cd07842    2 YEIEGCIGRGTYGRVYKAkrKNGKDGKEYAIKKFK--GDKEQYTGIsqsaCREIALLRELKHENVV-------------S 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  630 VTEIIssdseslsqsLNmavdfrqssslPADKlssldihfeddynssadeedpeasdisfqysntsdkegssdkdssiee 709
Cdd:cd07842   67 LVEVF----------LE-----------HADK------------------------------------------------ 77
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  710 assvktqenglnaTLYIQMEYCEKLSLQDI------IRDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFL--- 780
Cdd:cd07842   78 -------------SVYLLFDYAEHDLWQIIkfhrqaKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVmge 144
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  781 -DENRNVKLGDFGLATenenyqdnndKWKN--RQSADEDLTtgVGTALYVAPELLSrrnGVR-YDAKVDMYSLGIILFEM 856
Cdd:cd07842  145 gPERGVVKIGDLGLAR----------LFNAplKPLADLDPV--VVTIWYRAPELLL---GARhYTKAIDIWAIGCIFAEL 209
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  857 C-----------------MTFSTSMERIRII----------DTIRSP------SISFPSTFPFS-----------RASHE 892
Cdd:cd07842  210 LtlepifkgreakikksnPFQRDQLERIFEVlgtptekdwpDIKKMPeydtlkSDTKASTYPNSllakwmhkhkkPDSQG 289
                        410       420
                 ....*....|....*....|...
gi 63054755  893 FKVIHCLLQHDPTKRPSSQELLE 915
Cdd:cd07842  290 FDLLRKLLEYDPTKRITAEEALE 312
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
723-951 4.64e-17

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: 83.95  E-value: 4.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  723 TLYIQMEYC--EKLSLQDIIRDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAteneny 800
Cdd:cd06635   99 TAWLVMEYClgSASDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSA------ 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  801 qdnndkwknrqSADEDLTTGVGTALYVAPELLSRRNGVRYDAKVDMYSLGIILFEMC-----MTFSTSMERIRIIDTIRS 875
Cdd:cd06635  173 -----------SIASPANSFVGTPYWMAPEVILAMDEGQYDGKVDVWSLGITCIELAerkppLFNMNAMSALYHIAQNES 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  876 PSISFPSTFPFSRashefKVIHCLLQHDPTKRPSSQELLESEAI----PPKVGEEFIQEGLRLLSNPNTPYYLKLLKVLF 951
Cdd:cd06635  242 PTLQSNEWSDYFR-----NFVDSCLQKIPQDRPTSEELLKHMFVlrerPETVLIDLIQRTKDAVRELDNLQYRKMKKLLF 316
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
723-856 5.87e-17

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: 82.57  E-value: 5.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  723 TLYIQMEYCEKLSLQD--IIRDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAteneny 800
Cdd:cd14072   73 TLYLVMEYASGGEVFDylVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFS------ 146
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  801 qdnndkwkNRQSADEDLTTGVGTALYVAPELLSrrnGVRYDA-KVDMYSLGIILFEM 856
Cdd:cd14072  147 --------NEFTPGNKLDTFCGSPPYAAPELFQ---GKKYDGpEVDVWSLGVILYTL 192
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
724-919 6.15e-17

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: 82.80  E-value: 6.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDKiPVDEMW--RLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQ 801
Cdd:cd06642   77 LWIIMEYLGGGSALDLLKPG-PLEETYiaTILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQ 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  802 DNNDKWknrqsadedlttgVGTALYVAPELLSRRngvRYDAKVDMYSLGIILFEMCM--TFSTSMERIRIIDTIrsPSIS 879
Cdd:cd06642  156 IKRNTF-------------VGTPFWMAPEVIKQS---AYDFKADIWSLGITAIELAKgePPNSDLHPMRVLFLI--PKNS 217
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 63054755  880 FPS-TFPFSRASHEFkvIHCLLQHDPTKRPSSQELLESEAI 919
Cdd:cd06642  218 PPTlEGQHSKPFKEF--VEACLNKDPRFRPTAKELLKHKFI 256
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
728-915 6.25e-17

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: 82.55  E-value: 6.25e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  728 MEYCEKLSLQDIIRD-KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQDNNDK 806
Cdd:cd14027   70 MEYMEKGNLMHVLKKvSVPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLTKEE 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  807 WKNRQSADEDLTTGVGTALYVAPELLSRRNgVRYDAKVDMYSLGIILFEMcmtfstsmeririidtirspsisFPSTFPF 886
Cdd:cd14027  150 HNEQREVDGTAKKNAGTLYYMAPEHLNDVN-AKPTEKSDVYSFAIVLWAI-----------------------FANKEPY 205
                        170       180
                 ....*....|....*....|....*....
gi 63054755  887 SRASHEFKVIHCLLQHDptkRPSSQELLE 915
Cdd:cd14027  206 ENAINEDQIIMCIKSGN---RPDVDDITE 231
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
555-856 6.79e-17

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: 83.82  E-value: 6.79e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  555 DFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKL----VLLSDDKENSRILREVMTLSrlHHEHVVR-YYTawveteandt 629
Cdd:cd05599    2 DFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLrkseMLEKEQVAHVRAERDILAEA--DNPWVVKlYYS---------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  630 vteiissdseslsqslnmavdfrqssslpadklssldihFEDDYNssadeedpeasdisfqysntsdkegssdkdssiee 709
Cdd:cd05599   70 ---------------------------------------FQDEEN----------------------------------- 75
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  710 assvktqenglnatLYIQMEYC---EKLSLqdIIRDKIPVDEMWRLFrqILE---ALAYIHSRGMMHRDLKPGNIFLDEN 783
Cdd:cd05599   76 --------------LYLIMEFLpggDMMTL--LMKKDTLTEEETRFY--IAEtvlAIESIHKLGYIHRDIKPDNLLLDAR 137
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054755  784 RNVKLGDFGLATenenyqdnndKWKNRQSAdedLTTgVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEM 856
Cdd:cd05599  138 GHIKLSDFGLCT----------GLKKSHLA---YST-VGTPDYIAPEVFLQKG---YGKECDWWSLGVIMYEM 193
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
724-916 8.44e-17

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: 82.20  E-value: 8.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIR-----------DKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFG 792
Cdd:cd00192   71 LYLVMEYMEGGDLLDFLRksrpvfpspepSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFG 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  793 LAtenenyqdnndkwknRQ-SADEDLTTGVGTALYV---APELLSRRngvRYDAKVDMYSLGIILFEMCM-------TFS 861
Cdd:cd00192  151 LS---------------RDiYDDDYYRKKTGGKLPIrwmAPESLKDG---IFTSKSDVWSFGVLLWEIFTlgatpypGLS 212
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  862 TSmeriRIIDTIRSPS-ISFPSTFPfsrasHE-FKVIHCLLQHDPTKRPSSQELLES 916
Cdd:cd00192  213 NE----EVLEYLRKGYrLPKPENCP-----DElYELMLSCWQLDPEDRPTFSELVER 260
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
724-915 8.49e-17

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: 83.57  E-value: 8.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKlSLQDIIRDKIPV-DEMWRLF-RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQ 801
Cdd:cd07855   85 VYVVLDLMES-DLHHIIHSDQPLtLEHIRYFlYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSP 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  802 DNNDKWknrqsadedLTTGVGTALYVAPELLSRRNgvRYDAKVDMYSLGIILFEMC--------------------MTFS 861
Cdd:cd07855  164 EEHKYF---------MTEYVATRWYRAPELMLSLP--EYTQAIDMWSVGCIFAEMLgrrqlfpgknyvhqlqliltVLGT 232
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054755  862 TSMERIRII--DTIRSPSISFPS-------TFPFSRASHEFKVIHCLLQHDPTKRPSSQELLE 915
Cdd:cd07855  233 PSQAVINAIgaDRVRRYIQNLPNkqpvpweTLYPKADQQALDLLSQMLRFDPSERITVAEALQ 295
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
755-907 8.73e-17

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


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 82.62  E-value: 8.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQDnndkwKNRQSAdedlttgvGTALYVAPELLsr 834
Cdd:cd05608  113 QIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQT-----KTKGYA--------GTPGFMAPELL-- 177
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  835 rNGVRYDAKVDMYSLGIILFEMCMT---FSTSMERI---RIIDTIRSPSISFPSTfpFSRASHEFkvIHCLLQHDPTKR 907
Cdd:cd05608  178 -LGEEYDYSVDYFTLGVTLYEMIAArgpFRARGEKVenkELKQRILNDSVTYSEK--FSPASKSI--CEALLAKDPEKR 251
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
732-856 9.79e-17

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: 82.97  E-value: 9.79e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  732 EKLSLQDIirdkipvdemwRLF-RQILEALAYIHSRGMMHRDLKPGNIFLD-ENRNVKLGDFGLAtenENYqdnndkwkn 809
Cdd:cd14132  107 PTLTDYDI-----------RYYmYELLKALDYCHSKGIMHRDVKPHNIMIDhEKRKLRLIDWGLA---EFY--------- 163
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 63054755  810 rqSADEDLTTGVGTALYVAPELLSrrNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd14132  164 --HPGQEYNVRVASRYYKGPELLV--DYQYYDYSLDMWSLGCMLASM 206
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
744-856 1.03e-16

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 84.13  E-value: 1.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   744 IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLA--TENENYQDNNDKWknrqsadedlttgV 821
Cdd:PHA03207  182 LPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAAckLDAHPDTPQCYGW-------------S 248
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 63054755   822 GTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEM 856
Cdd:PHA03207  249 GTLETNSPELLALDP---YCAKTDIWSAGLVLFEM 280
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
756-907 1.16e-16

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: 83.03  E-value: 1.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  756 ILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQDNNdkwknrqsadedlTTGVGTALYVAPELLSRR 835
Cdd:cd05570  105 ICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGIWGGNTT-------------STFCGTPDYIAPEILREQ 171
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  836 ngvRYDAKVDMYSLGIILFEMcMT----FSTSMERiRIIDTIRSPSISFPSTfpFSRASheFKVIHCLLQHDPTKR 907
Cdd:cd05570  172 ---DYGFSVDWWALGVLLYEM-LAgqspFEGDDED-ELFEAILNDEVLYPRW--LSREA--VSILKGLLTKDPARR 238
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
721-919 1.19e-16

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: 1.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  721 NATLYIQMEYCEKLSLQDIIRDKiPVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENE 798
Cdd:cd06641   74 DTKLWIIMEYLGGGSALDLLEPG-PLDEtqIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLT 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  799 NYQDNNDKWknrqsadedlttgVGTALYVAPELLSRRngvRYDAKVDMYSLGIILFEMCM--TFSTSMERIRIIDTIrsp 876
Cdd:cd06641  153 DTQIKRN*F-------------VGTPFWMAPEVIKQS---AYDSKADIWSLGITAIELARgePPHSELHPMKVLFLI--- 213
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 63054755  877 sisfPSTFP------FSRASHEFkvIHCLLQHDPTKRPSSQELLESEAI 919
Cdd:cd06641  214 ----PKNNPptlegnYSKPLKEF--VEACLNKEPSFRPTAKELLKHKFI 256
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
676-933 1.34e-16

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: 82.46  E-value: 1.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  676 SADEEDPEASDISFQysntsdKEGSSDKDSSIEEASSVKTQENGLNATLYIQMEYCEKLSLQDIIRDKI--PVDEMWRLF 753
Cdd:cd06637   42 TGDEEEEIKQEINML------KKYSHHRNIATYYGAFIKKNPPGMDDQLWLVMEFCGAGSVTDLIKNTKgnTLKEEWIAY 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  754 --RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEnenyqdnNDKWKNRQSadedltTGVGTALYVAPEL 831
Cdd:cd06637  116 icREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ-------LDRTVGRRN------TFIGTPYWMAPEV 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  832 LS--RRNGVRYDAKVDMYSLGIILFEMCMTFS--TSMERIRIIDTI-RSPSISFPSTfPFSRASHEFkVIHCLLQHDpTK 906
Cdd:cd06637  183 IAcdENPDATYDFKSDLWSLGITAIEMAEGAPplCDMHPMRALFLIpRNPAPRLKSK-KWSKKFQSF-IESCLVKNH-SQ 259
                        250       260
                 ....*....|....*....|....*..
gi 63054755  907 RPSSQELLESEAIPPKVGEEFIQEGLR 933
Cdd:cd06637  260 RPSTEQLMKHPFIRDQPNERQVRIQLK 286
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
725-919 1.48e-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: 1.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  725 YIQMEYCEKLSLQD-IIRDK-IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNI-FLDENRN---VKLGDFGLAtene 798
Cdd:cd14091   70 YLVTELLRGGELLDrILRQKfFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNIlYADESGDpesLRICDFGFA---- 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  799 nyqdnndkwknRQSADED--LTTGVGTALYVAPELLsRRNGvrYDAKVDMYSLGIILFEM---CMTFSTSMERI--RIID 871
Cdd:cd14091  146 -----------KQLRAENglLMTPCYTANFVAPEVL-KKQG--YDAACDIWSLGVLLYTMlagYTPFASGPNDTpeVILA 211
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 63054755  872 TIRSPSISFPSTFpFSRASHEFK-VIHCLLQHDPTKRPSSQELLESEAI 919
Cdd:cd14091  212 RIGSGKIDLSGGN-WDHVSDSAKdLVRKMLHVDPSQRPTAAQVLQHPWI 259
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
744-908 1.65e-16

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: 81.61  E-value: 1.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  744 IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATenenyqdnndKWKNRQSADEDLttgVGT 823
Cdd:cd08228  103 IPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGR----------FFSSKTTAAHSL---VGT 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  824 ALYVAPELLsRRNGvrYDAKVDMYSLGIILFEMCMT----FSTSMERIRIIDTIRspSISFPStFPFSRASHEFK-VIHC 898
Cdd:cd08228  170 PYYMSPERI-HENG--YNFKSDIWSLGCLLYEMAALqspfYGDKMNLFSLCQKIE--QCDYPP-LPTEHYSEKLReLVSM 243
                        170
                 ....*....|
gi 63054755  899 LLQHDPTKRP 908
Cdd:cd08228  244 CIYPDPDQRP 253
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
556-917 1.87e-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: 1.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  556 FEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENSRI-LREVMTLSRLHHEHVVryytawveteandtvteii 634
Cdd:cd07846    3 YENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMVKKIaMREIKMLKQLRHENLV------------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  635 ssdseslsqslNMAVDFRQSSSLpadklssldihfeddynssadeedpeasdisfqysntsdkegssdkdssieeassvk 714
Cdd:cd07846   64 -----------NLIEVFRRKKRW--------------------------------------------------------- 75
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  715 tqenglnatlYIQMEYCEKLSLQDIIRDKIPVDEMW--RLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFG 792
Cdd:cd07846   76 ----------YLVFEFVDHTVLDDLEKYPNGLDESRvrKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFG 145
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  793 LAtenenyqdnndkwKNRQSADEDLTTGVGTALYVAPELLSrrNGVRYDAKVDMYSLGIILFEM---------------- 856
Cdd:cd07846  146 FA-------------RTLAAPGEVYTDYVATRWYRAPELLV--GDTKYGKAVDVWAVGCLVTEMltgeplfpgdsdidql 210
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  857 ----------CMTFSTSMERIRIIDTIRSPSISFPST----FP-FSRASHEFkvIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd07846  211 yhiikclgnlIPRHQELFQKNPLFAGVRLPEVKEVEPlerrYPkLSGVVIDL--AKKCLHIDPDKRPSCSELLHHE 284
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
724-873 2.31e-16

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: 81.23  E-value: 2.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQ---DIIRDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEneny 800
Cdd:cd14149   82 LAIVTQWCEGSSLYkhlHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATV---- 157
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054755  801 qdnndkwKNRQSADEDLTTGVGTALYVAPELLSRRNGVRYDAKVDMYSLGIILFEMcMTFSTSMERIRIIDTI 873
Cdd:cd14149  158 -------KSRWSGSQQVEQPTGSILWMAPEVIRMQDNNPFSFQSDVYSYGIVLYEL-MTGELPYSHINNRDQI 222
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
736-856 2.51e-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: 82.03  E-value: 2.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  736 LQDIIRDKIPV-DEMWRLF-RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLA-TENENyqdnndkwknrqs 812
Cdd:cd07858   95 LHQIIRSSQTLsDDHCQYFlYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLArTTSEK------------- 161
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 63054755  813 aDEDLTTGVGTALYVAPELLsrRNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd07858  162 -GDFMTEYVVTRWYRAPELL--LNCSEYTTAIDVWSVGCIFAEL 202
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
705-856 2.61e-16

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: 82.40  E-value: 2.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  705 SSIEEASSVKTQENGLNATLYiQMEYCEKLSlqdiirdkipVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENR 784
Cdd:cd07878   87 TSIENFNEVYLVTNLMGADLN-NIVKCQKLS----------DEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDC 155
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054755  785 NVKLGDFGLAtenenyqdnndkwknRQsADEDLTTGVGTALYVAPELLsrRNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd07878  156 ELRILDFGLA---------------RQ-ADDEMTGYVATRWYRAPEIM--LNWMHYNQTVDIWSVGCIMAEL 209
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
724-915 3.21e-16

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


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 80.84  E-value: 3.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRD-KIPVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENY 800
Cdd:cd06643   77 LWILIEFCAGGAVDAVMLElERPLTEpqIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRT 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  801 QDNNDKWknrqsadedlttgVGTALYVAPELL--SRRNGVRYDAKVDMYSLGIILFEMCMTFSTSMER--IRIIDTI--- 873
Cdd:cd06643  157 LQRRDSF-------------IGTPYWMAPEVVmcETSKDRPYDYKADVWSLGVTLIEMAQIEPPHHELnpMRVLLKIaks 223
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 63054755  874 RSPSISFPstfpfSRASHEFK-VIHCLLQHDPTKRPSSQELLE 915
Cdd:cd06643  224 EPPTLAQP-----SRWSPEFKdFLRKCLEKNVDARWTTSQLLQ 261
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
562-915 3.52e-16

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: 80.23  E-value: 3.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  562 LGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKEnsrILREVMTLSRLHHEHVVRYYTAWVETEANDTVTEIIssdsesl 641
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVMVMKELKRFDEQRS---FLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYV------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  642 sqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkegssdKDSSIEEassvktqengLN 721
Cdd:cd14065   71 -------------------------------------------------------------NGGTLEE----------LL 79
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  722 ATLYIQMEYCEKLSLQdiirdkipvdemwrlfRQILEALAYIHSRGMMHRDLKPGNIFL---DENRNVKLGDFGLATENE 798
Cdd:cd14065   80 KSMDEQLPWSQRVSLA----------------KDIASGMAYLHSKNIIHRDLNSKNCLVreaNRGRNAVVADFGLAREMP 143
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  799 NYQDNNDKWKNRQSAdedlttgVGTALYVAPELLsrrNGVRYDAKVDMYSLGIILFEM-------------CMTFSTSME 865
Cdd:cd14065  144 DEKTKKPDRKKRLTV-------VGSPYWMAPEML---RGESYDEKVDVFSFGIVLCEIigrvpadpdylprTMDFGLDVR 213
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 63054755  866 RIRIIDTIRSPsisfPSTFPFSrashefkvIHClLQHDPTKRPSSQELLE 915
Cdd:cd14065  214 AFRTLYVPDCP----PSFLPLA--------IRC-CQLDPEKRPSFVELEH 250
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
562-916 3.81e-16

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: 80.27  E-value: 3.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  562 LGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKEN--------SRILREVMTLSRLHHEHVVRYYtawveteandtvtei 633
Cdd:cd06628    8 IGSGSFGSVYLGMNASSGELMAVKQVELPSVSAENkdrkksmlDALQREIALLRELQHENIVQYL--------------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  634 issdseslsqslnmavdfrqSSSLPADKLssldihfeddynssadeedpeasDISFQYSNTSDKEGSSDKDSSIEEAssv 713
Cdd:cd06628   73 --------------------GSSSDANHL-----------------------NIFLEYVPGGSVATLLNNYGAFEES--- 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  714 ktqenglnatlyiqmeyceklslqdIIRDKIpvdemwrlfRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGL 793
Cdd:cd06628  107 -------------------------LVRNFV---------RQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGI 152
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  794 ATENENYQDNNDKWKNRQSADedlttgvGTALYVAPELLSRrngVRYDAKVDMYSLGIILFEMcMTFS------TSMERI 867
Cdd:cd06628  153 SKKLEANSLSTKNNGARPSLQ-------GSVFWMAPEVVKQ---TSYTRKADIWSLGCLVVEM-LTGThpfpdcTQMQAI 221
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 63054755  868 RIIDTIRSPsisfpsTFPFSRASHEFKVIHCLLQHDPTKRPSSQELLES 916
Cdd:cd06628  222 FKIGENASP------TIPSNISSEARDFLEKTFEIDHNKRPTADELLKH 264
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
721-907 4.07e-16

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: 80.91  E-value: 4.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  721 NATLYIQMEYCEKLSLQDIIRDKIPVDEMWRLF--RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATene 798
Cdd:cd14209   73 NSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFyaAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAK--- 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  799 nyqdnndKWKNRQSadedltTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMCMTFS--TSMERIRIIDTIRSP 876
Cdd:cd14209  150 -------RVKGRTW------TLCGTPEYLAPEIILSKG---YNKAVDWWALGVLIYEMAAGYPpfFADQPIQIYEKIVSG 213
                        170       180       190
                 ....*....|....*....|....*....|..
gi 63054755  877 SISFPSTFpfsraSHEFK-VIHCLLQHDPTKR 907
Cdd:cd14209  214 KVRFPSHF-----SSDLKdLLRNLLQVDLTKR 240
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
729-913 4.80e-16

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: 80.00  E-value: 4.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  729 EYCEKLSLQDIIRD---KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQDNND 805
Cdd:cd14221   70 EYIKGGTLRGIIKSmdsHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMVDEKTQPE 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  806 KWKNRQSAD-EDLTTGVGTALYVAPELLsrrNGVRYDAKVDMYSLGIILFEMCMTFSTSMERI-RIID---TIRS----- 875
Cdd:cd14221  150 GLRSLKKPDrKKRYTVVGNPYWMAPEMI---NGRSYDEKVDVFSFGIVLCEIIGRVNADPDYLpRTMDfglNVRGfldry 226
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 63054755  876 -PSISFPSTFPFSrashefkVIHCLLqhDPTKRPSSQEL 913
Cdd:cd14221  227 cPPNCPPSFFPIA-------VLCCDL--DPEKRPSFSKL 256
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
728-915 5.13e-16

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: 79.68  E-value: 5.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  728 MEYCEKLSLQDIIRDKIPVDEMW--RLFRQILEALAYIHSRGMMHRDLKPGNIFL--DENRNVKLGDFGlatenenyqdn 803
Cdd:cd13987   70 QEYAPYGDLFSIIPPQVGLPEERvkRCAAQLASALDFMHSKNLVHRDIKPENVLLfdKDCRRVKLCDFG----------- 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  804 ndkwknrqsadedLTTGVGTAL--------YVAPEL--LSRRNGVRYDAKVDMYSLGIILFeMCMTFSTSMERIRIIDT- 872
Cdd:cd13987  139 -------------LTRRVGSTVkrvsgtipYTAPEVceAKKNEGFVVDPSIDVWAFGVLLF-CCLTGNFPWEKADSDDQf 204
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 63054755  873 -------IRSPSISFPSTF-PFSraSHEFKVIHCLLQHDPTKRPSSQELLE 915
Cdd:cd13987  205 yeefvrwQKRKNTAVPSQWrRFT--PKALRMFKKLLAPEPERRCSIKEVFK 253
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
724-856 5.22e-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: 81.49  E-value: 5.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCeKLSLQDIIRDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenenyqdn 803
Cdd:cd07879   95 FYLVMPYM-QTDLQKIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLA--------- 164
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 63054755  804 ndkwknrQSADEDLTTGVGTALYVAPELLsrRNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd07879  165 -------RHADAEMTGYVVTRWYRAPEVI--LNWMHYNQTVDIWSVGCIMAEM 208
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
554-915 5.37e-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: 80.16  E-value: 5.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  554 TDFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENSRILREV-MTLSRLHHEHVVRYYTA-------WVETE 625
Cdd:cd06617    1 DDLEVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRATVNSQEQKRLLMDLdISMRSVDCPYTVTFYGAlfregdvWICME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  626 ANDTvteiissdseslsqslnmavdfrqssslpadklsSLDIHFEDDYnssadeedpeasdisfqysntsdkegssDKDS 705
Cdd:cd06617   81 VMDT----------------------------------SLDKFYKKVY----------------------------DKGL 98
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  706 SIEEassvktqenglnatlyiqmeyceklslqDIIrDKIPVdemwrlfrQILEALAYIHSR-GMMHRDLKPGNIFLDENR 784
Cdd:cd06617   99 TIPE----------------------------DIL-GKIAV--------SIVKALEYLHSKlSVIHRDVKPSNVLINRNG 141
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  785 NVKLGDFGLATeneNYQDNNDKwknrqsadedlTTGVGTALYVAPELLS-RRNGVRYDAKVDMYSLGIILFEMCM----- 858
Cdd:cd06617  142 QVKLCDFGISG---YLVDSVAK-----------TIDAGCKPYMAPERINpELNQKGYDVKSDVWSLGITMIELATgrfpy 207
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 63054755  859 -TFSTSMERIRIIdtIRSPSISFPSTfPFSRASHEFkvIHCLLQHDPTKRPSSQELLE 915
Cdd:cd06617  208 dSWKTPFQQLKQV--VEEPSPQLPAE-KFSPEFQDF--VNKCLKKNYKERPNYPELLQ 260
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
725-938 5.45e-16

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


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 80.85  E-value: 5.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  725 YIQMEYCEKLSLQDIIRDK--IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGN-IFLDENRN--VKLGDFGLAtenen 799
Cdd:cd14179   78 FLVMELLKGGELLERIKKKqhFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENlLFTDESDNseIKIIDFGFA----- 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  800 yqdnndkwKNRQSADEDLTTGVGTALYVAPELLsRRNGvrYDAKVDMYSLGIILFEM------------CMTFSTSMEri 867
Cdd:cd14179  153 --------RLKPPDNQPLKTPCFTLHYAAPELL-NYNG--YDESCDLWSLGVILYTMlsgqvpfqchdkSLTCTSAEE-- 219
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054755  868 rIIDTIRSPSISFPSTfPFSRASHEFK-VIHCLLQHDPTKRPSSQELLESeaippkvgeEFIQEGLRLLSNP 938
Cdd:cd14179  220 -IMKKIKQGDFSFEGE-AWKNVSQEAKdLIQGLLTVDPNKRIKMSGLRYN---------EWLQDGSQLSSNP 280
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
724-915 5.49e-16

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: 79.69  E-value: 5.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDKIPVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIF---LDENRNVKLGDFGLAtene 798
Cdd:cd14167   76 LYLIMQLVSGGELFDRIVEKGFYTErdASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLS---- 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  799 nyqdnndKWKNRQSAdedLTTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMCMTFSTSMER--IRIIDTIRSP 876
Cdd:cd14167  152 -------KIEGSGSV---MSTACGTPGYVAPEVLAQKP---YSKAVDCWSIGVIAYILLCGYPPFYDEndAKLFEQILKA 218
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 63054755  877 SISFPSTF--PFSRASHEFkvIHCLLQHDPTKRPSSQELLE 915
Cdd:cd14167  219 EYEFDSPYwdDISDSAKDF--IQHLMEKDPEKRFTCEQALQ 257
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
724-912 5.91e-16

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


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 80.89  E-value: 5.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDKIPVDEMWRLF--RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENyq 801
Cdd:cd05592   71 LFFVMEYLNGGDLMFHIQQSGRFDEDRARFygAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIY-- 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  802 dnndkwknrqsADEDLTTGVGTALYVAPELLSrrnGVRYDAKVDMYSLGIILFEMCM---TFSTSMERiRIIDTIRSPSI 878
Cdd:cd05592  149 -----------GENKASTFCGTPDYIAPEILK---GQKYNQSVDWWSFGVLLYEMLIgqsPFHGEDED-ELFWSICNDTP 213
                        170       180       190
                 ....*....|....*....|....*....|....
gi 63054755  879 SFPSTFPFSRAShefkVIHCLLQHDPTKRPSSQE 912
Cdd:cd05592  214 HYPRWLTKEAAS----CLSLLLERNPEKRLGVPE 243
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
755-907 6.10e-16

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 81.02  E-value: 6.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenenyqdnndkwknrQSADEDLTTGVGTALYVAPELLSR 834
Cdd:PTZ00263  126 ELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFA----------------KKVPDRTFTLCGTPEYLAPEVIQS 189
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63054755   835 RNgvrYDAKVDMYSLGIILFEMCMTFSTSMER--IRIIDTIRSPSISFPSTFPfSRAShefKVIHCLLQHDPTKR 907
Cdd:PTZ00263  190 KG---HGKAVDWWTMGVLLYEFIAGYPPFFDDtpFRIYEKILAGRLKFPNWFD-GRAR---DLVKGLLQTDHTKR 257
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
721-913 6.59e-16

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: 79.26  E-value: 6.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  721 NATLYIQMEYCEKLSLQDIIRDKIPVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFLdENRNVKLGDFGLATENE 798
Cdd:cd14163   73 DGKIYLVMELAEDGDVFDCVLHGGPLPEhrAKALFRQLVEAIRYCHGCGVAHRDLKCENALL-QGFTLKLTDFGFAKQLP 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  799 nyqdnndkwKNRQSADEdltTGVGTALYVAPELLsrrNGVRYDA-KVDMYSLGIILFEM-CMTFSTSMERIRIIDTIRSP 876
Cdd:cd14163  152 ---------KGGRELSQ---TFCGSTAYAAPEVL---QGVPHDSrKGDIWSMGVVLYVMlCAQLPFDDTDIPKMLCQQQK 216
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 63054755  877 SISFPSTFPFSRASHEfkVIHCLLQHDPTKRPSSQEL 913
Cdd:cd14163  217 GVSLPGHLGVSRTCQD--LLKRLLEPDMVLRPSIEEV 251
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
724-915 7.21e-16

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: 79.70  E-value: 7.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDKIPVDEMWRLF--RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEnenyq 801
Cdd:cd06645   83 LWICMEFCGGGSLQDIYHVTGPLSESQIAYvsRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQ----- 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  802 dNNDKWKNRQSAdedlttgVGTALYVAPELLSRRNGVRYDAKVDMYSLGIILFEMCMTFST--SMERIRIIDTIRSPSIS 879
Cdd:cd06645  158 -ITATIAKRKSF-------IGTPYWMAPEVAAVERKGGYNQLCDIWAVGITAIELAELQPPmfDLHPMRALFLMTKSNFQ 229
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 63054755  880 FPS---TFPFSRASHEFkvIHCLLQHDPTKRPSSQELLE 915
Cdd:cd06645  230 PPKlkdKMKWSNSFHHF--VKMALTKNPKKRPTAEKLLQ 266
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
713-919 7.29e-16

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: 79.67  E-value: 7.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  713 VKTQENGLNATLYIQMEYCEKLSLQDIIR----DKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKL 788
Cdd:cd06636   83 IKKSPPGHDDQLWLVMEFCGAGSVTDLVKntkgNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKL 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  789 GDFGLATEnenyqdnNDKWKNRQSadedltTGVGTALYVAPELLS--RRNGVRYDAKVDMYSLGIILFEMCMTFS--TSM 864
Cdd:cd06636  163 VDFGVSAQ-------LDRTVGRRN------TFIGTPYWMAPEVIAcdENPDATYDYRSDIWSLGITAIEMAEGAPplCDM 229
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 63054755  865 ERIRIIDTI-RSPsisfPSTFPFSRASHEFK--VIHCLLQHDPtKRPSSQELLESEAI 919
Cdd:cd06636  230 HPMRALFLIpRNP----PPKLKSKKWSKKFIdfIEGCLVKNYL-SRPSTEQLLKHPFI 282
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
718-858 8.32e-16

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: 79.79  E-value: 8.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  718 NGLNATLYIQMEYCEKLSLQDII-RDKIPVDEMWRLFRQILEALAYIHSR---------GMMHRDLKPGNIFLDENRNVK 787
Cdd:cd13998   62 TALRTELWLVTAFHPNGSL*DYLsLHTIDWVSLCRLALSVARGLAHLHSEipgctqgkpAIAHRDLKSKNILVKNDGTCC 141
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63054755  788 LGDFGLATENENYQDNNDKWKNRQsadedlttgVGTALYVAPELL-SRRNGVRYDA--KVDMYSLGIILFEMCM 858
Cdd:cd13998  142 IADFGLAVRLSPSTGEEDNANNGQ---------VGTKRYMAPEVLeGAINLRDFESfkRVDIYAMGLVLWEMAS 206
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
739-914 8.54e-16

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: 80.94  E-value: 8.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  739 IIRDKIPVDEMWRLF-RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATenenyqdnndKWKNRQSadEDL 817
Cdd:cd07853   94 IVSPQPLSSDHVKVFlYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLAR----------VEEPDES--KHM 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  818 TTGVGTALYVAPELL--SRrngvRYDAKVDMYSLGIILFEMC---MTFSTS--MERIR-IIDTIRSPSI----------- 878
Cdd:cd07853  162 TQEVVTQYYRAPEILmgSR----HYTSAVDIWSVGCIFAELLgrrILFQAQspIQQLDlITDLLGTPSLeamrsacegar 237
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 63054755  879 -----------SFPSTFPFS-RASHE-FKVIHCLLQHDPTKRPSSQELL 914
Cdd:cd07853  238 ahilrgphkppSLPVLYTLSsQATHEaVHLLCRMLVFDPDKRISAADAL 286
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
556-873 8.66e-16

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: 80.59  E-value: 8.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  556 FEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLlSDDKENSRILREVMTLSRLHHEHVVRYYtawveteandtvteiis 635
Cdd:cd07854    7 YMDLRPLGCGSNGLVFSAVDSDCDKRVAVKKIVL-TDPQSVKHALREIKIIRRLDHDNIVKVY----------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  636 sdseslsqslnmavdfrqssslpaDKLSSldihfeddynssadeedpeasdisfqysntsdkeGSSDKDSSIEEASSVkt 715
Cdd:cd07854   69 ------------------------EVLGP----------------------------------SGSDLTEDVGSLTEL-- 88
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  716 qenglnATLYIQMEYCEKlSLQDIIRDKIPVDEMWRLFR-QILEALAYIHSRGMMHRDLKPGNIFLD-ENRNVKLGDFGL 793
Cdd:cd07854   89 ------NSVYIVQEYMET-DLANVLEQGPLSEEHARLFMyQLLRGLKYIHSANVLHRDLKPANVFINtEDLVLKIGDFGL 161
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  794 A-TENENYqdnndkwknrqSADEDLTTGVGTALYVAPE-LLSRRNgvrYDAKVDMYSLGIILFEMC---MTFSTS--MER 866
Cdd:cd07854  162 ArIVDPHY-----------SHKGYLSEGLVTKWYRSPRlLLSPNN---YTKAIDMWAAGCIFAEMLtgkPLFAGAheLEQ 227

                 ....*...
gi 63054755  867 IR-IIDTI 873
Cdd:cd07854  228 MQlILESV 235
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
751-856 8.71e-16

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 79.45  E-value: 8.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  751 RLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAteNENYQDNNDKWKnrqsadedltTGVGTALYVAPE 830
Cdd:cd14076  110 RLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFA--NTFDHFNGDLMS----------TSCGSPCYAAPE 177
                         90       100
                 ....*....|....*....|....*..
gi 63054755  831 LLSRRNGvrYDA-KVDMYSLGIILFEM 856
Cdd:cd14076  178 LVVSDSM--YAGrKADIWSCGVILYAM 202
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
268-507 8.95e-16

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: 79.12  E-value: 8.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  268 LRTVRISTPYWSTEDGKREIQE-LEYELESLKVIRHDllaSIYEYQLERETRGYgwrLYVLQEYSPKFTLFSLLQTVLTL 346
Cdd:cd06628   30 VKQVELPSVSAENKDRKKSMLDaLQREIALLRELQHE---NIVQYLGSSSDANH---LNIFLEYVPGGSVATLLNNYGAF 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  347 DVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDMNASHPFNINSQSItnilpEG- 425
Cdd:cd06628  104 EESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGG---IKISDFGISKKLEANSLSTKNNGARPSL-----QGs 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  426 ---LYPPEVSESSFaaaSRKTDIWCFGLLVLQMLCGAHVLNKFSSLKLIM---THVIPLLPG----SYQDLVRRCLMRDS 495
Cdd:cd06628  176 vfwMAPEVVKQTSY---TRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIFkigENASPTIPSnissEARDFLEKTFEIDH 252
                        250
                 ....*....|..
gi 63054755  496 RKRPSAIDLLSS 507
Cdd:cd06628  253 NKRPTADELLKH 264
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
721-907 1.10e-15

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


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 80.05  E-value: 1.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  721 NATLYIQMEYC---EKLSLQDIiRDKIPVDEMWRLF-RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATe 796
Cdd:cd05601   73 SENLYLVMEYHpggDLLSLLSR-YDDIFEESMARFYlAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAA- 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  797 nenyqdnndkwknRQSADEDLTTG--VGTALYVAPELLSRRNGVR---YDAKVDMYSLGIILFEMC-----MTFSTSMER 866
Cdd:cd05601  151 -------------KLSSDKTVTSKmpVGTPDYIAPEVLTSMNGGSkgtYGVECDWWSLGIVAYEMLygktpFTEDTVIKT 217
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 63054755  867 I-RIIDTIRspSISFPSTFpfsRASHEFK-VIHCLLQhDPTKR 907
Cdd:cd05601  218 YsNIMNFKK--FLKFPEDP---KVSESAVdLIKGLLT-DAKER 254
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
755-856 1.11e-15

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: 80.43  E-value: 1.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQDNNDKwknrqsadedLTTGVGTALYVAPELLSR 834
Cdd:cd07849  114 QILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARIADPEHDHTGF----------LTEYVATRWYRAPEIMLN 183
                         90       100
                 ....*....|....*....|..
gi 63054755  835 RNGvrYDAKVDMYSLGIILFEM 856
Cdd:cd07849  184 SKG--YTKAIDIWSVGCILAEM 203
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
755-921 1.17e-15

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: 79.92  E-value: 1.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenenyqdnndkwknrQSADEDLTTGVGTALYVAPE-LLS 833
Cdd:cd07856  116 QILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLA----------------RIQDPQMTGYVSTRYYRAPEiMLT 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  834 RRngvRYDAKVDMYSLGIILFEMCM------------TFSTSMERI-----RIIDTIRSP-SISFPSTFPFSRA---SHE 892
Cdd:cd07856  180 WQ---KYDVEVDIWSAGCIFAEMLEgkplfpgkdhvnQFSIITELLgtppdDVINTICSEnTLRFVQSLPKRERvpfSEK 256
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 63054755  893 FK--------VIHCLLQHDPTKRPSSQELLESEAIPP 921
Cdd:cd07856  257 FKnadpdaidLLEKMLVFDPKKRISAAEALAHPYLAP 293
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
736-856 1.33e-15

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: 80.08  E-value: 1.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  736 LQDIIR-DKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenenyqdnndkwknRQSAD 814
Cdd:cd07877  108 LNNIVKcQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLA---------------RHTDD 172
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 63054755  815 EdLTTGVGTALYVAPELLsrRNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd07877  173 E-MTGYVATRWYRAPEIM--LNWMHYNQTVDIWSVGCIMAEL 211
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
755-907 1.34e-15

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: 79.02  E-value: 1.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATenenyqdnnDKWKNRQSAdedlttGVGTALYVAPELLSR 834
Cdd:cd05606  106 EVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLAC---------DFSKKKPHA------SVGTHGYMAPEVLQK 170
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  835 rnGVRYDAKVDMYSLGIILFEMCMTFS-----TSMERIRIIDTIRSPSISFPSTFpfsraSHEFK-VIHCLLQHDPTKR 907
Cdd:cd05606  171 --GVAYDSSADWFSLGCMLYKLLKGHSpfrqhKTKDKHEIDRMTLTMNVELPDSF-----SPELKsLLEGLLQRDVSKR 242
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
736-915 1.34e-15

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: 78.86  E-value: 1.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  736 LQDIIRDKIPVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENEnyqdnndkwknrqsA 813
Cdd:cd14181  103 LFDYLTEKVTLSEkeTRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHLE--------------P 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  814 DEDLTTGVGTALYVAPELLS---RRNGVRYDAKVDMYSLGIILFEMCMTFSTSMER--IRIIDTIRSPSISFPSTFPFSR 888
Cdd:cd14181  169 GEKLRELCGTPGYLAPEILKcsmDETHPGYGKEVDLWACGVILFTLLAGSPPFWHRrqMLMLRMIMEGRYQFSSPEWDDR 248
                        170       180
                 ....*....|....*....|....*..
gi 63054755  889 ASHEFKVIHCLLQHDPTKRPSSQELLE 915
Cdd:cd14181  249 SSTVKDLISRLLVVDPEIRLTAEQALQ 275
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
696-852 1.46e-15

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


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 78.57  E-value: 1.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  696 DKEGSSDKDSSIEEASSVKTQENGLN-----------ATLYIQMEYCEKLSLQDIIRDKIPVDE--MWRLFRQILEALAY 762
Cdd:cd14083   37 DKKALKGKEDSLENEIAVLRKIKHPNivqlldiyeskSHLYLVMELVTGGELFDRIVEKGSYTEkdASHLIRQVLEAVDY 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  763 IHSRGMMHRDLKPGNIF---LDENRNVKLGDFGLA-TENEnyqdnndkwknrqsadEDLTTGVGTALYVAPELLSRRNgv 838
Cdd:cd14083  117 LHSLGIVHRDLKPENLLyysPDEDSKIMISDFGLSkMEDS----------------GVMSTACGTPGYVAPEVLAQKP-- 178
                        170
                 ....*....|....
gi 63054755  839 rYDAKVDMYSLGII 852
Cdd:cd14083  179 -YGKAVDCWSIGVI 191
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
742-856 1.50e-15

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: 80.00  E-value: 1.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  742 DKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenenyqdnndkwknRQsADEDLTTGV 821
Cdd:cd07880  113 EKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLA---------------RQ-TDSEMTGYV 176
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 63054755  822 GTALYVAPELLsrRNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd07880  177 VTRWYRAPEVI--LNWMHYTQTVDIWSVGCIMAEM 209
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
290-506 1.54e-15

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: 78.58  E-value: 1.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  290 LEYELESLKVIRHDllaSIYEYQLERETRGYgwrLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLG 369
Cdd:cd06629   55 LKSEIDTLKDLDHP---NIVQYLGFEETEDY---FSIFLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKG 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  370 ISHKSLHLDNVVLFHSGhrtFAKLMDFGFTRTLRDMNASHPFNINSQSITNIlpeglyPPEVSESSFAAASRKTDIWCFG 449
Cdd:cd06629  129 ILHRDLKADNILVDLEG---ICKISDFGISKKSDDIYGNNGATSMQGSVFWM------APEVIHSQGQGYSAKVDIWSLG 199
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  450 LLVLQMLCGAHVLNKFSSLKLIM----THVIPLLPGSYQ------DLVRRCLMRDSRKRPSAIDLLS 506
Cdd:cd06629  200 CVVLEMLAGRRPWSDDEAIAAMFklgnKRSAPPVPEDVNlspealDFLNACFAIDPRDRPTAAELLS 266
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
728-855 1.57e-15

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: 78.60  E-value: 1.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  728 MEYCEKLSLQDIIRD--KIPVDeMWRL-FRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLA-------TEN 797
Cdd:cd05609   79 MEYVEGGDCATLLKNigPLPVD-MARMyFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSkiglmslTTN 157
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 63054755  798 EnYQDNNDKwKNRQSADEDLttgVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFE 855
Cdd:cd05609  158 L-YEGHIEK-DTREFLDKQV---CGTPEYIAPEVILRQG---YGKPVDWWAMGIILYE 207
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
725-915 1.59e-15

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: 78.20  E-value: 1.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  725 YIQME-YCEKLSLQDIIRDKIPVDEMW--RLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENEnyq 801
Cdd:cd14004   84 YLVMEkHGSGMDLFDFIERKPNMDEKEakYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSAAYIK--- 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  802 dnNDKWknrqsadedlTTGVGTALYVAPELLSrrnGVRYDAK-VDMYSLGIILFEMCMTFSTSMEririIDTIRSPSISF 880
Cdd:cd14004  161 --SGPF----------DTFVGTIDYAAPEVLR---GNPYGGKeQDIWALGVLLYTLVFKENPFYN----IEEILEADLRI 221
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 63054755  881 PstFPFSRASHEFkvIHCLLQHDPTKRPSSQELLE 915
Cdd:cd14004  222 P--YAVSEDLIDL--ISRMLNRDVGDRPTIEELLT 252
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
284-505 1.76e-15

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: 78.01  E-value: 1.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  284 KREIQELEYELESLKVIRHDLLASIYEYQLERETrgygwrLYVLQEYSPKFTLFSLLQ-TVLTLDVETVRAFSNNILEGL 362
Cdd:cd05122   38 KEKKESILNEIAILKKCKHPNIVKYYGSYLKKDE------LWIVMEFCSGGSLKDLLKnTNKTLTEQQIAYVCKEVLKGL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  363 AELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDMNASHPFnINSqsitnilpegLY--PPEV-SESSFaaa 439
Cdd:cd05122  112 EYLHSHGIIHRDIKAANILLTSDGE---VKLIDFGLSAQLSDGKTRNTF-VGT----------PYwmAPEViQGKPY--- 174
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63054755  440 SRKTDIWCFGLLVLQMLCGA---HVLNKFSSLKLIMTHVIPLLPGSY------QDLVRRCLMRDSRKRPSAIDLL 505
Cdd:cd05122  175 GFKADIWSLGITAIEMAEGKppySELPPMKALFLIATNGPPGLRNPKkwskefKDFLKKCLQKDPEKRPTAEQLL 249
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
755-881 1.83e-15

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: 79.37  E-value: 1.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenenyqdnndkwKNRQSADEDLTTGVGTALYVAPELLSR 834
Cdd:cd05584  108 EITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLC-------------KESIHDGTVTHTFCGTIEYMAPEILTR 174
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 63054755  835 RNgvrYDAKVDMYSLGIILFEMcMTFS---TSMERIRIIDTIRSPSISFP 881
Cdd:cd05584  175 SG---HGKAVDWWSLGALMYDM-LTGAppfTAENRKKTIDKILKGKLNLP 220
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
748-856 2.09e-15

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: 78.61  E-value: 2.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  748 EMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRN---VKLGDFGLATeneNYQDNNDkwKNRQSADEDLTTGVGTA 824
Cdd:cd14090  101 EASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKvspVKICDFDLGS---GIKLSST--SMTPVTTPELLTPVGSA 175
                         90       100       110
                 ....*....|....*....|....*....|....
gi 63054755  825 LYVAPELLSRRNG--VRYDAKVDMYSLGIILFEM 856
Cdd:cd14090  176 EYMAPEVVDAFVGeaLSYDKRCDLWSLGVILYIM 209
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
729-856 2.31e-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: 78.20  E-value: 2.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  729 EYCEKLSLQDIIRDK-IPVDEMWR--LFRQILEALAYIH-SRGMMHRDLKPGNIFLDENRNVKLGDFGLA---TENENYQ 801
Cdd:cd13992   76 EYCTRGSLQDVLLNReIKMDWMFKssFIKDIVKGMNYLHsSSIGYHGRLKSSNCLVDSRWVVKLTDFGLRnllEEQTNHQ 155
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  802 DNNDKWKNRQsadedlttgvgtaLYVAPELLS-RRNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd13992  156 LDEDAQHKKL-------------LWTAPELLRgSLLEVRGTQKGDVYSFAIILYEI 198
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
755-856 2.54e-15

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: 78.90  E-value: 2.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQDNNdkwknrqsadedlTTGVGTALYVAPELLSR 834
Cdd:cd05575  104 EIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEPSDTT-------------STFCGTPEYLAPEVLRK 170
                         90       100
                 ....*....|....*....|..
gi 63054755  835 RNgvrYDAKVDMYSLGIILFEM 856
Cdd:cd05575  171 QP---YDRTVDWWCLGAVLYEM 189
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
724-915 3.38e-15

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: 78.22  E-value: 3.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDKIpVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQ 801
Cdd:cd06656   91 LWVVMEYLAGGSLTDVVTETC-MDEgqIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQ 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  802 DNNdkwknrqsadedlTTGVGTALYVAPELLSRRngvRYDAKVDMYSLGIILFEMC-----MTFSTSMERIRIIDTIRSP 876
Cdd:cd06656  170 SKR-------------STMVGTPYWMAPEVVTRK---AYGPKVDIWSLGIMAIEMVegeppYLNENPLRALYLIATNGTP 233
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 63054755  877 SISFPstfpfSRASHEFK-VIHCLLQHDPTKRPSSQELLE 915
Cdd:cd06656  234 ELQNP-----ERLSAVFRdFLNRCLEMDVDRRGSAKELLQ 268
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
724-907 3.68e-15

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: 78.45  E-value: 3.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDKIPVDemwrLFR------QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEN 797
Cdd:cd05620   71 LFFVMEFLNGGDLMFHIQDKGRFD----LYRatfyaaEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKEN 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  798 EnYQDNNdkwknrqsadedLTTGVGTALYVAPELLsrrNGVRYDAKVDMYSLGIILFEMCMTFST--SMERIRIIDTIRS 875
Cdd:cd05620  147 V-FGDNR------------ASTFCGTPDYIAPEIL---QGLKYTFSVDWWSFGVLLYEMLIGQSPfhGDDEDELFESIRV 210
                        170       180       190
                 ....*....|....*....|....*....|..
gi 63054755  876 PSISFPSTfpFSRASHEfkVIHCLLQHDPTKR 907
Cdd:cd05620  211 DTPHYPRW--ITKESKD--ILEKLFERDPTRR 238
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
741-921 3.78e-15

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


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 78.51  E-value: 3.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  741 RDKIPVDEMWRLF-RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENenyqdnndkwknrQSADEDLTT 819
Cdd:cd05595   88 RERVFTEDRARFYgAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEG-------------ITDGATMKT 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  820 GVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFE-MC--MTFsTSMERIRIIDTIRSPSISFPSTFpfsrASHEFKVI 896
Cdd:cd05595  155 FCGTPEYLAPEVLEDND---YGRAVDWWGLGVVMYEmMCgrLPF-YNQDHERLFELILMEEIRFPRTL----SPEAKSLL 226
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 63054755  897 HCLLQHDPTKR----PSS---------------QELLESEAIPP 921
Cdd:cd05595  227 AGLLKKDPKQRlgggPSDakevmehrfflsinwQDVVQKKLLPP 270
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
282-505 4.21e-15

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: 77.06  E-value: 4.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  282 DGKREIQELEYELESLKVIRHdllASIYEYqleRETRGYGWRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEG 361
Cdd:cd06632   41 KSRESVKQLEQEIALLSKLRH---PNIVQY---YGTEREEDNLYIFLEYVPGGSIHKLLQRYGAFEEPVIRLYTRQILSG 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  362 LAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLrdMNASHPFNINSqSITNILPEGLyPPEVSESSFAAasr 441
Cdd:cd06632  115 LAYLHSRNTVHRDIKGANILVDTNGV---VKLADFGMAKHV--EAFSFAKSFKG-SPYWMAPEVI-MQKNSGYGLAV--- 184
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054755  442 ktDIWCFGLLVLQMLCGAHVLNKFSSL----KLIMTHVIPLLPGSY----QDLVRRCLMRDSRKRPSAIDLL 505
Cdd:cd06632  185 --DIWSLGCTVLEMATGKPPWSQYEGVaaifKIGNSGELPPIPDHLspdaKDFIRLCLQRDPEDRPTASQLL 254
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
724-917 4.23e-15

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: 77.84  E-value: 4.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDKIpVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQ 801
Cdd:cd06654   92 LWVVMEYLAGGSLTDVVTETC-MDEgqIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQ 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  802 DNNdkwknrqsadedlTTGVGTALYVAPELLSRRngvRYDAKVDMYSLGIILFEMC-----MTFSTSMERIRIIDTIRSP 876
Cdd:cd06654  171 SKR-------------STMVGTPYWMAPEVVTRK---AYGPKVDIWSLGIMAIEMIegeppYLNENPLRALYLIATNGTP 234
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 63054755  877 SISFPSTfpFSRASHEFkvIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd06654  235 ELQNPEK--LSAIFRDF--LNRCLEMDVEKRGSAKELLQHQ 271
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
562-908 4.42e-15

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: 77.76  E-value: 4.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  562 LGRGGFGEVVKVKNRIDGRFYAVKKLVL--LSDDKENSRILREVMTLSRLHHEHVVRYYTAWVETEANDTVTEIISsdse 639
Cdd:cd08229   32 IGRGQFSEVYRATCLLDGVPVALKKVQIfdLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELAD---- 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  640 slsqslnmavdfrqssslpADKLSSLDIHFEDDynssadeedpeasdisfqysntsdkegssdkdssieeassvktqeng 719
Cdd:cd08229  108 -------------------AGDLSRMIKHFKKQ----------------------------------------------- 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  720 lnatlyiqmeyceklslqdiiRDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATenen 799
Cdd:cd08229  122 ---------------------KRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGR---- 176
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  800 yqdnndKWKNRQSADEDLttgVGTALYVAPELLsRRNGvrYDAKVDMYSLGIILFEMCMT----FSTSMERIRIIDTIRs 875
Cdd:cd08229  177 ------FFSSKTTAAHSL---VGTPYYMSPERI-HENG--YNFKSDIWSLGCLLYEMAALqspfYGDKMNLYSLCKKIE- 243
                        330       340       350
                 ....*....|....*....|....*....|....
gi 63054755  876 pSISFPStFPFSRASHEF-KVIHCLLQHDPTKRP 908
Cdd:cd08229  244 -QCDYPP-LPSDHYSEELrQLVNMCINPDPEKRP 275
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
697-916 4.54e-15

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: 76.72  E-value: 4.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  697 KEGSSDKDSSIEEASSV-KTQENGL---------NATLYIQMEYCEKLSLQDIIRDKIPVDEMWRLF---RQILEALAYI 763
Cdd:cd05059   37 KEGSMSEDDFIEEAKVMmKLSHPKLvqlygvctkQRPIFIVTEYMANGCLLNYLRERRGKFQTEQLLemcKDVCEAMEYL 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  764 HSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenenyqdnndkwknRQSADEDLTTGVGTALYV---APELLSRRngvRY 840
Cdd:cd05059  117 ESNGFIHRDLAARNCLVGEQNVVKVSDFGLA---------------RYVLDDEYTSSVGTKFPVkwsPPEVFMYS---KF 178
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  841 DAKVDMYSLGIILFEMCMTFSTSMERIRIIDTIRSPSISFPSTFPFSRASHEFKVIHCLLQHDPTKRPSSQELLES 916
Cdd:cd05059  179 SSKSDVWSFGVLMWEVFSEGKMPYERFSNSEVVEHISQGYRLYRPHLAPTEVYTIMYSCWHEKPEERPTFKILLSQ 254
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
755-907 5.07e-15

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: 77.05  E-value: 5.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATE---NENYQDNndkwknrqsadedltTGVGTALYVAPEL 831
Cdd:cd05583  107 EIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEflpGENDRAY---------------SFCGTIEYMAPEV 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  832 LsRRNGVRYDAKVDMYSLGIILFEM---CMTFSTSMERI---RIIDTIRSPSISFPSTfpFSRASHEFkvIHCLLQHDPT 905
Cdd:cd05583  172 V-RGGSDGHDKAVDWWSLGVLTYELltgASPFTVDGERNsqsEISKRILKSHPPIPKT--FSAEAKDF--ILKLLEKDPK 246

                 ..
gi 63054755  906 KR 907
Cdd:cd05583  247 KR 248
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
710-915 6.29e-15

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: 77.16  E-value: 6.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  710 ASSVKTQENGLNATLY-IQMEYCEKlSLQDIIR---DKIPV--DEMWRLFRQILEALAYIHSRG--MMHRDLKPGNIFLD 781
Cdd:cd14036   66 AASIGKEESDQGQAEYlLLTELCKG-QLVDFVKkveAPGPFspDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIG 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  782 ENRNVKLGDFGLATENENYQDNNdkWK-NRQSADEDLTTGVGTALYVAPELLSRRNGVRYDAKVDMYSLGIILFEMCMT- 859
Cdd:cd14036  145 NQGQIKLCDFGSATTEAHYPDYS--WSaQKRSLVEDEITRNTTPMYRTPEMIDLYSNYPIGEKQDIWALGCILYLLCFRk 222
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054755  860 --FSTSmERIRIIDtirspsisfpSTFPFSRASHEFKVIHCL----LQHDPTKRPSSQELLE 915
Cdd:cd14036  223 hpFEDG-AKLRIIN----------AKYTIPPNDTQYTVFHDLirstLKVNPEERLSITEIVE 273
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
728-915 7.45e-15

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: 76.62  E-value: 7.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  728 MEYCEKLSLQDII--RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFL---DENRNVKLGDFGLAtenenyqd 802
Cdd:cd14106   87 LELAAGGELQTLLdeEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLtseFPLGDIKLCDFGIS-------- 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  803 nndkwkNRQSADEDLTTGVGTALYVAPELLSrrngvrYDA---KVDMYSLGIILFEMCMTFS-----TSMERIRiidTIR 874
Cdd:cd14106  159 ------RVIGEGEEIREILGTPDYVAPEILS------YEPislATDMWSIGVLTYVLLTGHSpfggdDKQETFL---NIS 223
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 63054755  875 SPSISFPSTFPFSRASHEFKVIHCLLQHDPTKRPSSQELLE 915
Cdd:cd14106  224 QCNLDFPEELFKDVSPLAIDFIKRLLVKDPEKRLTAKECLE 264
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
726-855 8.00e-15

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: 76.34  E-value: 8.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  726 IQMEYCEK---LSLQDIIRDKIPVDEMWRLFRQILEALAYIH--SRGMMHRDLKPGNIFLDENRNVKLGDFGLAteneny 800
Cdd:cd13978   69 LVMEYMENgslKSLLEREIQDVPWSLRFRIIHEIALGMNFLHnmDPPLLHHDLKPENILLDNHFHVKISDFGLS------ 142
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 63054755  801 qdnndKWKNR-QSADEDLTTG--VGTALYVAPELLSRRNGvRYDAKVDMYSLGIILFE 855
Cdd:cd13978  143 -----KLGMKsISANRRRGTEnlGGTPIYMAPEAFDDFNK-KPTSKSDVYSFAIVIWA 194
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
755-915 9.17e-15

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: 76.15  E-value: 9.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATenenyqdnndkwknrQSADEDLTTGVGTALYVAPELLSr 834
Cdd:cd14116  113 ELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSV---------------HAPSSRRTTLCGTLDYLPPEMIE- 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  835 rnGVRYDAKVDMYSLGIILFEMCM---TFSTSMERiriiDTIRSPS-ISFpsTFPFSRASHEFKVIHCLLQHDPTKRPSS 910
Cdd:cd14116  177 --GRMHDEKVDLWSLGVLCYEFLVgkpPFEANTYQ----ETYKRISrVEF--TFPDFVTEGARDLISRLLKHNPSQRPML 248

                 ....*
gi 63054755  911 QELLE 915
Cdd:cd14116  249 REVLE 253
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
724-915 9.48e-15

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 76.69  E-value: 9.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDKIpVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQ 801
Cdd:cd06655   91 LFVVMEYLAGGSLTDVVTETC-MDEaqIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQ 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  802 DNNdkwknrqsadedlTTGVGTALYVAPELLSRRngvRYDAKVDMYSLGIILFEMC-----MTFSTSMERIRIIDTIRSP 876
Cdd:cd06655  170 SKR-------------STMVGTPYWMAPEVVTRK---AYGPKVDIWSLGIMAIEMVegeppYLNENPLRALYLIATNGTP 233
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 63054755  877 SISFPSTF-PFSRashefKVIHCLLQHDPTKRPSSQELLE 915
Cdd:cd06655  234 ELQNPEKLsPIFR-----DFLNRCLEMDVEKRGSAKELLQ 268
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
751-915 1.12e-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: 75.77  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  751 RLFRQILEALAYIHSRGMMHRDLKPGNIFLDENR--NVKLGDFGLATEnenyqdnndkwknrqSADEdLTTGVGTALYVA 828
Cdd:cd14133  106 KIAQQILEALVFLHSLGLIHCDLKPENILLASYSrcQIKIIDFGSSCF---------------LTQR-LYSYIQSRYYRA 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  829 PELLSrrnGVRYDAKVDMYSLGIILFEMCM---TFS--TSMERI-RIIDTIRSPSISFPSTFPFSRAshEF-KVIHCLLQ 901
Cdd:cd14133  170 PEVIL---GLPYDEKIDMWSLGCILAELYTgepLFPgaSEVDQLaRIIGTIGIPPAHMLDQGKADDE--LFvDFLKKLLE 244
                        170
                 ....*....|....
gi 63054755  902 HDPTKRPSSQELLE 915
Cdd:cd14133  245 IDPKERPTASQALS 258
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
562-915 1.14e-14

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: 76.16  E-value: 1.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  562 LGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENSRILREVMTLSRL-HHEHVVRYytawveteandtvteiissdses 640
Cdd:cd07831    7 IGEGTFSEVLKAQSRKTGKYYAIKCMKKHFKSLEQVNNLREIQALRRLsPHPNILRL----------------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  641 lsqslnmavdfrqssslpadklssLDIHFEDdynssadeedpeasdisfqysntsdkegssdkdssieeassvktqengL 720
Cdd:cd07831   64 ------------------------IEVLFDR------------------------------------------------K 71
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  721 NATLYIQMEYCEkLSLQDIIRD-KIPVDEM--WRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENrNVKLGDFGLAten 797
Cdd:cd07831   72 TGRLALVFELMD-MNLYELIKGrKRPLPEKrvKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD-ILKLADFGSC--- 146
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  798 enyqdnndkwknRQSADED-LTTGVGTALYVAPE-LLSrrNGvRYDAKVDMYSLGIILFEMCMTF-----STSMERI-RI 869
Cdd:cd07831  147 ------------RGIYSKPpYTEYISTRWYRAPEcLLT--DG-YYGPKMDIWAVGCVFFEILSLFplfpgTNELDQIaKI 211
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  870 IDTIRSPSISF-----PST-----FPFSR----------ASHEF-KVIHCLLQHDPTKRPSSQELLE 915
Cdd:cd07831  212 HDVLGTPDAEVlkkfrKSRhmnynFPSKKgtglrkllpnASAEGlDLLKKLLAYDPDERITAKQALR 278
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
724-907 1.28e-14

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: 76.32  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDKIPVDEMWRLF--RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENenyq 801
Cdd:cd05612   76 LYMLMEYVPGGELFSYLRNSGRFSNSTGLFyaSEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKL---- 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  802 dNNDKWknrqsadedltTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMCMTFSTSMER--IRIIDTIRSPSIS 879
Cdd:cd05612  152 -RDRTW-----------TLCGTPEYLAPEVIQSKG---HNKAVDWWALGILIYEMLVGYPPFFDDnpFGIYEKILAGKLE 216
                        170       180
                 ....*....|....*....|....*...
gi 63054755  880 FPSTFPFsrasHEFKVIHCLLQHDPTKR 907
Cdd:cd05612  217 FPRHLDL----YAKDLIKKLLVVDRTRR 240
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
741-913 1.32e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 77.73  E-value: 1.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   741 RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLA------TENENYqdnndKWknrqsad 814
Cdd:PHA03212  176 KRNIAICDILAIERSVLRAIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGAAcfpvdiNANKYY-----GW------- 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   815 edlttgVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMCMTFSTSMERI---------RIIDTIRSPSISFPSTFP 885
Cdd:PHA03212  244 ------AGTIATNAPELLARDP---YGPAVDIWSAGIVLFEMATCHDSLFEKDgldgdcdsdRQIKLIIRRSGTHPNEFP 314
                         170       180
                  ....*....|....*....|....*...
gi 63054755   886 FSrASHEFKVIHCLLQHDPTKRPSSQEL 913
Cdd:PHA03212  315 ID-AQANLDEIYIGLAKKSSRKPGSRPL 341
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
726-914 1.39e-14

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: 75.22  E-value: 1.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  726 IQMEYCEKLSLQDIIRD--KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEnenYQDN 803
Cdd:cd14059   58 ILMEYCPYGQLYEVLRAgrEITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKE---LSEK 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  804 NDKwknrqsadedlTTGVGTALYVAPELLsrRNGvRYDAKVDMYSLGIILFEM--CMTFSTSMERIRIIDTIRSPSISF- 880
Cdd:cd14059  135 STK-----------MSFAGTVAWMAPEVI--RNE-PCSEKVDIWSFGVVLWELltGEIPYKDVDSSAIIWGVGSNSLQLp 200
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 63054755  881 -PSTFPfsrasHEFKVI--HClLQHDPTKRPSSQELL 914
Cdd:cd14059  201 vPSTCP-----DGFKLLmkQC-WNSKPRNRPSFRQIL 231
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
721-856 1.52e-14

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


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 75.72  E-value: 1.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  721 NATLYIQMEYCEKLSLQDIIRDKIPVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEne 798
Cdd:cd14182   82 NTFFFLVFDLMKKGELFDYLTEKVTLSEkeTRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQ-- 159
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 63054755  799 nyqdnndkwknrQSADEDLTTGVGTALYVAPELLS---RRNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd14182  160 ------------LDPGEKLREVCGTPGYLAPEIIEcsmDDNHPGYGKEVDMWSTGVIMYTL 208
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
736-915 1.56e-14

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: 75.73  E-value: 1.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  736 LQDIIRDKIPVDEMW--RLFRQILEALAYIHSRGMMHRDLKPGNIF---LDENR--NVKLGDFGLAtenenyqdnndkwk 808
Cdd:cd14000   99 LQQDSRSFASLGRTLqqRIALQVADGLRYLHSAMIIYRDLKSHNVLvwtLYPNSaiIIKIADYGIS-------------- 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  809 nRQSADEDLTTGVGTALYVAPELlsRRNGVRYDAKVDMYSLGIILFEMcMTFSTSM-------ERIRIIDTIRsPSISFP 881
Cdd:cd14000  165 -RQCCRMGAKGSEGTPGFRAPEI--ARGNVIYNEKVDVFSFGMLLYEI-LSGGAPMvghlkfpNEFDIHGGLR-PPLKQY 239
                        170       180       190
                 ....*....|....*....|....*....|....
gi 63054755  882 STFPFSRAshEFKVIHClLQHDPTKRPSSQELLE 915
Cdd:cd14000  240 ECAPWPEV--EVLMKKC-WKENPQQRPTAVTVVS 270
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
562-857 1.58e-14

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: 75.77  E-value: 1.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  562 LGRGGFGEVVKVKNRiDGRFYAVKKLVLLSDDKENSRILREVMTLSRLHHEHVVRYYtawveteandtvteiissdsesl 641
Cdd:cd14066    1 IGSGGFGTVYKGVLE-NGTVVAVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVRLL----------------------- 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  642 sqslnmavdfrqssslpadklssldihfeddynssadeedpeasdisfqysntsdkeGSSDkdssieeassvktqENGLN 721
Cdd:cd14066   57 ---------------------------------------------------------GYCL--------------ESDEK 65
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  722 ATLYiqmEYCEKLSLQDIIRDKIPVDEM-W----RLFRQILEALAYIHSRG---MMHRDLKPGNIFLDENRNVKLGDFGL 793
Cdd:cd14066   66 LLVY---EYMPNGSLEDRLHCHKGSPPLpWpqrlKIAKGIARGLEYLHEECpppIIHGDIKSSNILLDEDFEPKLTDFGL 142
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63054755  794 ATENENyqdnndkwknrqSADEDLTTGV-GTALYVAPELLSRRngvRYDAKVDMYSLGIILFEMC 857
Cdd:cd14066  143 ARLIPP------------SESVSKTSAVkGTIGYLAPEYIRTG---RVSTKSDVYSFGVVLLELL 192
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
724-915 1.76e-14

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: 75.70  E-value: 1.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDII--RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLD---ENRNVKLGDFGLAtene 798
Cdd:cd14169   76 LYLAMELVTGGELFDRIieRGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFGLS---- 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  799 nyqdnndkwknRQSADEDLTTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMCMTFSTSMER--IRIIDTIRSP 876
Cdd:cd14169  152 -----------KIEAQGMLSTACGTPGYVAPELLEQKP---YGKAVDVWAIGVISYILLCGYPPFYDEndSELFNQILKA 217
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 63054755  877 SISFPSTF--PFSRASHEFkvIHCLLQHDPTKRPSSQELLE 915
Cdd:cd14169  218 EYEFDSPYwdDISESAKDF--IRHLLERDPEKRFTCEQALQ 256
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
555-913 2.16e-14

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: 75.35  E-value: 2.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  555 DFEELEFLGRGGFGEVVKVKNRIDGRFYAVK--KLVLLSDDKENSrILREVMTLSRL-HHEHVVRYYTAWVeteandtvt 631
Cdd:cd14139    1 EFLELEKIGVGEFGSVYKCIKRLDGCVYAIKrsMRPFAGSSNEQL-ALHEVYAHAVLgHHPHVVRYYSAWA--------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  632 eiissdseslsqslnmavdfrqssslpadklssldihfEDDYnssadeedpeasdisfqysntsdkegssdkdssieeas 711
Cdd:cd14139   71 --------------------------------------EDDH-------------------------------------- 74
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  712 svktqenglnatLYIQMEYCEKLSLQDIIRDK------IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFL----- 780
Cdd:cd14139   75 ------------MIIQNEYCNGGSLQDAISENtksgnhFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFIchkmq 142
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  781 --------DENR-------NV--KLGDFGLATENENYQdnndkwknrqsADEdlttgvGTALYVAPELLsrRNGVRYDAK 843
Cdd:cd14139  143 sssgvgeeVSNEedeflsaNVvyKIGDLGHVTSINKPQ-----------VEE------GDSRFLANEIL--QEDYRHLPK 203
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63054755  844 VDMYSLGIILF-----EMCMTFSTSMERIRiidtirspSISFPStFPFSRASHEFKVIHCLLQHDPTKRPSSQEL 913
Cdd:cd14139  204 ADIFALGLTVAlaagaEPLPTNGAAWHHIR--------KGNFPD-VPQELPESFSSLLKNMIQPDPEQRPSATAL 269
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
728-915 2.24e-14

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


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 74.61  E-value: 2.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  728 MEYCEKLSLQDIIRDKIPVDE-MWRLF-RQILEALAYIHSRGMMHRDLKPGNIFLDENR--NVKLGDFGLATenenyqdn 803
Cdd:cd14006   68 LELCSGGELLDRLAERGSLSEeEVRTYmRQLLEGLQYLHNHHILHLDLKPENILLADRPspQIKIIDFGLAR-------- 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  804 ndkwknRQSADEDLTTGVGTALYVAPELlsrrngVRYDAKV---DMYSLGIILFeMCMT----FS--TSMERIRIIDTIR 874
Cdd:cd14006  140 ------KLNPGEELKEIFGTPEFVAPEI------VNGEPVSlatDMWSIGVLTY-VLLSglspFLgeDDQETLANISACR 206
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 63054755  875 SpSISFPSTFPFSRASHEFkvIHCLLQHDPTKRPSSQELLE 915
Cdd:cd14006  207 V-DFSEEYFSSVSQEAKDF--IRKLLVKEPRKRPTAQEALQ 244
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
718-921 2.39e-14

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 78.63  E-value: 2.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   718 NGLNATLYIQMEYCEKLSLQDIIRD------KIPVDEMWRLFRQILEALAYIHS-------RGMMHRDLKPGNIFLD--- 781
Cdd:PTZ00266   83 NKANQKLYILMEFCDAGDLSRNIQKcykmfgKIEEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLStgi 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   782 ----------ENRN----VKLGDFGLAtenenyqdnndkwknRQSADEDLT-TGVGTALYVAPELLSRRNGvRYDAKVDM 846
Cdd:PTZ00266  163 rhigkitaqaNNLNgrpiAKIGDFGLS---------------KNIGIESMAhSCVGTPYYWSPELLLHETK-SYDDKSDM 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   847 YSLGIILFEMC---MTFSTSMERIRIIDTI-RSPSIsfpstfPFSRASHEFKV-IHCLLQHDPTKRPSSQELLESEAI-- 919
Cdd:PTZ00266  227 WALGCIIYELCsgkTPFHKANNFSQLISELkRGPDL------PIKGKSKELNIlIKNLLNLSAKERPSALQCLGYQIIkn 300

                  ....
gi 63054755   920 --PP 921
Cdd:PTZ00266  301 vgPP 304
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
701-919 2.43e-14

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: 74.84  E-value: 2.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  701 SDKDSSIEEASSVKTQENGLNATLY--------IQMEYCEKLSLQDII-RDKIPVDEMWRLFRQILEALAYIHSRG--MM 769
Cdd:cd14025   37 SERMELLEEAKKMEMAKFRHILPVYgicsepvgLVMEYMETGSLEKLLaSEPLPWELRFRIIHETAVGMNFLHCMKppLL 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  770 HRDLKPGNIFLDENRNVKLGDFGLAtenenyqdnndKWkNRQSADEDLT--TGVGTALYVAPELLSRRNGVrYDAKVDMY 847
Cdd:cd14025  117 HLDLKPANILLDAHYHVKISDFGLA-----------KW-NGLSHSHDLSrdGLRGTIAYLPPERFKEKNRC-PDTKHDVY 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  848 SLGIILFEMCMT---FSTSMERIRIIDTI---RSPSIS-FPSTFPfSRASHEFKVIHCLLQHDPTKRPSSQEL-LESEAI 919
Cdd:cd14025  184 SFAIVIWGILTQkkpFAGENNILHIMVKVvkgHRPSLSpIPRQRP-SECQQMICLMKRCWDQDPRKRPTFQDItSETENL 262
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
752-915 2.77e-14

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: 74.76  E-value: 2.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  752 LFRQILEALAYIHSRGMMHRDLKPGNIFLDENRN---VKLGDFGLA--TENENYqdnndkwknRQSAdedlttgVGTALY 826
Cdd:cd14082  108 LVTQILVALRYLHSKNIVHCDLKPENVLLASAEPfpqVKLCDFGFAriIGEKSF---------RRSV-------VGTPAY 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  827 VAPELLSRRngvRYDAKVDMYSLGIILF-EMCMTFSTSmERIRIIDTIRSPSISFPSTfPFSRASHE-FKVIHCLLQHDP 904
Cdd:cd14082  172 LAPEVLRNK---GYNRSLDMWSVGVIIYvSLSGTFPFN-EDEDINDQIQNAAFMYPPN-PWKEISPDaIDLINNLLQVKM 246
                        170
                 ....*....|.
gi 63054755  905 TKRPSSQELLE 915
Cdd:cd14082  247 RKRYSVDKSLS 257
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
724-914 3.42e-14

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 78.35  E-value: 3.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755    724 LYIQMEYCEKLSLQDIIRDK--IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFL---DENRNVKLGDFGLATENE 798
Cdd:TIGR03903   54 LFAVFEYVPGRTLREVLAADgaLPAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVsqtGVRPHAKVLDFGIGTLLP 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755    799 NYQDNNDKWKNRQsadedlTTGVGTALYVAPELLsrrNGVRYDAKVDMYSLGIILFEmCMTFSTSMERIRIIDTIRSPSI 878
Cdd:TIGR03903  134 GVRDADVATLTRT------TEVLGTPTYCAPEQL---RGEPVTPNSDLYAWGLIFLE-CLTGQRVVQGASVAEILYQQLS 203
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 63054755    879 SFPSTFPFSRASHEF-KVIHCLLQHDPTKRPSSQELL 914
Cdd:TIGR03903  204 PVDVSLPPWIAGHPLgQVLRKALNKDPRQRAASAPAL 240
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
724-913 3.55e-14

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: 75.00  E-value: 3.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDKIPVDEMWRL-FRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENEnyqd 802
Cdd:cd14199  102 LYMVFELVKQGPVMEVPTLKPLSEDQARFyFQDLIKGIEYLHYQKIIHRDVKPSNLLVGEDGHIKIADFGVSNEFE---- 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  803 nndkwknrqSADEDLTTGVGTALYVAPELLSRRNGVRYDAKVDMYSLGIILFemCMTFSTSM---ERIRII-DTIRSPSI 878
Cdd:cd14199  178 ---------GSDALLTNTVGTPAFMAPETLSETRKIFSGKALDVWAMGVTLY--CFVFGQCPfmdERILSLhSKIKTQPL 246
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 63054755  879 SFPSTfpfSRASHEFK-VIHCLLQHDPTKRPSSQEL 913
Cdd:cd14199  247 EFPDQ---PDISDDLKdLLFRMLDKNPESRISVPEI 279
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
716-914 3.78e-14

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: 74.30  E-value: 3.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  716 QENGLNATLYIQMEYCEKLSLQDIIRDKIPVDEM--WRLFRQILEALAYIHSRGMMHRDLKPGNIFL----DENRNVKLG 789
Cdd:cd14184   66 EEMDTPAELYLVMELVKGGDLFDAITSSTKYTERdaSAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLG 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  790 DFGLATenenyqdnndkwknrqSADEDLTTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMCMTF----STSME 865
Cdd:cd14184  146 DFGLAT----------------VVEGPLYTVCGTPTYVAPEIIAETG---YGLKVDIWAAGVITYILLCGFppfrSENNL 206
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 63054755  866 RIRIIDTIRSPSISFPSTFPFSRASHEFKVIHCLLQHDPTKRPSSQELL 914
Cdd:cd14184  207 QEDLFDQILLGKLEFPSPYWDNITDSAKELISHMLQVNVEARYTAEQIL 255
hisZ_biosyn_reg TIGR00443
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ...
990-1272 4.48e-14

ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA synthetase, found in Bacillus subtilis, Synechocystis sp., Aquifex aeolicus, and others, are in fact a regulatory subunit of ATP phosphoribosyltransferase, and usually encoded by a gene adjacent to that encoding the catalytic subunit. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273081 [Multi-domain]  Cd Length: 313  Bit Score: 74.96  E-value: 4.48e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755    990 VRDHVVKVFRRHGAKEreshILFPKSSQYDKDQASVS--------LLDKNGTLLQLPYDTVLPYARNVA---RNAVEEEK 1058
Cdd:TIGR00443   14 IERQLQDVFRSWGYQE----IITPTLEYLDTLSAGSGilnedlfkLFDQLGRVLGLRPDMTAPIARLVStrlRDRPLPLR 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   1059 TYLISDVFR-EAKGGGRPKAIK----EISFDITTNSDnldwydAETIKALDEVLTEIpSLTESCILINHADILSSILDYL 1133
Cdd:TIGR00443   90 LCYAGNVFRtNESGGGRSREFTqagvELIGAGGPAAD------AEVIALLIEALKAL-GLKDFKIELGHVGLVRALLEEA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   1134 QVSKDKRRMATHILGQinqrltlsqvRNQLRIESLVPSTTLDD------LSLFDFRENYEEGASKLRKIFGKEmpqKMRT 1207
Cdd:TIGR00443  163 GLPEEAREALREALAR----------KDLVALEELVAELGLSPevrerlLALPRLRGDGEEVLEEARALAGSE---TAEA 229
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755   1208 ALNYMERVVKLLRALKISHQLYFmPLC-VYNFEFYDGgLMFQAInLAEKSELICAGGRYDKLVRFF 1272
Cdd:TIGR00443  230 ALDELEAVLELLEARGVEEYISL-DLGlVRGYHYYTG-LIFEGY-APGLGAPLAGGGRYDELLGRF 292
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
724-861 4.51e-14

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: 74.67  E-value: 4.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQD-IIRDKIPVD-EMWRLFRQILEALAYIHSRGMMHRDLKPGNI-FLDENRN---VKLGDFGLAten 797
Cdd:cd14178   72 VYLVMELMRGGELLDrILRQKCFSErEASAVLCTITKTVEYLHSQGVVHRDLKPSNIlYMDESGNpesIRICDFGFA--- 148
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63054755  798 enyqdnndkwKNRQSADEDLTTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMCMTFS 861
Cdd:cd14178  149 ----------KQLRAENGLLMTPCYTANFVAPEVLKRQG---YDAACDIWSLGILLYTMLAGFT 199
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
759-861 4.82e-14

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: 75.30  E-value: 4.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  759 ALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENenyqdnndkwknrQSADEDLTTGVGTALYVAPELLSRRNGv 838
Cdd:cd05586  108 ALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKAD-------------LTDNKTTNTFCGTTEYLAPEVLLDEKG- 173
                         90       100
                 ....*....|....*....|...
gi 63054755  839 rYDAKVDMYSLGIILFEMCMTFS 861
Cdd:cd05586  174 -YTKMVDFWSLGVLVFEMCCGWS 195
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
285-512 4.98e-14

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: 74.35  E-value: 4.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  285 REIQELEYELESLKVIRHDLLASIYEYQLERETRgygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAE 364
Cdd:cd06651   51 KEVSALECEIQLLKNLQHERIVQYYGCLRDRAEK----TLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSY 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  365 LHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDMNAShpfNINSQSITNIlPEGLYPPEVSESSFAaasRKTD 444
Cdd:cd06651  127 LHSNMIVHRDIKGANILRDSAGN---VKLGDFGASKRLQTICMS---GTGIRSVTGT-PYWMSPEVISGEGYG---RKAD 196
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63054755  445 IWCFGLLVLQMLCGAHVLNKFSSL----KLIMTHVIPLLPGSYQDLVR---RCLMRDSRKRPSAIDLLSSHVIRL 512
Cdd:cd06651  197 VWSLGCTVVEMLTEKPPWAEYEAMaaifKIATQPTNPQLPSHISEHARdflGCIFVEARHRPSAEELLRHPFAQL 271
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
748-921 5.13e-14

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: 74.69  E-value: 5.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  748 EMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRN---VKLGDFGLATENENYQdnndkwknrqsadeDLTTGVGTA 824
Cdd:cd14170  102 EASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPnaiLKLTDFGFAKETTSHN--------------SLTTPCYTP 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  825 LYVAPELLSRRngvRYDAKVDMYSLGIILF-EMC----------MTFSTSMERiriidTIRSPSISFPSTfPFSRASHEF 893
Cdd:cd14170  168 YYVAPEVLGPE---KYDKSCDMWSLGVIMYiLLCgyppfysnhgLAISPGMKT-----RIRMGQYEFPNP-EWSEVSEEV 238
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 63054755  894 K-VIHCLLQHDPTKRPSSQELL------ESEAIPP 921
Cdd:cd14170  239 KmLIRNLLKTEPTQRMTITEFMnhpwimQSTKVPQ 273
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
748-914 6.13e-14

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: 73.87  E-value: 6.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  748 EMWRLFRQILEALAYIHSRGMMHRDLKPGNIFL---DENRNVKLGDFGLATENenyqdnndkwknrqSADEDLTTGVGTA 824
Cdd:cd14172  104 EASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYtskEKDAVLKLTDFGFAKET--------------TVQNALQTPCYTP 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  825 LYVAPELLSRRngvRYDAKVDMYSLGIILFEMCMTF-----------STSMERiriidTIRSPSISFPSTfPFSRASHEF 893
Cdd:cd14172  170 YYVAPEVLGPE---KYDKSCDMWSLGVIMYILLCGFppfysntgqaiSPGMKR-----RIRMGQYGFPNP-EWAEVSEEA 240
                        170       180
                 ....*....|....*....|..
gi 63054755  894 K-VIHCLLQHDPTKRPSSQELL 914
Cdd:cd14172  241 KqLIRHLLKTDPTERMTITQFM 262
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
755-907 6.26e-14

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: 75.00  E-value: 6.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQDNNdkwknrqsadedlTTGVGTALYVAPELLSR 834
Cdd:cd05604  105 EIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDTT-------------TTFCGTPEYLAPEVIRK 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  835 RNgvrYDAKVDMYSLGIILFEM--------CMTFSTSMERIRIIDTIRSPSISFPStfpfsrasheFKVIHCLLQHDPTK 906
Cdd:cd05604  172 QP---YDNTVDWWCLGSVLYEMlyglppfyCRDTAEMYENILHKPLVLRPGISLTA----------WSILEELLEKDRQL 238

                 .
gi 63054755  907 R 907
Cdd:cd05604  239 R 239
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
741-914 6.68e-14

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 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 TRB3 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: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 72.99  E-value: 6.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  741 RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGN-IFLDENRNvKLGDFGLateNENYQDNNDkwknrqsaDEDLTT 819
Cdd:cd14024   78 RRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRfVFTDELRT-KLVLVNL---EDSCPLNGD--------DDSLTD 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  820 GVGTALYVAPELLSRRNGvrYDAK-VDMYSLGIILFEMCM---TFSTSmERIRIIDTIRSPSISFPSTF-PFSRAshefk 894
Cdd:cd14024  146 KHGCPAYVGPEILSSRRS--YSGKaADVWSLGVCLYTMLLgryPFQDT-EPAALFAKIRRGAFSLPAWLsPGARC----- 217
                        170       180
                 ....*....|....*....|
gi 63054755  895 VIHCLLQHDPTKRPSSQELL 914
Cdd:cd14024  218 LVSCMLRRSPAERLKASEIL 237
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
726-857 8.30e-14

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: 73.78  E-value: 8.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  726 IQMEYCEKLSLQDIIR-DKIPVDEMWR--LFRQILEALAYIHSRG-MMHRDLKPGNIFLDeNRNV-KLGDFGLAT---EN 797
Cdd:cd14042   79 ILTEYCPKGSLQDILEnEDIKLDWMFRysLIHDIVKGMHYLHDSEiKSHGNLKSSNCVVD-SRFVlKITDFGLHSfrsGQ 157
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054755  798 ENYQDNNDKWKNRqsadedlttgvgtaLYVAPELLsrRNGVRYDA---KVDMYSLGIILFEMC 857
Cdd:cd14042  158 EPPDDSHAYYAKL--------------LWTAPELL--RDPNPPPPgtqKGDVYSFGIILQEIA 204
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
285-505 9.41e-14

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: 73.15  E-value: 9.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  285 REIQELEYELESLKVIRHDLLASIYEYQLERETRgygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAE 364
Cdd:cd06652   46 KEVNALECEIQLLKNLLHERIVQYYGCLRDPQER----TLSIFMEYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHY 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  365 LHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDMNAShpfNINSQSITNIlPEGLYPPEVSESSFAaasRKTD 444
Cdd:cd06652  122 LHSNMIVHRDIKGANILRDSVGN---VKLGDFGASKRLQTICLS---GTGMKSVTGT-PYWMSPEVISGEGYG---RKAD 191
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63054755  445 IWCFGLLVLQMLCGAHVLNKFSSL----KLIMTHVIPLLPGSYQDLVRRCLMR---DSRKRPSAIDLL 505
Cdd:cd06652  192 IWSVGCTVVEMLTEKPPWAEFEAMaaifKIATQPTNPQLPAHVSDHCRDFLKRifvEAKLRPSADELL 259
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
755-907 1.17e-13

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: 73.85  E-value: 1.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENenyqdnndkwknrQSADEDLTTGVGTALYVAPELLSR 834
Cdd:cd05603  104 EVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEG-------------MEPEETTSTFCGTPEYLAPEVLRK 170
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63054755  835 RNgvrYDAKVDMYSLGIILFEMCMTFST--SMERIRIIDTIrspsISFPSTFPFSRASHEFKVIHCLLQHDPTKR 907
Cdd:cd05603  171 EP---YDRTVDWWCLGAVLYEMLYGLPPfySRDVSQMYDNI----LHKPLHLPGGKTVAACDLLQGLLHKDQRRR 238
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
728-854 1.20e-13

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: 1.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  728 MEYCEKLSLQDIIRdKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLD-ENRNVKLGDFGLAtenENYQDNNDK 806
Cdd:cd14019   83 LPYIEHDDFRDFYR-KMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNrETGKGVLVDFGLA---QREEDRPEQ 158
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 63054755  807 WKNRqsadedlttgVGTALYVAPELLSRRNgvRYDAKVDMYSLGIILF 854
Cdd:cd14019  159 RAPR----------AGTRGFRAPEVLFKCP--HQTTAIDIWSAGVILL 194
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
556-917 1.23e-13

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: 73.17  E-value: 1.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  556 FEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENSRI-LREVMTLSRLHHEHVVryytawveteandtvteii 634
Cdd:cd07847    3 YEKLSKIGEGSYGVVFKCRNRETGQIVAIKKFVESEDDPVIKKIaLREIRMLKQLKHPNLV------------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  635 ssdseslsqslNMAVDFRQSSSLpadklssldihfeddynssadeedpeasdisfqysntsdkegssdkdssieeassvk 714
Cdd:cd07847   64 -----------NLIEVFRRKRKL--------------------------------------------------------- 75
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  715 tqenglnatlYIQMEYCEKLSLQDIIRDKIPVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFG 792
Cdd:cd07847   76 ----------HLVFEYCDHTVLNELEKNPRGVPEhlIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFG 145
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  793 LAtenenyqdnndkwKNRQSADEDLTTGVGTALYVAPELLSrrNGVRYDAKVDMYSLGIILFEMCM-------------- 858
Cdd:cd07847  146 FA-------------RILTGPGDDYTDYVATRWYRAPELLV--GDTQYGPPVDVWAIGCVFAELLTgqplwpgksdvdql 210
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63054755  859 -----TFSTSMER-IRIIDT--------IRSPSISFPSTFPFSRAS-HEFKVIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd07847  211 ylirkTLGDLIPRhQQIFSTnqffkglsIPEPETREPLESKFPNISsPALSFLKGCLQMDPTERLSCEELLEHP 284
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
724-856 1.37e-13

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: 73.89  E-value: 1.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYC---EKLSLqdIIRDKIPVDEMWRLFrqILE---ALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEN 797
Cdd:cd05598   76 LYFVMDYIpggDLMSL--LIKKGIFEEDLARFY--IAElvcAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGF 151
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  798 ENYQDNndKWKNRQSAdedlttgVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEM 856
Cdd:cd05598  152 RWTHDS--KYYLAHSL-------VGTPNYIAPEVLLRTG---YTQLCDWWSVGVILYEM 198
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
724-907 1.86e-13

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


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 73.04  E-value: 1.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIR---DKIPVDEMWRLF-RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATE--- 796
Cdd:cd05574   76 LCFVMDYCPGGELFRLLQkqpGKRLPEEVARFYaAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKQssv 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  797 ----------NENYQDNNDKWKNRQSADEDLTTG---VGTALYVAPELLsrrNGVRYDAKVDMYSLGIILFEMC------ 857
Cdd:cd05574  156 tpppvrkslrKGSRRSSVKSIEKETFVAEPSARSnsfVGTEEYIAPEVI---KGDGHGSAVDWWTLGILLYEMLygttpf 232
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  858 ------MTFStsmeririidTIRSPSISFPSTFPFSRashEFK-VIHCLLQHDPTKR 907
Cdd:cd05574  233 kgsnrdETFS----------NILKKELTFPESPPVSS---EAKdLIRKLLVKDPSKR 276
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
759-856 1.91e-13

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: 73.20  E-value: 1.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  759 ALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEnenYQDNNDKwknrqsadedLTTGVGTALYVAPELLSRRNgv 838
Cdd:cd05582  109 ALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKE---SIDHEKK----------AYSFCGTVEYMAPEVVNRRG-- 173
                         90
                 ....*....|....*...
gi 63054755  839 rYDAKVDMYSLGIILFEM 856
Cdd:cd05582  174 -HTQSADWWSFGVLMFEM 190
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
724-872 1.94e-13

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: 73.36  E-value: 1.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDKIPVDEMWRLF-RQILEALAYIHSRGMMHRDLKPGNIFLDENRN---VKLGDFGLATENEN 799
Cdd:cd13977  110 LWFVMEFCDGGDMNEYLLSRRPDRQTNTSFmLQLSSALAFLHRNQIVHRDLKPDNILISHKRGepiLKVADFGLSKVCSG 189
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054755  800 YQDNNDKWKNRQSAdeDLTTGVGTALYVAPELLSRrngvRYDAKVDMYSLGIILFEMcmtfstsMERIRIIDT 872
Cdd:cd13977  190 SGLNPEEPANVNKH--FLSSACGSDFYMAPEVWEG----HYTAKADIFALGIIIWAM-------VERITFRDG 249
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
729-856 2.17e-13

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: 72.28  E-value: 2.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  729 EYCEKLSLQDIIR--DKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLA--TENENYQDNN 804
Cdd:cd14222   70 EFIEGGTLKDFLRadDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSrlIVEEKKKPPP 149
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  805 DKWKN-----RQSADEDLTTGVGTALYVAPELLsrrNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd14222  150 DKPTTkkrtlRKNDRKKRYTVVGNPYWMAPEML---NGKSYDEKVDIFSFGIVLCEI 203
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
723-917 2.22e-13

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: 71.84  E-value: 2.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  723 TLYIQMEYCEKLSLQDIIRDKIPVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFL--DENRNVKLGDFGLATENE 798
Cdd:cd14107   72 TLILILELCSSEELLDRLFLKGVVTEaeVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMvsPTREDIKICDFGFAQEIT 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  799 NYQDNNDKWknrqsadedlttgvGTALYVAPELLSrRNGVryDAKVDMYSLGIILFeMCMT----FSTSMERIRIIDTIR 874
Cdd:cd14107  152 PSEHQFSKY--------------GSPEFVAPEIVH-QEPV--SAATDIWALGVIAY-LSLTchspFAGENDRATLLNVAE 213
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 63054755  875 SP-SISFPSTFPFSRASHEFkvIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd14107  214 GVvSWDTPEITHLSEDAKDF--IKRVLQPDPEKRPSASECLSHE 255
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
755-907 2.31e-13

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: 73.16  E-value: 2.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQDNNdkwknrqsadedlTTGVGTALYVAPELLSR 834
Cdd:cd05571  103 EIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGATT-------------KTFCGTPEYLAPEVLED 169
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  835 RNgvrYDAKVDMYSLGIILFEM-C--MTFStSMERIRIIDTIRSPSISFPSTFpfsraSHEFK-VIHCLLQHDPTKR 907
Cdd:cd05571  170 ND---YGRAVDWWGLGVVMYEMmCgrLPFY-NRDHEVLFELILMEEVRFPSTL-----SPEAKsLLAGLLKKDPKKR 237
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
728-859 2.88e-13

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: 72.10  E-value: 2.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  728 MEYCEKLSLQDIIR--------DKIPVDEmwrLFRQILEALAYIHSRGMMHRDLKPGNIFLD--ENRNV-KLGDFGLATE 796
Cdd:cd13989   78 MEYCSGGDLRKVLNqpenccglKESEVRT---LLSDISSAISYLHENRIIHRDLKPENIVLQqgGGRVIyKLIDLGYAKE 154
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054755  797 nenyqdnndkwknrQSADEDLTTGVGTALYVAPELLSRRngvRYDAKVDMYSLGIILFEmCMT 859
Cdd:cd13989  155 --------------LDQGSLCTSFVGTLQYLAPELFESK---KYTCTVDYWSFGTLAFE-CIT 199
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
724-856 2.88e-13

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


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 73.50  E-value: 2.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDkIPVDEMWRLF--RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATenenyq 801
Cdd:cd05621  127 LYMVMEYMPGGDLVNLMSN-YDVPEKWAKFytAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCM------ 199
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  802 dnndkwKNRQSADEDLTTGVGTALYVAPELLSRRNGVRYDAK-VDMYSLGIILFEM 856
Cdd:cd05621  200 ------KMDETGMVHCDTAVGTPDYISPEVLKSQGGDGYYGReCDWWSVGVFLFEM 249
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
736-922 2.90e-13

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: 72.37  E-value: 2.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  736 LQDIIRDKIPVD-EMWRLFRQILEALAYIHSRGMMHRDLKPGNI-FLDENRN---VKLGDFGLAtenenyqdnndkwKNR 810
Cdd:cd14175   83 LDKILRQKFFSErEASSVLHTICKTVEYLHSQGVVHRDLKPSNIlYVDESGNpesLRICDFGFA-------------KQL 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  811 QSADEDLTTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEM---CMTFSTSMERI--RIIDTIRSPSISFPSTFP 885
Cdd:cd14175  150 RAENGLLMTPCYTANFVAPEVLKRQG---YDEGCDIWSLGILLYTMlagYTPFANGPSDTpeEILTRIGSGKFTLSGGNW 226
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 63054755  886 FSRASHEFKVIHCLLQHDPTKRPSSQELLESEAIPPK 922
Cdd:cd14175  227 NTVSDAAKDLVSKMLHVDPHQRLTAKQVLQHPWITQK 263
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
725-917 2.98e-13

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: 72.60  E-value: 2.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  725 YIQMEYCEKLSLQDIIRDK--IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNI-FLDENRN--VKLGDFGLAtenen 799
Cdd:cd14180   77 YLVMELLRGGELLDRIKKKarFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENIlYADESDGavLKVIDFGFA----- 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  800 yqdnndkwKNRQSADEDLTTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMC---MTF------STSMERIRII 870
Cdd:cd14180  152 --------RLRPQGSRPLQTPCFTLQYAAPELFSNQG---YDESCDLWSLGVILYTMLsgqVPFqskrgkMFHNHAADIM 220
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 63054755  871 DTIRSPSISFPSTfPFSRASHEFK-VIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd14180  221 HKIKEGDFSLEGE-AWKGVSEEAKdLVRGLLTVDPAKRLKLSELRESD 267
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
755-907 3.05e-13

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: 72.00  E-value: 3.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENEnyqdNNDKWKNRqsadedlttgVGTALYVAPELLsr 834
Cdd:cd05605  110 EITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIP----EGETIRGR----------VGTVGYMAPEVV-- 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  835 rNGVRYDAKVDMYSLGIILFEMCM---TFSTSMERIRIIDT---IRSPSISFPSTFpfsraSHEFKVIhC--LLQHDPTK 906
Cdd:cd05605  174 -KNERYTFSPDWWGLGCLIYEMIEgqaPFRARKEKVKREEVdrrVKEDQEEYSEKF-----SEEAKSI-CsqLLQKDPKT 246

                 .
gi 63054755  907 R 907
Cdd:cd05605  247 R 247
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
554-919 3.08e-13

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: 72.01  E-value: 3.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  554 TDFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENSRILREVMTLSRLHH-EHVVRYYTA-------WVETE 625
Cdd:cd06616    6 EDLKDLGEIGRGAFGTVNKMLHKPSGTIMAVKRIRSTVDEKEQKRLLMDLDVVMRSSDcPYIVKFYGAlfregdcWICME 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  626 ANDTvteiissdseslsqslnmavdfrqssSLpaDKLSSLdIHfeddynssadeedpeasdisfqysntsdkegssdkds 705
Cdd:cd06616   86 LMDI--------------------------SL--DKFYKY-VY------------------------------------- 99
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  706 sieeassvktqenglnatlyiqmeyceklslqDIIRDKIPVDEMWRLFRQILEALAYIHSR-GMMHRDLKPGNIFLDENR 784
Cdd:cd06616  100 --------------------------------EVLDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNG 147
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  785 NVKLGDFGLATEnenYQDNNDKwknrqsadedlTTGVGTALYVAPE-LLSRRNGVRYDAKVDMYSLGIILFEMCM----- 858
Cdd:cd06616  148 NIKLCDFGISGQ---LVDSIAK-----------TRDAGCRPYMAPErIDPSASRDGYDVRSDVWSLGITLYEVATgkfpy 213
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054755  859 -TFSTSMERIRIIDTIRSPSISFPSTFPFSRASHEFkVIHCLLQhDPTKRPSSQELLESEAI 919
Cdd:cd06616  214 pKWNSVFDQLTQVVKGDPPILSNSEEREFSPSFVNF-VNLCLIK-DESKRPKYKELLKHPFI 273
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
323-498 3.14e-13

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: 71.39  E-value: 3.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  323 RLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRtl 402
Cdd:cd05123   67 KLYLVLDYVPGGELFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGH---IKLTDFGLAK-- 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  403 rdMNASHPFNINSQSITnilPEGLyPPEV---SESSFAAasrktDIWCFGLLVLQMLCGahvLNKFSSLKL-IMTHVIPL 478
Cdd:cd05123  142 --ELSSDGDRTYTFCGT---PEYL-APEVllgKGYGKAV-----DWWSLGVLLYEMLTG---KPPFYAENRkEIYEKILK 207
                        170       180
                 ....*....|....*....|....*...
gi 63054755  479 LPGSY--------QDLVRRCLMRDSRKR 498
Cdd:cd05123  208 SPLKFpeyvspeaKSLISGLLQKDPTKR 235
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
724-919 3.16e-13

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


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 71.41  E-value: 3.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQD--IIRDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRN---VKLGDFGLATEne 798
Cdd:cd14087   72 VYMVMELATGGELFDriIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPdskIMITDFGLAST-- 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  799 nyqdnndkwkNRQSADEDLTTGVGTALYVAPELLSRrngVRYDAKVDMYSLGI---ILFEMCMTFSTSmERIRIIDTIRS 875
Cdd:cd14087  150 ----------RKKGPNCLMKTTCGTPEYIAPEILLR---KPYTQSVDMWAVGViayILLSGTMPFDDD-NRTRLYRQILR 215
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 63054755  876 PSISFpSTFPFSRASHEFK-VIHCLLQHDPTKRPSSQELLESEAI 919
Cdd:cd14087  216 AKYSY-SGEPWPSVSNLAKdFIDRLLTVNPGERLSATQALKHPWI 259
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
741-914 3.26e-13

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: 71.31  E-value: 3.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  741 RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGN-IFLDENRN-VKLgdfglatenENYQDNNDKwknrQSADEDLT 818
Cdd:cd13976   78 RKRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKfVFADEERTkLRL---------ESLEDAVIL----EGEDDSLS 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  819 TGVGTALYVAPELLsrRNGVRYDAK-VDMYSLGIILFEMCM---TFSTSmERIRIIDTIRSPSISFPSTF-PFSRAshef 893
Cdd:cd13976  145 DKHGCPAYVSPEIL--NSGATYSGKaADVWSLGVILYTMLVgryPFHDS-EPASLFAKIRRGQFAIPETLsPRARC---- 217
                        170       180
                 ....*....|....*....|.
gi 63054755  894 kVIHCLLQHDPTKRPSSQELL 914
Cdd:cd13976  218 -LIRSLLRREPSERLTAEDIL 237
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
755-914 3.31e-13

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 73.92  E-value: 3.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   755 QILEALAYIHSRGMMHRDLKPGNIFLDEN-RNVKLGDFGLAtenenyqdnndkwKNRQSADEDLTTgVGTALYVAPELLs 833
Cdd:PTZ00036  178 QLCRALAYIHSKFICHRDLKPQNLLIDPNtHTLKLCDFGSA-------------KNLLAGQRSVSY-ICSRFYRAPELM- 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   834 rRNGVRYDAKVDMYSLGIILFEMCMTF------STSMERIRIIDTIRSPS-------------ISFP--------STFPF 886
Cdd:PTZ00036  243 -LGATNYTTHIDLWSLGCIIAEMILGYpifsgqSSVDQLVRIIQVLGTPTedqlkemnpnyadIKFPdvkpkdlkKVFPK 321
                         170       180
                  ....*....|....*....|....*...
gi 63054755   887 SRASHEFKVIHCLLQHDPTKRPSSQELL 914
Cdd:PTZ00036  322 GTPDDAINFISQFLKYEPLKRLNPIEAL 349
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
744-856 3.31e-13

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: 71.92  E-value: 3.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  744 IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenenyqdnndkwkNRQSADEDLTTGVGT 823
Cdd:cd07863  105 LPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLA--------------RIYSCQMALTPVVVT 170
                         90       100       110
                 ....*....|....*....|....*....|...
gi 63054755  824 ALYVAPELLSRRNgvrYDAKVDMYSLGIILFEM 856
Cdd:cd07863  171 LWYRAPEVLLQST---YATPVDMWSVGCIFAEM 200
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
724-915 3.40e-13

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 71.99  E-value: 3.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDII-RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEnenyqd 802
Cdd:cd06658   94 LWVVMEFLEGGALTDIVtHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQ------ 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  803 NNDKWKNRQSAdedlttgVGTALYVAPELLSRrngVRYDAKVDMYSLGIILFEMC----MTFS----TSMERIRiidtir 874
Cdd:cd06658  168 VSKEVPKRKSL-------VGTPYWMAPEVISR---LPYGTEVDIWSLGIMVIEMIdgepPYFNepplQAMRRIR------ 231
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 63054755  875 spsISFPstfPFSRASHEFKVI-----HCLLQHDPTKRPSSQELLE 915
Cdd:cd06658  232 ---DNLP---PRVKDSHKVSSVlrgflDLMLVREPSQRATAQELLQ 271
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
724-856 3.59e-13

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: 72.79  E-value: 3.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIrDKIPVDEMWRLF--RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATE-NENY 800
Cdd:cd05596  101 LYMVMDYMPGGDLVNLM-SNYDVPEKWARFytAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCMKmDKDG 179
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  801 QDNNDkwknrqsadedltTGVGTALYVAPELLSRRNGV-RYDAKVDMYSLGIILFEM 856
Cdd:cd05596  180 LVRSD-------------TAVGTPDYISPEVLKSQGGDgVYGRECDWWSVGVFLYEM 223
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
723-856 3.61e-13

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: 71.61  E-value: 3.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  723 TLYIQMEYCEKLSLQDIIRDKIPVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAteneny 800
Cdd:cd06652   80 TLSIFMEYMPGGSIKDQLKSYGALTEnvTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGAS------ 153
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  801 qdnndkwKNRQS---ADEDLTTGVGTALYVAPELLSrrnGVRYDAKVDMYSLGIILFEM 856
Cdd:cd06652  154 -------KRLQTiclSGTGMKSVTGTPYWMSPEVIS---GEGYGRKADIWSVGCTVVEM 202
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
755-917 3.79e-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: 71.97  E-value: 3.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSR-GMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQDNNDKWKNRQSADEDLTTgvGTALYVAPELLS 833
Cdd:cd14011  122 QISEALSFLHNDvKLVHGNICPESVVINSNGEWKLAGFDFCISSEQATDQFPYFREYDPNLPPLAQ--PNLNYLAPEYIL 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  834 rrnGVRYDAKVDMYSLGIILFEMCMTFSTSMERIRIIDT--IRSPSISFPSTFPFSRASHEFKVIHCLLQH-DPTKRPSS 910
Cdd:cd14011  200 ---SKTCDPASDMFSLGVLIYAIYNKGKPLFDCVNNLLSykKNSNQLRQLSLSLLEKVPEELRDHVKTLLNvTPEVRPDA 276

                 ....*..
gi 63054755  911 QELLESE 917
Cdd:cd14011  277 EQLSKIP 283
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
754-914 3.79e-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: 3.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  754 RQILEALAYIHSRGMMHRDLKPGNIFLDEN-RNVKLGDFG----LATENenyqdnndkwknrQSADEDLTTGVGTALYVA 828
Cdd:cd06630  110 LQILRGLAYLHDNQIIHRDLKGANLLVDSTgQRLRIADFGaaarLASKG-------------TGAGEFQGQLLGTIAFMA 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  829 PELLsrrNGVRYDAKVDMYSLGIILFEMCMT--------FSTSMERI-RIIDTIRSPSIsfPSTfpFSRASHEFkVIHCL 899
Cdd:cd06630  177 PEVL---RGEQYGRSCDVWSVGCVIIEMATAkppwnaekISNHLALIfKIASATTPPPI--PEH--LSPGLRDV-TLRCL 248
                        170
                 ....*....|....*
gi 63054755  900 LQhDPTKRPSSQELL 914
Cdd:cd06630  249 EL-QPEDRPPARELL 262
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
754-914 4.13e-13

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: 71.72  E-value: 4.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  754 RQILEALAYIHSRGMMHRDLKPGNIFLDENRN---VKLGDFGLATENenyqdnndkwknrqsaDEDLTTGVGTALYVAPE 830
Cdd:cd14171  116 KQIALAVQHCHSLNIAHRDLKPENLLLKDNSEdapIKLCDFGFAKVD----------------QGDLMTPQFTPYYVAPQ 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  831 LLS-------RRNGV-------RYDAKVDMYSLGIILFEM-C-----------MTFSTSMERiriidTIRSPSISFPSTf 884
Cdd:cd14171  180 VLEaqrrhrkERSGIptsptpyTYDKSCDMWSLGVIIYIMlCgyppfysehpsRTITKDMKR-----KIMTGSYEFPEE- 253
                        170       180       190
                 ....*....|....*....|....*....|.
gi 63054755  885 PFSRASHEFK-VIHCLLQHDPTKRPSSQELL 914
Cdd:cd14171  254 EWSQISEMAKdIVRKLLCVDPEERMTIEEVL 284
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
724-856 4.22e-13

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: 72.38  E-value: 4.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYC---EKLSLQDIIRDKIPvDEMWRLF-RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFG--LATEN 797
Cdd:cd05597   76 LYLVMDYYcggDLLTLLSKFEDRLP-EEMARFYlAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGscLKLRE 154
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 63054755  798 ENYQDNNdkwknrqsadedltTGVGTALYVAPELL-SRRNGV-RYDAKVDMYSLGIILFEM 856
Cdd:cd05597  155 DGTVQSS--------------VAVGTPDYISPEILqAMEDGKgRYGPECDWWSLGVCMYEM 201
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
697-915 5.31e-13

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: 70.84  E-value: 5.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  697 KEGSSDKDSSIEEAS--------------SVKTQENGLnatlYIQMEYCEKLSLQDIIRDK----IPVDEMWRLFRQILE 758
Cdd:cd05039   38 KDDSTAAQAFLAEASvmttlrhpnlvqllGVVLEGNGL----YIVTEYMAKGSLVDYLRSRgravITRKDQLGFALDVCE 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  759 ALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQDNND---KWknrqsadedlttgvgtalyVAPELLsrR 835
Cdd:cd05039  114 GMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKEASSNQDGGKlpiKW-------------------TAPEAL--R 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  836 NGvRYDAKVDMYSLGIILFEMcmtFS---TSMERIRIIDTIRSPSISF----PSTFPfsraSHEFKVIHCLLQHDPTKRP 908
Cdd:cd05039  173 EK-KFSTKSDVWSFGILLWEI---YSfgrVPYPRIPLKDVVPHVEKGYrmeaPEGCP----PEVYKVMKNCWELDPAKRP 244

                 ....*..
gi 63054755  909 SSQELLE 915
Cdd:cd05039  245 TFKQLRE 251
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
736-915 5.44e-13

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: 71.98  E-value: 5.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  736 LQDIIRDKIPVD-EMWRLFRQILEALAYIHSRGMMHRDLKPGNI-FLDENRN---VKLGDFGLAtenenyqdnndkwKNR 810
Cdd:cd14176  101 LDKILRQKFFSErEASAVLFTITKTVEYLHAQGVVHRDLKPSNIlYVDESGNpesIRICDFGFA-------------KQL 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  811 QSADEDLTTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMCMTFS--------TSMErirIIDTIRSPSISFPS 882
Cdd:cd14176  168 RAENGLLMTPCYTANFVAPEVLERQG---YDAACDIWSLGVLLYTMLTGYTpfangpddTPEE---ILARIGSGKFSLSG 241
                        170       180       190
                 ....*....|....*....|....*....|....
gi 63054755  883 TFpFSRASHEFK-VIHCLLQHDPTKRPSSQELLE 915
Cdd:cd14176  242 GY-WNSVSDTAKdLVSKMLHVDPHQRLTAALVLR 274
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
753-914 5.45e-13

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: 71.94  E-value: 5.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  753 FRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEnenyqdnNDKWKNRQSADEDLTTGVGTALY-VAPEL 831
Cdd:cd08216  107 LRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYS-------MVKHGKRQRVVHDFPKSSEKNLPwLSPEV 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  832 LsRRNGVRYDAKVDMYSLGIILFEM---CMTFS----TSM--ERIR-----IIDTIRSP--------------------- 876
Cdd:cd08216  180 L-QQNLLGYNEKSDIYSVGITACELangVVPFSdmpaTQMllEKVRgttpqLLDCSTYPleedsmsqsedsstehpnnrd 258
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 63054755  877 SISFPSTFPFSRASHEFkVIHClLQHDPTKRPSSQELL 914
Cdd:cd08216  259 TRDIPYQRTFSEAFHQF-VELC-LQRDPELRPSASQLL 294
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
724-856 5.54e-13

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: 71.26  E-value: 5.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDII---RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLA---TEN 797
Cdd:cd05038   83 LRLIMEYLPSGSLRDYLqrhRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAkvlPED 162
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  798 ENYQDNNDKwknRQSAdedlttgvgtALYVAPELLSRRngvRYDAKVDMYSLGIILFEM 856
Cdd:cd05038  163 KEYYYVKEP---GESP----------IFWYAPECLRES---RFSSASDVWSFGVTLYEL 205
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
550-856 5.72e-13

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


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 71.37  E-value: 5.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  550 SRYETDFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKlVLLSDDKENSRI--LREVMTLSRLHHEHVVRYYtawvetean 627
Cdd:cd07864    3 KRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKK-VRLDNEKEGFPItaIREIKILRQLNHRSVVNLK--------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  628 DTVTEIISsdseslsqslnmAVDFRQssslpadklssldihfeddynssadeeDPEASDISFQYSntsdkegssDKD-SS 706
Cdd:cd07864   73 EIVTDKQD------------ALDFKK---------------------------DKGAFYLVFEYM---------DHDlMG 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  707 IEEASSVKTQENGLNAtlyiqmeyceklslqdiirdkipvdemwrLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNV 786
Cdd:cd07864  105 LLESGLVHFSEDHIKS-----------------------------FMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQI 155
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  787 KLGDFGLATENEnyQDNNDKWKNRqsadedlttgVGTALYVAPELLSRRNgvRYDAKVDMYSLGIILFEM 856
Cdd:cd07864  156 KLADFGLARLYN--SEESRPYTNK----------VITLWYRPPELLLGEE--RYGPAIDVWSCGCILGEL 211
pknD PRK13184
serine/threonine-protein kinase PknD;
725-877 6.17e-13

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 74.04  E-value: 6.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   725 YIQMEYCEKLSLQDIIR-------------DKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDF 791
Cdd:PRK13184   78 YYTMPYIEGYTLKSLLKsvwqkeslskelaEKTSVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDW 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   792 GLATENENYQDN--NDKWKNRQSADEDLTTG---VGTALYVAPEllsRRNGVRYDAKVDMYSLGIILFEMcMTFSTSMER 866
Cdd:PRK13184  158 GAAIFKKLEEEDllDIDVDERNICYSSMTIPgkiVGTPDYMAPE---RLLGVPASESTDIYALGVILYQM-LTLSFPYRR 233
                         170
                  ....*....|....*.
gi 63054755   867 -----IRIIDTIRSPS 877
Cdd:PRK13184  234 kkgrkISYRDVILSPI 249
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
724-921 6.32e-13

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: 71.21  E-value: 6.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDII-RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEnenyqd 802
Cdd:cd06657   92 LWVVMEFLEGGALTDIVtHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQ------ 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  803 NNDKWKNRQSAdedlttgVGTALYVAPELLSRrngVRYDAKVDMYSLGIILFEMCMTFSTSMER--IRIIDTIRS--Psi 878
Cdd:cd06657  166 VSKEVPRRKSL-------VGTPYWMAPELISR---LPYGPEVDIWSLGIMVIEMVDGEPPYFNEppLKAMKMIRDnlP-- 233
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 63054755  879 sfPSTFPFSRASHEFK-VIHCLLQHDPTKRPSSQELLE----SEAIPP 921
Cdd:cd06657  234 --PKLKNLHKVSPSLKgFLDRLLVRDPAQRATAAELLKhpflAKAGPP 279
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
755-907 6.77e-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: 71.97  E-value: 6.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQDNNdkwknrqsadedlTTGVGTALYVAPELLSR 834
Cdd:cd05602  116 EIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEPNGTT-------------STFCGTPEYLAPEVLHK 182
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63054755  835 RNgvrYDAKVDMYSLGIILFEMCMTFSTSMER--IRIIDTIRSPSISFPSTFPFSrASHefkVIHCLLQHDPTKR 907
Cdd:cd05602  183 QP---YDRTVDWWCLGAVLYEMLYGLPPFYSRntAEMYDNILNKPLQLKPNITNS-ARH---LLEGLLQKDRTKR 250
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
723-856 6.85e-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: 6.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  723 TLYIQMEYCEKLSLQDIIRD-KIPVDEMW-RLF-RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVkLGDFGL--ATEN 797
Cdd:cd14063   70 HLAIVTSLCKGRTLYSLIHErKEKFDFNKtVQIaQQICQGMGYLHAKGIIHKDLKSKNIFLENGRVV-ITDFGLfsLSGL 148
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  798 ENYQDNNDKWKNRQsadedlttgvGTALYVAPEL-------LSRRNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd14063  149 LQPGRREDTLVIPN----------GWLCYLAPEIiralspdLDFEESLPFTKASDVYAFGTVWYEL 204
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
723-919 7.43e-13

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: 70.42  E-value: 7.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  723 TLYIQMEYCEKLSLQDIIRDKIPVDE---MWrLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVkLGDFGLATenen 799
Cdd:cd13995   70 TVHLFMEAGEGGSVLEKLESCGPMREfeiIW-VTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV-LVDFGLSV---- 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  800 yQDNNDKWKNRqsadeDLTtgvGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMcMTFSTSMERiriidtiRSPSIS 879
Cdd:cd13995  144 -QMTEDVYVPK-----DLR---GTEIYMSPEVILCRG---HNTKADIYSLGATIIHM-QTGSPPWVR-------RYPRSA 203
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 63054755  880 FPSTF-------------PFSRASHEFKVIHCLLQHDPTKRPSSQELLESEAI 919
Cdd:cd13995  204 YPSYLyiihkqapplediAQDCSPAMRELLEAALERNPNHRSSAAELLKHEAL 256
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
724-915 7.52e-13

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: 70.41  E-value: 7.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIR--DKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFL----DENRNVKLGDFGLATen 797
Cdd:cd14183   79 LYLVMELVKGGDLFDAITstNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSLKLGDFGLAT-- 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  798 enyqdnndkwknrqSADEDLTTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMCMTF----STSMERIRIIDTI 873
Cdd:cd14183  157 --------------VVDGPLYTVCGTPTYVAPEIIAETG---YGLKVDIWAAGVITYILLCGFppfrGSGDDQEVLFDQI 219
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 63054755  874 RSPSISFPSTFPFSRASHEFKVIHCLLQHDPTKRPSSQELLE 915
Cdd:cd14183  220 LMGQVDFPSPYWDNVSDSAKELITMMLQVDVDQRYSALQVLE 261
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
723-914 7.96e-13

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 70.50  E-value: 7.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  723 TLYIQMEYCEKLSLQDIIRDKIPVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATeneny 800
Cdd:cd06651   85 TLTIFMEYMPGGSVKDQLKAYGALTEsvTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASK----- 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  801 qdnndKWKNRQSADEDLTTGVGTALYVAPELLSrrnGVRYDAKVDMYSLGIILFEMCMTFSTSMERIRIIDTIRSPSISF 880
Cdd:cd06651  160 -----RLQTICMSGTGIRSVTGTPYWMSPEVIS---GEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPT 231
                        170       180       190
                 ....*....|....*....|....*....|....
gi 63054755  881 PSTFPFSRASHEFKVIHCLLQhDPTKRPSSQELL 914
Cdd:cd06651  232 NPQLPSHISEHARDFLGCIFV-EARHRPSAEELL 264
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
724-899 8.40e-13

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: 72.01  E-value: 8.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDII--RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAT------ 795
Cdd:cd05627   77 LYLIMEFLPGGDMMTLLmkKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTglkkah 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  796 ------------------ENENYQDNNDKWKN--RQSAdedlTTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFE 855
Cdd:cd05627  157 rtefyrnlthnppsdfsfQNMNSKRKAETWKKnrRQLA----YSTVGTPDYIAPEVFMQTG---YNKLCDWWSLGVIMYE 229
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 63054755  856 MCMTF-----STSMERIRIIDTIRSpSISFPSTFPFSRASHEFKVIHCL 899
Cdd:cd05627  230 MLIGYppfcsETPQETYRKVMNWKE-TLVFPPEVPISEKAKDLILRFCT 277
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
723-855 8.62e-13

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


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 70.42  E-value: 8.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  723 TLYIQMEYCEKLSLQDIIRDKIPVDE-MWRLF-RQILEALAYIHSRGMMHRDLKPGNIFLD-ENRN--------VKLGDF 791
Cdd:cd14201   79 SVFLVMEYCNGGDLADYLQAKGTLSEdTIRVFlQQIAAAMRILHSKGIIHRDLKPQNILLSyASRKkssvsgirIKIADF 158
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63054755  792 GLATENENyqdnndkwkNRQSAdedltTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFE 855
Cdd:cd14201  159 GFARYLQS---------NMMAA-----TLCGSPMYMAPEVIMSQH---YDAKADLWSIGTVIYQ 205
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
280-505 9.27e-13

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: 70.44  E-value: 9.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  280 TEDGKREIQELEYELESLKVIRHDLLASIYEYQLERETRgygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNIL 359
Cdd:cd06653   41 SQETSKEVNALECEIQLLKNLRHDRIVQYYGCLRDPEEK----KLSIFVEYMPGGSVKDQLKAYGALTENVTRRYTRQIL 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  360 EGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDMNAShpfNINSQSITNIlPEGLYPPEVSESSFAaa 439
Cdd:cd06653  117 QGVSYLHSNMIVHRDIKGANILRDSAGN---VKLGDFGASKRIQTICMS---GTGIKSVTGT-PYWMSPEVISGEGYG-- 187
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054755  440 sRKTDIWCFGLLVLQMLCGAHVLNKFSSL----KLIMTHVIPLLPGSYQDLVRRCLMR---DSRKRPSAIDLL 505
Cdd:cd06653  188 -RKADVWSVACTVVEMLTEKPPWAEYEAMaaifKIATQPTKPQLPDGVSDACRDFLRQifvEEKRRPTAEFLL 259
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
754-917 1.10e-12

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: 69.56  E-value: 1.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  754 RQILEALAYIHSRGMMHRDLKPGNIF-LDENRN-VKLGDFGLAtenenyqdnndkwkNRQSADEDLTTGVGTALYVAPEL 831
Cdd:cd14103   98 RQICEGVQYMHKQGILHLDLKPENILcVSRTGNqIKIIDFGLA--------------RKYDPDKKLKVLFGTPEFVAPEV 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  832 LSrrngvrYDA---KVDMYSLGIILFEMCMTFS-----TSMERIRIIdTIRSPSISFPStfpFSRASHEFK-VIHCLLQH 902
Cdd:cd14103  164 VN------YEPisyATDMWSVGVICYVLLSGLSpfmgdNDAETLANV-TRAKWDFDDEA---FDDISDEAKdFISKLLVK 233
                        170
                 ....*....|....*
gi 63054755  903 DPTKRPSSQELLESE 917
Cdd:cd14103  234 DPRKRMSAAQCLQHP 248
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
755-856 1.16e-12

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


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 71.11  E-value: 1.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENenyqdnndkwknrQSADEDLTTGVGTALYVAPELLSr 834
Cdd:cd05619  114 EIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKEN-------------MLGDAKTSTFCGTPDYIAPEILL- 179
                         90       100
                 ....*....|....*....|..
gi 63054755  835 rnGVRYDAKVDMYSLGIILFEM 856
Cdd:cd05619  180 --GQKYNTSVDWWSFGVLLYEM 199
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
724-913 1.18e-12

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: 70.36  E-value: 1.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDKIPVDEMWRL-FRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENEnyqd 802
Cdd:cd14200  100 LYMVFDLLRKGPVMEVPSDKPFSEDQARLyFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGHVKIADFGVSNQFE---- 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  803 nndkwknrqSADEDLTTGVGTALYVAPELLSrRNGVRYDAK-VDMYSLGIILFemCMTFStsmeRIRIID--------TI 873
Cdd:cd14200  176 ---------GNDALLSSTAGTPAFMAPETLS-DSGQSFSGKaLDVWAMGVTLY--CFVYG----KCPFIDefilalhnKI 239
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 63054755  874 RSPSISFPSTfpfSRASHEFK-VIHCLLQHDPTKRPSSQEL 913
Cdd:cd14200  240 KNKPVEFPEE---PEISEELKdLILKMLDKNPETRITVPEI 277
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
323-511 1.26e-12

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: 69.94  E-value: 1.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  323 RLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGftrTL 402
Cdd:cd05581   75 KLYFVLEYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMH---IKITDFG---TA 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  403 RDMNASHPFNINSQSITNILPEGL-----------Y-PPEV-SESSFAAASrktDIWCFGLLVLQMLCGAHVLNKfSSLK 469
Cdd:cd05581  149 KVLGPDSSPESTKGDADSQIAYNQaraasfvgtaeYvSPELlNEKPAGKSS---DLWALGCIIYQMLTGKPPFRG-SNEY 224
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 63054755  470 LIMTHVI-------PLLPGSYQDLVRRCLMRDSRKRPSAIDLLSSHVIR 511
Cdd:cd05581  225 LTFQKIVkleyefpENFPPDAKDLIQKLLVLDPSKRLGVNENGGYDELK 273
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
755-856 1.28e-12

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: 71.60  E-value: 1.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQDNN--------------------DKWKNRQSAD 814
Cdd:cd05600  119 EMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASGTLSPKKIEsmkirleevkntafleltakERRNIYRAMR 198
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 63054755  815 EDLT----TGVGTALYVAPELLsrrNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd05600  199 KEDQnyanSVVGSPDYMAPEVL---RGEGYDLTVDYWSLGCILFEC 241
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
725-860 1.33e-12

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: 70.16  E-value: 1.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  725 YIQMEYCEKLSLQD-IIRDKIPVDEMWR-LFRQILEALAYIHSRGMMHRDLKPGNIF----------------------L 780
Cdd:cd14096   82 YIVLELADGGEIFHqIVRLTYFSEDLSRhVITQVASAVKYLHEIGVVHRDIKPENLLfepipfipsivklrkadddetkV 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  781 DENR-----------NVKLGDFGLAtenenyqdnndkwknRQSADEDLTTGVGTALYVAPELLsrrNGVRYDAKVDMYSL 849
Cdd:cd14096  162 DEGEfipgvggggigIVKLADFGLS---------------KQVWDSNTKTPCGTVGYTAPEVV---KDERYSKKVDMWAL 223
                        170
                 ....*....|.
gi 63054755  850 GIILFEMCMTF 860
Cdd:cd14096  224 GCVLYTLLCGF 234
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
724-856 1.50e-12

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: 71.58  E-value: 1.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYC---EKLSLQDIIRDKIPVDeMWRLF-RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATenen 799
Cdd:cd05624  147 LYLVMDYYvggDLLTLLSKFEDKLPED-MARFYiGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSCL---- 221
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  800 yqdnndkwKNRQSADEDLTTGVGTALYVAPELL-SRRNGV-RYDAKVDMYSLGIILFEM 856
Cdd:cd05624  222 --------KMNDDGTVQSSVAVGTPDYISPEILqAMEDGMgKYGPECDWWSLGVCMYEM 272
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
697-856 1.55e-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: 1.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  697 KEGSSDKDSSIEEASSVKT--QENGLN--------ATLYIQMEYCEK--LSLQDIIRDKIPVDEMWRLFRQILEALAYIH 764
Cdd:cd07848   38 EENEEVKETTLRELKMLRTlkQENIVElkeafrrrGKLYLVFEYVEKnmLELLEEMPNGVPPEKVRSYIYQLIKAIHWCH 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  765 SRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenENYQDNNDKwknrqsadeDLTTGVGTALYVAPELLSrrnGVRYDAKV 844
Cdd:cd07848  118 KNDIVHRDIKPENLLISHNDVLKLCDFGFA---RNLSEGSNA---------NYTEYVATRWYRSPELLL---GAPYGKAV 182
                        170
                 ....*....|..
gi 63054755  845 DMYSLGIILFEM 856
Cdd:cd07848  183 DMWSVGCILGEL 194
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
728-858 1.56e-12

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


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 70.08  E-value: 1.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  728 MEYCEKLSLQDIIRDKiPVD--EMWRLFRQILEALAYIHSR---------GMMHRDLKPGNIFLDENRNVKLGDFGLATe 796
Cdd:cd14054   73 LEYAPKGSLCSYLREN-TLDwmSSCRMALSLTRGLAYLHTDlrrgdqykpAIAHRDLNSRNVLVKADGSCVICDFGLAM- 150
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  797 neNYQDNNDKWKNRQSADEDLTTGVGTALYVAPELLSR----RNGVRYDAKVDMYSLGIILFEMCM 858
Cdd:cd14054  151 --VLRGSSLVRGRPGAAENASISEVGTLRYMAPEVLEGavnlRDCESALKQVDVYALGLVLWEIAM 214
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
327-507 1.58e-12

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: 69.64  E-value: 1.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  327 LQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDmn 406
Cdd:cd13994   76 VMEYCPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGV---LKLTDFGTAEVFGM-- 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  407 ashPFNINSqsitnILPEGLY------PPEV-SESSFAAasRKTDIWCFGLLVLQMLCGAHV--LNKFS-------SLKL 470
Cdd:cd13994  151 ---PAEKES-----PMSAGLCgsepymAPEVfTSGSYDG--RAVDVWSCGIVLFALFTGRFPwrSAKKSdsaykayEKSG 220
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 63054755  471 IMTHVIPLLPGSY-----QDLVRRCLMRDSRKRPSAIDLLSS 507
Cdd:cd13994  221 DFTNGPYEPIENLlpsecRRLIYRMLHPDPEKRITIDEALND 262
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
718-856 1.73e-12

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: 70.10  E-value: 1.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  718 NGLNATLYIQMEYCEKLSLQDII-RDKIPVDEMWRLFRQILEALAYIHSR----GMM-----HRDLKPGNIFLDENRNVK 787
Cdd:cd14055   68 VGLDRQYWLITAYHENGSLQDYLtRHILSWEDLCKMAGSLARGLAHLHSDrtpcGRPkipiaHRDLKSSNILVKNDGTCV 147
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054755  788 LGDFGLATenenyqdnndKWKNRQSADEDLTTG-VGTALYVAPELL-SRRNGVRYDA--KVDMYSLGIILFEM 856
Cdd:cd14055  148 LADFGLAL----------RLDPSLSVDELANSGqVGTARYMAPEALeSRVNLEDLESfkQIDVYSMALVLWEM 210
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
721-915 1.94e-12

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: 69.24  E-value: 1.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  721 NATLYIQMEYCEKLSLQDIIRDK----IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATE 796
Cdd:cd05082   72 KGGLYIVTEYMAKGSLVDYLRSRgrsvLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKE 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  797 NENYQDnndkwknrqsadedltTGVGTALYVAPELLSRRngvRYDAKVDMYSLGIILFEMCMTFSTSMERIRIIDTIRSP 876
Cdd:cd05082  152 ASSTQD----------------TGKLPVKWTAPEALREK---KFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPRV 212
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 63054755  877 SISFPSTFPFSRASHEFKVIHCLLQHDPTKRPSSQELLE 915
Cdd:cd05082  213 EKGYKMDAPDGCPPAVYDVMKNCWHLDAAMRPSFLQLRE 251
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
724-915 1.98e-12

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 69.12  E-value: 1.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDK---IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEneny 800
Cdd:cd14186   76 VYLVLEMCHNGEMSRYLKNRkkpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQ---- 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  801 qdnndkwknRQSADEDLTTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMCM--------TFSTSMERIRIIDT 872
Cdd:cd14186  152 ---------LKMPHEKHFTMCGTPNYISPEIATRSA---HGLESDVWSLGCMFYTLLVgrppfdtdTVKNTLNKVVLADY 219
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 63054755  873 IRSPSISFPSTfpfsrashefKVIHCLLQHDPTKRPSSQELLE 915
Cdd:cd14186  220 EMPAFLSREAQ----------DLIHQLLRKNPADRLSLSSVLD 252
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
752-914 2.09e-12

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: 69.69  E-value: 2.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  752 LFRQILEALAYIHSRGMMHRDLKPGNIFL---DENRNVKLGDFGLAtenenyqdnndkwkNRQSADEDLTTGVGTALYVA 828
Cdd:cd14168  113 LIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLS--------------KMEGKGDVMSTACGTPGYVA 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  829 PELLSRRNgvrYDAKVDMYSLGIILFEMCMTFSTSMER--IRIIDTIRSPSISFPSTF--PFSRASHEFkvIHCLLQHDP 904
Cdd:cd14168  179 PEVLAQKP---YSKAVDCWSIGVIAYILLCGYPPFYDEndSKLFEQILKADYEFDSPYwdDISDSAKDF--IRNLMEKDP 253
                        170
                 ....*....|
gi 63054755  905 TKRPSSQELL 914
Cdd:cd14168  254 NKRYTCEQAL 263
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
755-916 2.31e-12

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: 70.08  E-value: 2.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATenenyqdnnDKWKNRQSADedlttgVGTALYVAPELLSR 834
Cdd:cd14223  111 EIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLAC---------DFSKKKPHAS------VGTHGYMAPEVLQK 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  835 rnGVRYDAKVDMYSLGIILFEMCMTFST-SMERIRIIDTIRSPSISFPSTFPFSRASHEFKVIHCLLQHDPTKR-----P 908
Cdd:cd14223  176 --GVAYDSSADWFSLGCMLFKLLRGHSPfRQHKTKDKHEIDRMTLTMAVELPDSFSPELRSLLEGLLQRDVNRRlgcmgR 253

                 ....*...
gi 63054755  909 SSQELLES 916
Cdd:cd14223  254 GAQEVKEE 261
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
555-856 2.91e-12

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


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 68.99  E-value: 2.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  555 DFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKE-NSRILREVMTLSRLHHEHVVRyytawveteandtvtei 633
Cdd:cd07861    1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEEGvPSTAIREISLLKELQHPNIVC----------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  634 issdseslsqslnmavdfrqssslpadklssldihFEDdynssadeedpeasdisfqysntsdkegssdkdssieeassV 713
Cdd:cd07861   64 -----------------------------------LED-----------------------------------------V 67
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  714 KTQENglnaTLYIQMEYcekLSLqDIIR--DKIPVDEMWRLFR------QILEALAYIHSRGMMHRDLKPGNIFLDENRN 785
Cdd:cd07861   68 LMQEN----RLYLVFEF---LSM-DLKKylDSLPKGKYMDAELvksylyQILQGILFCHSRRVLHRDLKPQNLLIDNKGV 139
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 63054755  786 VKLGDFGLAtenenyqdnndkwKNRQSADEDLTTGVGTALYVAPELLsrRNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd07861  140 IKLADFGLA-------------RAFGIPVRVYTHEVVTLWYRAPEVL--LGSPRYSTPVDIWSIGTIFAEM 195
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
755-907 3.23e-12

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: 69.52  E-value: 3.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQDNNDkwknrqsadedltTGVGTALYVAPELLSr 834
Cdd:cd05585  102 ELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKDDDKTN-------------TFCGTPEYLAPELLL- 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  835 rnGVRYDAKVDMYSLGIILFEMCMTF-------STSMERIRIIDTIRspsisFPSTFPfsraSHEFKVIHCLLQHDPTKR 907
Cdd:cd05585  168 --GHGYTKAVDWWTLGVLLYEMLTGLppfydenTNEMYRKILQEPLR-----FPDGFD----RDAKDLLIGLLNRDPTKR 236
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
748-907 3.37e-12

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: 69.71  E-value: 3.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  748 EMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATenenyqdnnDKWKNRQSADedlttgVGTALYV 827
Cdd:cd05633  109 EMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLAC---------DFSKKKPHAS------VGTHGYM 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  828 APELLSRrnGVRYDAKVDMYSLGIILFEMCMTFS-----TSMERIRIIDTIRSPSISFPSTFpfsraSHEFK-VIHCLLQ 901
Cdd:cd05633  174 APEVLQK--GTAYDSSADWFSLGCMLFKLLRGHSpfrqhKTKDKHEIDRMTLTVNVELPDSF-----SPELKsLLEGLLQ 246

                 ....*.
gi 63054755  902 HDPTKR 907
Cdd:cd05633  247 RDVSKR 252
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
705-894 3.49e-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: 3.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  705 SSIEEASSVKTQENGLNATLY--IQMEYCEKLSLQDIIRD-KIPVDEMWRLFR---------QILEALAYIHSRGMMHRD 772
Cdd:cd07871   49 TAIREVSLLKNLKHANIVTLHdiIHTERCLTLVFEYLDSDlKQYLDNCGNLMSmhnvkifmfQLLRGLSYCHKRKILHRD 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  773 LKPGNIFLDENRNVKLGDFGLAtenenyqdnndkwKNRQSADEDLTTGVGTALYVAPELLsrRNGVRYDAKVDMYSLGII 852
Cdd:cd07871  129 LKPQNLLINEKGELKLADFGLA-------------RAKSVPTKTYSNEVVTLWYRPPDVL--LGSTEYSTPIDMWGVGCI 193
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 63054755  853 LFEMC-----MTFSTSMERIRIIdtIRSPSISFPSTFPFSRASHEFK 894
Cdd:cd07871  194 LYEMAtgrpmFPGSTVKEELHLI--FRLLGTPTEETWPGVTSNEEFR 238
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
697-856 4.29e-12

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: 68.53  E-value: 4.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  697 KEGSSDKDSSIEEASSVKT-QENGL---------NATLYIQMEYCEKLSLQDIIRD----KIPVDEMWRLFRQILEALAY 762
Cdd:cd05072   40 KPGTMSVQAFLEEANLMKTlQHDKLvrlyavvtkEEPIYIITEYMAKGSLLDFLKSdeggKVLLPKLIDFSAQIAEGMAY 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  763 IHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENEnyqdnNDKWKNRQSADEDLTtgvgtalYVAPELLsrrNGVRYDA 842
Cdd:cd05072  120 IERKNYIHRDLRAANVLVSESLMCKIADFGLARVIE-----DNEYTAREGAKFPIK-------WTAPEAI---NFGSFTI 184
                        170
                 ....*....|....
gi 63054755  843 KVDMYSLGIILFEM 856
Cdd:cd05072  185 KSDVWSFGILLYEI 198
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
556-856 4.47e-12

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: 68.61  E-value: 4.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  556 FEELEFLGRGGFGEVVKVKNRIDGRFYAVKKlVLLSDDKEN--SRILREVMTLSRLHHEHVVRYYTAwveteandtvtei 633
Cdd:cd07839    2 YEKLEKIGEGTYGTVFKAKNRETHEIVALKR-VRLDDDDEGvpSSALREICLLKELKHKNIVRLYDV------------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  634 issdseslsqslnmavdfrqssslpadklssldIHfeddynssadeedpeasdisfqysntSDKEgssdkdssieeassv 713
Cdd:cd07839   68 ---------------------------------LH--------------------------SDKK--------------- 73
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  714 ktqenglnatLYIQMEYCEKlSLQ---DIIRDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGD 790
Cdd:cd07839   74 ----------LTLVFEYCDQ-DLKkyfDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLAD 142
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  791 FGLAtenenyqdNNDKWKNRQSADEdlttgVGTALYVAPELLSRRNGvrYDAKVDMYSLGIILFEM 856
Cdd:cd07839  143 FGLA--------RAFGIPVRCYSAE-----VVTLWYRPPDVLFGAKL--YSTSIDMWSAGCIFAEL 193
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
726-856 4.54e-12

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


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 69.00  E-value: 4.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  726 IQMEYCEKLSLQDIIRD--KIPVDEMWRLFRQILEALAYIHS-RGMMHRDLKPGNIFLDENRNVKLGDFGLATenenyqd 802
Cdd:cd06615   76 ICMEHMDGGSLDQVLKKagRIPENILGKISIAVLRGLTYLREkHKIMHRDVKPSNILVNSRGEIKLCDFGVSG------- 148
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 63054755  803 nndkwknrQSADEDLTTGVGTALYVAPEllsRRNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd06615  149 --------QLIDSMANSFVGTRSYMSPE---RLQGTHYTVQSDIWSLGLSLVEM 191
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
724-898 4.71e-12

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: 69.68  E-value: 4.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDII--RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAT------ 795
Cdd:cd05628   76 LYLIMEFLPGGDMMTLLmkKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTglkkah 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  796 ------------------ENENYQDNNDKWK--NRQSAdedlTTGVGTALYVAPELLsRRNGvrYDAKVDMYSLGIILFE 855
Cdd:cd05628  156 rtefyrnlnhslpsdftfQNMNSKRKAETWKrnRRQLA----FSTVGTPDYIAPEVF-MQTG--YNKLCDWWSLGVIMYE 228
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 63054755  856 MCMTF-----STSMERIRIIDTIRSpSISFPSTFPFSRASHEFKVIHC 898
Cdd:cd05628  229 MLIGYppfcsETPQETYKKVMNWKE-TLIFPPEVPISEKAKDLILRFC 275
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
748-916 5.00e-12

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: 68.59  E-value: 5.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  748 EMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDE-NRNVKLGDFGLAtenenyqdnndkwKNRQSADEDLTTGVGTALY 826
Cdd:cd13974  133 EALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKrTRKITITNFCLG-------------KHLVSEDDLLKDQRGSPAY 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  827 VAPELLSrrnGVRYDAK-VDMYSLGIILFEMC---MTFSTSMERiRIIDTIRSPSISFPSTfpfSRASHEFK-VIHCLLQ 901
Cdd:cd13974  200 ISPDVLS---GKPYLGKpSDMWALGVVLFTMLygqFPFYDSIPQ-ELFRKIKAAEYTIPED---GRVSENTVcLIRKLLV 272
                        170
                 ....*....|....*
gi 63054755  902 HDPTKRPSSQELLES 916
Cdd:cd13974  273 LNPQKRLTASEVLDS 287
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
697-856 5.14e-12

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: 67.99  E-value: 5.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  697 KEGSSDKDSSIEEASSVKTQENG----LNAT-----LYIQMEYCEKLSLQDIIRD----KIPVDEMWRLFRQILEALAYI 763
Cdd:cd05067   40 KQGSMSPDAFLAEANLMKQLQHQrlvrLYAVvtqepIYIITEYMENGSLVDFLKTpsgiKLTINKLLDMAAQIAEGMAFI 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  764 HSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENEnyqdnNDKWKNRQSADEDLTtgvgtalYVAPELLsrrNGVRYDAK 843
Cdd:cd05067  120 EERNYIHRDLRAANILVSDTLSCKIADFGLARLIE-----DNEYTAREGAKFPIK-------WTAPEAI---NYGTFTIK 184
                        170
                 ....*....|...
gi 63054755  844 VDMYSLGIILFEM 856
Cdd:cd05067  185 SDVWSFGILLTEI 197
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
742-914 5.16e-12

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: 68.03  E-value: 5.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  742 DKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENR---NVKLGDFGLATENENyqdnndkwknrqsaDEDLT 818
Cdd:cd14198  105 EMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYplgDIKIVDFGMSRKIGH--------------ACELR 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  819 TGVGTALYVAPELLSrrngvrYD---AKVDMYSLGIILFeMCMTFSTSM---ERIRIIDTIRSPSISFpSTFPFSRASHE 892
Cdd:cd14198  171 EIMGTPEYLAPEILN------YDpitTATDMWNIGVIAY-MLLTHESPFvgeDNQETFLNISQVNVDY-SEETFSSVSQL 242
                        170       180
                 ....*....|....*....|...
gi 63054755  893 FK-VIHCLLQHDPTKRPSSQELL 914
Cdd:cd14198  243 ATdFIQKLLVKNPEKRPTAEICL 265
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
724-856 5.17e-12

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: 69.65  E-value: 5.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDkIPVDEMWRLF--RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATenenyq 801
Cdd:cd05622  148 LYMVMEYMPGGDLVNLMSN-YDVPEKWARFytAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCM------ 220
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  802 dnndkwKNRQSADEDLTTGVGTALYVAPELLSRRNGVRYDAK-VDMYSLGIILFEM 856
Cdd:cd05622  221 ------KMNKEGMVRCDTAVGTPDYISPEVLKSQGGDGYYGReCDWWSVGVFLYEM 270
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
748-915 5.42e-12

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: 68.52  E-value: 5.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  748 EMWRLFRQILEALAYIHSRGMMHRDLKPGNI---FLDENRNVKLGDFGLATeneNYQDNNdkwKNRQSADEDLTTGVGTA 824
Cdd:cd14174  101 EASRVVRDIASALDFLHTKGIAHRDLKPENIlceSPDKVSPVKICDFDLGS---GVKLNS---ACTPITTPELTTPCGSA 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  825 LYVAPELLS--RRNGVRYDAKVDMYSLGIILFEM----------CMTfSTSMER--------IRIIDTIRSPSISFPSTf 884
Cdd:cd14174  175 EYMAPEVVEvfTDEATFYDKRCDLWSLGVILYIMlsgyppfvghCGT-DCGWDRgevcrvcqNKLFESIQEGKYEFPDK- 252
                        170       180       190
                 ....*....|....*....|....*....|..
gi 63054755  885 PFSRASHEFK-VIHCLLQHDPTKRPSSQELLE 915
Cdd:cd14174  253 DWSHISSEAKdLISKLLVRDAKERLSAAQVLQ 284
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
726-854 5.92e-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: 68.67  E-value: 5.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  726 IQMEYCEKLSLQDIIRDK-----IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNI--FLDENRNV--KLGDFGLATE 796
Cdd:cd13988   70 LVMELCPCGSLYTVLEEPsnaygLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNImrVIGEDGQSvyKLTDFGAARE 149
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054755  797 NENyqdnndkwknrqsaDEDLTTGVGTALYVAPEL-----LSRRNGVRYDAKVDMYSLGIILF 854
Cdd:cd13988  150 LED--------------DEQFVSLYGTEEYLHPDMyeravLRKDHQKKYGATVDLWSIGVTFY 198
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
752-858 6.04e-12

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: 68.62  E-value: 6.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  752 LFRQILEALAYIHSRGMMHRDLKPGNIFLDE-NRNVKLGDFGLATE---NENYQDNNDKWKNRQSADEDLTTGVGT---- 823
Cdd:cd14013  125 IMRQILVALRKLHSTGIVHRDVKPQNIIVSEgDGQFKIIDLGAAADlriGINYIPKEFLLDPRYAPPEQYIMSTQTpsap 204
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 63054755  824 ----ALYVAPELLSRRNGVRYdakvDMYSLGIILFEMCM 858
Cdd:cd14013  205 papvAAALSPVLWQMNLPDRF----DMYSAGVILLQMAF 239
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
751-856 6.14e-12

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 70.11  E-value: 6.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   751 RLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQDNND-KWknrqsadedlttgVGTALYVAP 829
Cdd:PHA03210  271 AIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLGDFGTAMPFEKEREAFDyGW-------------VGTVATNSP 337
                          90       100
                  ....*....|....*....|....*..
gi 63054755   830 ELLSRRNgvrYDAKVDMYSLGIILFEM 856
Cdd:PHA03210  338 EILAGDG---YCEITDIWSCGLILLDM 361
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
724-930 6.81e-12

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: 68.90  E-value: 6.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKlSLQDIIRDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLA-TENENYQd 802
Cdd:cd07876  101 VYLVMELMDA-NLCQVIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLArTACTNFM- 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  803 nndkwknrqsadedLTTGVGTALYVAPELLSrrnGVRYDAKVDMYSLGIILFEMC---MTF-----------------ST 862
Cdd:cd07876  179 --------------MTPYVVTRYYRAPEVIL---GMGYKENVDIWSVGCIMGELVkgsVIFqgtdhidqwnkvieqlgTP 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  863 SMERI-RIIDTIRS--------PSISFPSTFP---FSRASHEFKV--------IHCLLQHDPTKRPSSQELL-------- 914
Cdd:cd07876  242 SAEFMnRLQPTVRNyvenrpqyPGISFEELFPdwiFPSESERDKLktsqardlLSKMLVIDPDKRISVDEALrhpyitvw 321
                        250       260
                 ....*....|....*....|
gi 63054755  915 ----ESEAIPPKVGEEFIQE 930
Cdd:cd07876  322 ydpaEAEAPPPQIYDAQLEE 341
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
718-857 8.30e-12

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: 67.68  E-value: 8.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  718 NGLNATLYIQMEYCEKLSLQDIIRD-KIPVDEMWRLFRQILEALAYIHSR--------GMMHRDLKPGNIFLDENRNVKL 788
Cdd:cd14056   62 TGSWTQLWLITEYHEHGSLYDYLQRnTLDTEEALRLAYSAASGLAHLHTEivgtqgkpAIAHRDLKSKNILVKRDGTCCI 141
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054755  789 GDFGLATENENYQDNNDKWKNRQsadedlttgVGTALYVAPELL-SRRNGVRYDA--KVDMYSLGIILFEMC 857
Cdd:cd14056  142 ADLGLAVRYDSDTNTIDIPPNPR---------VGTKRYMAPEVLdDSINPKSFESfkMADIYSFGLVLWEIA 204
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
755-914 8.73e-12

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: 67.53  E-value: 8.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenenyqdnndkwKNRQSADEDLTTGVGTALYVAPELLSr 834
Cdd:cd07860  108 QLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLA-------------RAFGVPVRTYTHEVVTLWYRAPEILL- 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  835 rnGVR-YDAKVDMYSLGIILFEMcMT----FSTSME---RIRIIDTIRSPSIS----------FPSTFP-FSRASHEFKV 895
Cdd:cd07860  174 --GCKyYSTAVDIWSLGCIFAEM-VTrralFPGDSEidqLFRIFRTLGTPDEVvwpgvtsmpdYKPSFPkWARQDFSKVV 250
                        170       180
                 ....*....|....*....|....*....
gi 63054755  896 ----------IHCLLQHDPTKRPSSQELL 914
Cdd:cd07860  251 ppldedgrdlLSQMLHYDPNKRISAKAAL 279
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
741-907 9.90e-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: 68.02  E-value: 9.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  741 RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenenyqdnndkwKNRQSADEDLT-T 819
Cdd:cd05614   99 RDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLS-------------KEFLTEEKERTyS 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  820 GVGTALYVAPELLSRRNGvrYDAKVDMYSLGIILFEM---CMTFSTSMER---IRIIDTIRSPSISFPSTF-PFSRashe 892
Cdd:cd05614  166 FCGTIEYMAPEIIRGKSG--HGKAVDWWSLGILMFELltgASPFTLEGEKntqSEVSRRILKCDPPFPSFIgPVAR---- 239
                        170
                 ....*....|....*
gi 63054755  893 fKVIHCLLQHDPTKR 907
Cdd:cd05614  240 -DLLQKLLCKDPKKR 253
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
724-856 1.04e-11

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 68.21  E-value: 1.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKlSLQDIIRDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLA-TENENYQd 802
Cdd:cd07850   80 VYLVMELMDA-NLCQVIQMDLDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLArTAGTSFM- 157
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 63054755  803 nndkwknrqsadedLTTGVGTALYVAPELLSrrnGVRYDAKVDMYSLGIILFEM 856
Cdd:cd07850  158 --------------MTPYVVTRYYRAPEVIL---GMGYKENVDIWSVGCIMGEM 194
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
751-917 1.06e-11

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


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 67.41  E-value: 1.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  751 RLFR-QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenenyqdnndkwKNRQSADEDLTTGVGTALYVAP 829
Cdd:cd07844  101 RLFLfQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLA-------------RAKSVPSKTYSNEVVTLWYRPP 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  830 E-LLSRRNgvrYDAKVDMYSLGIILFEMCM---TFSTS------MERI-RIIDTIRS---PSIS-----FPSTFPF---- 886
Cdd:cd07844  168 DvLLGSTE---YSTSLDMWGVGCIFYEMATgrpLFPGStdvedqLHKIfRVLGTPTEetwPGVSsnpefKPYSFPFyppr 244
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 63054755  887 ---------SRASHEFKVIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd07844  245 plinhaprlDRIPHGEELALKFLQYEPKKRISAAEAMKHP 284
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
724-915 1.17e-11

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: 67.32  E-value: 1.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDKIP----VDEM---WRLFRQILeALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATE 796
Cdd:cd06639   99 LWLVLELCNGGSVTELVKGLLKcgqrLDEAmisYILYGALL-GLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQ 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  797 nenyqdnndkwknRQSADEDLTTGVGTALYVAPELLS--RRNGVRYDAKVDMYSLGIILFEMCMTFS--TSMERIRIIDT 872
Cdd:cd06639  178 -------------LTSARLRRNTSVGTPFWMAPEVIAceQQYDYSYDARCDVWSLGITAIELADGDPplFDMHPVKALFK 244
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 63054755  873 I-RSPSISFPSTFPFSRASHEFkVIHCLLQhDPTKRPSSQELLE 915
Cdd:cd06639  245 IpRNPPPTLLNPEKWCRGFSHF-ISQCLIK-DFEKRPSVTHLLE 286
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
755-914 1.17e-11

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: 67.34  E-value: 1.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenenyqdnndkwKNRQSADEDLTTGVGTALYVAPELLsr 834
Cdd:cd07873  108 QLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLA-------------RAKSIPTKTYSNEVVTLWYRPPDIL-- 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  835 RNGVRYDAKVDMYSLGIILFEMC-----MTFSTSMERIRIIDTIR-SPSisfPSTFPFSRASHEFKVIH-------CLLQ 901
Cdd:cd07873  173 LGSTDYSTQIDMWGVGCIFYEMStgrplFPGSTVEEQLHFIFRILgTPT---EETWPGILSNEEFKSYNypkyradALHN 249
                        170
                 ....*....|...
gi 63054755  902 HDPTKRPSSQELL 914
Cdd:cd07873  250 HAPRLDSDGADLL 262
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
729-914 1.21e-11

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


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 66.80  E-value: 1.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  729 EYCEKLSlqDIIRDKIPVDEMW--RLFRQILEALAYIHSRGMMHRDLKPGNIFLDENR-NVKLGDFGLAT--ENENYQDN 803
Cdd:cd14101   90 QHCQDLF--DYITERGALDESLarRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLRTgDIKLIDFGSGAtlKDSMYTDF 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  804 NdkwknrqsadedlttgvGTALYVAPELLSRRngvRYDA-KVDMYSLGIILFEMcMTFSTSMERiriiDT-IRSPSISFP 881
Cdd:cd14101  168 D-----------------GTRVYSPPEWILYH---QYHAlPATVWSLGILLYDM-VCGDIPFER----DTdILKAKPSFN 222
                        170       180       190
                 ....*....|....*....|....*....|....
gi 63054755  882 stfpfSRASHEFK-VIHCLLQHDPTKRPSSQELL 914
Cdd:cd14101  223 -----KRVSNDCRsLIRSCLAYNPSDRPSLEQIL 251
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
288-511 1.22e-11

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: 66.85  E-value: 1.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  288 QELEYELESLKVIRHDLLASIYEYQLERETrgygwrLYVLQEYSPKFTLFSLLQTVLTLdVETVRAF-SNNILEGLAELH 366
Cdd:cd06623   44 KQLLRELKTLRSCESPYVVKCYGAFYKEGE------ISIVLEYMDGGSLADLLKKVGKI-PEPVLAYiARQILKGLDYLH 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  367 R-LGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDMNAshPFNINSQSITNILPEGLyppeVSES-SFAAasrktD 444
Cdd:cd06623  117 TkRHIIHRDIKPSNLLINSKGE---VKIADFGISKVLENTLD--QCNTFVGTVTYMSPERI----QGESySYAA-----D 182
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63054755  445 IWCFGLLVLQMLCGAH------VLNKFSSLKLIMTHVIPLLPGS-----YQDLVRRCLMRDSRKRPSAIDLLSSHVIR 511
Cdd:cd06623  183 IWSLGLTLLECALGKFpflppgQPSFFELMQAICDGPPPSLPAEefspeFRDFISACLQKDPKKRPSAAELLQHPFIK 260
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
721-861 1.29e-11

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: 67.42  E-value: 1.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  721 NATLYIQMEYCEKlSLQDIIRDK-------IPVDEMWRLFRQILEALAYIHS-RGMMHRDLKPGNIFLDEN-RNVKLGDF 791
Cdd:cd14001   78 DGSLCLAMEYGGK-SLNDLIEERyeaglgpFPAATILKVALSIARALEYLHNeKKILHGDIKSGNVLIKGDfESVKLCDF 156
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 63054755  792 GLATE-NENYQDNNDKWKNRqsadedlttgVGTALYVAPELLSRrNGVRYDaKVDMYSLGIILFEMcMTFS 861
Cdd:cd14001  157 GVSLPlTENLEVDSDPKAQY----------VGTEPWKAKEALEE-GGVITD-KADIFAYGLVLWEM-MTLS 214
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
755-907 1.34e-11

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: 67.80  E-value: 1.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENyqdnndkwknrqsadEDLTTGV--GTALYVAPELL 832
Cdd:cd05587  105 EIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIF---------------GGKTTRTfcGTPDYIAPEII 169
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63054755  833 SRRNgvrYDAKVDMYSLGIILFEMCM---TFSTSMERiRIIDTIRSPSISFPSTfpFSRASHEfkVIHCLLQHDPTKR 907
Cdd:cd05587  170 AYQP---YGKSVDWWAYGVLLYEMLAgqpPFDGEDED-ELFQSIMEHNVSYPKS--LSKEAVS--ICKGLLTKHPAKR 239
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
741-907 1.52e-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: 66.95  E-value: 1.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  741 RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATE---NENyqdnndkwknrqsadEDL 817
Cdd:cd05613   99 RERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEfllDEN---------------ERA 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  818 TTGVGTALYVAPELLsRRNGVRYDAKVDMYSLGIILFEMCM---TFSTSMERIRIIDTIRSPSISFPStFPFSRASHEFK 894
Cdd:cd05613  164 YSFCGTIEYMAPEIV-RGGDSGHDKAVDWWSLGVLMYELLTgasPFTVDGEKNSQAEISRRILKSEPP-YPQEMSALAKD 241
                        170
                 ....*....|...
gi 63054755  895 VIHCLLQHDPTKR 907
Cdd:cd05613  242 IIQRLLMKDPKKR 254
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
723-856 1.71e-11

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: 68.11  E-value: 1.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  723 TLYIQMEYC---EKLSLqdIIRDKIPVDEMWRLF-RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAT--- 795
Cdd:cd05626   75 NLYFVMDYIpggDMMSL--LIRMEVFPEVLARFYiAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTgfr 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  796 --ENENY--------QDN---NDKW---KNRQSADEDLT---------------TGVGTALYVAPELLSRRNgvrYDAKV 844
Cdd:cd05626  153 wtHNSKYyqkgshirQDSmepSDLWddvSNCRCGDRLKTleqratkqhqrclahSLVGTPNYIAPEVLLRKG---YTQLC 229
                        170
                 ....*....|..
gi 63054755  845 DMYSLGIILFEM 856
Cdd:cd05626  230 DWWSVGVILFEM 241
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
744-856 1.80e-11

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: 66.53  E-value: 1.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  744 IPVDEM--WRLFRQILEALAYIHSRGMMHRDLKPGNIFL-----DENRNVKLGDFGLAtenenyqdnndkwknRQSADED 816
Cdd:cd14067  109 MPLGHMltFKIAYQIAAGLAYLHKKNIIFCDLKSDNILVwsldvQEHINIKLSDYGIS---------------RQSFHEG 173
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 63054755  817 LTTGVGTALYVAPELlsrRNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd14067  174 ALGVEGTPGYQAPEI---RPRIVYDEKVDMFSYGMVLYEL 210
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
740-857 1.86e-11

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: 66.36  E-value: 1.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  740 IRDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEnenyqdnndkwknrqsadEDLTT 819
Cdd:cd13975   95 IKAGLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKP------------------EAMMS 156
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 63054755  820 G--VGTALYVAPELLSRrngvRYDAKVDMYSLGIILFEMC 857
Cdd:cd13975  157 GsiVGTPIHMAPELFSG----KYDNSVDVYAFGILFWYLC 192
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
754-854 1.94e-11

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: 66.77  E-value: 1.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  754 RQILEALAYIHSRGMMHRDLKPGNIFLDENRN---VKLGDFGLAtenenyqdnndkwknrQSADEDLT--TGVGTALYVA 828
Cdd:cd14085  105 KQILEAVAYLHENGIVHRDLKPENLLYATPAPdapLKIADFGLS----------------KIVDQQVTmkTVCGTPGYCA 168
                         90       100
                 ....*....|....*....|....*.
gi 63054755  829 PELLSrrnGVRYDAKVDMYSLGIILF 854
Cdd:cd14085  169 PEILR---GCAYGPEVDMWSVGVITY 191
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
697-856 1.97e-11

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: 65.77  E-value: 1.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  697 KEGSSDKDSSIEEASSVKT-QENGL---------NATLYIQMEYCEKLSLQDIIRD----KIPVDEMWRLFRQILEALAY 762
Cdd:cd05034   28 KPGTMSPEAFLQEAQIMKKlRHDKLvqlyavcsdEEPIYIVTELMSKGSLLDYLRTgegrALRLPQLIDMAAQIASGMAY 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  763 IHSRGMMHRDLKPGNIFLDENRNVKLGDFGLA--TENENYQDNND-----KWknrqsadedlttgvgtalyVAPELLSRR 835
Cdd:cd05034  108 LESRNYIHRDLAARNILVGENNVCKVADFGLArlIEDDEYTAREGakfpiKW-------------------TAPEAALYG 168
                        170       180
                 ....*....|....*....|.
gi 63054755  836 ngvRYDAKVDMYSLGIILFEM 856
Cdd:cd05034  169 ---RFTIKSDVWSFGILLYEI 186
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
729-915 2.03e-11

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: 65.96  E-value: 2.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  729 EYCEKLSLQDIIRDKIPVDemW----RLFRQILEALAYIHSRGMMHRDLKPGNIFL--DENR-NVKLGDFGLATENENYQ 801
Cdd:cd14155   68 EYINGGNLEQLLDSNEPLS--WtvrvKLALDIARGLSYLHSKGIFHRDLTSKNCLIkrDENGyTAVVGDFGLAEKIPDYS 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  802 DNNDKwknrqsadedLTTgVGTALYVAPELLsrrNGVRYDAKVDMYSLGIILFEmcmtfstsmerirIIDTIRSPSISFP 881
Cdd:cd14155  146 DGKEK----------LAV-VGSPYWMAPEVL---RGEPYNEKADVFSYGIILCE-------------IIARIQADPDYLP 198
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 63054755  882 STFPFSRASHEFK-------------VIHClLQHDPTKRPSSQELLE 915
Cdd:cd14155  199 RTEDFGLDYDAFQhmvgdcppdflqlAFNC-CNMDPKSRPSFHDIVK 244
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
755-919 2.21e-11

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


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 66.85  E-value: 2.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEnenyqdnndkwknrqSADEDLTTGV--GTALYVAPELL 832
Cdd:cd05590  104 EITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKE---------------GIFNGKTTSTfcGTPDYIAPEIL 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  833 SRrngVRYDAKVDMYSLGIILFEMC---MTFSTSMERiRIIDTIRSPSISFPSTFPFSRAShefkVIHCLLQHDPTKRPS 909
Cdd:cd05590  169 QE---MLYGPSVDWWAMGVLLYEMLcghAPFEAENED-DLFEAILNDEVVYPTWLSQDAVD----ILKAFMTKNPTMRLG 240
                        170
                 ....*....|
gi 63054755  910 SQELLESEAI 919
Cdd:cd05590  241 SLTLGGEEAI 250
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
754-856 2.36e-11

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


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 66.59  E-value: 2.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  754 RQILEALAYIHSRGMMHRDLKPGNIFLDENRN---VKLGDFGLATeneNYQDNNDkwkNRQSADEDLTTGVGTALYVAPE 830
Cdd:cd14173  107 QDIASALDFLHNKGIAHRDLKPENILCEHPNQvspVKICDFDLGS---GIKLNSD---CSPISTPELLTPCGSAEYMAPE 180
                         90       100
                 ....*....|....*....|....*...
gi 63054755  831 LLSRRN--GVRYDAKVDMYSLGIILFEM 856
Cdd:cd14173  181 VVEAFNeeASIYDKRCDLWSLGVILYIM 208
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
316-458 2.53e-11

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: 65.81  E-value: 2.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  316 ETRGYgwrlYV-LQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSgHRTFAKLM 394
Cdd:cd13987   61 ETEDY----YVfAQEYAPYGDLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDK-DCRRVKLC 135
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 63054755  395 DFGFTR----TLRDMNASHPFNinsqsitnilpeglyPPEVSESSFA---AASRKTDIWCFGLLVLQMLCG 458
Cdd:cd13987  136 DFGLTRrvgsTVKRVSGTIPYT---------------APEVCEAKKNegfVVDPSIDVWAFGVLLFCCLTG 191
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
723-856 2.80e-11

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: 65.82  E-value: 2.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  723 TLYIQMEYCEKLSLQDIIRDKIPVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAteneny 800
Cdd:cd06653   80 KLSIFVEYMPGGSVKDQLKAYGALTEnvTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGAS------ 153
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  801 qdnndkwKNRQS---ADEDLTTGVGTALYVAPELLSrrnGVRYDAKVDMYSLGIILFEM 856
Cdd:cd06653  154 -------KRIQTicmSGTGIKSVTGTPYWMSPEVIS---GEGYGRKADVWSVACTVVEM 202
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
726-915 3.18e-11

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: 66.06  E-value: 3.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  726 IQMEYCEKLSLqDIIRdKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATenenyqdnnd 805
Cdd:cd06619   76 ICTEFMDGGSL-DVYR-KIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVST---------- 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  806 kwknrQSADEDLTTGVGTALYVAPEllsRRNGVRYDAKVDMYSLGIILFEMCMTF---------STSMERIRIIDTIRSP 876
Cdd:cd06619  144 -----QLVNSIAKTYVGTNAYMAPE---RISGEQYGIHSDVWSLGISFMELALGRfpypqiqknQGSLMPLQLLQCIVDE 215
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 63054755  877 SisfPSTFPFSRASHEFK--VIHClLQHDPTKRPSSQELLE 915
Cdd:cd06619  216 D---PPVLPVGQFSEKFVhfITQC-MRKQPKERPAPENLMD 252
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
724-856 3.45e-11

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


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 66.36  E-value: 3.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDKIPVDEMWRLF--RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENyq 801
Cdd:cd05591   71 LFFVMEYVNGGDLMFQIQRARKFDEPRARFyaAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGIL-- 148
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 63054755  802 dnndkwknrqsADEDLTTGVGTALYVAPELLSRrngVRYDAKVDMYSLGIILFEM 856
Cdd:cd05591  149 -----------NGKTTTTFCGTPDYIAPEILQE---LEYGPSVDWWALGVLMYEM 189
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
756-856 3.51e-11

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: 66.19  E-value: 3.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  756 ILEALAYIHSRGMMHRDLKPGNI-FLDENRN---VKLGDFGLAtenenyqdnndkwKNRQSADEDLTTGVGTALYVAPEL 831
Cdd:cd14177  107 ITKTVDYLHCQGVVHRDLKPSNIlYMDDSANadsIRICDFGFA-------------KQLRGENGLLLTPCYTANFVAPEV 173
                         90       100
                 ....*....|....*....|....*
gi 63054755  832 LSRRNgvrYDAKVDMYSLGIILFEM 856
Cdd:cd14177  174 LMRQG---YDAACDIWSLGVLLYTM 195
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
755-856 3.53e-11

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: 66.29  E-value: 3.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQDNNdkwknrqsadedlTTGVGTALYVAPELLsr 834
Cdd:cd05588  104 EISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTT-------------STFCGTPNYIAPEIL-- 168
                         90       100
                 ....*....|....*....|..
gi 63054755  835 rNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd05588  169 -RGEDYGFSVDWWALGVLMFEM 189
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
755-914 3.61e-11

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: 66.34  E-value: 3.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQDNNDKWknrqsadedlTTGVGTALYVAPELLSR 834
Cdd:cd07859  111 QLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAFNDTPTAIFW----------TDYVATRWYRAPELCGS 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  835 RNGvRYDAKVDMYSLGIILFEMC--------------------MTFSTSMERI---------RIIDTIR-SPSISFPSTF 884
Cdd:cd07859  181 FFS-KYTPAIDIWSIGCIFAEVLtgkplfpgknvvhqldlitdLLGTPSPETIsrvrnekarRYLSSMRkKQPVPFSQKF 259
                        170       180       190
                 ....*....|....*....|....*....|
gi 63054755  885 PFSRAShEFKVIHCLLQHDPTKRPSSQELL 914
Cdd:cd07859  260 PNADPL-ALRLLERLLAFDPKDRPTAEEAL 288
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
697-915 3.81e-11

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: 65.90  E-value: 3.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  697 KEGSSDKD-----SSIEEASSVKTQENGLN--------ATLYIQMEYCEKLSLQDIIRDKIPVDEMWRLFRQI------- 756
Cdd:cd05053   52 KDDATEKDlsdlvSEMEMMKMIGKHKNIINllgactqdGPLYVVVEYASKGNLREFLRARRPPGEEASPDDPRvpeeqlt 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  757 ---LEALAYIHSRGM--------MHRDLKPGNIFLDENRNVKLGDFGLATENEnyqdNNDKWKNRqsadedlTTGVGTAL 825
Cdd:cd05053  132 qkdLVSFAYQVARGMeylaskkcIHRDLAARNVLVTEDNVMKIADFGLARDIH----HIDYYRKT-------TNGRLPVK 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  826 YVAPELLSRRngvRYDAKVDMYSLGIILFEMcMTFSTSmeririidtiRSPSISFPSTFPFSR----------ASHEFKV 895
Cdd:cd05053  201 WMAPEALFDR---VYTHQSDVWSFGVLLWEI-FTLGGS----------PYPGIPVEELFKLLKeghrmekpqnCTQELYM 266
                        250       260
                 ....*....|....*....|.
gi 63054755  896 IHCLLQH-DPTKRPSSQELLE 915
Cdd:cd05053  267 LMRDCWHeVPSQRPTFKQLVE 287
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
753-917 4.14e-11

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 65.38  E-value: 4.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  753 FRQILEALAYIHSRGMMHRDLKPGNIFLDENRN---VKLGDFGLATE-NENYQdnndkwknrqsadedLTTGVGTALYVA 828
Cdd:cd14113  109 LREILEALQYLHNCRIAHLDLKPENILVDQSLSkptIKLADFGDAVQlNTTYY---------------IHQLLGSPEFAA 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  829 PELLSrrnGVRYDAKVDMYSLGIILFEMCMTFS----TSMERIRIidTIRSPSISFPSTFpFSRASHEFKVIHC-LLQHD 903
Cdd:cd14113  174 PEIIL---GNPVSLTSDLWSIGVLTYVLLSGVSpfldESVEETCL--NICRLDFSFPDDY-FKGVSQKAKDFVCfLLQMD 247
                        170
                 ....*....|....
gi 63054755  904 PTKRPSSQELLESE 917
Cdd:cd14113  248 PAKRPSAALCLQEQ 261
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
697-856 4.54e-11

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: 65.05  E-value: 4.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  697 KEGSSDKDSSIEEASSVKTQENG----LNAT-----LYIQMEYCEKLSLQDIIR----DKIPVDEMWRLFRQILEALAYI 763
Cdd:cd05073   44 KPGSMSVEAFLAEANVMKTLQHDklvkLHAVvtkepIYIITEFMAKGSLLDFLKsdegSKQPLPKLIDFSAQIAEGMAFI 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  764 HSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENEnyqdnNDKWKNRQSADEDLTtgvgtalYVAPELLsrrNGVRYDAK 843
Cdd:cd05073  124 EQRNYIHRDLRAANILVSASLVCKIADFGLARVIE-----DNEYTAREGAKFPIK-------WTAPEAI---NFGSFTIK 188
                        170
                 ....*....|...
gi 63054755  844 VDMYSLGIILFEM 856
Cdd:cd05073  189 SDVWSFGILLMEI 201
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
715-856 4.94e-11

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


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 65.63  E-value: 4.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  715 TQENGlNATLYIQMEYCEKlSLQDII-------RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNV- 786
Cdd:cd07837   72 VEENG-KPLLYLVFEYLDT-DLKKFIdsygrgpHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGLl 149
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  787 KLGDFGLAtenenyqdnndkwKNRQSADEDLTTGVGTALYVAPELLsrRNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd07837  150 KIADLGLG-------------RAFTIPIKSYTHEIVTLWYRAPEVL--LGSTHYSTPVDMWSVGCIFAEM 204
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
743-915 5.92e-11

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: 64.29  E-value: 5.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  743 KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGN-IFLDENRN-VKlgdfgLATENENYQDNNDkwknrqsaDEDLTTG 820
Cdd:cd14022   80 KLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKfVFKDEERTrVK-----LESLEDAYILRGH--------DDSLSDK 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  821 VGTALYVAPELLSrRNGVRYDAKVDMYSLGIILFEMCM---TFStSMERIRIIDTIRSPSISFPSTF-PFSRAshefkVI 896
Cdd:cd14022  147 HGCPAYVSPEILN-TSGSYSGKAADVWSLGVMLYTMLVgryPFH-DIEPSSLFSKIRRGQFNIPETLsPKAKC-----LI 219
                        170
                 ....*....|....*....
gi 63054755  897 HCLLQHDPTKRPSSQELLE 915
Cdd:cd14022  220 RSILRREPSERLTSQEILD 238
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
716-856 6.06e-11

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


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 65.16  E-value: 6.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  716 QENGLNATLYIQMEYCEKLSLQDII-RDKIPVDEMWRLFRQILEALAYIHSR--------GMMHRDLKPGNIFLDENRNV 786
Cdd:cd14143   60 KDNGTWTQLWLVSDYHEHGSLFDYLnRYTVTVEGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDLKSKNILVKKNGTC 139
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054755  787 KLGDFGLATENENYQDNNDKWKNRQsadedlttgVGTALYVAPELLSRRNGVR-YDA--KVDMYSLGIILFEM 856
Cdd:cd14143  140 CIADLGLAVRHDSATDTIDIAPNHR---------VGTKRYMAPEVLDDTINMKhFESfkRADIYALGLVFWEI 203
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
748-856 6.46e-11

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


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 64.96  E-value: 6.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  748 EMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENR---NVKLGDFGLATENENyqdnndkwknrqsaDEDLTTGVGTA 824
Cdd:cd14197  112 DVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESplgDIKIVDFGLSRILKN--------------SEELREIMGTP 177
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 63054755  825 LYVAPELLSrrngvrYD---AKVDMYSLGIILFEM 856
Cdd:cd14197  178 EYVAPEILS------YEpisTATDMWSIGVLAYVM 206
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
293-458 6.94e-11

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: 64.65  E-value: 6.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  293 ELESLKVIRHDLLASIYEYQlerETRGygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISH 372
Cdd:cd14202   51 EIKILKELKHENIVALYDFQ---EIAN---SVYLVMEYCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIH 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  373 KSLHLDNVVLFHSGHRTF------AKLMDFGFTRTLRDmnashpfniNSQSITNILPEGLYPPEVSESSFAAAsrKTDIW 446
Cdd:cd14202  125 RDLKPQNILLSYSGGRKSnpnnirIKIADFGFARYLQN---------NMMAATLCGSPMYMAPEVIMSQHYDA--KADLW 193
                        170
                 ....*....|..
gi 63054755  447 CFGLLVLQMLCG 458
Cdd:cd14202  194 SIGTIIYQCLTG 205
PLN03225 PLN03225
Serine/threonine-protein kinase SNT7; Provisional
751-858 7.21e-11

Serine/threonine-protein kinase SNT7; Provisional


Pssm-ID: 215638 [Multi-domain]  Cd Length: 566  Bit Score: 66.74  E-value: 7.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   751 RLFRQILEALAYIHSRGMMHRDLKPGN-IFLDENRNVKLGDFGLATE---NENYQDNNDKWKNRQSADEDL--------- 817
Cdd:PLN03225  259 TIMRQILFALDGLHSTGIVHRDVKPQNiIFSEGSGSFKIIDLGAAADlrvGINYIPKEFLLDPRYAAPEQYimstqtpsa 338
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 63054755   818 -TTGVGTALyvAPELLSRRNGVRYdakvDMYSLGIILFEMCM 858
Cdd:PLN03225  339 pSAPVATAL--SPVLWQLNLPDRF----DIYSAGLIFLQMAF 374
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
324-507 7.27e-11

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: 64.70  E-value: 7.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  324 LYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLR 403
Cdd:cd14046   79 LYIQMEYCEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGN---VKIGDFGLATSNK 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  404 DMNASHPFNINSQSITNILPEG---------LY-PPEVSESSFAAASRKTDIWCFGLLVLQMlC--------GAHVLNKF 465
Cdd:cd14046  156 LNVELATQDINKSTSAALGSSGdltgnvgtaLYvAPEVQSGTKSTYNEKVDMYSLGIIFFEM-CypfstgmeRVQILTAL 234
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 63054755  466 SSLKLIMTHVIPLLPGSYQDLVRRCLM-RDSRKRPSAIDLLSS 507
Cdd:cd14046  235 RSVSIEFPPDFDDNKHSKQAKLIRWLLnHDPAKRPSAQELLKS 277
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
297-506 7.88e-11

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: 64.42  E-value: 7.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  297 LKVIRHDLLASIY-EYQLERE------------TRGYGW-----RLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNI 358
Cdd:cd14007   30 LKVISKSQLQKSGlEHQLRREieiqshlrhpniLRLYGYfedkkRIYLILEYAPNGELYKELKKQKRFDEKEAAKYIYQL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  359 LEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFtrtlrdmnASHPFNINSQSITNILPeglY-PPE-VSESSF 436
Cdd:cd14007  110 ALALDYLHSKNIIHRDIKPENILLGSNGE---LKLADFGW--------SVHAPSNRRKTFCGTLD---YlPPEmVEGKEY 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  437 aaaSRKTDIWCFGLLVLQMLCGA---------HVLNKFSSLKLimtHVIPLLPGSYQDLVRRCLMRDSRKRPSAIDLLS 506
Cdd:cd14007  176 ---DYKVDIWSLGVLCYELLVGKppfeskshqETYKRIQNVDI---KFPSSVSPEAKDLISKLLQKDPSKRLSLEQVLN 248
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
726-909 7.98e-11

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: 65.08  E-value: 7.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  726 IQMEYCEKLSLQDIIRD--KIPVDEMWRLFRQILEALAYIHSR-GMMHRDLKPGNIFLDENRNVKLGDFGLATenenyqd 802
Cdd:cd06650   80 ICMEHMDGGSLDQVLKKagRIPEQILGKVSIAVIKGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSG------- 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  803 nndkwknrQSADEDLTTGVGTALYVAPEllsRRNGVRYDAKVDMYSLGIILFEMCMTF-------STSMERIRIIDTIRS 875
Cdd:cd06650  153 --------QLIDSMANSFVGTRSYMSPE---RLQGTHYSVQSDIWSMGLSLVEMAVGRypipppdAKELELMFGCQVEGD 221
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 63054755  876 PSISFPSTFPFSRASHE-----------FKVIHCLLQHDPTKRPS 909
Cdd:cd06650  222 AAETPPRPRTPGRPLSSygmdsrppmaiFELLDYIVNEPPPKLPS 266
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
724-855 8.75e-11

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: 65.64  E-value: 8.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQD-IIRDKIPVDEMWRLF-RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAT------ 795
Cdd:cd05629   76 LYLIMEFLPGGDLMTmLIKYDTFSEDVTRFYmAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLSTgfhkqh 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  796 ENENYQ------DNNDKWKNRQSADED---LT-------------------TGVGTALYVAPELLSRRNgvrYDAKVDMY 847
Cdd:cd05629  156 DSAYYQkllqgkSNKNRIDNRNSVAVDsinLTmsskdqiatwkknrrlmaySTVGTPDYIAPEIFLQQG---YGQECDWW 232

                 ....*...
gi 63054755  848 SLGIILFE 855
Cdd:cd05629  233 SLGAIMFE 240
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
741-907 1.03e-10

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


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 65.10  E-value: 1.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  741 RDKIPVDEMWRLF-RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENenyqdnndkwknrQSADEDLTT 819
Cdd:cd05593  108 RERVFSEDRTRFYgAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEG-------------ITDAATMKT 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  820 GVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFE-MCMTFS-TSMERIRIIDTIRSPSISFPSTFpfsrASHEFKVIH 897
Cdd:cd05593  175 FCGTPEYLAPEVLEDND---YGRAVDWWGLGVVMYEmMCGRLPfYNQDHEKLFELILMEDIKFPRTL----SADAKSLLS 247
                        170
                 ....*....|
gi 63054755  898 CLLQHDPTKR 907
Cdd:cd05593  248 GLLIKDPNKR 257
RWD_RWDD1 cd23816
RWD domain of RWD domain-containing protein 1 (RWDD1) and related proteins; RWDD1, also called ...
10-125 1.06e-10

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: 60.38  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   10 CKEIQENEIEALKAIFMDDFEELkvrnawNVTNGHVYCIHLCSR-SANSKSIAKLDLCIELGRSYPYVKPVIKLQNGENV 88
Cdd:cd23816    1 YKEEQRNELEALESIYPDEFTVL------SEEPPISFTITVTSEeEENEDETVSVTLKFTYTEKYPDEAPLIEIISHENL 74
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 63054755   89 LNSQIRFLLDKLDTKAKDLLGEEMIFELASIVQDYLN 125
Cdd:cd23816   75 EDEDIEDLLELLEQQAEENLGMVMVFTIVSAVQEKLN 111
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
755-856 1.16e-10

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 64.45  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   755 QILEALAYIHSRGMMHRDLKPGNIFLDENRN-VKLGDFGLAtenenyqdnndkwKNRQSADEDLTTGVGTALYVAPELL- 832
Cdd:PLN00009  110 QILRGIAYCHSHRVLHRDLKPQNLLIDRRTNaLKLADFGLA-------------RAFGIPVRTFTHEVVTLWYRAPEILl 176
                          90       100
                  ....*....|....*....|....*
gi 63054755   833 -SRrngvRYDAKVDMYSLGIILFEM 856
Cdd:PLN00009  177 gSR----HYSTPVDIWSVGCIFAEM 197
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
358-507 1.17e-10

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: 63.77  E-value: 1.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  358 ILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLrdmNASHPfNINSQSITnilPeglY--PPEVSESS 435
Cdd:cd06614  106 VLQGLEYLHSQNVIHRDIKSDNILLSKDGS---VKLADFGFAAQL---TKEKS-KRNSVVGT---P---YwmAPEVIKRK 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  436 faAASRKTDIWCFGLLVLQMLCGAHVLNKFSSLK---LIMTHVIPLLPGS------YQDLVRRCLMRDSRKRPSAIDLLS 506
Cdd:cd06614  173 --DYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRalfLITTKGIPPLKNPekwspeFKDFLNKCLVKDPEKRPSAEELLQ 250

                 .
gi 63054755  507 S 507
Cdd:cd06614  251 H 251
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
755-856 1.30e-10

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: 64.63  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenenyqdnndkwKNRQSADEDLTTGVGTALYVAPELLsr 834
Cdd:cd07872  112 QILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLA-------------RAKSVPTKTYSNEVVTLWYRPPDVL-- 176
                         90       100
                 ....*....|....*....|..
gi 63054755  835 RNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd07872  177 LGSSEYSTQIDMWGVGCIFFEM 198
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
724-856 1.33e-10

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: 63.63  E-value: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDII--RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDEN--RNVKLGDFGlatenen 799
Cdd:cd14662   71 LAIVMEYAAGGELFERIcnAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSpaPRLKICDFG------- 143
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 63054755  800 YQDNNDKWKNRQSAdedlttgVGTALYVAPELLSRRngvRYDAKV-DMYSLGIILFEM 856
Cdd:cd14662  144 YSKSSVLHSQPKST-------VGTPAYIAPEVLSRK---EYDGKVaDVWSCGVTLYVM 191
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
321-511 1.34e-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: 63.79  E-value: 1.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  321 GWRLYVLQEYSPKFTLFSLLqTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTR 400
Cdd:cd06647   76 GDELWVVMEYLAGGSLTDVV-TETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGS---VKLTDFGFCA 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  401 TLRDMNASHPFNINSqsitnilPEGLYPPEVSESSFAAasrKTDIWCFGLLVLQMLCGAHVL---NKFSSLKLIMTHVIP 477
Cdd:cd06647  152 QITPEQSKRSTMVGT-------PYWMAPEVVTRKAYGP---KVDIWSLGIMAIEMVEGEPPYlneNPLRALYLIATNGTP 221
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 63054755  478 LLPG------SYQDLVRRCLMRDSRKRPSAIDLLSSHVIR 511
Cdd:cd06647  222 ELQNpeklsaIFRDFLNRCLEMDVEKRGSAKELLQHPFLK 261
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
743-915 1.34e-10

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: 63.87  E-value: 1.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  743 KIPVDEMWRlfRQILEALAYIHSRG--MMHRDLKPGNIFLD-ENRNVKLGDFGLATenenyqdnndkwKNRQSADEDLtt 819
Cdd:cd14033  102 KLKLLQRWS--RQILKGLHFLHSRCppILHRDLKCDNIFITgPTGSVKIGDLGLAT------------LKRASFAKSV-- 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  820 gVGTALYVAPELLSRRngvrYDAKVDMYSLGIILFEMCMT---FSTSMERIRIIDTIRSPSIsfPSTFPFSRASHEFKVI 896
Cdd:cd14033  166 -IGTPEFMAPEMYEEK----YDEAVDVYAFGMCILEMATSeypYSECQNAAQIYRKVTSGIK--PDSFYKVKVPELKEII 238
                        170
                 ....*....|....*....
gi 63054755  897 HCLLQHDPTKRPSSQELLE 915
Cdd:cd14033  239 EGCIRTDKDERFTIQDLLE 257
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
717-856 1.49e-10

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: 63.77  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  717 ENGLNATLYIQMEYCEKLSLQDII-RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAT 795
Cdd:cd05080   76 SEQGGKSLQLIMEYVPLGSLRDYLpKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAK 155
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63054755  796 ---ENENYqdnndkWKNRQSADEDLttgvgtaLYVAPELLsRRNGVRYDAkvDMYSLGIILFEM 856
Cdd:cd05080  156 avpEGHEY------YRVREDGDSPV-------FWYAPECL-KEYKFYYAS--DVWSFGVTLYEL 203
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
286-506 1.51e-10

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: 63.44  E-value: 1.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  286 EIQELEYELESLKVIRHDLLASIY-EYQLEREtrgygwrLYVLQEYSPKFTLFSLLQ-TVLTLDVETVRAFSNNILEGLA 363
Cdd:cd06612   41 DLQEIIKEISILKQCDSPYIVKYYgSYFKNTD-------LWIVMEYCGAGSVSDIMKiTNKTLTEEEIAAILYQTLKGLE 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  364 ELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDMNASHPFNINSqsitnilPEGLYPPEVSESSFaaaSRKT 443
Cdd:cd06612  114 YLHSNKKIHRDIKAGNILLNEEGQ---AKLADFGVSGQLTDTMAKRNTVIGT-------PFWMAPEVIQEIGY---NNKA 180
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054755  444 DIWCFGLLVLQMLCGA---HVLNKFSSLKLIMTHVIPLL--PG----SYQDLVRRCLMRDSRKRPSAIDLLS 506
Cdd:cd06612  181 DIWSLGITAIEMAEGKppySDIHPMRAIFMIPNKPPPTLsdPEkwspEFNDFVKKCLVKDPEERPSAIQLLQ 252
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
724-856 1.60e-10

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: 65.04  E-value: 1.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYC---EKLSLQDIIRDKIPvDEMWRLF-RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATenen 799
Cdd:cd05623  147 LYLVMDYYvggDLLTLLSKFEDRLP-EDMARFYlAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCL---- 221
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  800 yqdnndkwKNRQSADEDLTTGVGTALYVAPELLSRRNG--VRYDAKVDMYSLGIILFEM 856
Cdd:cd05623  222 --------KLMEDGTVQSSVAVGTPDYISPEILQAMEDgkGKYGPECDWWSLGVCMYEM 272
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
741-907 1.62e-10

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: 64.67  E-value: 1.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  741 RDKIPVDEMWRLF-RQILEALAYIHS-RGMMHRDLKPGNIFLDENRNVKLGDFGLAteNENYQDNndkwknrqsadEDLT 818
Cdd:cd05594  118 RERVFSEDRARFYgAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLC--KEGIKDG-----------ATMK 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  819 TGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFE-MCMTFS-TSMERIRIIDTIRSPSISFPSTF-PFSRAshefkV 895
Cdd:cd05594  185 TFCGTPEYLAPEVLEDND---YGRAVDWWGLGVVMYEmMCGRLPfYNQDHEKLFELILMEEIRFPRTLsPEAKS-----L 256
                        170
                 ....*....|..
gi 63054755  896 IHCLLQHDPTKR 907
Cdd:cd05594  257 LSGLLKKDPKQR 268
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
724-859 1.71e-10

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


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 63.65  E-value: 1.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIR-DKIPVDEMWRLFRQILEALAYIHSR--------GMMHRDLKPGNIFLDENRNVKLGDFGLA 794
Cdd:cd14144   68 LYLITDYHENGSLYDFLRgNTLDTQSMLKLAYSAACGLAHLHTEifgtqgkpAIAHRDIKSKNILVKKNGTCCIADLGLA 147
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 63054755  795 TENENYQDNNDKWKNrqsadedltTGVGTALYVAPELLS---RRNGVRYDAKVDMYSLGIILFEM---CMT 859
Cdd:cd14144  148 VKFISETNEVDLPPN---------TRVGTKRYMAPEVLDeslNRNHFDAYKMADMYSFGLVLWEIarrCIS 209
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
726-917 1.71e-10

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: 63.58  E-value: 1.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  726 IQMEYCEKLSLQDIIRDK---IPVDEMWRLF--RQILEALAYIHSRGMMHRDLKPGNIFLDE-NRNVKLGDFG----LAT 795
Cdd:cd06624   82 IFMEQVPGGSLSALLRSKwgpLKDNENTIGYytKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGtskrLAG 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  796 ENENyqdnndkwknrqsadedLTTGVGTALYVAPELLSRrnGVR-YDAKVDMYSLGIILFEMCMT--------------F 860
Cdd:cd06624  162 INPC-----------------TETFTGTLQYMAPEVIDK--GQRgYGPPADIWSLGCTIIEMATGkppfielgepqaamF 222
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  861 STSMERIRiidtirsPSIsfPSTfpFSRASHEFkvIHCLLQHDPTKRPSSQELLESE 917
Cdd:cd06624  223 KVGMFKIH-------PEI--PES--LSEEAKSF--ILRCFEPDPDKRATASDLLQDP 266
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
724-856 1.85e-10

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: 64.25  E-value: 1.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSL----QDIIRDKIPVDEMWRlfRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENen 799
Cdd:cd05616   76 LYFVMEYVNGGDLmyhiQQVGRFKEPHAVFYA--AEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEN-- 151
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  800 yqdnndKWKNRQSadedlTTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEM 856
Cdd:cd05616  152 ------IWDGVTT-----KTFCGTPDYIAPEIIAYQP---YGKSVDWWAFGVLLYEM 194
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
741-914 1.86e-10

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: 63.44  E-value: 1.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  741 RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNI-FLDEN---RNVKLGDFGLATENEnyqdNNDKWKNRqsaded 816
Cdd:cd14196  102 KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNipiPHIKLIDFGLAHEIE----DGVEFKNI------ 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  817 lttgVGTALYVAPELlsrrngVRYDA---KVDMYSLGIILFEMCMTFSTSMERIR--IIDTIRSPSISFPSTFpFSRASH 891
Cdd:cd14196  172 ----FGTPEFVAPEI------VNYEPlglEADMWSIGVITYILLSGASPFLGDTKqeTLANITAVSYDFDEEF-FSHTSE 240
                        170       180
                 ....*....|....*....|....
gi 63054755  892 EFK-VIHCLLQHDPTKRPSSQELL 914
Cdd:cd14196  241 LAKdFIRKLLVKETRKRLTIQEAL 264
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
749-916 1.94e-10

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: 63.80  E-value: 1.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  749 MWRL---FRQILEALAYIHSRGMMHRDLKPGNIFLD-ENRNVKLGDFGLAtenenYQDNNDKWKNRQsadedlTTGvgta 824
Cdd:cd14020  109 MWMIqhcARDVLEALAFLHHEGYVHADLKPRNILWSaEDECFKLIDFGLS-----FKEGNQDVKYIQ------TDG---- 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  825 lYVAPELLSR----RNGVRYD----AKVDMYSLGIILFEMcmtFSTsmerIRIIDTIRSPSISFPST------------- 883
Cdd:cd14020  174 -YRAPEAELQnclaQAGLQSEtectSAVDLWSLGIVLLEM---FSG----MKLKHTVRSQEWKDNSSaiidhifasnavv 245
                        170       180       190
                 ....*....|....*....|....*....|...
gi 63054755  884 FPFSRASHEFKVIHCLLQHDPTKRPSSQELLES 916
Cdd:cd14020  246 NPAIPAYHLRDLIKSMLHNDPGKRATAEAALCS 278
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
760-856 1.95e-10

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


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 64.24  E-value: 1.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  760 LAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQDnndkwknRQSadedltTGVGTALYVAPELLSRRNgvr 839
Cdd:cd05589  114 LQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFGD-------RTS------TFCGTPEFLAPEVLTDTS--- 177
                         90
                 ....*....|....*..
gi 63054755  840 YDAKVDMYSLGIILFEM 856
Cdd:cd05589  178 YTRAVDWWGLGVLIYEM 194
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
724-930 1.98e-10

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: 64.34  E-value: 1.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKlSLQDIIRDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLA-TENENYQd 802
Cdd:cd07874   97 VYLVMELMDA-NLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLArTAGTSFM- 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  803 nndkwknrqsadedLTTGVGTALYVAPELLSrrnGVRYDAKVDMYSLGIILFEM-------------------------- 856
Cdd:cd07874  175 --------------MTPYVVTRYYRAPEVIL---GMGYKENVDIWSVGCIMGEMvrhkilfpgrdyidqwnkvieqlgtp 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  857 CMTFSTSME---RIRIIDTIRSPSISFPSTFPFS-----------RASHEFKVIHCLLQHDPTKRPSSQELL-------- 914
Cdd:cd07874  238 CPEFMKKLQptvRNYVENRPKYAGLTFPKLFPDSlfpadsehnklKASQARDLLSKMLVIDPAKRISVDEALqhpyinvw 317
                        250       260
                 ....*....|....*....|
gi 63054755  915 ----ESEAIPPKVGEEFIQE 930
Cdd:cd07874  318 ydpaEVEAPPPQIYDKQLDE 337
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
724-919 2.04e-10

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: 63.49  E-value: 2.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIR------DKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEN 797
Cdd:cd06638   95 LWLVLELCNGGSVTDLVKgflkrgERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  798 ENYQDNNDkwknrqsadedltTGVGTALYVAPELLS--RRNGVRYDAKVDMYSLGIILFEMC-----MTFSTSMERIRII 870
Cdd:cd06638  175 TSTRLRRN-------------TSVGTPFWMAPEVIAceQQLDSTYDARCDVWSLGITAIELGdgdppLADLHPMRALFKI 241
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 63054755  871 DTIRSPSISFPSTFpfsraSHEFK--VIHCLLQhDPTKRPSSQELLESEAI 919
Cdd:cd06638  242 PRNPPPTLHQPELW-----SNEFNdfIRKCLTK-DYEKRPTVSDLLQHVFI 286
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
278-506 2.06e-10

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: 62.67  E-value: 2.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  278 WSTEDGK---REIQELEYELESLKVIRHDLLASIYEYQLERETRGygwrlyVLQEYSPKFTLFSLLQTVLT--LDVETVR 352
Cdd:cd14060   14 WVSQDKEvavKKLLKIEKEAEILSVLSHRNIIQFYGAILEAPNYG------IVTEYASYGSLFDYLNSNESeeMDMDQIM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  353 AFSNNILEGLAELHR---LGISHKSLHLDNVVLFHSGhrtFAKLMDFGFTRTLrdmnaSHPFNInsqSITnilpeGLYP- 428
Cdd:cd14060   88 TWATDIAKGMHYLHMeapVKVIHRDLKSRNVVIAADG---VLKICDFGASRFH-----SHTTHM---SLV-----GTFPw 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  429 --PEVSESsfAAASRKTDIWCFGLLVLQMLCGAHVLNKFSSLKLIMTHV-------IP-LLPGSYQDLVRRCLMRDSRKR 498
Cdd:cd14060  152 maPEVIQS--LPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVeknerptIPsSCPRSFAELMRRCWEADVKER 229

                 ....*...
gi 63054755  499 PSAIDLLS 506
Cdd:cd14060  230 PSFKQIIG 237
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
324-501 2.07e-10

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: 63.39  E-value: 2.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  324 LYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTR--- 400
Cdd:cd05579   68 LYLVMEYLPGGDLYSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGH---LKLTDFGLSKvgl 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  401 TLRDMNASHPFNINSQSITNIL-----PEGLyPPEVSESSfaAASRKTDIWCFGLLVLQMLCGAHVLNKFSSLKL---IM 472
Cdd:cd05579  145 VRRQIKLSIQKKSNGAPEKEDRrivgtPDYL-APEILLGQ--GHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIfqnIL 221
                        170       180       190
                 ....*....|....*....|....*....|....
gi 63054755  473 THVI-----PLLPGSYQDLVRRCLMRDSRKRPSA 501
Cdd:cd05579  222 NGKIewpedPEVSDEAKDLISKLLTPDPEKRLGA 255
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
743-911 2.09e-10

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: 64.27  E-value: 2.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  743 KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQDNNdkwknrqsadedlTTGVG 822
Cdd:cd05617  112 KLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTT-------------STFCG 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  823 TALYVAPELLsrrNGVRYDAKVDMYSLGIILFEMCMTFS-----TSMERIRIIDTIRSPSISFPSTFPFSRASHEFKVIH 897
Cdd:cd05617  179 TPNYIAPEIL---RGEEYGFSVDWWALGVLMFEMMAGRSpfdiiTDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLK 255
                        170
                 ....*....|....
gi 63054755  898 CLLQHDPTKRPSSQ 911
Cdd:cd05617  256 GFLNKDPKERLGCQ 269
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
744-857 2.19e-10

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: 63.75  E-value: 2.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  744 IPVDEMWRLFRQILEALAYIHSR-GMMHRDLKPGNIFLDENR-NVKLGDFGLATenenyqdnndkWKNRQSADEdlttgV 821
Cdd:cd14136  116 IPLPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVLLCISKiEVKIADLGNAC-----------WTDKHFTED-----I 179
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 63054755  822 GTALYVAPELLSrrnGVRYDAKVDMYSLGIILFEMC 857
Cdd:cd14136  180 QTRQYRSPEVIL---GAGYGTPADIWSTACMAFELA 212
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
285-498 2.44e-10

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: 63.22  E-value: 2.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  285 REIQELEYELESLKVIRHDLLASIYEYQLERETrgygwrLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAE 364
Cdd:cd05612   43 KQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRF------LYMLMEYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEY 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  365 LHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDMnashpfninsqsiTNIL---PEGLyPPEVSESSfaAASR 441
Cdd:cd05612  117 LHSKEIVYRDLKPENILLDKEGH---IKLTDFGFAKKLRDR-------------TWTLcgtPEYL-APEVIQSK--GHNK 177
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054755  442 KTDIWCFGLLVLQMLCGAHVL---NKFSSLKLIMTHVIPL---LPGSYQDLVRRCLMRDSRKR 498
Cdd:cd05612  178 AVDWWALGILIYEMLVGYPPFfddNPFGIYEKILAGKLEFprhLDLYAKDLIKKLLVVDRTRR 240
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
290-498 2.47e-10

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: 62.63  E-value: 2.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  290 LEYELESLKVIRHDLLASIYEYQLEREtrgygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLG 369
Cdd:cd14009   39 LESEIAILKSIKHPNIVRLYDVQKTED------FIYLVLEYCAGGDLSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKN 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  370 ISHKSLHLDNVVLFHSGHRTFAKLMDFGFTRTLRDMNASH-----PfninsqsitnilpegLY-PPEVSESSFAAAsrKT 443
Cdd:cd14009  113 IIHRDLKPQNLLLSTSGDDPVLKIADFGFARSLQPASMAEtlcgsP---------------LYmAPEILQFQKYDA--KA 175
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63054755  444 DIWCFGLLVLQMLCG-------AHV---LNKFSSLKLIMTHVIPLLPGSYQDLVRRCLMRDSRKR 498
Cdd:cd14009  176 DLWSVGAILFEMLVGkppfrgsNHVqllRNIERSDAVIPFPIAAQLSPDCKDLLRRLLRRDPAER 240
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
744-856 2.64e-10

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


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 63.13  E-value: 2.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  744 IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenenyqdnndKWKNRQSAdedLTTGVGT 823
Cdd:cd07862  107 VPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLA-----------RIYSFQMA---LTSVVVT 172
                         90       100       110
                 ....*....|....*....|....*....|...
gi 63054755  824 ALYVAPELLSRRNgvrYDAKVDMYSLGIILFEM 856
Cdd:cd07862  173 LWYRAPEVLLQSS---YATPVDLWSVGCIFAEM 202
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
729-913 2.78e-10

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


Pssm-ID: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 62.81  E-value: 2.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  729 EYCEKLSLQDIIR-DKIPVDEMWR--LFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLateNENYQDNNd 805
Cdd:cd14043   76 EHCSRGSLEDLLRnDDMKLDWMFKssLLLDLIKGMRYLHHRGIVHGRLKSRNCVVDGRFVLKITDYGY---NEILEAQN- 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  806 kWKNRQSADEDLttgvgtaLYVAPELLSRRNGVRYDA-KVDMYSLGIILFEM-------CMTFSTSMErirIIDTIRSPS 877
Cdd:cd14043  152 -LPLPEPAPEEL-------LWTAPELLRDPRLERRGTfPGDVFSFAIIMQEVivrgapyCMLGLSPEE---IIEKVRSPP 220
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 63054755  878 isfpstfPFSRAS-----HEFKVIHCLLQ---HDPTKRPSSQEL 913
Cdd:cd14043  221 -------PLCRPSvsmdqAPLECIQLMKQcwsEAPERRPTFDQI 257
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
726-859 2.85e-10

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


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 63.06  E-value: 2.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  726 IQMEYCEKLSLQDIIRD-----KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLD--ENRNV-KLGDFGLATEN 797
Cdd:cd14038   75 LAMEYCQGGDLRKYLNQfenccGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQqgEQRLIhKIIDLGYAKEL 154
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054755  798 ENyqdnndkwknrqsaDEDLTTGVGTALYVAPELLSRRngvRYDAKVDMYSLGIILFEmCMT 859
Cdd:cd14038  155 DQ--------------GSLCTSFVGTLQYLAPELLEQQ---KYTVTVDYWSFGTLAFE-CIT 198
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
551-915 3.21e-10

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 63.48  E-value: 3.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  551 RYETDFEELEF---LGRGGFGEVVK-----VKNRIDGRFYAVKKLVLLSDDKENSRILREVMTLSRL-HHEHVVRYYTAW 621
Cdd:cd14207    1 KWEFARERLKLgksLGRGAFGKVVQasafgIKKSPTCRVVAVKMLKEGATASEYKALMTELKILIHIgHHLNVVNLLGAC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  622 VETEAndtvteiissdseslsqSLNMAVDFRQSSSLPADKLSSLDIHFEDdynssadeedpeaSDISFQYSNTSDKEGSS 701
Cdd:cd14207   81 TKSGG-----------------PLMVIVEYCKYGNLSNYLKSKRDFFVTN-------------KDTSLQEELIKEKKEAE 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  702 DKDSSIEEASSVKTQENglnatlYIQMEYCEKLSLQDIIRDKIPVDEMWRL-----------FrQILEALAYIHSRGMMH 770
Cdd:cd14207  131 PTGGKKKRLESVTSSES------FASSGFQEDKSLSDVEEEEEDSGDFYKRpltmedlisysF-QVARGMEFLSSRKCIH 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  771 RDLKPGNIFLDENRNVKLGDFGLATE---NENYQDNND-----KWknrqsadedlttgvgtalyVAPELLSRRngvRYDA 842
Cdd:cd14207  204 RDLAARNILLSENNVVKICDFGLARDiykNPDYVRKGDarlplKW-------------------MAPESIFDK---IYST 261
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  843 KVDMYSLGIILFEMCMTFSTSMERIRIIDT----------IRSPSISFPSTFPFsrashefkVIHClLQHDPTKRPSSQE 912
Cdd:cd14207  262 KSDVWSYGVLLWEIFSLGASPYPGVQIDEDfcsklkegirMRAPEFATSEIYQI--------MLDC-WQGDPNERPRFSE 332

                 ...
gi 63054755  913 LLE 915
Cdd:cd14207  333 LVE 335
RWD_RNF25 cd23818
RWD domain of RING finger protein 25 (RNF25) and related proteins; RNF25 (EC 2.3.2.27), also ...
15-124 3.30e-10

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: 58.71  E-value: 3.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   15 ENEIEALKAIFMDDFEelKVRNAWNVTnghVYCIHLCSRSANSKS--IAKLDLCIELGRSYPYVKPVIKLQN----GENV 88
Cdd:cd23818    2 EEELEALEAIYPDELK--VVSEDGAPT---ELSITLHPATADDESeqYVRLTLVITLPPGYPEEPPKISLRNprglSDAR 76
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 63054755   89 LNSqirfLLDKLDTKAKDLLGEEMIFELASIVQDYL 124
Cdd:cd23818   77 LAR----LLSLLKELAEERAGEPMLFELIELAKEFL 108
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
720-856 3.33e-10

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: 63.14  E-value: 3.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  720 LNATLYIQMEYCEKLSLQDIIR-DKIPVDEMWRLFRQILEALAYIHSR----------GMMHRDLKPGNIFLDENRNVKL 788
Cdd:cd14141   64 LDVDLWLITAFHEKGSLTDYLKaNVVSWNELCHIAQTMARGLAYLHEDipglkdghkpAIAHRDIKSKNVLLKNNLTACI 143
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  789 GDFGLATenenyqdnndKWKNRQSADeDLTTGVGTALYVAPELLSRRNGVRYDA--KVDMYSLGIILFEM 856
Cdd:cd14141  144 ADFGLAL----------KFEAGKSAG-DTHGQVGTRRYMAPEVLEGAINFQRDAflRIDMYAMGLVLWEL 202
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
721-858 3.33e-10

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: 63.53  E-value: 3.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  721 NATLYIQMEYCEKLSLQDIIRD--KIPVDEMWRLFRQILEALAYIHSR-GMMHRDLKPGNIFLDENRNVKLGDFGLATen 797
Cdd:cd06649   75 DGEISICMEHMDGGSLDQVLKEakRIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRGEIKLCDFGVSG-- 152
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 63054755  798 enyqdnndkwknrQSADEDLTTGVGTALYVAPEllsRRNGVRYDAKVDMYSLGIILFEMCM 858
Cdd:cd06649  153 -------------QLIDSMANSFVGTRSYMSPE---RLQGTHYSVQSDIWSMGLSLVELAI 197
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
754-885 3.46e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 64.14  E-value: 3.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   754 RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATenenyqdnndkwKNRQSADEDLTTGV-GTALYVAPELL 832
Cdd:PHA03211  267 RQLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFGAAC------------FARGSWSTPFHYGIaGTVDTNAPEVL 334
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054755   833 SrrnGVRYDAKVDMYSLGIILFEMCM----TFSTSMERIR------IIDTIRSPSISfPSTFP 885
Cdd:PHA03211  335 A---GDPYTPSVDIWSAGLVIFEAAVhtasLFSASRGDERrpydaqILRIIRQAQVH-VDEFP 393
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
741-915 3.49e-10

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: 62.73  E-value: 3.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  741 RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLdENRNV-----KLGDFGLATEnenyQDNNDKWKNRqsade 815
Cdd:cd14194  102 KESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIML-LDRNVpkpriKIIDFGLAHK----IDFGNEFKNI----- 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  816 dlttgVGTALYVAPELlsrrngVRYDA---KVDMYSLGIILFEMCMTFSTSM--ERIRIIDTIRSPSISFPSTFpFSRAS 890
Cdd:cd14194  172 -----FGTPEFVAPEI------VNYEPlglEADMWSIGVITYILLSGASPFLgdTKQETLANVSAVNYEFEDEY-FSNTS 239
                        170       180
                 ....*....|....*....|....*.
gi 63054755  891 HEFK-VIHCLLQHDPTKRPSSQELLE 915
Cdd:cd14194  240 ALAKdFIRRLLVKDPKKRMTIQDSLQ 265
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
725-856 3.52e-10

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: 62.45  E-value: 3.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  725 YIQMEYCEKLSLQDIIRDK----IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLA--TENE 798
Cdd:cd05148   78 YIITELMEKGSLLAFLRSPegqvLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLArlIKED 157
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 63054755  799 NYQDNNDKWKNRqsadedlttgvgtalYVAPELLSRRngvRYDAKVDMYSLGIILFEM 856
Cdd:cd05148  158 VYLSSDKKIPYK---------------WTAPEAASHG---TFSTKSDVWSFGILLYEM 197
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
724-856 4.01e-10

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: 62.63  E-value: 4.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDK-IPVDEMWRLFRQILEALA----YIH--SRGMMHRDLKPGNIFLDENRNVKLGDFGLAte 796
Cdd:cd14026   72 LGIVTEYMTNGSLNELLHEKdIYPDVAWPLRLRILYEIAlgvnYLHnmSPPLLHHDLKTQNILLDGEFHVKIADFGLS-- 149
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63054755  797 nenyqdnndKWK----NRQSADEDLTTGvGTALYVAPELLSRRNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd14026  150 ---------KWRqlsiSQSRSSKSAPEG-GTIIYMPPEEYEPSQKRRASVKHDIYSYAIIMWEV 203
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
755-856 4.21e-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: 62.61  E-value: 4.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENyqdnndkwknrqsaDEDLTTGVGTALYVAPELLSR 834
Cdd:cd05607  112 QITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKE--------------GKPITQRAGTNGYMAPEILKE 177
                         90       100
                 ....*....|....*....|..
gi 63054755  835 RNgvrYDAKVDMYSLGIILFEM 856
Cdd:cd05607  178 ES---YSYPVDWFAMGCSIYEM 196
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
751-856 4.22e-10

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: 62.95  E-value: 4.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  751 RLF-RQILEALAYIHSRGMMHRDLKPGNIFLDENR--NVKLGDFGLA-TENE---NYQdnndkwknrQSadedlttgvgt 823
Cdd:cd14210  119 RKFaKQILQALQFLHKLNIIHCDLKPENILLKQPSksSIKVIDFGSScFEGEkvyTYI---------QS----------- 178
                         90       100       110
                 ....*....|....*....|....*....|...
gi 63054755  824 ALYVAPELLSrrnGVRYDAKVDMYSLGIILFEM 856
Cdd:cd14210  179 RFYRAPEVIL---GLPYDTAIDMWSLGCILAEL 208
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
358-510 4.51e-10

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: 62.09  E-value: 4.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  358 ILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRdmnashpfNINSQSITNIlpeG--LY-PPEVSES 434
Cdd:cd08215  112 ICLALKYLHSRKILHRDLKTQNIFLTKDGV---VKLGDFGISKVLE--------STTDLAKTVV---GtpYYlSPELCEN 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  435 SfaAASRKTDIWCFGLLVLQMLCGAHVLNKFSSLKL---IMTHVIPLLPGSY----QDLVRRCLMRDSRKRPSAIDLLSS 507
Cdd:cd08215  178 K--PYNYKSDIWALGCVLYELCTLKHPFEANNLPALvykIVKGQYPPIPSQYsselRDLVNSMLQKDPEKRPSANEILSS 255

                 ...
gi 63054755  508 HVI 510
Cdd:cd08215  256 PFI 258
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
734-915 5.09e-10

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: 62.97  E-value: 5.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  734 LSLQDIIRDK----IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENR-------------------NVKLGD 790
Cdd:cd14134   98 PSLYDFLKKNnygpFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDSDyvkvynpkkkrqirvpkstDIKLID 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  791 FGLATENenyqdnndkwknrqsaDEDLTTGVGTALYVAPE-LLSrrNGVRYDAkvDMYSLGIILFEMCM---TFSTS--- 863
Cdd:cd14134  178 FGSATFD----------------DEYHSSIVSTRHYRAPEvILG--LGWSYPC--DVWSIGCILVELYTgelLFQTHdnl 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  864 -----MERI--RIIDTIRSPSISFPSTFPFSR------------------------------ASHE--FKVIHCLLQHDP 904
Cdd:cd14134  238 ehlamMERIlgPLPKRMIRRAKKGAKYFYFYHgrldwpegsssgrsikrvckplkrlmllvdPEHRllFDLIRKMLEYDP 317
                        250
                 ....*....|.
gi 63054755  905 TKRPSSQELLE 915
Cdd:cd14134  318 SKRITAKEALK 328
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
725-857 5.22e-10

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


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 62.36  E-value: 5.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  725 YIQMEYCEKLSLQDIIRDKIPVDEMWRLFR------------QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFG 792
Cdd:cd05032   85 LVVMELMAKGDLKSYLRSRRPEAENNPGLGpptlqkfiqmaaEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGDFG 164
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63054755  793 LaTENENYQDNNDKwknrqsadedltTGVGtALYV---APELLsrRNGVrYDAKVDMYSLGIILFEMC 857
Cdd:cd05032  165 M-TRDIYETDYYRK------------GGKG-LLPVrwmAPESL--KDGV-FTTKSDVWSFGVVLWEMA 215
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
724-915 5.28e-10

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: 61.77  E-value: 5.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDKiPVDEMWR----LFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVK---LGDFGLATE 796
Cdd:cd14156   63 LHPILEYVSGGCLEELLARE-ELPLSWRekveLACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLARE 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  797 NENYQDNNDKWKnrqsadedlTTGVGTALYVAPELLsrrNGVRYDAKVDMYSLGIILFEmcmtfstsmerirIIDTIRSP 876
Cdd:cd14156  142 VGEMPANDPERK---------LSLVGSAFWMAPEML---RGEPYDRKVDVFSFGIVLCE-------------ILARIPAD 196
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 63054755  877 SISFPSTFPFSRASHEFK--VIHC----------LLQHDPTKRPSSQELLE 915
Cdd:cd14156  197 PEVLPRTGDFGLDVQAFKemVPGCpepfldlaasCCRMDAFKRPSFAELLD 247
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
724-857 5.35e-10

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: 62.46  E-value: 5.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDII-RDKIPVDEMWRLFRQILEALAYIHSR--------GMMHRDLKPGNIFLDENRNVKLGDFGLA 794
Cdd:cd14142   78 LWLITHYHENGSLYDYLqRTTLDHQEMLRLALSAASGLVHLHTEifgtqgkpAIAHRDLKSKNILVKSNGQCCIADLGLA 157
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  795 TENENYQDNNDKWKNRQsadedlttgVGTALYVAPELLSRRNGVR-YDA--KVDMYSLGIILFEMC 857
Cdd:cd14142  158 VTHSQETNQLDVGNNPR---------VGTKRYMAPEVLDETINTDcFESykRVDIYAFGLVLWEVA 214
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
743-856 5.90e-10

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: 63.13  E-value: 5.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  743 KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQDNNdkwknrqsadedlTTGVG 822
Cdd:cd05618  117 KLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTT-------------STFCG 183
                         90       100       110
                 ....*....|....*....|....*....|....
gi 63054755  823 TALYVAPELLsrrNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd05618  184 TPNYIAPEIL---RGEDYGFSVDWWALGVLMFEM 214
HisZ COG3705
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
1096-1272 6.04e-10

ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];


Pssm-ID: 442919 [Multi-domain]  Cd Length: 312  Bit Score: 62.50  E-value: 6.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755 1096 DAETIKALDEVLTEIpSLTESCILINHADILSSILDYLQVSKDKRRMATHILGQinqrltlsqvRNQLRIESLVPSTTLD 1175
Cdd:COG3705  124 DAEVIALALEALKAA-GLEDFTLDLGHVGLFRALLEALGLSEEQREELRRALAR----------KDAVELEELLAELGLS 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755 1176 D------LSLFDFRENyEEGASKLRKIFGKEmpqKMRTALNYMERVVKLLRALKISHQLYFMPLCVYNFEFYDGgLMFQA 1249
Cdd:COG3705  193 EelaealLALPELYGG-EEVLARARALLLDA---AIRAALDELEALAEALAARGPDVRLTFDLSELRGYDYYTG-IVFEA 267
                        170       180
                 ....*....|....*....|...
gi 63054755 1250 InLAEKSELICAGGRYDKLVRFF 1272
Cdd:COG3705  268 Y-APGVGDPLARGGRYDGLLAAF 289
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
286-505 6.12e-10

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: 61.99  E-value: 6.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  286 EIQELEYELESLKVIRHDLLASIYEYQLERETrgygwrLYVLQEYSPKFTLFSLLQTVLTLDV---ETVRAFSNNILEGL 362
Cdd:cd06610   42 SMDELRKEIQAMSQCNHPNVVSYYTSFVVGDE------LWLVMPLLSGGSLLDIMKSSYPRGGldeAIIATVLKEVLKGL 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  363 AELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDmnashPFNINSQSITNILPEGLY-PPEVSESSfAAASR 441
Cdd:cd06610  116 EYLHSNGQIHRDVKAGNILLGEDGS---VKIADFGVSASLAT-----GGDRTRKVRKTFVGTPCWmAPEVMEQV-RGYDF 186
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  442 KTDIWCFGLLVLQMLCGAHVLNKFSSLKLIM---THVIPLLP---------GSYQDLVRRCLMRDSRKRPSAIDLL 505
Cdd:cd06610  187 KADIWSFGITAIELATGAAPYSKYPPMKVLMltlQNDPPSLEtgadykkysKSFRKMISLCLQKDPSKRPTAEELL 262
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
290-458 6.46e-10

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: 61.54  E-value: 6.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  290 LEYELESLKVIRHDLLASIYEyQLERETRgygwrLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLG 369
Cdd:cd14162   47 LPREIEVIKGLKHPNLICFYE-AIETTSR-----VYIIMELAENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKG 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  370 ISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRtlRDMNASHPFNINSQ----SITNILPEGL----YPPEVSessfaaasr 441
Cdd:cd14162  121 VVHRDLKCENLLLDKNNN---LKITDFGFAR--GVMKTKDGKPKLSEtycgSYAYASPEILrgipYDPFLS--------- 186
                        170
                 ....*....|....*..
gi 63054755  442 ktDIWCFGLLVLQMLCG 458
Cdd:cd14162  187 --DIWSMGVVLYTMVYG 201
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
719-861 7.48e-10

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: 61.96  E-value: 7.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  719 GLNATLYIQMEYCEKLSLQDIIRDK-IPVDEMWRLFRQILEALAYIHSR----------GMMHRDLKPGNIFLDENRNVK 787
Cdd:cd14053   63 SLEAEYWLITEFHERGSLCDYLKGNvISWNELCKIAESMARGLAYLHEDipatngghkpSIAHRDFKSKNVLLKSDLTAC 142
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  788 LGDFGLATEnenYQDNNDKwknrqsadEDLTTGVGTALYVAPELLSRRNGVRYDA--KVDMYSLGIILFEMCMTFS 861
Cdd:cd14053  143 IADFGLALK---FEPGKSC--------GDTHGQVGTRRYMAPEVLEGAINFTRDAflRIDMYAMGLVLWELLSRCS 207
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
697-914 7.70e-10

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 61.50  E-value: 7.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  697 KEGSSDKDSSIEEASSV-KTQENGL---------NATLYIQMEYCEKLSLQDIIRDK---IPVDEMWRLFRQILEALAYI 763
Cdd:cd05112   37 REGAMSEEDFIEEAEVMmKLSHPKLvqlygvcleQAPICLVFEFMEHGCLSDYLRTQrglFSAETLLGMCLDVCEGMAYL 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  764 HSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenenyqdnndkwknRQSADEDLTTGVGTALYV---APELLSRRngvRY 840
Cdd:cd05112  117 EEASVIHRDLAARNCLVGENQVVKVSDFGMT---------------RFVLDDQYTSSTGTKFPVkwsSPEVFSFS---RY 178
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63054755  841 DAKVDMYSLGIILFEMCMTFSTSMERIRIIDTIRSPSISFPSTFPFSRASHEFKVIHCLLQHDPTKRPSSQELL 914
Cdd:cd05112  179 SSKSDVWSFGVLMWEVFSEGKIPYENRSNSEVVEDINAGFRLYKPRLASTHVYEIMNHCWKERPEDRPSFSLLL 252
hisZ PRK12292
ATP phosphoribosyltransferase regulatory subunit; Provisional
990-1272 8.06e-10

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 237043 [Multi-domain]  Cd Length: 391  Bit Score: 62.58  E-value: 8.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   990 VRDHVVKVFRRHG-------AKERESHILFpkSSQYDKDQASVSLLDK-NGTLLQLPYDTVLPYARNVARNAVEEE---K 1058
Cdd:PRK12292   23 IRRRLLDLFRRWGyeevitpTLEYLDTLLA--GGGAILDLRTFKLVDQlSGRTLGLRPDMTAQIARIAATRLANRPgplR 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  1059 TYLISDVFREA-KGGGRPKAIK----EISFDITTNSDnldwydAETIKALDEVL--TEIPSLTescILINHADILSSILD 1131
Cdd:PRK12292  101 LCYAGNVFRAQeRGLGRSREFLqsgvELIGDAGLEAD------AEVILLLLEALkaLGLPNFT---LDLGHVGLFRALLE 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  1132 YLQVSKDKRRMATHILGQinqrltlsqvRNQLRIESLV--PSTTLDD--LSLFDFRENyEEGASKLRKIFGKEmpqKMRT 1207
Cdd:PRK12292  172 AAGLSEELEEVLRRALAN----------KDYVALEELVldLSEELRDalLALPRLRGG-REVLEEARKLLPSL---PIKR 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63054755  1208 ALNYMERVVKLLRALKISHQLYFMPLCVYNFEFYDGgLMFQAInLAEKSELICAGGRYDKLVRFF 1272
Cdd:PRK12292  238 ALDELEALAEALEKYGYGIPLSLDLGLLRHLDYYTG-IVFEGY-VDGVGNPIASGGRYDDLLGRF 300
HisS COG0124
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ...
990-1368 8.07e-10

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: 62.83  E-value: 8.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  990 VRDHVVKVFRRHGAKE-R----ESHILFPKSSQYDKDQASV-SLLDKNGTLLQLPYD-TVlPYARNVARNAVEEE---KT 1059
Cdd:COG0124   24 VEDTIREVFERYGFQEiRtpifEYTELFARKIGEDIVEKEMyTFEDRGGRSLTLRPEgTA-PVARAVAEHGNELPfpfKL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755 1060 YLISDVFReakgGGRPKAike---isFDI-TTNSDNLDwYDAETIKALDEVLTE--IPSLTescILINH----ADILSSI 1129
Cdd:COG0124  103 YYIGPVFR----YERPQKgryrqfhqFGVeVIGSDSPL-ADAEVIALAADLLKAlgLKDFT---LEINSrglpEERAEAL 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755 1130 LDYLQvSKDKRRMATHILGQINQRLTLSQVRNQLRIESLVPSTTLDDL-SLFDFRenyeegasklrkifGKEmpqkmrtA 1208
Cdd:COG0124  175 LRYLD-KLDKIGHEDVLDEDSQRRLETNPLRAILDSKGPDCQEVLADApKLLDYL--------------GEE-------G 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755 1209 LNYMERVVKLLRALKISHQL---------YfmplcvYN---FEFYDGGLMFQAInlaekselICAGGRYDKLVRFFDppl 1276
Cdd:COG0124  233 LAHFEEVLELLDALGIPYVIdprlvrgldY------YTgtvFEIVTDGLGAQGS--------VCGGGRYDGLVEQLG--- 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755 1277 mrtarKKHVVGICFA--LEKLVFSMLRyirfhnskqsskhspsptlKSVGPWAPRRVDVLVTSIGKDSILEKCSLLQELW 1354
Cdd:COG0124  296 -----GPPTPAVGFAigLERLLLLLEE-------------------LGLLPAAEPPPDVYVVPLGEEARAEALKLAQELR 351
                        410
                 ....*....|....
gi 63054755 1355 ALNIQADIVLRGAS 1368
Cdd:COG0124  352 AAGIRVELDLGGRK 365
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
285-507 8.39e-10

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: 61.27  E-value: 8.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  285 REIQELEYELESLKVIRHDLLASIYEYQLERETrgygwrLYVLQEYSPKFTLFSLLQTVLT--LDVETVRAFSNNILEGL 362
Cdd:cd08529   41 KMREEAIDEARVLSKLNSPYVIKYYDSFVDKGK------LNIVMEYAENGDLHSLIKSQRGrpLPEDQIWKFFIQTLLGL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  363 AELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDmnashpfniNSQSITNILPEGLY-PPEVSESSfaAASR 441
Cdd:cd08529  115 SHLHSKKILHRDIKSMNIFLDKGDN---VKIGDLGVAKILSD---------TTNFAQTIVGTPYYlSPELCEDK--PYNE 180
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054755  442 KTDIWCFGLLVLQMLCGAH---VLNKFSSLKLIMTHVIPLLPGSYQ----DLVRRCLMRDSRKRPSAIDLLSS 507
Cdd:cd08529  181 KSDVWALGCVLYELCTGKHpfeAQNQGALILKIVRGKYPPISASYSqdlsQLIDSCLTKDYRQRPDTTELLRN 253
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
743-915 8.88e-10

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: 61.06  E-value: 8.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  743 KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENR--NVKLGDFGLATenenyqdnndkwknRQSADEDLTTG 820
Cdd:cd14114   96 KMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRsnEVKLIDFGLAT--------------HLDPKESVKVT 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  821 VGTALYVAPELLSRRNGVRYdakVDMYSLGIILFEMCMTFS--TSMERIRIIDTIRSPSISFPSTfPFSRASHEFK-VIH 897
Cdd:cd14114  162 TGTAEFAAPEIVEREPVGFY---TDMWAVGVLSYVLLSGLSpfAGENDDETLRNVKSCDWNFDDS-AFSGISEEAKdFIR 237
                        170
                 ....*....|....*...
gi 63054755  898 CLLQHDPTKRPSSQELLE 915
Cdd:cd14114  238 KLLLADPNKRMTIHQALE 255
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
556-914 9.11e-10

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


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 61.73  E-value: 9.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  556 FEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENSRILREVMTLSRLHHEHVVRYYTAwVETEandtvteiis 635
Cdd:cd07836    2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIHLDAEEGTPSTAIREISLMKELKHENIVRLHDV-IHTE---------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  636 sdseslsqslnmavdfrqssslpaDKLSSLDIHFEDDYNssadeedpeasdisfQYSNTSDKEGSSDkdssieeASSVKT 715
Cdd:cd07836   71 ------------------------NKLMLVFEYMDKDLK---------------KYMDTHGVRGALD-------PNTVKS 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  716 QenglnatlyiqmeyceklslqdiirdkipvdeMWrlfrQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAt 795
Cdd:cd07836  105 F--------------------------------TY----QLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLA- 147
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  796 enENYQDNNDKWKNRqsadedlttgVGTALYVAPELL--SRrngvRYDAKVDMYSLGIILFEMCM--------TFSTSME 865
Cdd:cd07836  148 --RAFGIPVNTFSNE----------VVTLWYRAPDVLlgSR----TYSTSIDIWSVGCIMAEMITgrplfpgtNNEDQLL 211
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63054755  866 RI-RIIDTIRSPSISFPSTFP-----FSRASHE-------------FKVIHCLLQHDPTKRPSSQELL 914
Cdd:cd07836  212 KIfRIMGTPTESTWPGISQLPeykptFPRYPPQdlqqlfphadplgIDLLHRLLQLNPELRISAHDAL 279
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
724-915 1.02e-09

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 61.40  E-value: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDI-----IRDKIPVDEMWRLFRQILEALAYIHSR-GMMHRDLKPGNIFLDENRNVKLGDFGLATen 797
Cdd:cd06622   74 VYMCMEYMDAGSLDKLyaggvATEGIPEDVLRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGNGQVKLCDFGVSG-- 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  798 eNYQDNNDKwknrqsadedltTGVGTALYVAPELLSRRNGVR---YDAKVDMYSLGIILFEMCM--------TFSTSMER 866
Cdd:cd06622  152 -NLVASLAK------------TNIGCQSYMAPERIKSGGPNQnptYTVQSDVWSLGLSILEMALgrypyppeTYANIFAQ 218
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 63054755  867 IRIIdtIRSPSISFPSTfpFSRASHEFkVIHClLQHDPTKRPSSQELLE 915
Cdd:cd06622  219 LSAI--VDGDPPTLPSG--YSDDAQDF-VAKC-LNKIPNRRPTYAQLLE 261
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
697-913 1.05e-09

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


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 61.24  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  697 KEGSSDKDSSIEEASSVKTQENGLNATLY---------IQMEYCEKLSLQDIIRD------KIPvdEMWRLFRQILEALA 761
Cdd:cd05070   42 KPGTMSPESFLEEAQIMKKLKHDKLVQLYavvseepiyIVTEYMSKGSLLDFLKDgegralKLP--NLVDMAAQVAAGMA 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  762 YIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLA---TENENYQDNNDKWKNRQSADEdlttgvgTALYvapellsrrngV 838
Cdd:cd05070  120 YIERMNYIHRDLRSANILVGNGLICKIADFGLArliEDNEYTARQGAKFPIKWTAPE-------AALY-----------G 181
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  839 RYDAKVDMYSLGIILFEMCMTFST---SMERIRIIDTI-RSPSISFPSTFPFSRasHEFkVIHClLQHDPTKRPSSQEL 913
Cdd:cd05070  182 RFTIKSDVWSFGILLTELVTKGRVpypGMNNREVLEQVeRGYRMPCPQDCPISL--HEL-MIHC-WKKDPEERPTFEYL 256
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
706-856 1.20e-09

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


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 60.77  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  706 SIEEASSVKTQENGLNAT-LYIQMEYCEKLSLQDIIRD--KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDE 782
Cdd:cd14665   52 SLRHPNIVRFKEVILTPThLAIVMEYAAGGELFERICNagRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDG 131
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  783 NR--NVKLGDFGLAtenenyqdnndkwKNRQSADEDLTTgVGTALYVAPELLSRRngvRYDAKV-DMYSLGIILFEM 856
Cdd:cd14665  132 SPapRLKICDFGYS-------------KSSVLHSQPKST-VGTPAYIAPEVLLKK---EYDGKIaDVWSCGVTLYVM 191
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
720-856 1.29e-09

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: 61.20  E-value: 1.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  720 LNATLYIQMEYCEKLSLQDIIR-DKIPVDEMWRLFRQILEALAYIH-----SRG------MMHRDLKPGNIFLDENRNVK 787
Cdd:cd14140   64 LEMELWLITAFHDKGSLTDYLKgNIVSWNELCHIAETMARGLSYLHedvprCKGeghkpaIAHRDFKSKNVLLKNDLTAV 143
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054755  788 LGDFGLATENENYQDNNDkwknrqsadedlTTG-VGTALYVAPELLSRRNGVRYDA--KVDMYSLGIILFEM 856
Cdd:cd14140  144 LADFGLAVRFEPGKPPGD------------THGqVGTRRYMAPEVLEGAINFQRDSflRIDMYAMGLVLWEL 203
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
724-913 1.35e-09

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: 60.70  E-value: 1.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRD------KIPvdEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEN 797
Cdd:cd14203   64 IYIVTEFMSKGSLLDFLKDgegkylKLP--QLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLI 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  798 EnyqdnNDKWKNRQSADEDLT-TGVGTALYvapellsrrngVRYDAKVDMYSLGIILFEMCMTFST---SMERIRIIDTI 873
Cdd:cd14203  142 E-----DNEYTARQGAKFPIKwTAPEAALY-----------GRFTIKSDVWSFGILLTELVTKGRVpypGMNNREVLEQV 205
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 63054755  874 -RSPSISFPSTFPFSRasHEFKvIHClLQHDPTKRPSSQEL 913
Cdd:cd14203  206 eRGYRMPCPPGCPESL--HELM-CQC-WRKDPEERPTFEYL 242
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
755-912 1.39e-09

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: 61.53  E-value: 1.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATenenyqdnndkwknrQSADEDLTTG-VGTALYVAPELLs 833
Cdd:cd05632  112 EILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAV---------------KIPEGESIRGrVGTVGYMAPEVL- 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  834 rrNGVRYDAKVDMYSLGIILFEMC---MTFSTSMERI-------RIIDTIRSPSISFpstfpfsraSHEFKVI-HCLLQH 902
Cdd:cd05632  176 --NNQRYTLSPDYWGLGCLIYEMIegqSPFRGRKEKVkreevdrRVLETEEVYSAKF---------SEEAKSIcKMLLTK 244
                        170
                 ....*....|
gi 63054755  903 DPTKRPSSQE 912
Cdd:cd05632  245 DPKQRLGCQE 254
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
751-856 1.41e-09

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


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 61.13  E-value: 1.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  751 RLFR-QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenenyqdnndkwKNRQSADEDLTTGVGTALYVAP 829
Cdd:cd07870  101 RLFMfQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLA-------------RAKSIPSQTYSSEVVTLWYRPP 167
                         90       100
                 ....*....|....*....|....*..
gi 63054755  830 ELLsrRNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd07870  168 DVL--LGATDYSSALDIWGAGCIFIEM 192
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
724-915 1.46e-09

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


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 60.69  E-value: 1.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDII-RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRN--VKLGDFGLATEneny 800
Cdd:cd14108   73 VIIVTELCHEELLERITkRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTdqVRICDFGNAQE---- 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  801 qdnndkwknrQSADEDLTTGVGTALYVAPELLsrrNGVRYDAKVDMYSLGIILFeMCMT----FSTSMERIRIIDtIRSP 876
Cdd:cd14108  149 ----------LTPNEPQYCKYGTPEFVAPEIV---NQSPVSKVTDIWPVGVIAY-LCLTgispFVGENDRTTLMN-IRNY 213
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 63054755  877 SISFPSTFpFSRASHEFK--VIHCLLQHdpTKRPSSQELLE 915
Cdd:cd14108  214 NVAFEESM-FKDLCREAKgfIIKVLVSD--RLRPDAEETLE 251
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
697-916 1.61e-09

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: 60.28  E-value: 1.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  697 KEGSSDKDSSIEEASSVK-------TQENGLNAT---LYIQMEYCEKLSLQDIIRDKIPVDEMWRLF---RQILEALAYI 763
Cdd:cd05113   37 KEGSMSEDEFIEEAKVMMnlsheklVQLYGVCTKqrpIFIITEYMANGCLLNYLREMRKRFQTQQLLemcKDVCEAMEYL 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  764 HSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenenyqdnndkwknRQSADEDLTTGVGTALYV---APELLSRrngVRY 840
Cdd:cd05113  117 ESKQFLHRDLAARNCLVNDQGVVKVSDFGLS---------------RYVLDDEYTSSVGSKFPVrwsPPEVLMY---SKF 178
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  841 DAKVDMYSLGIILFEMCMTFSTSMERIRIIDTIRSPSISFPSTFPFSRASHEFKVIHCLLQHDPTKRPSSQELLES 916
Cdd:cd05113  179 SSKSDVWAFGVLMWEVYSLGKMPYERFTNSETVEHVSQGLRLYRPHLASEKVYTIMYSCWHEKADERPTFKILLSN 254
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
293-507 1.72e-09

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: 60.48  E-value: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  293 ELESLKVIRHDLLASIYEYqleRETRGYgwrLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISH 372
Cdd:cd14084   61 EIEILKKLSHPCIIKIEDF---FDAEDD---YYIVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIH 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  373 KSLHLDNVVLFHSGHRTFAKLMDFGFTRTLRDmnashpfninsQSITNIL---PEGLYPPEVSESSFAAASRKTDIWCFG 449
Cdd:cd14084  135 RDLKPENVLLSSQEEECLIKITDFGLSKILGE-----------TSLMKTLcgtPTYLAPEVLRSFGTEGYTRAVDCWSLG 203
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054755  450 LLVLQMLCGAHvlnKFSSLKLIMTHVIPLLPGSY--------------QDLVRRCLMRDSRKRPSAIDLLSS 507
Cdd:cd14084  204 VILFICLSGYP---PFSEEYTQMSLKEQILSGKYtfipkawknvseeaKDLVKKMLVVDPSRRPSIEEALEH 272
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
724-856 1.84e-09

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: 61.60  E-value: 1.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKlSLQDIIRDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLA-TENENYQd 802
Cdd:cd07875  104 VYIVMELMDA-NLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLArTAGTSFM- 181
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 63054755  803 nndkwknrqsadedLTTGVGTALYVAPELLSrrnGVRYDAKVDMYSLGIILFEM 856
Cdd:cd07875  182 --------------MTPYVVTRYYRAPEVIL---GMGYKENVDIWSVGCIMGEM 218
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
736-914 2.06e-09

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


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 59.98  E-value: 2.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  736 LQDIIRDK--IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENR-NVKLGDFGlatenenyqdNNDKWKNRQS 812
Cdd:cd14100   93 LFDFITERgaLPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDLNTgELKLIDFG----------SGALLKDTVY 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  813 ADEDlttgvGTALYVAPELLSRRngvRYDAK-VDMYSLGIILFEM-C--MTFSTSMERIRiidtirspsisfPSTFPFSR 888
Cdd:cd14100  163 TDFD-----GTRVYSPPEWIRFH---RYHGRsAAVWSLGILLYDMvCgdIPFEHDEEIIR------------GQVFFRQR 222
                        170       180
                 ....*....|....*....|....*..
gi 63054755  889 ASHEFK-VIHCLLQHDPTKRPSSQELL 914
Cdd:cd14100  223 VSSECQhLIKWCLALRPSDRPSFEDIQ 249
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
723-913 2.94e-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: 2.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  723 TLYIQMEYCEKLSLQDIIRDK--IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDEN-RNVKLGDFGLAtenEN 799
Cdd:cd13991   72 WVNIFMDLKEGGSLGQLIKEQgcLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDgSDAFLCDFGHA---EC 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  800 YQdnNDKWknrqsADEDLTTGV--GTALYVAPELLSrrnGVRYDAKVDMYSLGIILFEM---------------CMTFST 862
Cdd:cd13991  149 LD--PDGL-----GKSLFTGDYipGTETHMAPEVVL---GKPCDAKVDVWSSCCMMLHMlngchpwtqyysgplCLKIAN 218
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 63054755  863 SMERIRIIDtirspsisfPSTFPFSrasheFKVIHCLLQHDPTKRPSSQEL 913
Cdd:cd13991  219 EPPPLREIP---------PSCAPLT-----AQAIQAGLRKEPVHRASAAEL 255
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
279-508 3.27e-09

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


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 60.01  E-value: 3.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  279 STEDGKREIQELEYeleslkvIRHDLLASIYEYQLERETRgygwrLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNI 358
Cdd:cd05613   47 TAEHTRTERQVLEH-------IRQSPFLVTLHYAFQTDTK-----LHLILDYINGGELFTHLSQRERFTENEVQIYIGEI 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  359 LEGLAELHRLGISHKSLHLDNVVLFHSGHRTfakLMDFGFTRTLRDMNASHPFNInSQSITNIlpeglyPPEVSESSFAA 438
Cdd:cd05613  115 VLALEHLHKLGIIYRDIKLENILLDSSGHVV---LTDFGLSKEFLLDENERAYSF-CGTIEYM------APEIVRGGDSG 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  439 ASRKTDIWCFGLLVLQMLCGAH---VLNKFSSLKLIMTHVI---PLLPGSY----QDLVRRCLMRDSRKR----PSAIDL 504
Cdd:cd05613  185 HDKAVDWWSLGVLMYELLTGASpftVDGEKNSQAEISRRILksePPYPQEMsalaKDIIQRLLMKDPKKRlgcgPNGADE 264

                 ....
gi 63054755  505 LSSH 508
Cdd:cd05613  265 IKKH 268
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
724-916 3.38e-09

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


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 59.38  E-value: 3.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIR---DKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAteneny 800
Cdd:cd05041   68 IMIVMELVPGGSLLTFLRkkgARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMS------ 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  801 qdnndkwknRQSADEDLTTGVGTAL----YVAPELLsrrNGVRYDAKVDMYSLGIILFEmcmTFS----------TSMER 866
Cdd:cd05041  142 ---------REEEDGEYTVSDGLKQipikWTAPEAL---NYGRYTSESDVWSFGILLWE---IFSlgatpypgmsNQQTR 206
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 63054755  867 IRIIDTIRSPSisfPSTFPfsrashefKVIHCLLQH----DPTKRPSSQELLES 916
Cdd:cd05041  207 EQIESGYRMPA---PELCP--------EAVYRLMLQcwayDPENRPSFSEIYNE 249
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
720-860 4.12e-09

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: 59.55  E-value: 4.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  720 LNATLYIQMEYCEKLSLQDIIRDK-----IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFL-DENRNV--KLGDF 791
Cdd:cd14039   67 VNDVPLLAMEYCSGGDLRKLLNKPenccgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLqEINGKIvhKIIDL 146
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63054755  792 GLAtenenyqdnndkwknrqsadEDLTTG------VGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMCMTF 860
Cdd:cd14039  147 GYA--------------------KDLDQGslctsfVGTLQYLAPELFENKS---YTVTVDYWSFGTMVFECIAGF 198
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
281-511 4.78e-09

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: 59.18  E-value: 4.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  281 EDGKREIQELEyELESLKVIRHdllasiYEYQLEretrgyGWRLYVLQEYSPKFTLFSLLQTVlTLDVETVRAFSNNILE 360
Cdd:cd06609   44 EDIQQEIQFLS-QCDSPYITKY------YGSFLK------GSKLWIIMEYCGGGSVLDLLKPG-PLDETYIAFILREVLL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  361 GLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFG------FTRTLRDMNASHPFNInsqsitnilpeglyPPEV-SE 433
Cdd:cd06609  110 GLEYLHSEGKIHRDIKAANILLSEEGD---VKLADFGvsgqltSTMSKRNTFVGTPFWM--------------APEViKQ 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  434 SSFaaaSRKTDIWCFGLLVLQMLCGAHVLNKFSSLK---LIMTHVIPLLPGS-----YQDLVRRCLMRDSRKRPSAIDLL 505
Cdd:cd06609  173 SGY---DEKADIWSLGITAIELAKGEPPLSDLHPMRvlfLIPKNNPPSLEGNkfskpFKDFVELCLNKDPKERPSAKELL 249

                 ....*.
gi 63054755  506 SSHVIR 511
Cdd:cd06609  250 KHKFIK 255
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
760-856 5.00e-09

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: 59.44  E-value: 5.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  760 LAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenenyqdnndkwknRQSADEDLTTG----VGTALYVAPELLsrR 835
Cdd:cd14158  130 INYLHENNHIHRDIKSANILLDETFVPKISDFGLA---------------RASEKFSQTIMteriVGTTAYMAPEAL--R 192
                         90       100
                 ....*....|....*....|.
gi 63054755  836 NGVryDAKVDMYSLGIILFEM 856
Cdd:cd14158  193 GEI--TPKSDIFSFGVVLLEI 211
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
358-506 5.85e-09

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


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 58.82  E-value: 5.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  358 ILEGLAELHRLGISHKSLHLDNVVLFHSGHRTFAKLM--DFGFTRTLrDMNASHPFNINSQSITnilpEGLYPPEV-SES 434
Cdd:cd13982  108 IASGLAHLHSLNIVHRDLKPQNILISTPNAHGNVRAMisDFGLCKKL-DVGRSSFSRRSGVAGT----SGWIAPEMlSGS 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  435 SFAAASRKTDIWCFGLLVLQMLCGAH-------------VLNKFSSLKLI-MTHVIPLLpgsyQDLVRRCLMRDSRKRPS 500
Cdd:cd13982  183 TKRRQTRAVDIFSLGCVFYYVLSGGShpfgdklereaniLKGKYSLDKLLsLGEHGPEA----QDLIERMIDFDPEKRPS 258

                 ....*.
gi 63054755  501 AIDLLS 506
Cdd:cd13982  259 AEEVLN 264
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
747-915 6.57e-09

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: 58.65  E-value: 6.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  747 DEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDE----NRNVKLGDFGLATENENYQDnndkWKNRqsadedlttgVG 822
Cdd:cd14105  108 EEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDknvpIPRIKLIDFGLAHKIEDGNE----FKNI----------FG 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  823 TALYVAPELlsrrngVRYDA---KVDMYSLGI---ILFEMCMTF--STSMErirIIDTIRSPSISFPSTFpFSRASHEFK 894
Cdd:cd14105  174 TPEFVAPEI------VNYEPlglEADMWSIGVityILLSGASPFlgDTKQE---TLANITAVNYDFDDEY-FSNTSELAK 243
                        170       180
                 ....*....|....*....|..
gi 63054755  895 -VIHCLLQHDPTKRPSSQELLE 915
Cdd:cd14105  244 dFIRQLLVKDPRKRMTIQESLR 265
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
754-856 6.87e-09

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: 59.16  E-value: 6.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  754 RQILEALAYIHSRGMMHRDLKPGNIFLDENRNV-KLGDFGLATEnenyqdnndkwknrqSADEDLTTGVGTALYVAPELL 832
Cdd:cd14135  112 QQLFLALKHLKKCNILHADIKPDNILVNEKKNTlKLCDFGSASD---------------IGENEITPYLVSRFYRAPEII 176
                         90       100
                 ....*....|....*....|....
gi 63054755  833 SrrnGVRYDAKVDMYSLGIILFEM 856
Cdd:cd14135  177 L---GLPYDYPIDMWSVGCTLYEL 197
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
293-505 7.05e-09

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: 58.97  E-value: 7.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  293 ELESLKVIRHDLLASIYEYQLEREtrgygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISH 372
Cdd:cd07846   50 EIKMLKQLRHENLVNLIEVFRRKK------RWYLVFEFVDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIH 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  373 KSLHLDNVVLFHSGhrtFAKLMDFGFTRTLrdmnashpfNINSQSITNILPEGLY-PPE--VSESSFAaasRKTDIWCFG 449
Cdd:cd07846  124 RDIKPENILVSQSG---VVKLCDFGFARTL---------AAPGEVYTDYVATRWYrAPEllVGDTKYG---KAVDVWAVG 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  450 LLVLQMLCGA-------------HVLNKFSSL----KLIMT--------------HVIPL------LPGSYQDLVRRCLM 492
Cdd:cd07846  189 CLVTEMLTGEplfpgdsdidqlyHIIKCLGNLiprhQELFQknplfagvrlpevkEVEPLerrypkLSGVVIDLAKKCLH 268
                        250
                 ....*....|...
gi 63054755  493 RDSRKRPSAIDLL 505
Cdd:cd07846  269 IDPDKRPSCSELL 281
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
728-915 7.06e-09

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 58.56  E-value: 7.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  728 MEYCEKLSLQDII-RDKIPVDEM--WRLfrQILEALAYIHSRGMM---HRDLKPGNIFLDE--------NRNVKLGDFGL 793
Cdd:cd14061   72 MEYARGGALNRVLaGRKIPPHVLvdWAI--QIARGMNYLHNEAPVpiiHRDLKSSNILILEaienedleNKTLKITDFGL 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  794 ATENENYQdnndkwknRQSAdedlttgVGTALYVAPELLSRRngvRYDAKVDMYSLGIILFEMCmtfsTSMERIRIID-- 871
Cdd:cd14061  150 AREWHKTT--------RMSA-------AGTYAWMAPEVIKSS---TFSKASDVWSYGVLLWELL----TGEVPYKGIDgl 207
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 63054755  872 ------TIRSPSISFPSTFP--FSRASHEfkvihClLQHDPTKRPSSQELLE 915
Cdd:cd14061  208 avaygvAVNKLTLPIPSTCPepFAQLMKD-----C-WQPDPHDRPSFADILK 253
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
293-507 7.24e-09

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: 58.35  E-value: 7.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  293 ELESLKVIRHDLLASIYEYqLERETRgygwrLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISH 372
Cdd:cd14080   52 ELEILRKLRHPNIIQVYSI-FERGSK-----VFIFMEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAH 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  373 KSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDMNAShpfnINSQ----SITNILPEGL----YPPevsessfaaasRKTD 444
Cdd:cd14080  126 RDLKCENILLDSNNN---VKLSDFGFARLCPDDDGD----VLSKtfcgSAAYAAPEILqgipYDP-----------KKYD 187
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63054755  445 IWCFGLLVLQMLCGAHVLNKfSSLKLIM-----------THVIPLLPgSYQDLVRRCLMRDSRKRPSAIDLLSS 507
Cdd:cd14080  188 IWSLGVILYIMLCGSMPFDD-SNIKKMLkdqqnrkvrfpSSVKKLSP-ECKDLIDQLLEPDPTKRATIEEILNH 259
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
282-508 7.56e-09

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: 58.60  E-value: 7.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  282 DGKREIQ-ELEYELESLKVIRHDLLASIY-EYQLERETrgygwrLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNIL 359
Cdd:cd06620   41 DAKSSVRkQILRELQILHECHSPYIVSFYgAFLNENNN------IIICMEYMDCGSLDKILKKKGPFPEEVLGKIAVAVL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  360 EGLAELHR-LGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLrdmnashpfnINSQSITNilpeglyppeVSESSFAA 438
Cdd:cd06620  115 EGLTYLYNvHRIIHRDIKPSNILVNSKGQ---IKLCDFGVSGEL----------INSIADTF----------VGTSTYMS 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  439 ASR--------KTDIWCFGLLVLQMLCG--------------AHVLNKFSSLKLIMTHVIPLLPGS------YQDLVRRC 490
Cdd:cd06620  172 PERiqggkysvKSDVWSLGLSIIELALGefpfagsnddddgyNGPMGILDLLQRIVNEPPPRLPKDrifpkdLRDFVDRC 251
                        250
                 ....*....|....*...
gi 63054755  491 LMRDSRKRPSAIDLLSSH 508
Cdd:cd06620  252 LLKDPRERPSPQLLLDHD 269
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
562-915 7.63e-09

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 59.22  E-value: 7.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  562 LGRGGFGEVVKVKN-RIDG----RFYAVKKLVLLSDDKENSRILREVMTLSRL-HHEHVVRYYTAW----------VETE 625
Cdd:cd05103   15 LGRGAFGQVIEADAfGIDKtatcRTVAVKMLKEGATHSEHRALMSELKILIHIgHHLNVVNLLGACtkpggplmviVEFC 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  626 ANDTVTEIISSDSESLSQSLNMAVDFRQSSSLPADklSSLDIHFEDDYNSSAdeedpeasdisfqysntsdkeGSSDKDS 705
Cdd:cd05103   95 KFGNLSAYLRSKRSEFVPYKTKGARFRQGKDYVGD--ISVDLKRRLDSITSS---------------------QSSASSG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  706 SIEEASSVKTQEnglnatlyiqmeycEKLSLQDIIRDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRN 785
Cdd:cd05103  152 FVEEKSLSDVEE--------------EEAGQEDLYKDFLTLEDLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNV 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  786 VKLGDFGLAteNENYQDNNdkWKNRQSADEDLTtgvgtalYVAPELLSRRngvRYDAKVDMYSLGIILFEMCMTFSTSME 865
Cdd:cd05103  218 VKICDFGLA--RDIYKDPD--YVRKGDARLPLK-------WMAPETIFDR---VYTIQSDVWSFGVLLWEIFSLGASPYP 283
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  866 RIRIIDT----------IRSPSISFPSTFPfsrashefKVIHClLQHDPTKRPSSQELLE 915
Cdd:cd05103  284 GVKIDEEfcrrlkegtrMRAPDYTTPEMYQ--------TMLDC-WHGEPSQRPTFSELVE 334
RWD_DRWD_ELF-like cd11605
RWD, DRWD, and ELF domain family; The family includes the RWD, double-RWD (DRWD), and ELF ...
20-120 8.44e-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: 54.50  E-value: 8.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   20 ALKAIFMDDFEELkvrnawNVTNGHVYCIHLcsRSANSKSIAKLDLCIELGRSY-PYVKPVIKLQNGENVLNSQIRFLLD 98
Cdd:cd11605    1 ALESIYGDELEVL------SDDSPLRFSIRL--SPEEEEDDPPLELEFTLPPGYpPEEPPLITLRSPKLSSAERLSLLKL 72
                         90       100
                 ....*....|....*....|..
gi 63054755   99 KLDTKAKDLLGEEMIFELASIV 120
Cdd:cd11605   73 ELEEAAEENLGEPMLFDLVEAL 94
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
724-856 8.73e-09

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: 59.29  E-value: 8.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYC---EKLSLqdIIRDKIPVDEMWRLF-RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAT---- 795
Cdd:cd05625   76 LYFVMDYIpggDMMSL--LIRMGVFPEDLARFYiAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrw 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  796 --ENENYQ----------DNNDKWKN------------------RQSADEDLTTGVGTALYVAPELLSRRNgvrYDAKVD 845
Cdd:cd05625  154 thDSKYYQsgdhlrqdsmDFSNEWGDpencrcgdrlkplerraaRQHQRCLAHSLVGTPNYIAPEVLLRTG---YTQLCD 230
                        170
                 ....*....|.
gi 63054755  846 MYSLGIILFEM 856
Cdd:cd05625  231 WWSVGVILFEM 241
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
724-907 8.75e-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: 59.24  E-value: 8.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDKIPVDEMWRLF--RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENenyq 801
Cdd:cd05615   86 LYFVMEYVNGGDLMYHIQQVGKFKEPQAVFyaAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEH---- 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  802 dnndkwknrqsADEDLTTGV--GTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMCM---TFSTSMERiRIIDTIRSP 876
Cdd:cd05615  162 -----------MVEGVTTRTfcGTPDYIAPEIIAYQP---YGRSVDWWAYGVLLYEMLAgqpPFDGEDED-ELFQSIMEH 226
                        170       180       190
                 ....*....|....*....|....*....|.
gi 63054755  877 SISFPSTFpfsrASHEFKVIHCLLQHDPTKR 907
Cdd:cd05615  227 NVSYPKSL----SKEAVSICKGLMTKHPAKR 253
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
725-925 9.93e-09

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


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 58.55  E-value: 9.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  725 YIQMEYCEKLslqdiirDKIP----VDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAteneny 800
Cdd:cd07869   84 YVHTDLCQYM-------DKHPgglhPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLA------ 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  801 qdnndkwKNRQSADEDLTTGVGTALYVAPELLsrRNGVRYDAKVDMYSLGIILFEMCMTFST---------SMERIRII- 870
Cdd:cd07869  151 -------RAKSVPSHTYSNEVVTLWYRPPDVL--LGSTEYSTCLDMWGVGCIFVEMIQGVAAfpgmkdiqdQLERIFLVl 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  871 -----DTIrsPSI-SFPSTFP-----------------FSRASHEFKVIHCLLQHDPTKRPSSQELLESE---AIPPKVG 924
Cdd:cd07869  222 gtpneDTW--PGVhSLPHFKPerftlyspknlrqawnkLSYVNHAEDLASKLLQCFPKNRLSAQAALSHEyfsDLPPRLW 299

                 .
gi 63054755  925 E 925
Cdd:cd07869  300 E 300
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
720-915 1.09e-08

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


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 57.96  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  720 LNATLYIQMEYCEKLSLQDIIRDK----IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAT 795
Cdd:cd05083   69 LHNGLYIVMELMSKGNLVNFLRSRgralVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAK 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  796 ENENYQDNND---KWknrqsadedlttgvgtalyVAPELLSRRngvRYDAKVDMYSLGIILFEMCMTFSTSMERIRIIDT 872
Cdd:cd05083  149 VGSMGVDNSRlpvKW-------------------TAPEALKNK---KFSSKSDVWSYGVLLWEVFSYGRAPYPKMSVKEV 206
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 63054755  873 IRSPSISFPSTFPFSRASHEFKVIHCLLQHDPTKRPSSQELLE 915
Cdd:cd05083  207 KEAVEKGYRMEPPEGCPPDVYSIMTSCWEAEPGKRPSFKKLRE 249
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
719-859 1.18e-08

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 58.13  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  719 GLNATLYIQMEYCEKLSLQDIIR-DKIPVDEMWRLFRQILEALAYIHSR--------GMMHRDLKPGNIFLDENRNVKLG 789
Cdd:cd14220   63 GSWTQLYLITDYHENGSLYDFLKcTTLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGTCCIA 142
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  790 DFGLATENENyqDNNDkwknrqsADEDLTTGVGTALYVAPELLSR---RNGVRYDAKVDMYSLGIILFEM---CMT 859
Cdd:cd14220  143 DLGLAVKFNS--DTNE-------VDVPLNTRVGTKRYMAPEVLDEslnKNHFQAYIMADIYSFGLIIWEMarrCVT 209
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
323-458 1.21e-08

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: 58.77  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  323 RLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRT- 401
Cdd:cd05590   70 RLFFVMEFVNGGDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGH---CKLADFGMCKEg 146
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 63054755  402 LRDMNASHPFNINSQSIT-NILPEGLYPPEVsessfaaasrktDIWCFGLLVLQMLCG 458
Cdd:cd05590  147 IFNGKTTSTFCGTPDYIApEILQEMLYGPSV------------DWWAMGVLLYEMLCG 192
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
724-856 1.32e-08

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: 57.71  E-value: 1.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDK---IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDeNRNVKLGDFGLATENENY 800
Cdd:cd14153   71 LAIITSLCKGRTLYSVVRDAkvvLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFTISGVL 149
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054755  801 QDNNDKWKNRQSAdedlttgvGTALYVAPELL------SRRNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd14153  150 QAGRREDKLRIQS--------GWLCHLAPEIIrqlspeTEEDKLPFSKHSDVFAFGTIWYEL 203
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
759-913 1.51e-08

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: 58.35  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  759 ALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLA--------------TENENYQDNND------------------- 805
Cdd:cd05610  116 ALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSkvtlnrelnmmdilTTPSMAKPKNDysrtpgqvlslisslgfnt 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  806 -------KWKNRQSADEDLTTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEMcMT----FSTSMERiRIIDTIR 874
Cdd:cd05610  196 ptpyrtpKSVRRGAARVEGERILGTPDYLAPELLLGKP---HGPAVDWWALGVCLFEF-LTgippFNDETPQ-QVFQNIL 270
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 63054755  875 SPSISFPS-TFPFSRASHEfkVIHCLLQHDPTKRPSSQEL 913
Cdd:cd05610  271 NRDIPWPEgEEELSVNAQN--AIEILLTMDPTKRAGLKEL 308
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
755-870 1.71e-08

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: 57.73  E-value: 1.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEnenyqdnndkwknrQSADEDLTTGVGTALYVAPELLSR 834
Cdd:cd05630  110 EICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVH--------------VPEGQTIKGRVGTVGYMAPEVVKN 175
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 63054755  835 RngvRYDAKVDMYSLGIILFEMCMTFSTSMERIRII 870
Cdd:cd05630  176 E---RYTFSPDWWALGCLLYEMIAGQSPFQQRKKKI 208
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
286-511 1.75e-08

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


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 57.81  E-value: 1.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  286 EIQELEYELESLKVIRHDL-LASIYEYQLERETRGYGWRLYVLQEYSPKFTLFSLLQTVL--TLDVETVRAFSNNILEGL 362
Cdd:cd06637   45 EEEEIKQEINMLKKYSHHRnIATYYGAFIKKNPPGMDDQLWLVMEFCGAGSVTDLIKNTKgnTLKEEWIAYICREILRGL 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  363 AELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTL-RDMNASHPFninsqsitnILPEGLYPPEV---SESSFAA 438
Cdd:cd06637  125 SHLHQHKVIHRDIKGQNVLLTENAE---VKLVDFGVSAQLdRTVGRRNTF---------IGTPYWMAPEViacDENPDAT 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  439 ASRKTDIWCFGLLVLQMLCGAHVL---NKFSSLKLIMTHVIPLLPGS-----YQDLVRRCLMRDSRKRPSAIDLLSSHVI 510
Cdd:cd06637  193 YDFKSDLWSLGITAIEMAEGAPPLcdmHPMRALFLIPRNPAPRLKSKkwskkFQSFIESCLVKNHSQRPSTEQLMKHPFI 272

                 .
gi 63054755  511 R 511
Cdd:cd06637  273 R 273
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
697-854 1.75e-08

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: 57.24  E-value: 1.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  697 KEGSSDKDSSIEEASsVKTQENGLN-ATLY----------IQMEYCEKLSL-QDIIRDKIP---VDEMwRLFRQILEALA 761
Cdd:cd14190   39 KQNSKDKEMVLLEIQ-VMNQLNHRNlIQLYeaietpneivLFMEYVEGGELfERIVDEDYHlteVDAM-VFVRQICEGIQ 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  762 YIHSRGMMHRDLKPGNIFL--DENRNVKLGDFGLAtenenyqdnndkwkNRQSADEDLTTGVGTALYVAPELlsrrngVR 839
Cdd:cd14190  117 FMHQMRVLHLDLKPENILCvnRTGHQVKIIDFGLA--------------RRYNPREKLKVNFGTPEFLSPEV------VN 176
                        170
                 ....*....|....*...
gi 63054755  840 YDA---KVDMYSLGIILF 854
Cdd:cd14190  177 YDQvsfPTDMWSMGVITY 194
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
697-942 1.78e-08

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


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 58.05  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  697 KEGSSDKD-----SSIEEASSVKTQENGLN--------ATLYIQMEYCEKLSLQDIIRDKIP-----------VDEMWRL 752
Cdd:cd05099   53 KDNATDKDladliSEMELMKLIGKHKNIINllgvctqeGPLYVIVEYAAKGNLREFLRARRPpgpdytfditkVPEEQLS 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  753 FR-------QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYqdnnDKWKNRqsadedlTTGVGTAL 825
Cdd:cd05099  133 FKdlvscayQVARGMEYLESRRCIHRDLAARNVLVTEDNVMKIADFGLARGVHDI----DYYKKT-------SNGRLPVK 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  826 YVAPELLSRRngvRYDAKVDMYSLGIILFEMcMTFSTSmeririidtiRSPSISFPSTFPFSRASHEF-KVIHC-----L 899
Cdd:cd05099  202 WMAPEALFDR---VYTHQSDVWSFGILMWEI-FTLGGS----------PYPGIPVEELFKLLREGHRMdKPSNCthelyM 267
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 63054755  900 LQHD-----PTKRPSSQELLES-EAIPPKVGEEFIQeglrlLSNPNTPY 942
Cdd:cd05099  268 LMREcwhavPTQRPTFKQLVEAlDKVLAAVSEEYLD-----LSMPFEQY 311
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
265-508 2.14e-08

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: 57.22  E-value: 2.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  265 VFLLRTVRISTPYWSTEDGKreIQELEYeLESLK----VIRhdllasIYEYQLeRETRGYgwrLYVLQEYSpKFTLFSLL 340
Cdd:cd14131   27 IYALKRVDLEGADEQTLQSY--KNEIEL-LKKLKgsdrIIQ------LYDYEV-TDEDDY---LYMVMECG-EIDLATIL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  341 QTVL--TLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFhsghRTFAKLMDFGF--------TRTLRDMNASHP 410
Cdd:cd14131   93 KKKRpkPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLV----KGRLKLIDFGIakaiqndtTSIVRDSQVGTL 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  411 FNINSQSITNILPEGLYPPEVSessfaaASRKTDIWCFGLLVLQMLCG----AHVLNKFSSLKLIM--THVI---PLLPG 481
Cdd:cd14131  169 NYMSPEAIKDTSASGEGKPKSK------IGRPSDVWSLGCILYQMVYGktpfQHITNPIAKLQAIIdpNHEIefpDIPNP 242
                        250       260
                 ....*....|....*....|....*..
gi 63054755  482 SYQDLVRRCLMRDSRKRPSaIDLLSSH 508
Cdd:cd14131  243 DLIDVMKRCLQRDPKKRPS-IPELLNH 268
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
293-458 2.94e-08

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: 57.20  E-value: 2.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  293 ELESLKVIRHDLLASIY-EYQLEretrgygWRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGIS 371
Cdd:cd05580   51 EKRILSEVRHPFIVNLLgSFQDD-------RNLYMVMEYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIV 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  372 HKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDmnashpfniNSQSI--TnilPEGLyPPEVSESS---FAAasrktDIW 446
Cdd:cd05580  124 YRDLKPENLLLDSDGH---IKITDFGFAKRVKD---------RTYTLcgT---PEYL-APEIILSKghgKAV-----DWW 182
                        170
                 ....*....|..
gi 63054755  447 CFGLLVLQMLCG 458
Cdd:cd05580  183 ALGILIYEMLAG 194
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
729-856 3.01e-08

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: 56.58  E-value: 3.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  729 EYCEKLSLQDIIRD---KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLA---TENENYQD 802
Cdd:cd05040   77 ELAPLGSLLDRLRKdqgHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMralPQNEDHYV 156
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 63054755  803 NNDKWKnrqsadedlttgVGTAlYVAPELLSRRngvRYDAKVDMYSLGIILFEM 856
Cdd:cd05040  157 MQEHRK------------VPFA-WCAPESLKTR---KFSHASDVWMFGVTLWEM 194
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
726-915 3.36e-08

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: 56.50  E-value: 3.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  726 IQMEYCEKLS-LQDIIRDKIPVDE--MWRLFRQILEALAYIHSRGMMHRDLKPGNIFLD-ENRNVKLGDFGlatenenyq 801
Cdd:cd14102   81 IVMERPEPVKdLFDFITEKGALDEdtARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDlRTGELKLIDFG--------- 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  802 dNNDKWKNRQSADEDlttgvGTALYVAPELLSRRngvRYDAK-VDMYSLGIILFEMC---MTFSTSMERIRIIDTIRsps 877
Cdd:cd14102  152 -SGALLKDTVYTDFD-----GTRVYSPPEWIRYH---RYHGRsATVWSLGVLLYDMVcgdIPFEQDEEILRGRLYFR--- 219
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 63054755  878 isfpstfpfSRASHEF-KVIHCLLQHDPTKRPSSQELLE 915
Cdd:cd14102  220 ---------RRVSPECqQLIKWCLSLRPSDRPTLEQIFD 249
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
755-907 3.61e-08

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 57.30  E-value: 3.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenenyqdnndkwknrQSADEDLTTGVGTALYVAPELLSr 834
Cdd:PTZ00426  139 QIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFA----------------KVVDTRTYTLCGTPEYIAPEILL- 201
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755   835 rnGVRYDAKVDMYSLGIILFEM---CMTFSTSmERIRIIDTIRSPSISFPStFPFSRASHEFKVihcLLQHDPTKR 907
Cdd:PTZ00426  202 --NVGHGKAADWWTLGIFIYEIlvgCPPFYAN-EPLLIYQKILEGIIYFPK-FLDNNCKHLMKK---LLSHDLTKR 270
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
724-856 3.74e-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: 56.52  E-value: 3.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRD-KIPVD--EMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRnVKLGDFGLATENENY 800
Cdd:cd14152   71 LAIITSFCKGRTLYSFVRDpKTSLDinKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGK-VVITDFGLFGISGVV 149
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054755  801 QDnnDKWKNrqsadeDLTTGVGTALYVAPELLSR------RNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd14152  150 QE--GRREN------ELKLPHDWLCYLAPEIVREmtpgkdEDCLPFSKAADVYAFGTIWYEL 203
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
754-859 3.86e-08

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: 56.65  E-value: 3.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  754 RQILEALAYIHSRG--MMHRDLKPGNIFLD-ENRNVKLGDFGLATenenyqdnndkwKNRQSADEDLttgVGTALYVAPE 830
Cdd:cd14031  120 RQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLAT------------LMRTSFAKSV---IGTPEFMAPE 184
                         90       100
                 ....*....|....*....|....*....
gi 63054755  831 LLSRRngvrYDAKVDMYSLGIILFEMCMT 859
Cdd:cd14031  185 MYEEH----YDESVDVYAFGMCMLEMATS 209
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
717-854 3.88e-08

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


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 56.51  E-value: 3.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  717 ENGLNATLYiqMEYCEKLSLQDIIrdkipVDEMWRLF--------RQILEALAYIHSRGMMHRDLKPGNIFL--DENRNV 786
Cdd:cd14192   71 ESKTNLTLI--MEYVDGGELFDRI-----TDESYQLTeldailftRQICEGVHYLHQHYILHLDLKPENILCvnSTGNQI 143
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 63054755  787 KLGDFGLATenenyqdnndKWKNRqsadEDLTTGVGTALYVAPELlsrrngVRYD---AKVDMYSLGIILF 854
Cdd:cd14192  144 KIIDFGLAR----------RYKPR----EKLKVNFGTPEFLAPEV------VNYDfvsFPTDMWSVGVITY 194
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
283-507 3.89e-08

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


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 56.59  E-value: 3.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  283 GKREIQELEYELESLKVIRHDLLASIYEYQLERETrgygwrLYVLQEYSPKFTLFSLLQTVLTLDVETVRA--FSNNILE 360
Cdd:cd05072   42 GTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEP------IYIITEYMAKGSLLDFLKSDEGGKVLLPKLidFSAQIAE 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  361 GLAELHRLGISHKSLHLDNVVLFHSghrTFAKLMDFGFTRTLRD------MNASHPFNINSqsitnilPEGLyppevses 434
Cdd:cd05072  116 GMAYIERKNYIHRDLRAANVLVSES---LMCKIADFGLARVIEDneytarEGAKFPIKWTA-------PEAI-------- 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  435 SFAAASRKTDIWCFGLLVLQMLCGAHVLNKFSSLKLIMTHV-----IPLL---PGSYQDLVRRCLMRDSRKRPSaIDLLS 506
Cdd:cd05072  178 NFGSFTIKSDVWSFGILLYEIVTYGKIPYPGMSNSDVMSALqrgyrMPRMencPDELYDIMKTCWKEKAEERPT-FDYLQ 256

                 .
gi 63054755  507 S 507
Cdd:cd05072  257 S 257
PRK12420 PRK12420
histidyl-tRNA synthetase; Provisional
962-1418 4.62e-08

histidyl-tRNA synthetase; Provisional


Pssm-ID: 237097 [Multi-domain]  Cd Length: 423  Bit Score: 57.43  E-value: 4.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   962 TYDFnLSEESGVlskvsdRGWdsllaclVRDHVVKVFRRHGAKERESHILFPK---SSQYDKDQASV----SLLDKNGTL 1034
Cdd:PRK12420   10 TKDY-LPEEQVL------RNK-------IKRALEDVFERYGCKPLETPTLNMYelmSSKYGGGDEILkeiyTLTDQGKRD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  1035 LQLPYDTVLPYARNVARNAVEEE--KTYLISDVFREAK-GGGRPKAIKEISFDITTNSDNLDwyDAETIKALDEVLTEIP 1111
Cdd:PRK12420   76 LALRYDLTIPFAKVVAMNPNIRLpfKRYEIGKVFRDGPiKQGRFREFIQCDVDIVGVESVMA--EAELMSMAFELFRRLN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  1112 slTESCILINHADILSSILDYLQVSKDKRRMATHILGQInQRLTLSQVRNQLRIESLVPSTTLDDLSLFDFRENYeeGAS 1191
Cdd:PRK12420  154 --LEVTIQYNNRKLLNGILQAIGIPTELTSDVILSLDKI-EKIGIDGVRKDLLERGISEEMADTICNTVLSCLQL--SIA 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  1192 KLRKIFGKempQKMRTALNYMERVVKLLRALKISHQLYFMPLCVYNFEFYDGGLMfqAINLAEKS--ELICAGGRYDKLV 1269
Cdd:PRK12420  229 DFKEAFNN---PLVAEGVNELQQLQQYLIALGINENCIFNPFLARGLTMYTGTVY--EIFLKDGSitSSIGSGGRYDNII 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  1270 rffdPPLMRTARKKHVVGICFALEkLVFSMLRyirfhnskqsSKHSPSPTLksvgpwaprrvDVLVTSIGKDsiLEKCSL 1349
Cdd:PRK12420  304 ----GAFRGDDMNYPTVGISFGLD-VIYTALS----------QKETISSTA-----------DVFIIPLGTE--LQCLQI 355
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  1350 LQELWALN-IQADIVLRGaSSLEEIVTHYRSEGINWVLVVRQKNTQMEhSVKARNILKNEDDEIRFDEVG 1418
Cdd:PRK12420  356 AQQLRSTTgLKVELELAG-RKLKKALNYANKENIPYVLIIGEEEVSTG-TVMLRNMKEGSEVKVPLSSLS 423
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
724-856 4.70e-08

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 56.23  E-value: 4.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRD------KIPvdEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATEN 797
Cdd:cd05069   81 IYIVTEFMGKGSLLDFLKEgdgkylKLP--QLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLI 158
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  798 EnyqdnNDKWKNRQSADEDLT-TGVGTALYvapellsrrngVRYDAKVDMYSLGIILFEM 856
Cdd:cd05069  159 E-----DNEYTARQGAKFPIKwTAPEAALY-----------GRFTIKSDVWSFGILLTEL 202
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
741-919 5.01e-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: 56.16  E-value: 5.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  741 RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDE----NRNVKLGDFGLATENEnyqdnndkwknrqsADED 816
Cdd:cd14195  102 KESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDknvpNPRIKLIDFGIAHKIE--------------AGNE 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  817 LTTGVGTALYVAPELlsrrngVRYDA---KVDMYSLGIILFEMCMTFSTSMERIR--IIDTIRSPSISFPSTFpFSRASH 891
Cdd:cd14195  168 FKNIFGTPEFVAPEI------VNYEPlglEADMWSIGVITYILLSGASPFLGETKqeTLTNISAVNYDFDEEY-FSNTSE 240
                        170       180
                 ....*....|....*....|....*....
gi 63054755  892 EFK-VIHCLLQHDPTKRPSSQELLESEAI 919
Cdd:cd14195  241 LAKdFIRRLLVKDPKKRMTIAQSLEHSWI 269
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
358-507 5.14e-08

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: 56.15  E-value: 5.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  358 ILEGLAELHRLGISHKSLHLDNVvLFHSGHRTfAKLMDFGFTRTL------RDMNASHPFNINSQ------SITNILPEG 425
Cdd:cd13996  116 ILKGVSYIHSKGIVHRDLKPSNI-FLDNDDLQ-VKIGDFGLATSIgnqkreLNNLNNNNNGNTSNnsvgigTPLYASPEQ 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  426 LYPPEVSEssfaaasrKTDIWCFGLLVLQMLCG-------AHVLNKFSSLKL---IMTHVIPLLpgsyqDLVRRCLMRDS 495
Cdd:cd13996  194 LDGENYNE--------KADIYSLGIILFEMLHPfktamerSTILTDLRNGILpesFKAKHPKEA-----DLIQSLLSKNP 260
                        170
                 ....*....|..
gi 63054755  496 RKRPSAIDLLSS 507
Cdd:cd13996  261 EERPSAEQLLRS 272
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
755-853 5.39e-08

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: 55.93  E-value: 5.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGN--IFLDENRN-VKLGDFGLATEnenYQDNNDK----WKNRQSadedlttGVGTALY- 826
Cdd:cd14016  104 QMISRLEYLHSKGYIHRDIKPENflMGLGKNSNkVYLIDFGLAKK---YRDPRTGkhipYREGKS-------LTGTARYa 173
                         90       100       110
                 ....*....|....*....|....*....|.
gi 63054755  827 -VAPEL---LSRRngvryDakvDMYSLGIIL 853
Cdd:cd14016  174 sINAHLgieQSRR-----D---DLESLGYVL 196
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
556-907 5.47e-08

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: 56.15  E-value: 5.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  556 FEELEFLGRGGFGEVVKVKNRIDGRFYAVKKL--VLLSDDKENSRILREVMTLSRLHHEHVVRYYTAWVETEANDTVTEI 633
Cdd:cd05631    2 FRHYRVLGKGGFGEVCACQVRATGKMYACKKLekKRIKKRKGEAMALNEKRILEKVNSRFVVSLAYAYETKDALCLVLTI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  634 ISSdseslsqslnmavdfrqssslpadklSSLDIHFEDDYNSSADEEdpeasdisfqysntsdkegssdkdssieeassv 713
Cdd:cd05631   82 MNG--------------------------GDLKFHIYNMGNPGFDEQ--------------------------------- 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  714 ktqenglNATLYiQMEYCekLSLQDIIRDKIpvdemwrlfrqilealayihsrgmMHRDLKPGNIFLDENRNVKLGDFGL 793
Cdd:cd05631  103 -------RAIFY-AAELC--CGLEDLQRERI------------------------VYRDLKPENILLDDRGHIRISDLGL 148
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  794 ATEnenyqdnndkwknrQSADEDLTTGVGTALYVAPELLsrrNGVRYDAKVDMYSLGIILFEMCM---TFSTSMERIR-- 868
Cdd:cd05631  149 AVQ--------------IPEGETVRGRVGTVGYMAPEVI---NNEKYTFSPDWWGLGCLIYEMIQgqsPFRKRKERVKre 211
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 63054755  869 -IIDTIRSPSISFPSTFpfsraSHEFKVI-HCLLQHDPTKR 907
Cdd:cd05631  212 eVDRRVKEDQEEYSEKF-----SEDAKSIcRMLLTKNPKER 247
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
748-864 5.47e-08

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: 55.78  E-value: 5.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  748 EMWRLFRQILEALAYIHSRGMMHRDLKPGNIFL--DENRNVKLGDFGLATENENYQdnndkwknrqsadeDLTTGVGTAL 825
Cdd:cd14191  101 ECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTKIKLIDFGLARRLENAG--------------SLKVLFGTPE 166
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 63054755  826 YVAPELLSrrngvrYDA---KVDMYSLGIILFEMCMTFSTSM 864
Cdd:cd14191  167 FVAPEVIN------YEPigyATDMWSIGVICYILVSGLSPFM 202
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
293-507 5.80e-08

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: 55.88  E-value: 5.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  293 ELESLKVIRHDLLASIYEYqLERETRgygwrLYVLQEYSPKFTLFS-LLQTVLTLDVETVRAFSNNILEGLAELHRLGIS 371
Cdd:cd14074   52 EVRCMKLVQHPNVVRLYEV-IDTQTK-----LYLILELGDGGDMYDyIMKHENGLNEDLARKYFRQIVSAISYCHKLHVV 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  372 HKSLHLDNVVLFhsGHRTFAKLMDFGFtrtlrdmnaSHPFNINSQSITNILPEGLYPPEVSESSFAAASrKTDIWCFGLL 451
Cdd:cd14074  126 HRDLKPENVVFF--EKQGLVKLTDFGF---------SNKFQPGEKLETSCGSLAYSAPEILLGDEYDAP-AVDIWSLGVI 193
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054755  452 VLQMLCGA---HVLNKFSSLKLIMT---HVIPLLPGSYQDLVRRCLMRDSRKRPSAIDLLSS 507
Cdd:cd14074  194 LYMLVCGQppfQEANDSETLTMIMDckyTVPAHVSPECKDLIRRMLIRDPKKRASLEEIENH 255
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
755-915 5.82e-08

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: 56.03  E-value: 5.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQDNndkwknrqsadedltTGVGTALYVAPELLSr 834
Cdd:cd14117  114 ELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVHAPSLRRR---------------TMCGTLDYLPPEMIE- 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  835 rnGVRYDAKVDMYSLGIILFEMCM--------TFSTSMERIRIIDTirspsisfpsTFPFSRASHEFKVIHCLLQHDPTK 906
Cdd:cd14117  178 --GRTHDEKVDLWCIGVLCYELLVgmppfesaSHTETYRRIVKVDL----------KFPPFLSDGSRDLISKLLRYHPSE 245

                 ....*....
gi 63054755  907 RPSSQELLE 915
Cdd:cd14117  246 RLPLKGVME 254
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
697-915 5.93e-08

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: 56.18  E-value: 5.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  697 KEGSSDKD-----SSIEEASSVKTQENGLN--------ATLYIQMEYCEKLSLQDIIRDKIP-----------VDEMWRL 752
Cdd:cd05101   65 KDDATEKDlsdlvSEMEMMKMIGKHKNIINllgactqdGPLYVIVEYASKGNLREYLRARRPpgmeysydinrVPEEQMT 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  753 FR-------QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYqdnnDKWKNRqsadedlTTGVGTAL 825
Cdd:cd05101  145 FKdlvsctyQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINNI----DYYKKT-------TNGRLPVK 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  826 YVAPELLSRRngvRYDAKVDMYSLGIILFEMcMTFSTSmeririidtiRSPSISFPSTFPFSRASHEF-KVIHC-----L 899
Cdd:cd05101  214 WMAPEALFDR---VYTHQSDVWSFGVLMWEI-FTLGGS----------PYPGIPVEELFKLLKEGHRMdKPANCtnelyM 279
                        250       260
                 ....*....|....*....|.
gi 63054755  900 LQHD-----PTKRPSSQELLE 915
Cdd:cd05101  280 MMRDcwhavPSQRPTFKQLVE 300
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
293-506 6.02e-08

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: 55.67  E-value: 6.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  293 ELESLKVIRHDLLASIYEYQLERETRgygwrLYVLQEYSPKFTLFSLLQTVLTLDVEtVRAFSNNILEGLAELHRLGISH 372
Cdd:cd14107   48 ERDILARLSHRRLTCLLDQFETRKTL-----ILILELCSSEELLDRLFLKGVVTEAE-VKLYIQQVLEGIGYLHGMNILH 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  373 KSLHLDNVVLFHSGhRTFAKLMDFGFTRTLRdmNASHPFninSQSITnilPEGLYPPEVSESSFAAAsrkTDIWCFGLLV 452
Cdd:cd14107  122 LDIKPDNILMVSPT-REDIKICDFGFAQEIT--PSEHQF---SKYGS---PEFVAPEIVHQEPVSAA---TDIWALGVIA 189
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63054755  453 -LQMLCG---------AHVLNKFSSLKLIMTHVIPLLPGSYQDLVRRCLMRDSRKRPSAIDLLS 506
Cdd:cd14107  190 yLSLTCHspfagendrATLLNVAEGVVSWDTPEITHLSEDAKDFIKRVLQPDPEKRPSASECLS 253
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
323-505 6.66e-08

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: 55.81  E-value: 6.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  323 RLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELH-RLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRT 401
Cdd:cd06605   73 DISICMEYMDGGSLDKILKEVGRIPERILGKIAVAVVKGLIYLHeKHKIIHRDVKPSNILVNSRGQ---VKLCDFGVSGQ 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  402 LrdmnashpfnINSQSITNI------LPEGLYPPEVSESSfaaasrktDIWCFGLLVLQMLCG---------AHVLNKFS 466
Cdd:cd06605  150 L----------VDSLAKTFVgtrsymAPERISGGKYTVKS--------DIWSLGLSLVELATGrfpypppnaKPSMMIFE 211
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 63054755  467 SLKLIMTHVIPLLPG-----SYQDLVRRCLMRDSRKRPSAIDLL 505
Cdd:cd06605  212 LLSYIVDEPPPLLPSgkfspDFQDFVSQCLQKDPTERPSYKELM 255
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
285-510 6.93e-08

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: 55.49  E-value: 6.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  285 REIQELEYELESLKVIRHdllASIYEYQLERETRGYgwrLYVLQEYSPKFTLFSLLQTV---LTLDVETVRAFSNNILEG 361
Cdd:cd06624   47 REVQPLHEEIALHSRLSH---KNIVQYLGSVSEDGF---FKIFMEQVPGGSLSALLRSKwgpLKDNENTIGYYTKQILEG 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  362 LAELHRLGISHKSLHLDNV-VLFHSGhrtFAKLMDFGFTRTLRDMNAshpfniNSQSITNILPegLYPPEVSESSFAAAS 440
Cdd:cd06624  121 LKYLHDNKIVHRDIKGDNVlVNTYSG---VVKISDFGTSKRLAGINP------CTETFTGTLQ--YMAPEVIDKGQRGYG 189
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  441 RKTDIWCFGLLVLQMLCGAHVLNKFSS-----LKLIMTHVIPLLPGSY----QDLVRRCLMRDSRKRPSAIDLLSSHVI 510
Cdd:cd06624  190 PPADIWSLGCTIIEMATGKPPFIELGEpqaamFKVGMFKIHPEIPESLseeaKSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
754-859 7.15e-08

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: 55.47  E-value: 7.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  754 RQILEALAYIHSRG--MMHRDLKPGNIFLD-ENRNVKLGDFGLATenenyqdnndkwKNRQSADEDLttgVGTALYVAPE 830
Cdd:cd14032  111 RQILKGLLFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLAT------------LKRASFAKSV---IGTPEFMAPE 175
                         90       100
                 ....*....|....*....|....*....
gi 63054755  831 LLSRRngvrYDAKVDMYSLGIILFEMCMT 859
Cdd:cd14032  176 MYEEH----YDESVDVYAFGMCMLEMATS 200
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
697-860 7.26e-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: 55.49  E-value: 7.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  697 KEGSSDKDSSIEEASSVK--------------TQENglnaTLYIQMEYCEKLSLQDIIRDK---IPVDEMWRLFRQILEA 759
Cdd:cd05068   41 KPGTMDPEDFLREAQIMKklrhpkliqlyavcTLEE----PIYIITELMKHGSLLEYLQGKgrsLQLPQLIDMAAQVASG 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  760 LAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENyqdnndkwknrqsaDEDLTTGVGTAL---YVAPELLsrrN 836
Cdd:cd05068  117 MAYLESQNYIHRDLAARNVLVGENNICKVADFGLARVIKV--------------EDEYEAREGAKFpikWTAPEAA---N 179
                        170       180
                 ....*....|....*....|....
gi 63054755  837 GVRYDAKVDMYSLGIILFEMcMTF 860
Cdd:cd05068  180 YNRFSIKSDVWSFGILLTEI-VTY 202
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
752-854 7.34e-08

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: 55.42  E-value: 7.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  752 LFRQILEALAYIHSRGMMHRDLKPGN-IFLDENRNVK--LGDFGLATenenyqdnndkwknrqsadedLTTGV-----GT 823
Cdd:cd14088  104 VIRQVLEAVAYLHSLKIVHRNLKLENlVYYNRLKNSKivISDFHLAK---------------------LENGLikepcGT 162
                         90       100       110
                 ....*....|....*....|....*....|.
gi 63054755  824 ALYVAPELLSRRngvRYDAKVDMYSLGIILF 854
Cdd:cd14088  163 PEYLAPEVVGRQ---RYGRPVDCWAIGVIMY 190
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
725-808 7.56e-08

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


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 53.42  E-value: 7.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  725 YIQMEYCEKLSLQDIIRDKIPVDEMWRlfrQILEALAYIHSRGMMHRDLKPGNIFLDENRnVKLGDFGLAtenenYQDNN 804
Cdd:COG3642   32 DLVMEYIEGETLADLLEEGELPPELLR---ELGRLLARLHRAGIVHGDLTTSNILVDDGG-VYLIDFGLA-----RYSDP 102

                 ....
gi 63054755  805 DKWK 808
Cdd:COG3642  103 LEDK 106
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
279-562 8.00e-08

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: 55.79  E-value: 8.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  279 STEDGKREIQEleyELESLKVIRHDLLASIYEYQLEREtrgygwRLYVLQEYSPKfTLFSLLQTVLT-LDVETVRAFSNN 357
Cdd:cd07833   39 DDEDVKKTALR---EVKVLRQLRHENIVNLKEAFRRKG------RLYLVFEYVER-TLLELLEASPGgLPPDAVRSYIWQ 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  358 ILEGLAELHRLGISHKSLHLDNVVLFHSGhrtFAKLMDFGFTRTLRDMNASHpfninsqsITNILPEGLY-PPE--VSES 434
Cdd:cd07833  109 LLQAIAYCHSHNIIHRDIKPENILVSESG---VLKLCDFGFARALTARPASP--------LTDYVATRWYrAPEllVGDT 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  435 SFAAAsrkTDIWCFGLLVLQMLCGAhvlnkfsslklimthviPLLPGSyqdlvrrclmrdsrkrpSAIDLLSshVIRLGT 514
Cdd:cd07833  178 NYGKP---VDVWAIGCIMAELLDGE-----------------PLFPGD-----------------SDIDQLY--LIQKCL 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 63054755  515 AVLPPVEQGTFSKSARpsYGGQQdgIIDLLYRKSVS-RYETDFE--ELEFL 562
Cdd:cd07833  219 GPLPPSHQELFSSNPR--FAGVA--FPEPSQPESLErRYPGKVSspALDFL 265
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
755-915 8.13e-08

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: 55.43  E-value: 8.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRG---MMHRDLKPGNIFLDE--------NRNVKLGDFGLATEnenyqdnndkWKNRQSadedlTTGVGT 823
Cdd:cd14146  110 QIARGMLYLHEEAvvpILHRDLKSSNILLLEkiehddicNKTLKITDFGLARE----------WHRTTK-----MSAAGT 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  824 ALYVAPELLSRRngvRYDAKVDMYSLGIILFEMCmtfsTSMERIRIID--------TIRSPSISFPSTFPFSRAshefKV 895
Cdd:cd14146  175 YAWMAPEVIKSS---LFSKGSDIWSYGVLLWELL----TGEVPYRGIDglavaygvAVNKLTLPIPSTCPEPFA----KL 243
                        170       180
                 ....*....|....*....|
gi 63054755  896 IHCLLQHDPTKRPSSQELLE 915
Cdd:cd14146  244 MKECWEQDPHIRPSFALILE 263
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
720-856 9.15e-08

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: 55.72  E-value: 9.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  720 LNATLY--IQMEYCEKLSLQDIirdkipvdemwRLF-RQILEALAYIHSRGMMHRDLKPGNIFLDENR--NVKLGDFGLA 794
Cdd:cd14212   84 LGVNLYelLKQNQFRGLSLQLI-----------RKFlQQLLDALSVLKDARIIHCDLKPENILLVNLDspEIKLIDFGSA 152
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054755  795 TEnENYQdnndkwknrqsadedLTTGVGTALYVAPELLSrrnGVRYDAKVDMYSLGIILFEM 856
Cdd:cd14212  153 CF-ENYT---------------LYTYIQSRFYRSPEVLL---GLPYSTAIDMWSLGCIAAEL 195
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
760-856 9.15e-08

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: 55.19  E-value: 9.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  760 LAYIH---SRGMMHRDLKPGNIFLDENRNVKLGDFGLATEnenyqdNNDKwknrqsADEDLTTGVGTALYVAPELLSRrn 836
Cdd:cd14664  107 LAYLHhdcSPLIIHRDVKSNNILLDEEFEAHVADFGLAKL------MDDK------DSHVMSSVAGSYGYIAPEYAYT-- 172
                         90       100
                 ....*....|....*....|
gi 63054755  837 gVRYDAKVDMYSLGIILFEM 856
Cdd:cd14664  173 -GKVSEKSDVYSYGVVLLEL 191
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
724-913 1.02e-07

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: 55.01  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYC---EKLSLQDIIRDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAteneny 800
Cdd:cd05085   68 IYIVMELVpggDFLSFLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMS------ 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  801 qdnndkwknRQSaDEDLTTGVGTAL----YVAPELLsrrNGVRYDAKVDMYSLGIILFE-----MC----MTFSTSMERI 867
Cdd:cd05085  142 ---------RQE-DDGVYSSSGLKQipikWTAPEAL---NYGRYSSESDVWSFGILLWEtfslgVCpypgMTNQQAREQV 208
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 63054755  868 RiidtiRSPSISFPSTFPfsraSHEFKVIHCLLQHDPTKRPSSQEL 913
Cdd:cd05085  209 E-----KGYRMSAPQRCP----EDIYKIMQRCWDYNPENRPKFSEL 245
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
284-505 1.03e-07

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: 55.17  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  284 KREIQELEYELESLKVIRHDLLASIYEYQLERETrgygwrLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLA 363
Cdd:cd14098   42 DKNLQLFQREINILKSLEHPGIVRLIDWYEDDQH------IYLVMEYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  364 ELHRLGISHKSLHLDNVVLFHSGHRtFAKLMDFGFTRTLRDMNASHPFninSQSITNILPEGLYPPEVSESSfaAASRKT 443
Cdd:cd14098  116 YTHSMGITHRDLKPENILITQDDPV-IVKISDFGLAKVIHTGTFLVTF---CGTMAYLAPEILMSKEQNLQG--GYSNLV 189
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054755  444 DIWCFGLLVLQMLCGAHVLNKFSSLKLIMT------HVIPLLPGSYQ----DLVRRCLMRDSRKRPSAIDLL 505
Cdd:cd14098  190 DMWSVGCLVYVMLTGALPFDGSSQLPVEKRirkgryTQPPLVDFNISeeaiDFILRLLDVDPEKRMTAAQAL 261
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
691-919 1.04e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 57.02  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   691 YSNTSD-KEGSSDKDSSIEEASSVKT--------QENGLNATLYIQMEYCEKLSLQ---DIIRDKIPVDEMWRLFRQILE 758
Cdd:PLN00181   12 LNNTSGvSEFCTDGSKSLSHIDYVRSllgshkegNLDGLDDDSIVRALECEDVSLRqwlDNPDRSVDAFECFHVFRQIVE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   759 ALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQDNNDKWKN-------------RQSADEDLTT------ 819
Cdd:PLN00181   92 IVNAAHSQGIVVHNVRPSCFVMSSFNHVSFIESASCSDSGSDEDATTKSREigssrreeilserRIEKLEEVKKqpfpmk 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   820 ---GVGTALYVAPEllsRRNGVRYDAKVDMYSLGIILFEMCMTFSTSMERIRIIDTIR----SPSI--SFPSTFPFsras 890
Cdd:PLN00181  172 qilAMEMSWYTSPE---EDNGSSSNCASDVYRLGVLLFELFCPVSSREEKSRTMSSLRhrvlPPQIllNWPKEASF---- 244
                         250       260       270
                  ....*....|....*....|....*....|.
gi 63054755   891 hefkvihC--LLQHDPTKRPSSQELLESEAI 919
Cdd:PLN00181  245 -------ClwLLHPEPSCRPSMSELLQSEFI 268
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
724-909 1.08e-07

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: 54.94  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDKIP---VDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENy 800
Cdd:cd05084   69 IYIVMELVQGGDFLTFLRTEGPrlkVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREEED- 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  801 qdnndkwknrqsadedlttGVGTAL---------YVAPELLsrrNGVRYDAKVDMYSLGIILFEmcmTFS------TSME 865
Cdd:cd05084  148 -------------------GVYAATggmkqipvkWTAPEAL---NYGRYSSESDVWSFGILLWE---TFSlgavpyANLS 202
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 63054755  866 RIRIIDTI-RSPSISFPSTFPfsraSHEFKVIHCLLQHDPTKRPS 909
Cdd:cd05084  203 NQQTREAVeQGVRLPCPENCP----DEVYRLMEQCWEYDPRKRPS 243
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
728-854 1.28e-07

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


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 54.92  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  728 MEYCEKLSLQDIIrdkipVDEMWRL--------FRQILEALAYIHSRGMMHRDLKPGNIFL--DENRNVKLGDFGLATen 797
Cdd:cd14193   80 MEYVDGGELFDRI-----IDENYNLteldtilfIKQICEGIQYMHQMYILHLDLKPENILCvsREANQVKIIDFGLAR-- 152
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  798 enyqdnndKWKNRqsadEDLTTGVGTALYVAPELlsrrngVRYDA---KVDMYSLGIILF 854
Cdd:cd14193  153 --------RYKPR----EKLRVNFGTPEFLAPEV------VNYEFvsfPTDMWSLGVIAY 194
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
279-498 1.41e-07

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: 55.31  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  279 STEDGKREIQELEYELES-LKVIRHdllasiYEYQLERetrgygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNN 357
Cdd:cd05614   47 TVEHTRTERNVLEHVRQSpFLVTLH------YAFQTDA-------KLHLILDYVSGGELFTHLYQRDHFSEDEVRFYSGE 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  358 ILEGLAELHRLGISHKSLHLDNVVLFHSGHRTfakLMDFGFTRTLRDMNASHPFNInSQSITNILPEGLyppevseSSFA 437
Cdd:cd05614  114 IILALEHLHKLGIVYRDIKLENILLDSEGHVV---LTDFGLSKEFLTEEKERTYSF-CGTIEYMAPEII-------RGKS 182
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 63054755  438 AASRKTDIWCFGLLVLQMLCGAHVL------NKFSSLKLIMTHVIPLLPGSY----QDLVRRCLMRDSRKR 498
Cdd:cd05614  183 GHGKAVDWWSLGILMFELLTGASPFtlegekNTQSEVSRRILKCDPPFPSFIgpvaRDLLQKLLCKDPKKR 253
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
279-506 1.45e-07

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: 54.61  E-value: 1.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  279 STEDGKREiqELEYELESLKVIRHDLLASIYEYQlerETRGYGWrlyVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNI 358
Cdd:cd14010   32 CVDKSKRP--EVLNEVRLTHELKHPNVLKFYEWY---ETSNHLW---LVVEYCTGGDLETLLRQDGNLPESSVRKFGRDL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  359 LEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDMNASHPFNINSQSITNILPEGLYP--------PE 430
Cdd:cd14010  104 VRGLHYIHSKGIIYCDLKPSNILLDGNGT---LKLSDFGLARREGEILKELFGQFSDEGNVNKVSKKQAKrgtpyymaPE 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  431 V---SESSFAaasrkTDIWCFGLLVLQMLCG--AHVLNKFSSLK-LIMTHVIPLLPG--------SYQDLVRRCLMRDSR 496
Cdd:cd14010  181 LfqgGVHSFA-----SDLWALGCVLYEMFTGkpPFVAESFTELVeKILNEDPPPPPPkvsskpspDFKSLLKGLLEKDPA 255
                        250
                 ....*....|
gi 63054755  497 KRPSAIDLLS 506
Cdd:cd14010  256 KRLSWDELVK 265
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
725-794 1.65e-07

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: 54.57  E-value: 1.65e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63054755  725 YIQMEYCEKlSLQDIIRD----KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFL----DENRNVKLGDFGLA 794
Cdd:cd14017   72 YIVMTLLGP-NLAELRRSqprgKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIgrgpSDERTVYILDFGLA 148
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
724-856 1.70e-07

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1b, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 55.06  E-value: 1.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIR-DKIPVDEMWRLFRQILEALAYIHSR--------GMMHRDLKPGNIFLDENRNVKLGDFGLA 794
Cdd:cd14219   78 LYLITDYHENGSLYDYLKsTTLDTKAMLKLAYSSVSGLCHLHTEifstqgkpAIAHRDLKSKNILVKKNGTCCIADLGLA 157
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63054755  795 TenENYQDNNDkwknrqsADEDLTTGVGTALYVAPELLSR---RNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd14219  158 V--KFISDTNE-------VDIPPNTRVGTKRYMPPEVLDEslnRNHFQSYIMADMYSFGLILWEV 213
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
697-915 1.77e-07

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


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 55.03  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  697 KEGSSDKD-----SSIEEASSVKTQENGLN--------ATLYIQMEYCEKLSLQDIIRDKIP-----------VDEMWRL 752
Cdd:cd05100   53 KDDATDKDlsdlvSEMEMMKMIGKHKNIINllgactqdGPLYVLVEYASKGNLREYLRARRPpgmdysfdtckLPEEQLT 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  753 FR-------QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYqdnnDKWKNRqsadedlTTGVGTAL 825
Cdd:cd05100  133 FKdlvscayQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNI----DYYKKT-------TNGRLPVK 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  826 YVAPELLSRRngvRYDAKVDMYSLGIILFEMCMTFSTSMERIRIIDTIRSPSISFPSTFPfSRASHEFKVIHCLLQHD-P 904
Cdd:cd05100  202 WMAPEALFDR---VYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKP-ANCTHELYMIMRECWHAvP 277
                        250
                 ....*....|.
gi 63054755  905 TKRPSSQELLE 915
Cdd:cd05100  278 SQRPTFKQLVE 288
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
752-909 1.77e-07

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: 54.81  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  752 LFRQILEALAYIHSRGMMHRDLKPGNIFL----DENRNVKLGDFG--LATENENYQDNNDKWknrqsadeDLTTGvGTAL 825
Cdd:cd14018  143 MILQLLEGVDHLVRHGIAHRDLKSDNILLeldfDGCPWLVIADFGccLADDSIGLQLPFSSW--------YVDRG-GNAC 213
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  826 YVAPELLSRRNG----VRYdAKVDMYSLGIILFEMC------MTFSTSMERIRIIDTIRSPSIsfPSTFPFSRAshefKV 895
Cdd:cd14018  214 LMAPEVSTAVPGpgvvINY-SKADAWAVGAIAYEIFglsnpfYGLGDTMLESRSYQESQLPAL--PSAVPPDVR----QV 286
                        170
                 ....*....|....
gi 63054755  896 IHCLLQHDPTKRPS 909
Cdd:cd14018  287 VKDLLQRDPNKRVS 300
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
755-914 2.06e-07

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


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 54.38  E-value: 2.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATE--NENYQ---DNND---KWknrqsadedlttgvgtaly 826
Cdd:cd05043  124 QIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNALSRDlfPMDYHclgDNENrpiKW------------------- 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  827 VAPELLSRRNgvrYDAKVDMYSLGIILFEMCMTFSTSMERIRIIDTIRSPSISFPSTFPFSRASHEFKVIHCLLQHDPTK 906
Cdd:cd05043  185 MSLESLVNKE---YSSASDVWSFGVLLWELMTLGQTPYVEIDPFEMAAYLKDGYRLAQPINCPDELFAVMACCWALDPEE 261

                 ....*...
gi 63054755  907 RPSSQELL 914
Cdd:cd05043  262 RPSFQQLV 269
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
743-859 2.09e-07

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: 54.29  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  743 KIPVDEMWrlFRQILEALAYIHSRG--MMHRDLKPGNIFLD-ENRNVKLGDFGLATenenyqdnndkwKNRQSADEDLtt 819
Cdd:cd14030  126 KIKVLRSW--CRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLAT------------LKRASFAKSV-- 189
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 63054755  820 gVGTALYVAPELLSRRngvrYDAKVDMYSLGIILFEMCMT 859
Cdd:cd14030  190 -IGTPEFMAPEMYEEK----YDESVDVYAFGMCMLEMATS 224
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
724-861 2.11e-07

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: 54.25  E-value: 2.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDII---RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLateNENY 800
Cdd:cd14205   82 LRLIMEYLPYGSLRDYLqkhKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGL---TKVL 158
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 63054755  801 QDNNDKWKNRQSADEDLttgvgtaLYVAPELLSRRngvRYDAKVDMYSLGIILFEMcMTFS 861
Cdd:cd14205  159 PQDKEYYKVKEPGESPI-------FWYAPESLTES---KFSVASDVWSFGVVLYEL-FTYI 208
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
724-913 2.15e-07

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 54.41  E-value: 2.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDK----IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENEN 799
Cdd:cd05055  114 ILVITEYCCYGDLLNFLRRKresfLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLARDIMN 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  800 yqDNNdkWKNRQSADEDLTtgvgtalYVAPEllSRRNGVrYDAKVDMYSLGIILFEMCMTFSTSMERIRIIDTIRSPsis 879
Cdd:cd05055  194 --DSN--YVVKGNARLPVK-------WMAPE--SIFNCV-YTFESDVWSYGILLWEIFSLGSNPYPGMPVDSKFYKL--- 256
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 63054755  880 FPSTFPFSRASHEFKVIHCLLQH----DPTKRPSSQEL 913
Cdd:cd05055  257 IKEGYRMAQPEHAPAEIYDIMKTcwdaDPLKRPTFKQI 294
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
724-858 2.26e-07

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: 53.97  E-value: 2.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDII---RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAteneny 800
Cdd:cd05056   81 VWIVMELAPLGELRSYLqvnKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLS------ 154
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 63054755  801 qdnndkwknRQSADEDLTTGVGTAL---YVAPELLSRRngvRYDAKVDMYSLGIILFEMCM 858
Cdd:cd05056  155 ---------RYMEDESYYKASKGKLpikWMAPESINFR---RFTSASDVWMFGVCMWEILM 203
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
697-916 2.28e-07

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: 54.10  E-value: 2.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  697 KEGSSDKDSSIEEAS--------------SVKTQENglnaTLYIQMEYCEKLSLQDIIRD---KIPVDEMWRLFRQILEA 759
Cdd:cd05114   37 REGAMSEEDFIEEAKvmmklthpklvqlyGVCTQQK----PIYIVTEFMENGCLLNYLRQrrgKLSRDMLLSMCQDVCEG 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  760 LAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenenyqdnndkwknRQSADEDLTTGVGTALYV---APELLsrrN 836
Cdd:cd05114  113 MEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMT---------------RYVLDDQYTSSSGAKFPVkwsPPEVF---N 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  837 GVRYDAKVDMYSLGIILFEMCMTFSTSMERIRIIDTIRSPSISFPSTFPFSRASHEFKVIHCLLQHDPTKRPSSQELLES 916
Cdd:cd05114  175 YSKFSSKSDVWSFGVLMWEVFTEGKMPFESKSNYEVVEMVSRGHRLYRPKLASKSVYEVMYSCWHEKPEGRPTFADLLRT 254
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
293-500 2.48e-07

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: 53.77  E-value: 2.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  293 ELESLKVIRHDLLASIYEYQLEREtrgygwrLYVLQEYSPKFTLFSLLQTVL--TLDVETVRAFSNNILEGLAELHRLGI 370
Cdd:cd14203   40 EAQIMKKLRHDKLVQLYAVVSEEP-------IYIVTEFMSKGSLLDFLKDGEgkYLKLPQLVDMAAQIASGMAYIERMNY 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  371 SHKSLHLDNVVLfhsGHRTFAKLMDFGFTRTLRDmNASHPFNINSQSITNILPEGlyppevseSSFAAASRKTDIWCFGL 450
Cdd:cd14203  113 IHRDLRAANILV---GDNLVCKIADFGLARLIED-NEYTARQGAKFPIKWTAPEA--------ALYGRFTIKSDVWSFGI 180
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 63054755  451 LVLQMLCGAHV----LNKFSSLKLI-MTHVIPLLPG---SYQDLVRRCLMRDSRKRPS 500
Cdd:cd14203  181 LLTELVTKGRVpypgMNNREVLEQVeRGYRMPCPPGcpeSLHELMCQCWRKDPEERPT 238
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
724-913 2.51e-07

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 53.92  E-value: 2.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDK----IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENEn 799
Cdd:cd05071   78 IYIVTEYMSKGSLLDFLKGEmgkyLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIE- 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  800 yqdnNDKWKNRQSADEDLT-TGVGTALYvapellsrrngVRYDAKVDMYSLGIILFEMCMTFST---SMERIRIIDTI-R 874
Cdd:cd05071  157 ----DNEYTARQGAKFPIKwTAPEAALY-----------GRFTIKSDVWSFGILLTELTTKGRVpypGMVNREVLDQVeR 221
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 63054755  875 SPSISFPSTFPFSRasHEFkVIHClLQHDPTKRPSSQEL 913
Cdd:cd05071  222 GYRMPCPPECPESL--HDL-MCQC-WRKEPEERPTFEYL 256
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
728-863 2.88e-07

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: 53.78  E-value: 2.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  728 MEYCEKLSLQDII---RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLateNENYQDNn 804
Cdd:cd05079   87 MEFLPSGSLKEYLprnKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGL---TKAIETD- 162
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  805 dkwKNRQSADEDLTTGVgtaLYVAPELLSRrngVRYDAKVDMYSLGIILFEMcMTFSTS 863
Cdd:cd05079  163 ---KEYYTVKDDLDSPV---FWYAPECLIQ---SKFYIASDVWSFGVTLYEL-LTYCDS 211
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
723-914 3.02e-07

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


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 53.53  E-value: 3.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  723 TLYIQMEYCEKLSLQDIIRD---KIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENEn 799
Cdd:cd05033   79 PVMIVTEYMENGSLDKFLREndgKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLE- 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  800 yqdnndkwknrqSADEDLTTGVG--TALYVAPELLSRRngvRYDAKVDMYSLGIILFEMcMTFST----SMERIRIIDTI 873
Cdd:cd05033  158 ------------DSEATYTTKGGkiPIRWTAPEAIAYR---KFTSASDVWSFGIVMWEV-MSYGErpywDMSNQDVIKAV 221
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 63054755  874 RS-----PSISFPStfpfsrashefkVIHCLL----QHDPTKRPSSQELL 914
Cdd:cd05033  222 EDgyrlpPPMDCPS------------ALYQLMldcwQKDRNERPTFSQIV 259
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
346-505 3.04e-07

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 53.70  E-value: 3.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  346 LDVETVRAFSNNILEGLAEL-HRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLrdmnashpfnINSQSITNILPE 424
Cdd:cd06622   99 IPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQ---VKLCDFGVSGNL----------VASLAKTNIGCQ 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  425 GLYPPEVSESSFAAA----SRKTDIWCFGLLVLQMLCGAH------VLNKFSSLKLIMTHVIPLLPGSY----QDLVRRC 490
Cdd:cd06622  166 SYMAPERIKSGGPNQnptyTVQSDVWSLGLSILEMALGRYpyppetYANIFAQLSAIVDGDPPTLPSGYsddaQDFVAKC 245
                        170
                 ....*....|....*
gi 63054755  491 LMRDSRKRPSAIDLL 505
Cdd:cd06622  246 LNKIPNRRPTYAQLL 260
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
284-510 3.57e-07

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: 53.20  E-value: 3.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  284 KREIQELEYELESLKVIRHDLLASIYEYQLERETrgygwrLYVLQEYSPKFTLFSLLQTV--LTLDVETVRAFSNNILEG 361
Cdd:cd08220   40 KEERQAALNEVKVLSMLHHPNIIEYYESFLEDKA------LMIVMEYAPGGTLFEYIQQRkgSLLSEEEILHFFVQILLA 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  362 LAELHRLGISHKSLHLDNVVLfhSGHRTFAKLMDFGFTRTLrdmnashpfNINSQSITNILPEGLYPPEVSESSfaAASR 441
Cdd:cd08220  114 LHHVHSKQILHRDLKTQNILL--NKKRTVVKIGDFGISKIL---------SSKSKAYTVVGTPCYISPELCEGK--PYNQ 180
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  442 KTDIWCFG--LLVLQMLCGAHVLNKFSSLKL-IMTHVIPLLPGSYQDLVRR----CLMRDSRKRPSAIDLLSSHVI 510
Cdd:cd08220  181 KSDIWALGcvLYELASLKRAFEAANLPALVLkIMRGTFAPISDRYSEELRHlilsMLHLDPNKRPTLSEIMAQPII 256
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
751-915 3.64e-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: 53.42  E-value: 3.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  751 RLFRQILEALAYIHSRGMMHRDLKPGNIFL-----DENRNVKLGDFGLAtenenyqdnndkwknRQSADEDLTTGVGTAL 825
Cdd:cd14068   90 RIALHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIA---------------QYCCRMGIKTSEGTPG 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  826 YVAPELlsRRNGVRYDAKVDMYSLGIILFEMCmtfsTSMERIriidtirSPSISFPSTF-------------------PF 886
Cdd:cd14068  155 FRAPEV--ARGNVIYNQQADVYSFGLLLYDIL----TCGERI-------VEGLKFPNEFdelaiqgklpdpvkeygcaPW 221
                        170       180
                 ....*....|....*....|....*....
gi 63054755  887 SRAShefKVIHCLLQHDPTKRPSSQELLE 915
Cdd:cd14068  222 PGVE---ALIKDCLKENPQCRPTSAQVFD 247
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
293-500 4.40e-07

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 53.15  E-value: 4.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  293 ELESLKVIRHDLLASIYEYQLEREtrgygwrLYVLQEYSPKFTLFSLL--QTVLTLDVETVRAFSNNILEGLAELHRLGI 370
Cdd:cd05071   54 EAQVMKKLRHEKLVQLYAVVSEEP-------IYIVTEYMSKGSLLDFLkgEMGKYLRLPQLVDMAAQIASGMAYVERMNY 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  371 SHKSLHLDNVVLfhsGHRTFAKLMDFGFTRTLRDmnashpfNINSQSITNILPEGLYPPEVSesSFAAASRKTDIWCFGL 450
Cdd:cd05071  127 VHRDLRAANILV---GENLVCKVADFGLARLIED-------NEYTARQGAKFPIKWTAPEAA--LYGRFTIKSDVWSFGI 194
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 63054755  451 LVLQMLCGAHVLNKFSSLKLIMTHV--------IPLLPGSYQDLVRRCLMRDSRKRPS 500
Cdd:cd05071  195 LLTELTTKGRVPYPGMVNREVLDQVergyrmpcPPECPESLHDLMCQCWRKEPEERPT 252
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
724-915 4.43e-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: 53.12  E-value: 4.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDK-IPVDEMWRLFRQILEALAYIHSRGM---MHRDLKPGNIFLDE--------NRNVKLGDF 791
Cdd:cd14145   80 LCLVMEFARGGPLNRVLSGKrIPPDILVNWAVQIARGMNYLHCEAIvpvIHRDLKSSNILILEkvengdlsNKILKITDF 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  792 GLATEnenyqdnndkWKNRQSadedlTTGVGTALYVAPELLsrrNGVRYDAKVDMYSLGIILFEMCmtfsTSMERIRIID 871
Cdd:cd14145  160 GLARE----------WHRTTK-----MSAAGTYAWMAPEVI---RSSMFSKGSDVWSYGVLLWELL----TGEVPFRGID 217
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 63054755  872 --------TIRSPSISFPSTFPFSRAshefKVIHCLLQHDPTKRPSSQELLE 915
Cdd:cd14145  218 glavaygvAMNKLSLPIPSTCPEPFA----RLMEDCWNPDPHSRPPFTNILD 265
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
729-856 4.50e-07

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


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 52.90  E-value: 4.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  729 EYCE-KLSLQDII-RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenENYQDNNDK 806
Cdd:cd14111   79 EFCSgKELLHSLIdRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSA---QSFNPLSLR 155
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 63054755  807 WKNRQsadedlttgVGTALYVAPELLsrrNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd14111  156 QLGRR---------TGTLEYMAPEMV---KGEPVGPPADIWSIGVLTYIM 193
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
728-856 4.69e-07

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


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 53.12  E-value: 4.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  728 MEYCEKLSLQDIIRDK--IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLA----TENENYQ 801
Cdd:cd05060   74 MELAPLGPLLKYLKKRreIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSralgAGSDYYR 153
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  802 -DNNDKWKNRqsadedlttgvgtalYVAPELLsrrNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd05060  154 aTTAGRWPLK---------------WYAPECI---NYGKFSSKSDVWSYGVTLWEA 191
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
726-856 5.13e-07

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: 52.94  E-value: 5.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  726 IQMEYCEKLSLQDII-RDKIPVDemWRlFR-----QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAT-ENE 798
Cdd:cd14045   79 IITEYCPKGSLNDVLlNEDIPLN--WG-FRfsfatDIARGMAYLHQHKIYHGRLKSSNCVIDDRWVCKIADYGLTTyRKE 155
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 63054755  799 NYQDNNDKWKNRQsadedlttgvgTALYVAPELLSrRNGVRYDAKVDMYSLGIILFEM 856
Cdd:cd14045  156 DGSENASGYQQRL-----------MQVYLPPENHS-NTDTEPTQATDVYSYAIILLEI 201
RWD_RWDD3 cd23819
RWD domain of RWD domain-containing protein 3 (RWDD3) and related proteins; RWDD3, also called ...
17-125 5.72e-07

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: 49.63  E-value: 5.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   17 EIEALKAIFMDDfEELKVRNAWNVTNGHVYCIHLCSRSANSKSiaKLDLCIELGRSYPYVKPVIKLQNgENVLNSQIRFL 96
Cdd:cd23819    2 ELSVLQAIFCGP-GEFEVLSSSETSDGVSFKIQISVEGFDEDI--VLKLTFHLSPNYPSSLPDISVSS-EQLTRAQCNDL 77
                         90       100
                 ....*....|....*....|....*....
gi 63054755   97 LDKLDTKAKDLLGEEMIFELASIVQDYLN 125
Cdd:cd23819   78 QDSLLEYANSLLGEPMVLELVLWLQENLL 106
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
280-510 6.45e-07

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


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 52.70  E-value: 6.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  280 TEDgkrEIQELEYELESLKVIRHDL-LASIYEYQLERETRGYGWRLYVLQEYSPKFTLFSLLQTVL--TLDVETVRAFSN 356
Cdd:cd06636   52 TED---EEEEIKLEINMLKKYSHHRnIATYYGAFIKKSPPGHDDQLWLVMEFCGAGSVTDLVKNTKgnALKEDWIAYICR 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  357 NILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTL-RDMNASHPFninsqsitnILPEGLYPPEV---S 432
Cdd:cd06636  129 EILRGLAHLHAHKVIHRDIKGQNVLLTENAE---VKLVDFGVSAQLdRTVGRRNTF---------IGTPYWMAPEViacD 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  433 ESSFAAASRKTDIWCFGLLVLQMLCGAHVL---NKFSSLKLIMTHVIPLLPG-----SYQDLVRRCLMRDSRKRPSAIDL 504
Cdd:cd06636  197 ENPDATYDYRSDIWSLGITAIEMAEGAPPLcdmHPMRALFLIPRNPPPKLKSkkwskKFIDFIEGCLVKNYLSRPSTEQL 276

                 ....*.
gi 63054755  505 LSSHVI 510
Cdd:cd06636  277 LKHPFI 282
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
297-498 6.72e-07

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


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 53.18  E-value: 6.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  297 LKVIRHDLLAS-IYEYQlereTRGygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSL 375
Cdd:cd05584   54 LEAVKHPFIVDlHYAFQ----TGG---KLYLILEYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  376 HLDNVVLFHSGHrtfAKLMDFGFTR-TLRDMNASHPFninSQSITNILPEGLyppevsesSFAAASRKTDIWCFGLLVLQ 454
Cdd:cd05584  127 KPENILLDAQGH---VKLTDFGLCKeSIHDGTVTHTF---CGTIEYMAPEIL--------TRSGHGKAVDWWSLGALMYD 192
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 63054755  455 MLCGA---------HVLNKFSSLKLIMThviPLLPGSYQDLVRRCLMRDSRKR 498
Cdd:cd05584  193 MLTGAppftaenrkKTIDKILKGKLNLP---PYLTNEARDLLKKLLKRNVSSR 242
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
288-520 6.76e-07

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: 52.56  E-value: 6.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  288 QELEYELESLKVIRHDLLASIYEYQLEREtrgygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHR 367
Cdd:cd14117   51 HQLRREIEIQSHLRHPNILRLYNYFHDRK------RIYLILEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHE 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  368 LGISHKSLHLDNVVLfhsGHRTFAKLMDFGFTrtlrdmnaSHPFNINSQSITNILpeGLYPPEVSESSfaAASRKTDIWC 447
Cdd:cd14117  125 KKVIHRDIKPENLLM---GYKGELKIADFGWS--------VHAPSLRRRTMCGTL--DYLPPEMIEGR--THDEKVDLWC 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  448 FGLLVLQMLCG------AHVLNKFSSLKLIMTHVIPLLPGSYQDLVRRCLMRDSRKRPSAIDLLSSHVIRLGTA-VLPPV 520
Cdd:cd14117  190 IGVLCYELLVGmppfesASHTETYRRIVKVDLKFPPFLSDGSRDLISKLLRYHPSERLPLKGVMEHPWVKANSRrVLPPV 269
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
266-505 7.50e-07

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: 52.36  E-value: 7.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  266 FLLRTVRISTPYWSTEDGKREIQELEYELESL-KVIRHdllASIYEYQLERETRGYgwrLYVLQEYSPKFTLFSLLQTVL 344
Cdd:cd14093   31 FAVKIIDITGEKSSENEAEELREATRREIEILrQVSGH---PNIIELHDVFESPTF---IFLVFELCRKGELFDYLTEVV 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  345 TLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDmnashpfninSQSITNIL-- 422
Cdd:cd14093  105 TLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLN---VKISDFGFATRLDE----------GEKLRELCgt 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  423 PeGLYPPEVSESS----FAAASRKTDIWCFGLLVLQMLCGA----HvLNKFSSLKLIMThvipllpGSYQ---------- 484
Cdd:cd14093  172 P-GYLAPEVLKCSmydnAPGYGKEVDMWACGVIMYTLLAGCppfwH-RKQMVMLRNIME-------GKYEfgspewddis 242
                        250       260
                 ....*....|....*....|....*
gi 63054755  485 ----DLVRRCLMRDSRKRPSAIDLL 505
Cdd:cd14093  243 dtakDLISKLLVVDPKKRLTAEEAL 267
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
358-510 7.92e-07

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: 52.43  E-value: 7.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  358 ILEGLAELHRLGISHKSLHLDNVVLfhsgHRTFAKLMDFGFTRTLrdMNASHPFNINSQSITNILPEGLyppevsesSFA 437
Cdd:cd08222  115 LLLAVQYMHERRILHRDLKAKNIFL----KNNVIKVGDFGISRIL--MGTSDLATTFTGTPYYMSPEVL--------KHE 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  438 AASRKTDIWCFGLLVLQMLCGAHVLNKFSSLKLIMTHV---IPLLPGSY----QDLVRRCLMRDSRKRPSAIDLLSSHVI 510
Cdd:cd08222  181 GYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVegeTPSLPDKYskelNAIYSRMLNKDPALRPSAAEILKIPFI 260
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
324-504 8.43e-07

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: 52.29  E-value: 8.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  324 LYVLQEYSPKFTLFSLLQTV--LTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLfhsGHRTFAKLMDFGFTRt 401
Cdd:cd05082   75 LYIVTEYMAKGSLVDYLRSRgrSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLV---SEDNVAKVSDFGLTK- 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  402 lrdmnashpfNINSQSITNILPEGLYPPE-VSESSFaaaSRKTDIWCFGLLVLQMlcgaHVLNKFSSLKLIMTHVIPLLP 480
Cdd:cd05082  151 ----------EASSTQDTGKLPVKWTAPEaLREKKF---STKSDVWSFGILLWEI----YSFGRVPYPRIPLKDVVPRVE 213
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 63054755  481 GSYQ------------DLVRRCLMRDSRKRPSAIDL 504
Cdd:cd05082  214 KGYKmdapdgcppavyDVMKNCWHLDAAMRPSFLQL 249
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
297-503 8.69e-07

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: 53.10  E-value: 8.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  297 LKVIRHDLLASI-YEYQLERetrgygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSL 375
Cdd:cd05602   62 LKNVKHPFLVGLhFSFQTTD-------KLYFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDL 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  376 HLDNVVLFHSGHRTfakLMDFGFTRTlrdmnashpfNINSQSITNIL---PEGLYPPEVSESSFaaaSRKTDIWCFGLLV 452
Cdd:cd05602  135 KPENILLDSQGHIV---LTDFGLCKE----------NIEPNGTTSTFcgtPEYLAPEVLHKQPY---DRTVDWWCLGAVL 198
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63054755  453 LQMLCGA-------------HVLNKFSSLKlimthviPLLPGSYQDLVRRCLMRDSRKRPSAID 503
Cdd:cd05602  199 YEMLYGLppfysrntaemydNILNKPLQLK-------PNITNSARHLLEGLLQKDRTKRLGAKD 255
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
726-914 9.12e-07

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 51.88  E-value: 9.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  726 IQMEYCEKLSLQDII----RDKIPVDEMWRLFRQILEALAYIHSRG---MMHRDLKPGNIFLDENRNVKLGDFGlatene 798
Cdd:cd14060   59 IVTEYASYGSLFDYLnsneSEEMDMDQIMTWATDIAKGMHYLHMEApvkVIHRDLKSRNVVIAADGVLKICDFG------ 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  799 nyqdnndkwKNRQSADEDLTTGVGTALYVAPELLsrrNGVRYDAKVDMYSLGIILFEMcMTFSTSMERIR-------IID 871
Cdd:cd14060  133 ---------ASRFHSHTTHMSLVGTFPWMAPEVI---QSLPVSETCDTYSYGVVLWEM-LTREVPFKGLEglqvawlVVE 199
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 63054755  872 TIRSPSIsfPSTFPFSRAShefkVIHCLLQHDPTKRPSSQELL 914
Cdd:cd14060  200 KNERPTI--PSSCPRSFAE----LMRRCWEADVKERPSFKQII 236
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
353-505 9.34e-07

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


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 52.43  E-value: 9.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  353 AFSnnILEGLAELH-RLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDMNAShpfNINSQSITNILPEGLYPpev 431
Cdd:cd06617  109 AVS--IVKALEYLHsKLSVIHRDVKPSNVLINRNGQ---VKLCDFGISGYLVDSVAK---TIDAGCKPYMAPERINP--- 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  432 sESSFAAASRKTDIWCFGLLVLQMLCGAHVL----NKFSSLKLIMTHVIPLLPG-----SYQDLVRRCLMRDSRKRPSAI 502
Cdd:cd06617  178 -ELNQKGYDVKSDVWSLGITMIELATGRFPYdswkTPFQQLKQVVEEPSPQLPAekfspEFQDFVNKCLKKNYKERPNYP 256

                 ...
gi 63054755  503 DLL 505
Cdd:cd06617  257 ELL 259
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
290-508 9.35e-07

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: 51.92  E-value: 9.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  290 LEYELESLKVIRHDLLASIYEyQLErETRGygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLG 369
Cdd:cd14163   47 LPRELQIVERLDHKNIIHVYE-MLE-SADG---KIYLVMELAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCG 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  370 ISHKSLHLDNVVLfhSGHRTfaKLMDFGFTRTLrdmnashPFNINSQSITNILPEGLYPPEVSESsFAAASRKTDIWCFG 449
Cdd:cd14163  122 VAHRDLKCENALL--QGFTL--KLTDFGFAKQL-------PKGGRELSQTFCGSTAYAAPEVLQG-VPHDSRKGDIWSMG 189
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  450 LLVLQMLCGAHVLNKFSSLKLIMTHVIPL-LPGSY------QDLVRRCLMRDSRKRPSaIDLLSSH 508
Cdd:cd14163  190 VVLYVMLCAQLPFDDTDIPKMLCQQQKGVsLPGHLgvsrtcQDLLKRLLEPDMVLRPS-IEEVSWH 254
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
751-792 9.77e-07

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


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 49.75  E-value: 9.77e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 63054755  751 RLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFG 792
Cdd:cd13968   95 SIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
290-509 1.13e-06

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: 51.71  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  290 LEYELESLKVIRHDLLASIYEyqLERETRGygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLG 369
Cdd:cd14165   48 LPRELEILARLNHKSIIKTYE--IFETSDG---KVYIVMELGVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELD 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  370 ISHKSLHLDNVVLfhsgHRTFA-KLMDFGFTR-TLRDMNASHPFninsqSITNILPEGLYPPEVSESsFAAASRKTDIWC 447
Cdd:cd14165  123 IVHRDLKCENLLL----DKDFNiKLTDFGFSKrCLRDENGRIVL-----SKTFCGSAAYAAPEVLQG-IPYDPRIYDIWS 192
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  448 FGLLVLQMLCGAHVL---NKFSSLKLIMTHVIPL-----LPGSYQDLVRRCLMRDSRKRpSAIDLLSSHV 509
Cdd:cd14165  193 LGVILYIMVCGSMPYddsNVKKMLKIQKEHRVRFprsknLTSECKDLIYRLLQPDVSQR-LCIDEVLSHP 261
tRNA-synt_His pfam13393
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ...
1096-1272 1.15e-06

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: 52.20  E-value: 1.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   1096 DAETIKALDEVL--TEIPSLTescILINHADILSSILDYLQVSKDKRRMATHILgqinQRLTLSQVRNQLRiESLVPSTT 1173
Cdd:pfam13393  127 DAEIISLLLEALaaAGVPGVT---LDLGHVGLVRALLEAAGLSEALEEALRAAL----QRKDAAELAELAA-EAGLPPAL 198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   1174 LDDLSLFDFRENYEEGASKLRKIFGKemPQKMRTALNYMERVVKLLRALKISHQLYFMPLCVYNFEFYDGgLMFQAInLA 1253
Cdd:pfam13393  199 RRALLALPDLYGGPEVLDEARAALPG--LPALQEALDELEALAALLEALGDGVRLTFDLAELRGYEYYTG-IVFAAY-AP 274
                          170
                   ....*....|....*....
gi 63054755   1254 EKSELICAGGRYDKLVRFF 1272
Cdd:pfam13393  275 GVGEPLARGGRYDDLGAAF 293
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
754-915 1.18e-06

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


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 51.50  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  754 RQILEALAYIHSRGMMHRDLKPGNIFLDENR---NVKLGDFGLATEnenyqdnndkwknrQSADEDLTTGVGTALYVAPE 830
Cdd:cd14115   96 RDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLEDAVQ--------------ISGHRHVHHLLGNPEFAAPE 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  831 LLsrrNGVRYDAKVDMYSLGIILFEMCMTFSTSMERIR---IIDTIRSpSISFPSTFpFSRASHEFK-VIHCLLQHDPTK 906
Cdd:cd14115  162 VI---QGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKeetCINVCRV-DFSFPDEY-FGDVSQAARdFINVILQEDPRR 236

                 ....*....
gi 63054755  907 RPSSQELLE 915
Cdd:cd14115  237 RPTAATCLQ 245
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
755-915 1.21e-06

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


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 52.29  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAteNENYQDNNdkWKNRQSADEDLTtgvgtalYVAPELLSR 834
Cdd:cd05102  180 QVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLA--RDIYKDPD--YVRKGSARLPLK-------WMAPESIFD 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  835 RngvRYDAKVDMYSLGIILFEMcmtFSTSM-------------ERIRIIDTIRSPSISFPSTfpfsrasheFKVIHCLLQ 901
Cdd:cd05102  249 K---VYTTQSDVWSFGVLLWEI---FSLGAspypgvqineefcQRLKDGTRMRAPEYATPEI---------YRIMLSCWH 313
                        170
                 ....*....|....
gi 63054755  902 HDPTKRPSSQELLE 915
Cdd:cd05102  314 GDPKERPTFSDLVE 327
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
286-505 1.24e-06

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: 52.05  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  286 EIQELEYELESLKVIRHDLLASIYEyqlereTRGYGWRLYVLQEYSPKFTLFSL-LQTVLTLDVETVRAFSNNILEGLAE 364
Cdd:cd06611   45 ELEDFMVEIDILSECKHPNIVGLYE------AYFYENKLWILIEFCDGGALDSImLELERGLTEPQIRYVCRQMLEALNF 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  365 LHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDMNASHPFNINSqsitnilPEGLYPPEVSESSF--AAASRK 442
Cdd:cd06611  119 LHSHKVIHRDLKAGNILLTLDGD---VKLADFGVSAKNKSTLQKRDTFIGT-------PYWMAPEVVACETFkdNPYDYK 188
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054755  443 TDIWCFGLLVLQMLCGA---HVLNKFSSLKLIMTHVIPLL------PGSYQDLVRRCLMRDSRKRPSAIDLL 505
Cdd:cd06611  189 ADIWSLGITLIELAQMEpphHELNPMRVLLKILKSEPPTLdqpskwSSSFNDFLKSCLVKDPDDRPTAAELL 260
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
293-523 1.54e-06

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 51.61  E-value: 1.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  293 ELESLKVIRHDLLASIYEYQLEREtrgygwrLYVLQEYSPKFTLFSLLQTV--LTLDVETVRAFSNNILEGLAELHRLGI 370
Cdd:cd05069   57 EAQIMKKLRHDKLVPLYAVVSEEP-------IYIVTEFMGKGSLLDFLKEGdgKYLKLPQLVDMAAQIADGMAYIERMNY 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  371 SHKSLHLDNVVLfhsGHRTFAKLMDFGFTRTLRDmnashpfNINSQSITNILPEGLYPPEVSesSFAAASRKTDIWCFGL 450
Cdd:cd05069  130 IHRDLRAANILV---GDNLVCKIADFGLARLIED-------NEYTARQGAKFPIKWTAPEAA--LYGRFTIKSDVWSFGI 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  451 LVLQMLCGAHV-----LNKFSSLKLIMTHVIPL---LPGSYQDLVRRCLMRDSRKRPSaIDLLSSHVIRLGTAVLPPVEQ 522
Cdd:cd05069  198 LLTELVTKGRVpypgmVNREVLEQVERGYRMPCpqgCPESLHELMKLCWKKDPDERPT-FEYIQSFLEDYFTATEPQYQP 276

                 .
gi 63054755  523 G 523
Cdd:cd05069  277 G 277
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
762-856 1.64e-06

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: 51.38  E-value: 1.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  762 YIH--SRGMMHRDLKPGNIFLDENRNVKLGDFGlatenenyqdnndkwKNR--QSADED-LTTGVGTALYVAPELLSRRN 836
Cdd:cd14064  108 YLHnlTQPIIHRDLNSHNILLYEDGHAVVADFG---------------ESRflQSLDEDnMTKQPGNLRWMAPEVFTQCT 172
                         90       100
                 ....*....|....*....|
gi 63054755  837 gvRYDAKVDMYSLGIILFEM 856
Cdd:cd14064  173 --RYSIKADVFSYALCLWEL 190
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
724-880 1.94e-06

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: 51.43  E-value: 1.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIRDKIPVDEMWRLF---RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenENY 800
Cdd:cd05081   82 LRLVMEYLPSGCLRDFLQRHRARLDASRLLlysSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLA---KLL 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  801 QDNNDKWKNRQSadedlttGVGTALYVAPELLSRRngvRYDAKVDMYSLGIILFEMcMTFStsmeririiDTIRSPSISF 880
Cdd:cd05081  159 PLDKDYYVVREP-------GQSPIFWYAPESLSDN---IFSRQSDVWSFGVVLYEL-FTYC---------DKSCSPSAEF 218
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
293-523 2.07e-06

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: 51.22  E-value: 2.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  293 ELESLKVIRHDLLASIYEYQLEREtrgygwrLYVLQEYSPKFTLFSLLQ--TVLTLDVETVRAFSNNILEGLAELHRLGI 370
Cdd:cd05070   54 EAQIMKKLKHDKLVQLYAVVSEEP-------IYIVTEYMSKGSLLDFLKdgEGRALKLPNLVDMAAQVAAGMAYIERMNY 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  371 SHKSLHLDNVVLfhsGHRTFAKLMDFGFTRTLRDmnashpfNINSQSITNILPEGLYPPEVSesSFAAASRKTDIWCFGL 450
Cdd:cd05070  127 IHRDLRSANILV---GNGLICKIADFGLARLIED-------NEYTARQGAKFPIKWTAPEAA--LYGRFTIKSDVWSFGI 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  451 LVLQMLCGAHV----LNKFSSLKLI-MTHVIPL---LPGSYQDLVRRCLMRDSRKRPSaIDLLSSHVIRLGTAVLPPVEQ 522
Cdd:cd05070  195 LLTELVTKGRVpypgMNNREVLEQVeRGYRMPCpqdCPISLHELMIHCWKKDPEERPT-FEYLQGFLEDYFTATEPQYQP 273

                 .
gi 63054755  523 G 523
Cdd:cd05070  274 G 274
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
296-458 2.09e-06

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: 51.11  E-value: 2.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  296 SLKVI-RHDLLASIYEYQLERET------------RGYGW-----RLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNN 357
Cdd:cd14116   34 ALKVLfKAQLEKAGVEHQLRREVeiqshlrhpnilRLYGYfhdatRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITE 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  358 ILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTrtlrdmnaSHPFNINSQSITNILpeGLYPPEVSESSfa 437
Cdd:cd14116  114 LANALSYCHSKRVIHRDIKPENLLLGSAGE---LKIADFGWS--------VHAPSSRRTTLCGTL--DYLPPEMIEGR-- 178
                        170       180
                 ....*....|....*....|.
gi 63054755  438 AASRKTDIWCFGLLVLQMLCG 458
Cdd:cd14116  179 MHDEKVDLWSLGVLCYEFLVG 199
PLN03224 PLN03224
probable serine/threonine protein kinase; Provisional
741-872 2.28e-06

probable serine/threonine protein kinase; Provisional


Pssm-ID: 178763 [Multi-domain]  Cd Length: 507  Bit Score: 52.00  E-value: 2.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   741 RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATE---NENYQDNNDKWKNRQSADEDL 817
Cdd:PLN03224  303 QDKRDINVIKGVMRQVLTGLRKLHRIGIVHRDIKPENLLVTVDGQVKIIDFGAAVDmctGINFNPLYGMLDPRYSPPEEL 382
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   818 TTGVGTALYVAP---ELLSRRNGV--RYDAkVDMYSLGIILFEMCMTFSTSMERIRIIDT 872
Cdd:PLN03224  383 VMPQSCPRAPAPamaALLSPFAWLygRPDL-FDSYTAGVLLMQMCVPELRPVANIRLFNT 441
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
751-915 2.29e-06

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: 50.99  E-value: 2.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  751 RLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRN--VKLGDFGLAtenenyqdnndkwknRQSADEDLTTGVGTALYVA 828
Cdd:cd14112  103 TTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSwqVKLVDFGRA---------------QKVSKLGKVPVDGDTDWAS 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  829 PELLSRRNGVRydAKVDMYSLGIILFEMCMTFSTSMERIRIIDTIRSpSISFPSTFP---FSRASHE-FKVIHCLLQHDP 904
Cdd:cd14112  168 PEFHNPETPIT--VQSDIWGLGVLTFCLLSGFHPFTSEYDDEEETKE-NVIFVKCRPnliFVEATQEaLRFATWALKKSP 244
                        170
                 ....*....|.
gi 63054755  905 TKRPSSQELLE 915
Cdd:cd14112  245 TRRMRTDEALE 255
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
734-856 2.41e-06

kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of KIND only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features


Pssm-ID: 214801  Cd Length: 176  Bit Score: 49.32  E-value: 2.41e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755     734 LSLQDII--RDK-IPVDEMWRLFRQILEALAYIHSRGmmhrdlKPGNIFLDENRNVKLgdFGLATenenyqdnndkwknr 810
Cdd:smart00750    1 VSLADILevRGRpLNEEEIWAVCLQCLGALRELHRQA------KSGNILLTWDGLLKL--DGSVA--------------- 57
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 63054755     811 QSADEdltTGVGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEM 856
Cdd:smart00750   58 FKTPE---QSRPDPYFMAPEVIQGQS---YTEKADIYSLGITLYEA 97
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
323-498 2.82e-06

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: 50.85  E-value: 2.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  323 RLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTL 402
Cdd:cd05583   73 KLHLILDYVNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGH---VVLTDFGLSKEF 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  403 rdmnashpfninsqsitniLPEGLY------------PPEVSESSFAAASRKTDIWCFGLLVLQMLCGAHVL------NK 464
Cdd:cd05583  150 -------------------LPGENDraysfcgtieymAPEVVRGGSDGHDKAVDWWSLGVLTYELLTGASPFtvdgerNS 210
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 63054755  465 FSSL-KLIMTHVIPL---LPGSYQDLVRRCLMRDSRKR 498
Cdd:cd05583  211 QSEIsKRILKSHPPIpktFSAEAKDFILKLLEKDPKKR 248
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
724-856 3.04e-06

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


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 50.50  E-value: 3.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  724 LYIQMEYCEKLSLQDIIR--DKIPVDEMWRLF--RQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenen 799
Cdd:cd05052   77 FYIITEFMPYGNLLDYLRecNREELNAVVLLYmaTQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLS----- 151
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  800 yqdnndkwknRQSADEDLTTGVGTAL---YVAPELLSRRngvRYDAKVDMYSLGIILFEM 856
Cdd:cd05052  152 ----------RLMTGDTYTAHAGAKFpikWTAPESLAYN---KFSIKSDVWAFGVLLWEI 198
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
720-856 3.16e-06

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 50.63  E-value: 3.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   720 LNATLYIqMEYCEKLSLQDIIR--DKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRN-VKLGDFGLAte 796
Cdd:PHA03390   81 LKGHVLI-MDYIKDGDLFDLLKkeGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAKDrIYLCDYGLC-- 157
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   797 nenyqdnndKWKNRQSADEdlttgvGTALYVAPELLSRRNgvrYDAKVDMYSLGIILFEM 856
Cdd:PHA03390  158 ---------KIIGTPSCYD------GTLDYFSPEKIKGHN---YDVSFDWWAVGVLTYEL 199
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
726-908 3.44e-06

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: 50.36  E-value: 3.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  726 IQMEYCEKLSLQDIIRDK---IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQD 802
Cdd:cd05063   83 IITEYMENGALDKYLRDHdgeFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLEDDPE 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  803 nndkwknrqsADEDLTTGVGTALYVAPELLSRRngvRYDAKVDMYSLGIILFEMcMTFS-------TSMERIRII-DTIR 874
Cdd:cd05063  163 ----------GTYTTSGGKIPIRWTAPEAIAYR---KFTSASDVWSFGIVMWEV-MSFGerpywdmSNHEVMKAInDGFR 228
                        170       180       190
                 ....*....|....*....|....*....|....
gi 63054755  875 SPSisfpstfPFSRASHEFKVIHCLLQHDPTKRP 908
Cdd:cd05063  229 LPA-------PMDCPSAVYQLMLQCWQQDRARRP 255
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
692-915 3.55e-06

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 50.78  E-value: 3.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  692 SNTSDKEgSSDKDSSIEEASSVKTQENGLN--------ATLYIQMEYCEKLSLQDIIR-------------DKIPVDEMW 750
Cdd:cd05098   55 SDATEKD-LSDLISEMEMMKMIGKHKNIINllgactqdGPLYVIVEYASKGNLREYLQarrppgmeycynpSHNPEEQLS 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  751 -----RLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYqdnnDKWKNRqsadedlTTGVGTAL 825
Cdd:cd05098  134 skdlvSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHI----DYYKKT-------TNGRLPVK 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  826 YVAPELLSRRngvRYDAKVDMYSLGIILFEMcMTFSTSmeririidtiRSPSISFPSTFPFSRASHEF-KVIHC-----L 899
Cdd:cd05098  203 WMAPEALFDR---IYTHQSDVWSFGVLLWEI-FTLGGS----------PYPGVPVEELFKLLKEGHRMdKPSNCtnelyM 268
                        250       260
                 ....*....|....*....|.
gi 63054755  900 LQHD-----PTKRPSSQELLE 915
Cdd:cd05098  269 MMRDcwhavPSQRPTFKQLVE 289
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
351-505 3.89e-06

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: 50.32  E-value: 3.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  351 VRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHRTFAKLMDFGFTRTLRdmnashpfniNSQSITNILPEGLY-PP 429
Cdd:cd14197  113 VKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLGDIKIVDFGLSRILK----------NSEELREIMGTPEYvAP 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  430 EVseSSFAAASRKTDIWCFGLLVLQMLCGAH----------VLNkFSSLKLIMT-HVIPLLPGSYQDLVRRCLMRDSRKR 498
Cdd:cd14197  183 EI--LSYEPISTATDMWSIGVLAYVMLTGISpflgddkqetFLN-ISQMNVSYSeEEFEHLSESAIDFIKTLLIKKPENR 259

                 ....*..
gi 63054755  499 PSAIDLL 505
Cdd:cd14197  260 ATAEDCL 266
Pkinase pfam00069
Protein kinase domain;
293-507 4.24e-06

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 49.55  E-value: 4.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755    293 ELESLKVIRHDLLASIYEYqLERETRgygwrLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAelhrlgish 372
Cdd:pfam00069   48 EIKILKKLNHPNIVRLYDA-FEDKDN-----LYLVLEYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLE--------- 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755    373 KSLHLDNVVlfhsGHRTFAklmdfgftrtlrdmnashpfninsqsitnilpeglyPPEVSESSfaAASRKTDIWCFGLLV 452
Cdd:pfam00069  113 SGSSLTTFV----GTPWYM------------------------------------APEVLGGN--PYGPKVDVWSLGCIL 150
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63054755    453 LQMLCG----AHVLNKFSSLKLIMTHVIPLLPGSY-----QDLVRRCLMRDSRKRPSAIDLLSS 507
Cdd:pfam00069  151 YELLTGkppfPGINGNEIYELIIDQPYAFPELPSNlseeaKDLLKKLLKKDPSKRLTATQALQH 214
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
284-510 4.28e-06

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: 50.12  E-value: 4.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  284 KREIQELEYELESLKVIRHDLLASIYEYQLERETrgygwrLYVLQEYSPKFTLFS--LLQTVLTLDVETVRAFSNNILEG 361
Cdd:cd08221   40 EKERRDALNEIDILSLLNHDNIITYYNHFLDGES------LFIEMEYCNGGNLHDkiAQQKNQLFPEEVVLWYLYQIVSA 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  362 LAELHRLGISHKSLHLDNVVLFHSGhrtFAKLMDFGFTRTLrdmnashpfNINSQSITNILPEGLY-PPEVSESsfAAAS 440
Cdd:cd08221  114 VSHIHKAGILHRDIKTLNIFLTKAD---LVKLGDFGISKVL---------DSESSMAESIVGTPYYmSPELVQG--VKYN 179
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  441 RKTDIWCFGLLVLQMLCGAHVLNKFSSLKL-------IMTHVIPLLPGSYQDLVRRCLMRDSRKRPSAIDLLSSHVI 510
Cdd:cd08221  180 FKSDIWAVGCVLYELLTLKRTFDATNPLRLavkivqgEYEDIDEQYSEEIIQLVHDCLHQDPEDRPTAEELLERPLL 256
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
324-458 4.29e-06

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: 49.92  E-value: 4.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  324 LYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGhrtFAKLMDFGFTRTLR 403
Cdd:cd05572   68 LYMLMEYCLGGELWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNG---YVKLVDFGFAKKLG 144
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  404 DMNASHPFNINsqsitnilPEglY-PPEVSES---SFAAasrktDIWCFGLLVLQMLCG 458
Cdd:cd05572  145 SGRKTWTFCGT--------PE--YvAPEIILNkgyDFSV-----DYWSLGILLYELLTG 188
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
278-513 4.30e-06

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: 50.35  E-value: 4.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  278 WSTEDGKREIQELEYELESLKVIRHDLLASIYEYQLERETRgygwrLYVLqEYSPKFTLFSLLQTVLT---LDVETVRAF 354
Cdd:cd14066   25 LNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEK-----LLVY-EYMPNGSLEDRLHCHKGsppLPWPQRLKI 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  355 SNNILEGLAELHRlGISHKSLHLD----NVVLFHSGHrtfAKLMDFGFTRtlrdmnASHPFNINSQSITNILPEGLYPPE 430
Cdd:cd14066   99 AKGIARGLEYLHE-ECPPPIIHGDikssNILLDEDFE---PKLTDFGLAR------LIPPSESVSKTSAVKGTIGYLAPE 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  431 VSESSfaAASRKTDIWCFGLLVLQMLCG---AHVLNKFSSLKLIMTHVIPLLPGSYQDLVRRCLMRDSRKRPSAIDLLss 507
Cdd:cd14066  169 YIRTG--RVSTKSDVYSFGVVLLELLTGkpaVDENRENASRKDLVEWVESKGKEELEDILDKRLVDDDGVEEEEVEAL-- 244

                 ....*.
gi 63054755  508 hvIRLG 513
Cdd:cd14066  245 --LRLA 248
STKc_CK1_alpha cd14128
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze ...
752-853 4.41e-06

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. CK1alpha plays a role in cell cycle progression, spindle dynamics, and chromosome segregation. It is also involved in regulating apoptosis mediated by Fas or the retinoid X receptor (RXR), and is a positive regulator of Wnt signaling. CK1alpha phosphorylates the NS5A protein of flaviviruses such as the Hepatitis C virus (HCV) and yellow fever virus (YFV), and influences flaviviral replication. The CK1 alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271030 [Multi-domain]  Cd Length: 266  Bit Score: 50.20  E-value: 4.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  752 LFRQILEALAYIHSRGMMHRDLKPGNIFLDENRN---VKLGDFGLAtenENYQDNNDKWKNRQSADEDLTtgvGTALYVA 828
Cdd:cd14128  101 LADQMIGRIEYVHNKNFIHRDIKPDNFLMGIGRHcnkLFLIDFGLA---KKYRDSRTRQHIPYREDKNLT---GTARYAS 174
                         90       100
                 ....*....|....*....|....*
gi 63054755  829 pelLSRRNGVRYDAKVDMYSLGIIL 853
Cdd:cd14128  175 ---INAHLGIEQSRRDDMESLGYVL 196
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
282-500 4.66e-06

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: 50.13  E-value: 4.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  282 DGKREIQELEYELESLKVIRHDLLASIYEYQLERETrgygwrLYVLQEYSPKFTLFSLLQTV--LTLDVETVRAFSNNIL 359
Cdd:cd05148   41 DDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEP------VYIITELMEKGSLLAFLRSPegQVLPVASLIDMACQVA 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  360 EGLAELHRLGISHKSLHLDNVVLfhsGHRTFAKLMDFGFTRTLRDmnashpfNINSQSITNILPEGLYPPEVSESSFaaa 439
Cdd:cd05148  115 EGMAYLEEQNSIHRDLAARNILV---GEDLVCKVADFGLARLIKE-------DVYLSSDKKIPYKWTAPEAASHGTF--- 181
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  440 SRKTDIWCFGLLVLQMLCGAHV----LNKFSSLKLIMT-HVIPL---LPGSYQDLVRRCLMRDSRKRPS 500
Cdd:cd05148  182 STKSDVWSFGILLYEMFTYGQVpypgMNNHEVYDQITAgYRMPCpakCPQEIYKIMLECWAAEPEDRPS 250
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
324-498 5.02e-06

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: 50.33  E-value: 5.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  324 LYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGftrtlr 403
Cdd:cd05620   71 LFFVMEFLNGGDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGH---IKIADFG------ 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  404 dMNASHPFNINSQSITNILPEGLYPPEVSESSFaaaSRKTDIWCFGLLVLQMLCGAHVLNK------FSSLKLIMTHVIP 477
Cdd:cd05620  142 -MCKENVFGDNRASTFCGTPDYIAPEILQGLKY---TFSVDWWSFGVLLYEMLIGQSPFHGddedelFESIRVDTPHYPR 217
                        170       180
                 ....*....|....*....|.
gi 63054755  478 LLPGSYQDLVRRCLMRDSRKR 498
Cdd:cd05620  218 WITKESKDILEKLFERDPTRR 238
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
284-458 5.62e-06

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: 50.39  E-value: 5.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  284 KREIQELEYELESLKVIRHDLLASI-YEYQLERetrgygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGL 362
Cdd:cd05595   36 KDEVAHTVTESRVLQNTRHPFLTALkYAFQTHD-------RLCFVMEYANGGELFFHLSRERVFTEDRARFYGAEIVSAL 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  363 AELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTR-------TLRDMNAShpfninsqsitnilPEGLYPPEVSESS 435
Cdd:cd05595  109 EYLHSRDVVYRDIKLENLMLDKDGH---IKITDFGLCKegitdgaTMKTFCGT--------------PEYLAPEVLEDND 171
                        170       180
                 ....*....|....*....|...
gi 63054755  436 FAaasRKTDIWCFGLLVLQMLCG 458
Cdd:cd05595  172 YG---RAVDWWGLGVVMYEMMCG 191
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
728-855 5.72e-06

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: 50.06  E-value: 5.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  728 MEYCEKLSLQDIIRDK--IPVDEMWRLFRQILEALAYIHS--RGMMHRDLKPGNIFLDENR---NVKLGDFGLA--TENE 798
Cdd:cd14041   90 LEYCEGNDLDFYLKQHklMSEKEARSIIMQIVNALKYLNEikPPIIHYDLKPGNILLVNGTacgEIKITDFGLSkiMDDD 169
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 63054755  799 NYqdnndkwkNRQSADEDLTTGVGTALYVAPE-LLSRRNGVRYDAKVDMYSLGIILFE 855
Cdd:cd14041  170 SY--------NSVDGMELTSQGAGTYWYLPPEcFVVGKEPPKISNKVDVWSVGVIFYQ 219
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
748-856 6.01e-06

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 49.97  E-value: 6.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  748 EMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAT---ENENYQDNNdkwknrqsadedltTGVGTA 824
Cdd:cd05061  120 EMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGMTRdiyETDYYRKGG--------------KGLLPV 185
                         90       100       110
                 ....*....|....*....|....*....|..
gi 63054755  825 LYVAPEllSRRNGVrYDAKVDMYSLGIILFEM 856
Cdd:cd05061  186 RWMAPE--SLKDGV-FTTSSDMWSFGVVLWEI 214
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
323-458 6.05e-06

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: 50.29  E-value: 6.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  323 RLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTl 402
Cdd:cd05570   70 RLYFVMEYVNGGDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGH---IKIADFGMCKE- 145
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  403 rdmnashpfNINSQSITNIL---PEGLYPPEVSESSFAAAsrkTDIWCFGLLVLQMLCG 458
Cdd:cd05570  146 ---------GIWGGNTTSTFcgtPDYIAPEILREQDYGFS---VDWWALGVLLYEMLAG 192
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
755-856 6.24e-06

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


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 50.01  E-value: 6.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSR--GMMHRDLKPGNIFL-DENRN-VKLGDFGLATenenyQDNNDKWKNRQSAdedlttgvgtaLYVAPE 830
Cdd:cd14226  124 QLCTALLFLSTPelSIIHCDLKPENILLcNPKRSaIKIIDFGSSC-----QLGQRIYQYIQSR-----------FYRSPE 187
                         90       100
                 ....*....|....*....|....*.
gi 63054755  831 LLSrrnGVRYDAKVDMYSLGIILFEM 856
Cdd:cd14226  188 VLL---GLPYDLAIDMWSLGCILVEM 210
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
326-511 6.31e-06

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: 49.74  E-value: 6.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  326 VLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHRTfaKLMDFGFT-RTLRD 404
Cdd:cd06630   80 IFVEWMAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGQRL--RIADFGAAaRLASK 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  405 MNASHPFNinSQSITNIlpeGLYPPEV--SESSfaaaSRKTDIWCFGLLVLQMLCGAHVLN--KFSS-LKLIM------- 472
Cdd:cd06630  158 GTGAGEFQ--GQLLGTI---AFMAPEVlrGEQY----GRSCDVWSVGCVIIEMATAKPPWNaeKISNhLALIFkiasatt 228
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 63054755  473 THVIP--LLPGSyQDLVRRCLMRDSRKRPSAIDLLSSHVIR 511
Cdd:cd06630  229 PPPIPehLSPGL-RDVTLRCLELQPEDRPPARELLKHPVFT 268
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
359-510 6.59e-06

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: 49.62  E-value: 6.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  359 LEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGF------TRTLRDMNASHPFNInsqsitniLPEGLYPPEVS 432
Cdd:cd06638  134 LMGLQHLHVNKTIHRDVKGNNILLTTEGG---VKLVDFGVsaqltsTRLRRNTSVGTPFWM--------APEVIACEQQL 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  433 ESSFAAasrKTDIWCFGLLVLQMLCGAHVLNKFSSLKLIMThvIPLLP-----------GSYQDLVRRCLMRDSRKRPSA 501
Cdd:cd06638  203 DSTYDA---RCDVWSLGITAIELGDGDPPLADLHPMRALFK--IPRNPpptlhqpelwsNEFNDFIRKCLTKDYEKRPTV 277

                 ....*....
gi 63054755  502 IDLLSSHVI 510
Cdd:cd06638  278 SDLLQHVFI 286
RWD_YLR419W-like cd23827
RWD domain of Saccharomyces cerevisiae putative ATP-dependent RNA helicase YLR419W and related ...
15-127 7.29e-06

RWD domain of Saccharomyces cerevisiae putative ATP-dependent RNA helicase YLR419W and related proteins; YLR419W (EC 3.6.4.13) may act as an ATP-binding RNA helicase. The RWD domain may mediate protein-protein interactions.


Pssm-ID: 467662  Cd Length: 104  Bit Score: 46.09  E-value: 7.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   15 ENEIEALKAIFMDDFEELkvrnawnvtNGHVYCIHLCSRSANsksiaKLDLCIELGRS--YPYVKPVIKLQnGENVLNSQ 92
Cdd:cd23827    2 DEEIEALEAIYGEKFEVI---------SDDSCEITLNSPTKT-----KPSLKLKFYKSssYPNSLPGIFIS-SSDKLPAY 66
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 63054755   93 IRF-LLDKLDTKAKD-LLGEEMIFELASIVQDYLNDW 127
Cdd:cd23827   67 IKLaIIRQLLQYARDnLLGDPMIFSIVEWLEENIEEI 103
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
755-915 7.58e-06

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 49.80  E-value: 7.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  755 QILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenenyqdnNDKWKnrqsaDEDLTTGVGTAL---YVAPEL 831
Cdd:cd05054  146 QVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLA---------RDIYK-----DPDYVRKGDARLplkWMAPES 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  832 LSRRngvRYDAKVDMYSLGIILFEmCMTFSTS-----------MERIRIIDTIRSPsisfpstfpfSRASHEFKVIHCLL 900
Cdd:cd05054  212 IFDK---VYTTQSDVWSFGVLLWE-IFSLGASpypgvqmdeefCRRLKEGTRMRAP----------EYTTPEIYQIMLDC 277
                        170
                 ....*....|....*.
gi 63054755  901 QH-DPTKRPSSQELLE 915
Cdd:cd05054  278 WHgEPKERPTFSELVE 293
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
744-874 7.65e-06

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 49.62  E-value: 7.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  744 IPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENEnyqdNNDKWKNRQSADEDLTtgvgt 823
Cdd:cd05075  110 LPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLSKKIY----NGDYYRQGRISKMPVK----- 180
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 63054755  824 alYVAPELLSRRngvRYDAKVDMYSLGIILFEMCMTFST---SMERIRIIDTIR 874
Cdd:cd05075  181 --WIAIESLADR---VYTTKSDVWSFGVTMWEIATRGQTpypGVENSEIYDYLR 229
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
728-856 7.97e-06

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


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 49.57  E-value: 7.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  728 MEYCEKLSLQDIIRDKIPVDEM------------WRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAT 795
Cdd:cd14206   76 MEFCQLGDLKRYLRAQRKADGMtpdlptrdlrtlQRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLSH 155
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63054755  796 EN--ENYQDNNDK-WKNRQsadedlttgvgtalYVAPELLSRRNG----VRYDAKVDMYSLGIILFEM 856
Cdd:cd14206  156 NNykEDYYLTPDRlWIPLR--------------WVAPELLDELHGnlivVDQSKESNVWSLGVTIWEL 209
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
728-913 8.13e-06

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


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 49.22  E-value: 8.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  728 MEYCEKLSLQDIIRDKIPVDEM-------WRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLA---TEN 797
Cdd:cd05087   76 MEFCPLGDLKGYLRSCRAAESMapdpltlQRMACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLShckYKE 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  798 ENYQDNNDKWKNRQsadedlttgvgtalYVAPELLSRRNG----VRYDAKVDMYSLGIILFEM----CMTFSTSMERIRI 869
Cdd:cd05087  156 DYFVTADQLWVPLR--------------WIAPELVDEVHGnllvVDQTKQSNVWSLGVTIWELfelgNQPYRHYSDRQVL 221
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 63054755  870 IDTIRSPSISFPS-TFPFSRASHEFKVIH-CLLQhdPTKRPSSQEL 913
Cdd:cd05087  222 TYTVREQQLKLPKpQLKLSLAERWYEVMQfCWLQ--PEQRPTAEEV 265
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
741-914 8.50e-06

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: 48.89  E-value: 8.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  741 RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGN-IFLDENR-NVKLgdfglatenENYQDNNDKWKNrqsaDEDLT 818
Cdd:cd14023   78 CKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKfVFSDEERtQLRL---------ESLEDTHIMKGE----DDALS 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  819 TGVGTALYVAPELLSrRNGVRYDAKVDMYSLGIILFEMCM---TFSTSmERIRIIDTIRSPSISFPSTF-PFSRAshefk 894
Cdd:cd14023  145 DKHGCPAYVSPEILN-TTGTYSGKSADVWSLGVMLYTLLVgryPFHDS-DPSALFSKIRRGQFCIPDHVsPKARC----- 217
                        170       180
                 ....*....|....*....|
gi 63054755  895 VIHCLLQHDPTKRPSSQELL 914
Cdd:cd14023  218 LIRSLLRREPSERLTAPEIL 237
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
326-507 9.46e-06

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: 48.92  E-value: 9.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  326 VLQEYSPKFTLFSLL-QTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLfhSGHRTfAKLMDFGFTRTLRD 404
Cdd:cd13979   79 IIMEYCGNGTLQQLIyEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILI--SEQGV-CKLCDFGCSVKLGE 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  405 MN-ASHPFNINSQSITNILPEGLYPPEVSEssfaaasrKTDIWCFGLLVLQMLCGA---HVLNKFSSLKLIMTHVIPLLP 480
Cdd:cd13979  156 GNeVGTPRSHIGGTYTYRAPELLKGERVTP--------KADIYSFGITLWQMLTRElpyAGLRQHVLYAVVAKDLRPDLS 227
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 63054755  481 GS--------YQDLVRRCLMRDSRKRPSA-IDLLSS 507
Cdd:cd13979  228 GLedsefgqrLRSLISRCWSAQPAERPNAdESLLKS 263
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
324-458 9.71e-06

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: 49.02  E-value: 9.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  324 LYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLR 403
Cdd:cd05611   72 LYLVMEYLNGGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGH---LKLTDFGLSRNGL 148
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 63054755  404 dmnashpfnINSQSITNILPEGLYPPEVSESsfAAASRKTDIWCFGLLVLQMLCG 458
Cdd:cd05611  149 ---------EKRHNKKFVGTPDYLAPETILG--VGDDKMSDWWSLGCVIFEFLFG 192
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
741-860 1.03e-05

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: 48.95  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  741 RDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLAtenenyqdnndkwkNRQSADEDLTTG 820
Cdd:cd05057  103 RDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLA--------------KLLDVDEKEYHA 168
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 63054755  821 VGTAL---YVAPELLSRRngvRYDAKVDMYSLGIILFEMcMTF 860
Cdd:cd05057  169 EGGKVpikWMALESIQYR---IYTHKSDVWSYGVTVWEL-MTF 207
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
323-505 1.11e-05

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: 48.80  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  323 RLYVLQEYSPKFTLFSLL--QTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGhrTFAKLMDFGFTR 400
Cdd:cd08225   73 RLFIVMEYCDGGDLMKRInrQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNG--MVAKLGDFGIAR 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  401 TLRDMN------ASHPFNINsqsitnilpeglypPEVSESSfaAASRKTDIWCFGLLVLQMLCGAHVL--NKFSS--LKL 470
Cdd:cd08225  151 QLNDSMelaytcVGTPYYLS--------------PEICQNR--PYNNKTDIWSLGCVLYELCTLKHPFegNNLHQlvLKI 214
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 63054755  471 IMTHVIPLLPG-SY--QDLVRRCLMRDSRKRPSAIDLL 505
Cdd:cd08225  215 CQGYFAPISPNfSRdlRSLISQLFKVSPRDRPSITSIL 252
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
297-502 1.16e-05

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: 49.20  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  297 LKVIRHDLLASI-YEYQLERetrgygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSL 375
Cdd:cd05603   50 LKNLKHPFLVGLhYSFQTSE-------KLYFVLDYVNGGELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDL 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  376 HLDNVVLFHSGHrtfAKLMDFGFTRTlrdmnashpfNINSQSITNIL---PEGLYPPEVSESSFaaaSRKTDIWCFGLLV 452
Cdd:cd05603  123 KPENILLDCQGH---VVLTDFGLCKE----------GMEPEETTSTFcgtPEYLAPEVLRKEPY---DRTVDWWCLGAVL 186
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  453 LQMLCGahvLNKFSSLKLI-MTHVI---PL-LPGSYQ----DLVRRCLMRDSRKRPSAI 502
Cdd:cd05603  187 YEMLYG---LPPFYSRDVSqMYDNIlhkPLhLPGGKTvaacDLLQGLLHKDQRRRLGAK 242
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
285-510 1.20e-05

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: 48.69  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  285 REIQELEYELESLKVIRHDLLASIYEYQLERETRgygwRLYVLQEYSPKFTLFSLLQTVLT----LDVETVRAFSNNILE 360
Cdd:cd08217   41 KEKQQLVSEVNILRELKHPNIVRYYDRIVDRANT----TLYIVMEYCEGGDLAQLIKKCKKenqyIPEEFIWKIFTQLLL 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  361 GLAELH-RLGISHKSLHLD----NVVLFHSGHrtfAKLMDFGFTRTLrdmnashpfNINSQSITNILPEGLY-PPE-VSE 433
Cdd:cd08217  117 ALYECHnRSVGGGKILHRDlkpaNIFLDSDNN---VKLGDFGLARVL---------SHDSSFAKTYVGTPYYmSPElLNE 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  434 SSFaaaSRKTDIWCFGLLVLQMLCGAHVLNKFSSLKL---IMTHVIPLLPGSY----QDLVRRCLMRDSRKRPSAIDLLS 506
Cdd:cd08217  185 QSY---DEKSDIWSLGCLIYELCALHPPFQAANQLELakkIKEGKFPRIPSRYsselNEVIKSMLNVDPDKRPSVEELLQ 261

                 ....
gi 63054755  507 SHVI 510
Cdd:cd08217  262 LPLI 265
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
284-506 1.25e-05

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: 48.54  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  284 KREIQELEYELESLKVIRHDLLASIYEYQLEREtrgygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLA 363
Cdd:cd14073   42 EQDMVRIRREIEIMSSLNHPHIIRIYEVFENKD------KIVIVMEYASGGELYDYISERRRLPEREARRIFRQIVSAVH 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  364 ELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDMNASHPFN----INSQSITNILPegLYPPEVsessfaaa 439
Cdd:cd14073  116 YCHKNGVVHRDLKLENILLDQNGN---AKIADFGLSNLYSKDKLLQTFCgsplYASPEIVNGTP--YQGPEV-------- 182
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054755  440 srktDIWCFGLLVLQMLCGAHVLN--KFSSLKLIMT---HVIPLLPGSYQDLVRRCLMRDSRKRPSAIDLLS 506
Cdd:cd14073  183 ----DCWSLGVLLYTLVYGTMPFDgsDFKRLVKQISsgdYREPTQPSDASGLIRWMLTVNPKRRATIEDIAN 250
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
359-504 1.27e-05

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: 48.66  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  359 LEGLAELHRLGISHKSLHLDNVVLFHSGHRTFakLMDFGFTRTLrdmnasHPFNINSQSITNILPEGL---YPPEVSESS 435
Cdd:cd13991  108 LEGLEYLHSRKILHGDVKADNVLLSSDGSDAF--LCDFGHAECL------DPDGLGKSLFTGDYIPGTethMAPEVVLGK 179
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63054755  436 faAASRKTDIWCFGLLVLQMLCGAHVLNKFSSLKL---IMTHVIPL--LPGSYQDL----VRRCLMRDSRKRPSAIDL 504
Cdd:cd13991  180 --PCDAKVDVWSSCCMMLHMLNGCHPWTQYYSGPLclkIANEPPPLreIPPSCAPLtaqaIQAGLRKEPVHRASAAEL 255
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
284-408 1.66e-05

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: 49.11  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  284 KREIQELEYELESLKVIRHDLLASIYeYQLERETRgygwrLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLA 363
Cdd:cd05610   45 KNMVHQVQAERDALALSKSPFIVHLY-YSLQSANN-----VYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALD 118
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 63054755  364 ELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTR-TL-RDMNAS 408
Cdd:cd05610  119 YLHRHGIIHRDLKPDNMLISNEGH---IKLTDFGLSKvTLnRELNMM 162
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
324-458 1.70e-05

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: 48.54  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  324 LYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTlr 403
Cdd:cd05592   71 LFFVMEYLNGGDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGH---IKIADFGMCKE-- 145
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 63054755  404 dmnashpfNINSQSITNIL---PEGLyPPEVSESSFAAASrkTDIWCFGLLVLQMLCG 458
Cdd:cd05592  146 --------NIYGENKASTFcgtPDYI-APEILKGQKYNQS--VDWWSFGVLLYEMLIG 192
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
284-760 2.04e-05

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 49.35  E-value: 2.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   284 KREIQELEYELESLKVIRHDllaSIYEYqLERETRGYGWRLYVLQEYSPKFTLFSLLQTVLTL----DVETVRAFSNNIL 359
Cdd:PTZ00266   53 EREKSQLVIEVNVMRELKHK---NIVRY-IDRFLNKANQKLYILMEFCDAGDLSRNIQKCYKMfgkiEEHAIVDITRQLL 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   360 EGLAELHRLG-------ISHKSLHLDNVVLF----HSGH----------RTFAKLMDFGFTRTLrdmnashpfNINSQSI 418
Cdd:PTZ00266  129 HALAYCHNLKdgpngerVLHRDLKPQNIFLStgirHIGKitaqannlngRPIAKIGDFGLSKNI---------GIESMAH 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   419 TNILPEGLYPPEVSESSFAAASRKTDIWCFGLLVLQMLCGA---HVLNKFSSLKLIMTHViPLLP--GSYQD---LVRRC 490
Cdd:PTZ00266  200 SCVGTPYYWSPELLLHETKSYDDKSDMWALGCIIYELCSGKtpfHKANNFSQLISELKRG-PDLPikGKSKElniLIKNL 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   491 LMRDSRKRPSAIDLLSSHVIRlgtAVLPPVEQGTFSKSARPSYGGqqdgiidLLYRKSVSRYETDFeELEFLGRGGFGEV 570
Cdd:PTZ00266  279 LNLSAKERPSALQCLGYQIIK---NVGPPVGAAGGGAGVAAAPGA-------VVARRNPSKEHPGL-QLAAMEKAKHAEA 347
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   571 VKvknridgrfYAVKKLVLLSDDKENSRILREVMTLSRLHHEHVvryytawveteANDTVTEIISSDSESLSQSLNMAVD 650
Cdd:PTZ00266  348 AN---------YGISPNTLINQRNEEQHGRRSSSCASRQSANNV-----------TNITSITSVTSVASVASVASVPSKD 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   651 FRQSSSLPADKLSSLDIHfeddYNSSADEEDPEASDISFQYSNTSDKEGSSDKDSSIEEASSVKTQ--ENGLNATLYIQM 728
Cdd:PTZ00266  408 DRKYPQDGATHCHAVNGH----YGGRVDKDHAERARIEKENAHRKALEMKILEKKRIERLEREERErlERERMERIERER 483
                         490       500       510
                  ....*....|....*....|....*....|..
gi 63054755   729 EYCEKLSLQDIIRDKIPVDEMWRLFRQILEAL 760
Cdd:PTZ00266  484 LERERLERERLERDRLERDRLDRLERERVDRL 515
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
283-458 2.24e-05

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: 48.54  E-value: 2.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  283 GKREIQELEYELESLKVIRHDLLASI-YEYQLERetrgygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEG 361
Cdd:cd05593   55 AKDEVAHTLTESRVLKNTRHPFLTSLkYSFQTKD-------RLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSA 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  362 LAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRT-LRDMNASHPFNINsqsitnilPEGLYPPEVSESSFAaas 440
Cdd:cd05593  128 LDYLHSGKIVYRDLKLENLMLDKDGH---IKITDFGLCKEgITDAATMKTFCGT--------PEYLAPEVLEDNDYG--- 193
                        170
                 ....*....|....*...
gi 63054755  441 RKTDIWCFGLLVLQMLCG 458
Cdd:cd05593  194 RAVDWWGLGVVMYEMMCG 211
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
283-505 2.45e-05

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: 47.64  E-value: 2.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  283 GKREIqeLEYELESLKVIRHDLLASIYE-YQLEREtrgygwrLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEG 361
Cdd:cd14185   40 GKEDM--IESEILIIKSLSHPNIVKLFEvYETEKE-------IYLILEYVRGGDLFDAIIESVKFTEHDAALMIIDLCEA 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  362 LAELHRLGISHKSLHLDNVVLFHSGHR-TFAKLMDFGFTRtlrdmNASHPFNINSQSITNILPEGLyppevSESSFAAas 440
Cdd:cd14185  111 LVYIHSKHIVHRDLKPENLLVQHNPDKsTTLKLADFGLAK-----YVTGPIFTVCGTPTYVAPEIL-----SEKGYGL-- 178
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  441 rKTDIWCFGLLVLQMLCG-----AHVLNKFSSLKLIMTHVIPLLPGSY-------QDLVRRCLMRDSRKRPSAIDLL 505
Cdd:cd14185  179 -EVDMWAAGVILYILLCGfppfrSPERDQEELFQIIQLGHYEFLPPYWdniseaaKDLISRLLVVDPEKRYTAKQVL 254
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
311-508 2.85e-05

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: 47.38  E-value: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  311 YQLERETRGYGWRLYVLQEYSPKftlfsllqtvltLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtf 390
Cdd:cd14004   83 YYLVMEKHGSGMDLFDFIERKPN------------MDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGT--- 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  391 AKLMDFGFTRTLRdmnaSHPFNINSQSITNILPEGL----YppevsessfaaASRKTDIWCFGLLVLQMLCGAhvlNKFS 466
Cdd:cd14004  148 IKLIDFGSAAYIK----SGPFDTFVGTIDYAAPEVLrgnpY-----------GGKEQDIWALGVLLYTLVFKE---NPFY 209
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 63054755  467 SLKLIM---THVIPLLPGSYQDLVRRCLMRDSRKRPSAIDLLSSH 508
Cdd:cd14004  210 NIEEILeadLRIPYAVSEDLIDLISRMLNRDVGDRPTIEELLTDP 254
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
323-458 2.96e-05

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


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 48.07  E-value: 2.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  323 RLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTl 402
Cdd:cd05616   75 RLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGH---IKIADFGMCKE- 150
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  403 rdmnashpfNINSQSITNIL---PEGLYPPEVSESSFAaasRKTDIWCFGLLVLQMLCG 458
Cdd:cd05616  151 ---------NIWDGVTTKTFcgtPDYIAPEIIAYQPYG---KSVDWWAFGVLLYEMLAG 197
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
359-511 3.40e-05

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: 47.68  E-value: 3.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  359 LEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGF------TRTLRDMNASHPFNInsqsitniLPEGLYPPEVS 432
Cdd:cd06639  138 LLGLQHLHNNRIIHRDVKGNNILLTTEGG---VKLVDFGVsaqltsARLRRNTSVGTPFWM--------APEVIACEQQY 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  433 ESSFAAasrKTDIWCFGLLVLQMLCGAHVLNKFSSLKLIMThvIP-------LLPG----SYQDLVRRCLMRDSRKRPSA 501
Cdd:cd06639  207 DYSYDA---RCDVWSLGITAIELADGDPPLFDMHPVKALFK--IPrnppptlLNPEkwcrGFSHFISQCLIKDFEKRPSV 281
                        170
                 ....*....|
gi 63054755  502 IDLLSSHVIR 511
Cdd:cd06639  282 THLLEHPFIK 291
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
323-458 3.50e-05

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


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 47.68  E-value: 3.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  323 RLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGftrtl 402
Cdd:cd05615   85 RLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGH---IKIADFG----- 156
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  403 rdMNASHPFNINSQSITNILPEGLYPPEVSESSFAaasRKTDIWCFGLLVLQMLCG 458
Cdd:cd05615  157 --MCKEHMVEGVTTRTFCGTPDYIAPEIIAYQPYG---RSVDWWAYGVLLYEMLAG 207
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
288-506 4.40e-05

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: 47.26  E-value: 4.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  288 QELEYELESLKVIRHD---LLASIYEYQLEretrgygwrLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAE 364
Cdd:cd14196   53 EEIEREVSILRQVLHPniiTLHDVYENRTD---------VVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNY 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  365 LHRLGISHKSLHLDNVVLF-HSGHRTFAKLMDFGFTRTLRDmnashpfNINSQSITNIlPEGLYPPEVSESSFAAASrkt 443
Cdd:cd14196  124 LHTKKIAHFDLKPENIMLLdKNIPIPHIKLIDFGLAHEIED-------GVEFKNIFGT-PEFVAPEIVNYEPLGLEA--- 192
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  444 DIWCFGLLVLQMLCGAHVL---NKFSSLKLI-----------MTHVIPLLpgsyQDLVRRCLMRDSRKRPSAIDLLS 506
Cdd:cd14196  193 DMWSIGVITYILLSGASPFlgdTKQETLANItavsydfdeefFSHTSELA----KDFIRKLLVKETRKRLTIQEALR 265
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
284-458 4.89e-05

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 47.51  E-value: 4.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   284 KREI------QELEYELESLKVIRHDLLASIYE-YQLERetrgygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSN 356
Cdd:PTZ00263   53 KREIlkmkqvQHVAQEKSILMELSHPFIVNMMCsFQDEN-------RVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHA 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755   357 NILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDmnasHPFNINSQsitnilPEGLyPPEVSESSf 436
Cdd:PTZ00263  126 ELVLAFEYLHSKDIIYRDLKPENLLLDNKGH---VKVTDFGFAKKVPD----RTFTLCGT------PEYL-APEVIQSK- 190
                         170       180
                  ....*....|....*....|..
gi 63054755   437 aAASRKTDIWCFGLLVLQMLCG 458
Cdd:PTZ00263  191 -GHGKAVDWWTMGVLLYEFIAG 211
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
272-504 5.71e-05

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: 46.99  E-value: 5.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  272 RISTPYWSTEDGKREIqeleyelESLKVIRHDllaSIYEYQLERETRGyGWRLYVLQEYSPKFTLFSLLQ-TVLTLDVET 350
Cdd:cd05038   42 QPSGEEQHMSDFKREI-------EILRTLDHE---YIVKYKGVCESPG-RRSLRLIMEYLPSGSLRDYLQrHRDQIDLKR 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  351 VRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDMNASHPFNINSQSitnilPEGLYPPE 430
Cdd:cd05038  111 LLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDL---VKISDFGLAKVLPEDKEYYYVKEPGES-----PIFWYAPE 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  431 -VSESSFaaaSRKTDIWCFGLLVLQMLC-GAH---------VLNKFSSLKLIMTHVIPLL------------PGSYQDLV 487
Cdd:cd05038  183 cLRESRF---SSASDVWSFGVTLYELFTyGDPsqsppalflRMIGIAQGQMIVTRLLELLksgerlprppscPDEVYDLM 259
                        250
                 ....*....|....*..
gi 63054755  488 RRCLMRDSRKRPSAIDL 504
Cdd:cd05038  260 KECWEYEPQDRPSFSDL 276
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
347-511 6.86e-05

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: 46.95  E-value: 6.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  347 DVEtVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDMNA--SHPFNINSQSITnILPE 424
Cdd:cd06633  120 EVE-IAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQ---VKLADFGSASIASPANSfvGTPYWMAPEVIL-AMDE 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  425 GLYppevsessfaaaSRKTDIWCFGLLVLQMLCGAHVL---NKFSSLKLIMTHVIPLLPG-----SYQDLVRRCLMRDSR 496
Cdd:cd06633  195 GQY------------DGKVDIWSLGITCIELAERKPPLfnmNAMSALYHIAQNDSPTLQSnewtdSFRGFVDYCLQKIPQ 262
                        170
                 ....*....|....*
gi 63054755  497 KRPSAIDLLSSHVIR 511
Cdd:cd06633  263 ERPSSAELLRHDFVR 277
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
351-458 6.93e-05

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: 46.67  E-value: 6.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  351 VRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHRTFAKLMDFGFTRTLRDMNASHPFNINSQSITnilpeglypPE 430
Cdd:cd13989  104 VRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRVIYKLIDLGYAKELDQGSLCTSFVGTLQYLA---------PE 174
                         90       100
                 ....*....|....*....|....*...
gi 63054755  431 VSESSFAAASrkTDIWCFGLLVLQMLCG 458
Cdd:cd13989  175 LFESKKYTCT--VDYWSFGTLAFECITG 200
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
324-500 7.08e-05

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: 46.38  E-value: 7.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  324 LYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLfhSGHRTFAKLMDFGFTRTLR 403
Cdd:cd14101   83 LLVLERPQHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILV--DLRTGDIKLIDFGSGATLK 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  404 DmnashpfninsQSITNILPEGLY-PPEVSESSFAAASRKTdIWCFGLLVLQMLCGAHVLNKFSSLKLIMTHVIPLLPGS 482
Cdd:cd14101  161 D-----------SMYTDFDGTRVYsPPEWILYHQYHALPAT-VWSLGILLYDMVCGDIPFERDTDILKAKPSFNKRVSND 228
                        170
                 ....*....|....*...
gi 63054755  483 YQDLVRRCLMRDSRKRPS 500
Cdd:cd14101  229 CRSLIRSCLAYNPSDRPS 246
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
323-458 7.48e-05

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


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 46.62  E-value: 7.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  323 RLYVLQEYSPKFTLFSLLQTVLTLDvETVRAF-SNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRT 401
Cdd:cd05587   71 RLYFVMEYVNGGDLMYHIQQVGKFK-EPVAVFyAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGH---IKIADFGMCKE 146
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  402 lrdmnashpfNINSQSITN--------ILPE-GLYPPevsessfaaASRKTDIWCFGLLVLQMLCG 458
Cdd:cd05587  147 ----------GIFGGKTTRtfcgtpdyIAPEiIAYQP---------YGKSVDWWAYGVLLYEMLAG 193
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
347-456 9.00e-05

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: 46.40  E-value: 9.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  347 DVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHRTFAKLMDFGFTRTLRD--MNASHPFNINSQSITNILPE 424
Cdd:cd13977  132 DRQTNTSFMLQLSSALAFLHRNQIVHRDLKPDNILISHKRGEPILKVADFGLSKVCSGsgLNPEEPANVNKHFLSSACGS 211
                         90       100       110
                 ....*....|....*....|....*....|...
gi 63054755  425 GLY-PPEVSESSFAAasrKTDIWCFGLLVLQML 456
Cdd:cd13977  212 DFYmAPEVWEGHYTA---KADIFALGIIIWAMV 241
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
326-507 9.27e-05

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: 46.08  E-value: 9.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  326 VLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHRTfaKLMDFGFTRTLRDM 405
Cdd:cd14005   84 IMERPEPCQDLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRTGEV--KLIDFGCGALLKDS 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  406 NASHPfninsqsitnilpEG---LYPPE-VSESSFAAasRKTDIWCFGLLVLQMLCGAHvlnKFSSLKLIMT---HVIPL 478
Cdd:cd14005  162 VYTDF-------------DGtrvYSPPEwIRHGRYHG--RPATVWSLGILLYDMLCGDI---PFENDEQILRgnvLFRPR 223
                        170       180
                 ....*....|....*....|....*....
gi 63054755  479 LPGSYQDLVRRCLMRDSRKRPSAIDLLSS 507
Cdd:cd14005  224 LSKECCDLISRCLQFDPSKRPSLEQILSH 252
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
272-508 9.40e-05

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: 45.76  E-value: 9.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  272 RISTPYWSTEDGKREIQELE-YEleslKVIRHDLLASIYEYQLEREtrgygwRLYVLQEYSPKftlfSLLQTVL---TLD 347
Cdd:cd14050   33 RSRSRFRGEKDRKRKLEEVErHE----KLGEHPNCVRFIKAWEEKG------ILYIQTELCDT----SLQQYCEethSLP 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  348 VETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGhrtFAKLMDFGFTRTLRDMNASHpfninsqsitniLPEG-- 425
Cdd:cd14050   99 ESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDG---VCKLGDFGLVVELDKEDIHD------------AQEGdp 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  426 -LYPPEVSESSFAAASrktDIWCFGLLVLQMLCGAHVLNKFSSLKLIMTHVIPL-----LPGSYQDLVRRCLMRDSRKRP 499
Cdd:cd14050  164 rYMAPELLQGSFTKAA---DIFSLGITILELACNLELPSGGDGWHQLRQGYLPEeftagLSPELRSIIKLMMDPDPERRP 240

                 ....*....
gi 63054755  500 SAIDLLSSH 508
Cdd:cd14050  241 TAEDLLALP 249
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
324-458 9.91e-05

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: 46.46  E-value: 9.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  324 LYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRtlR 403
Cdd:cd05619   81 LFFVMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGH---IKIADFGMCK--E 155
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 63054755  404 DMNASHPFNINSQSITNILPEGLYPPEVSESsfaaasrkTDIWCFGLLVLQMLCG 458
Cdd:cd05619  156 NMLGDAKTSTFCGTPDYIAPEILLGQKYNTS--------VDWWSFGVLLYEMLIG 202
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
283-508 1.06e-04

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: 45.68  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  283 GKREIQELEYELESLKVIRHDLLASIYEYQLERETRgygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGL 362
Cdd:cd13983   40 PKAERQRFKQEIEILKSLKHPNIIKFYDSWESKSKK----EVIFITELMTSGTLKQYLKRFKRLKLKVIKSWCRQILEGL 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  363 AELHRLG--ISHKSLHLDNVvlFHSGHRTFAKLMDFGFTRTLRDMNAshpfninsQSI--TnilPEgLYPPEVSESSFaa 438
Cdd:cd13983  116 NYLHTRDppIIHRDLKCDNI--FINGNTGEVKIGDLGLATLLRQSFA--------KSVigT---PE-FMAPEMYEEHY-- 179
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  439 aSRKTDIWCFGLLVLQMLCGAHVLNKFSSLKLIMTHVIP-LLPGSYQ--------DLVRRCLmRDSRKRPSAIDLLSSH 508
Cdd:cd13983  180 -DEKVDIYAFGMCLLEMATGEYPYSECTNAAQIYKKVTSgIKPESLSkvkdpelkDFIEKCL-KPPDERPSARELLEHP 256
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
284-506 1.20e-04

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: 45.80  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  284 KREIQELEYELESLKVIRhdlLASIYEYQLEretrgygwrLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLA 363
Cdd:cd14106   55 LHEIAVLELCKDCPRVVN---LHEVYETRSE---------LILILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQ 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  364 ELHRLGISHKSLHLDNVVLFHSGHRTFAKLMDFGFTRTLRdmnashpfniNSQSITNILPEGLY-PPEVseSSFAAASRK 442
Cdd:cd14106  123 YLHERNIVHLDLKPQNILLTSEFPLGDIKLCDFGISRVIG----------EGEEIREILGTPDYvAPEI--LSYEPISLA 190
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  443 TDIWCFGLLVLQMLCGAH----------VLNkFSSLKL-----IMTHVIPllpgSYQDLVRRCLMRDSRKRPSAIDLLS 506
Cdd:cd14106  191 TDMWSIGVLTYVLLTGHSpfggddkqetFLN-ISQCNLdfpeeLFKDVSP----LAIDFIKRLLVKDPEKRLTAKECLE 264
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
324-506 1.30e-04

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: 45.88  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  324 LYVLQEYSPKFTLFSLLQTVLTLDVET----VRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFT 399
Cdd:cd06621   76 IGIAMEYCEGGSLDSIYKKVKKKGGRIgekvLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQ---VKLCDFGVS 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  400 RTLrdmnashpfnINSQSITNILPEGLYPPE-VSESSFaaaSRKTDIWCFGLLVLQM--LC------GAHVLNKFSSLKL 470
Cdd:cd06621  153 GEL----------VNSLAGTFTGTSYYMAPErIQGGPY---SITSDVWSLGLTLLEVaqNRfpfppeGEPPLGPIELLSY 219
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 63054755  471 IMTHVIPLLPG----------SYQDLVRRCLMRDSRKRPSAIDLLS 506
Cdd:cd06621  220 IVNMPNPELKDepengikwseSFKDFIEKCLEKDGTRRPGPWQMLA 265
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
279-504 1.37e-04

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: 45.78  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  279 STEDgkrEIQELEYELESLKVIRHDllaSIYEYQLERETRGYGwRLYVLQEYSPKFTLFSLLQTVLT-LDVETVRAFSNN 357
Cdd:cd14205   44 STEE---HLRDFEREIEILKSLQHD---NIVKYKGVCYSAGRR-NLRLIMEYLPYGSLRDYLQKHKErIDHIKLLQYTSQ 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  358 ILEGLAELHRLGISHKSLHLDNvVLFHSGHRTfaKLMDFGFTRTLRDMNASHPFNINSQSitnilPEGLYPPE-VSESSF 436
Cdd:cd14205  117 ICKGMEYLGTKRYIHRDLATRN-ILVENENRV--KIGDFGLTKVLPQDKEYYKVKEPGES-----PIFWYAPEsLTESKF 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  437 AAASrktDIWCFGLLVLQMLC--------GAHVLNKFSSLK---LIMTHVIPLL------------PGSYQDLVRRCLMR 493
Cdd:cd14205  189 SVAS---DVWSFGVVLYELFTyiekskspPAEFMRMIGNDKqgqMIVFHLIELLknngrlprpdgcPDEIYMIMTECWNN 265
                        250
                 ....*....|.
gi 63054755  494 DSRKRPSAIDL 504
Cdd:cd14205  266 NVNQRPSFRDL 276
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
324-397 1.61e-04

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: 45.74  E-value: 1.61e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63054755  324 LYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFG 397
Cdd:cd05573   76 LYLVMEYMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGH---IKLADFG 146
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
284-459 1.63e-04

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 45.35  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  284 KREiqELEYELESLKVIRHDLLASIYEyQLERETRgygwrlYVL-QEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGL 362
Cdd:cd14113   46 KRD--QVTHELGVLQSLQHPQLVGLLD-TFETPTS------YILvLEMADQGRLLDYVVRWGNLTEEKIRFYLREILEAL 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  363 AELHRLGISHKSLHLDNVVLFHSGHRTFAKLMDFGFTRTLRDMNASHPFNINSQSITnilPEGLYPPEVSESSfaaasrk 442
Cdd:cd14113  117 QYLHNCRIAHLDLKPENILVDQSLSKPTIKLADFGDAVQLNTTYYIHQLLGSPEFAA---PEIILGNPVSLTS------- 186
                        170
                 ....*....|....*..
gi 63054755  443 tDIWCFGLLVLQMLCGA 459
Cdd:cd14113  187 -DLWSIGVLTYVLLSGV 202
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
281-456 2.01e-04

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: 45.27  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  281 EDGKREIQELEYELESLKVIRHDLLASIYEYQLERETRGygwrLYVLQEYSPKFTLFSLLQ-TVLTLDVETVRAFSNNIL 359
Cdd:cd05081   43 HSGPDQQRDFQREIQILKALHSDFIVKYRGVSYGPGRRS----LRLVMEYLPSGCLRDFLQrHRARLDASRLLLYSSQIC 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  360 EGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDMNASHPFNINSQSitnilPEGLYPPE-VSESSFaa 438
Cdd:cd05081  119 KGMEYLGSRRCVHRDLAARNILVESEAH---VKIADFGLAKLLPLDKDYYVVREPGQS-----PIFWYAPEsLSDNIF-- 188
                        170
                 ....*....|....*...
gi 63054755  439 aSRKTDIWCFGLLVLQML 456
Cdd:cd05081  189 -SRQSDVWSFGVVLYELF 205
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
286-498 2.53e-04

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: 44.92  E-value: 2.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  286 EIQELEYELESLKVIRHDLLASIYeYQLERETRgygwrLYVLQEYSPKFTLFSLLQTVLT--LDVETVRAFSNNILEGLA 363
Cdd:cd05574   44 KVKRVLTEREILATLDHPFLPTLY-ASFQTSTH-----LCFVMDYCPGGELFRLLQKQPGkrLPEEVARFYAAEVLLALE 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  364 ELHRLGISHKSLHLDNVVLFHSGHRTfakLMDFG-------FTRTLRD--MNASHPFNINSQSITNILPEGLYP------ 428
Cdd:cd05574  118 YLHLLGFVYRDLKPENILLHESGHIM---LTDFDlskqssvTPPPVRKslRKGSRRSSVKSIEKETFVAEPSARsnsfvg 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  429 ------PEV---SESSFAaasrkTDIWCFGLLVLQMLCG-------------AHVLNKfsslKLIMTHVIPLLPgSYQDL 486
Cdd:cd05574  195 teeyiaPEVikgDGHGSA-----VDWWTLGILLYEMLYGttpfkgsnrdetfSNILKK----ELTFPESPPVSS-EAKDL 264
                        250
                 ....*....|..
gi 63054755  487 VRRCLMRDSRKR 498
Cdd:cd05574  265 IRKLLVKDPSKR 276
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
290-507 2.60e-04

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: 44.56  E-value: 2.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  290 LEYELESLKVIRHDLLASIYeyqlereTRGYGWRLYVLqEYSPKFTLFSLLQ---TVLTLDVETVRAFsnNILEGLAELH 366
Cdd:cd14068   34 LRQELVVLSHLHHPSLVALL-------AAGTAPRMLVM-ELAPKGSLDALLQqdnASLTRTLQHRIAL--HVADGLRYLH 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  367 RLGISHKSLHLDNVVLF--HSGHRTFAKLMDFGFTRTLRDMnashpfNINSQSITnilpEGLYPPEVSESSfAAASRKTD 444
Cdd:cd14068  104 SAMIIYRDLKPHNVLLFtlYPNCAIIAKIADYGIAQYCCRM------GIKTSEGT----PGFRAPEVARGN-VIYNQQAD 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  445 IWCFGLLVLQML-CGAHVL------NKFSSLKLIMTHVIPL-------LPGsYQDLVRRCLMRDSRKRPSAI---DLLSS 507
Cdd:cd14068  173 VYSFGLLLYDILtCGERIVeglkfpNEFDELAIQGKLPDPVkeygcapWPG-VEALIKDCLKENPQCRPTSAqvfDILNS 251
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
323-458 2.84e-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: 44.72  E-value: 2.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  323 RLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRT- 401
Cdd:cd05588   70 RLFFVIEFVNGGDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGH---IKLTDYGMCKEg 146
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  402 LRDMNASHPFninSQSITNILPEGLYPPEVSESsfaaasrkTDIWCFGLLVLQMLCG 458
Cdd:cd05588  147 LRPGDTTSTF---CGTPNYIAPEILRGEDYGFS--------VDWWALGVLMFEMLAG 192
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
284-506 3.36e-04

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: 44.35  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  284 KREIQELEYELESLKVIRHDLLASiYEYQLERETrGYgwrLYVLQEYSPKFTLFSLL--QTVLTLDVETVRAFSNNILEG 361
Cdd:cd08223   40 KRERKAAEQEAKLLSKLKHPNIVS-YKESFEGED-GF---LYIVMGFCEGGDLYTRLkeQKGVLLEERQVVEWFVQIAMA 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  362 LAELHRLGISHKSLHLDNVVLFHSghrTFAKLMDFGFTRTLRdmnashpfNINSQSITNI-LPEGLYPPEVSESSFaaaS 440
Cdd:cd08223  115 LQYMHERNILHRDLKTQNIFLTKS---NIIKVGDLGIARVLE--------SSSDMATTLIgTPYYMSPELFSNKPY---N 180
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054755  441 RKTDIWCFGLLVLQMLCGAHVLN--KFSSLKL-IMTHVIPLLPGSYQ----DLVRRCLMRDSRKRPSAIDLLS 506
Cdd:cd08223  181 HKSDVWALGCCVYEMATLKHAFNakDMNSLVYkILEGKLPPMPKQYSpelgELIKAMLHQDPEKRPSVKRILR 253
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
326-500 3.37e-04

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: 44.46  E-value: 3.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  326 VLQEYSPKFTLFS-LLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLfhsGHRTFAKLMDFGFtRTLRD 404
Cdd:cd14045   79 IITEYCPKGSLNDvLLNEDIPLNWGFRFSFATDIARGMAYLHQHKIYHGRLKSSNCVI---DDRWVCKIADYGL-TTYRK 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  405 MNASHPFNINSQSITNIlpegLYPPEVSESSFAAASRKTDIWCFGLLVLQMLCGAHVL-NKFSSLKLIMTHVIPLL---- 479
Cdd:cd14045  155 EDGSENASGYQQRLMQV----YLPPENHSNTDTEPTQATDVYSYAIILLEIATRNDPVpEDDYSLDEAWCPPLPELisgk 230
                        170       180
                 ....*....|....*....|....*...
gi 63054755  480 -------PGSYQDLVRRCLMRDSRKRPS 500
Cdd:cd14045  231 tenscpcPADYVELIRRCRKNNPAQRPT 258
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
284-506 3.45e-04

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: 44.33  E-value: 3.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  284 KREIQELEYELESLKVIRHDLLASIYEyqlERETRGYGWRLYVL-QEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGL 362
Cdd:cd14031   50 KAEQQRFKEEAEMLKGLQHPNIVRFYD---SWESVLKGKKCIVLvTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  363 AELHRLG--ISHKSLHLDNVvlFHSGHRTFAKLMDFGFTRTLRDMNAshpfninsQSITNIlPEgLYPPEVSESSFaaaS 440
Cdd:cd14031  127 QFLHTRTppIIHRDLKCDNI--FITGPTGSVKIGDLGLATLMRTSFA--------KSVIGT-PE-FMAPEMYEEHY---D 191
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63054755  441 RKTDIWCFGLLVLQMLCGAHVLNKFSSLKLIMTHVIP-LLPGSY--------QDLVRRCLMRDSRKRPSAIDLLS 506
Cdd:cd14031  192 ESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTSgIKPASFnkvtdpevKEIIEGCIRQNKSERLSIKDLLN 266
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
365-511 4.16e-04

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: 44.29  E-value: 4.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  365 LHRLGISHKSLHLD----NVVLFHSGHrtfAKLMDFGFTRTLRDMNAshpfniNSQSI---TNILPEGLYPPEVSESSFA 437
Cdd:cd06618  127 LHYLKEKHGVIHRDvkpsNILLDESGN---VKLCDFGISGRLVDSKA------KTRSAgcaAYMAPERIDPPDNPKYDIR 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  438 AasrktDIWCFGLLVLQMLCG----AHVLNKFSSLKLIMTHVIPLLPGS------YQDLVRRCLMRDSRKRPSAIDLLSS 507
Cdd:cd06618  198 A-----DVWSLGISLVELATGqfpyRNCKTEFEVLTKILNEEPPSLPPNegfspdFCSFVDLCLTKDHRYRPKYRELLQH 272

                 ....
gi 63054755  508 HVIR 511
Cdd:cd06618  273 PFIR 276
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
318-500 4.31e-04

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: 43.79  E-value: 4.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  318 RGYGWrLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVL-FHSGHrtfAKLMDF 396
Cdd:cd14102   75 RPDGF-LIVMERPEPVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVdLRTGE---LKLIDF 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  397 GFTRTLRDMnashpfninsqSITNILPEGLYPPEVSESSFAAASRKTDIWCFGLLVLQMLCGAHVLNKFSSLKLIMTHVI 476
Cdd:cd14102  151 GSGALLKDT-----------VYTDFDGTRVYSPPEWIRYHRYHGRSATVWSLGVLLYDMVCGDIPFEQDEEILRGRLYFR 219
                        170       180
                 ....*....|....*....|....
gi 63054755  477 PLLPGSYQDLVRRCLMRDSRKRPS 500
Cdd:cd14102  220 RRVSPECQQLIKWCLSLRPSDRPT 243
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
290-458 4.37e-04

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: 43.69  E-value: 4.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  290 LEYELESLKVIRHDLLASIYEYqlereTRGYGWRLYVLQEYSPKfTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLG 369
Cdd:cd14164   47 LPRELSILRRVNHPNIVQMFEC-----IEVANGRLYIVMEAAAT-DLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMN 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  370 ISHKSLHLDNVVLFHSGHRtfAKLMDFGFTRTLRDM-NASHPFnINSQSITnilpeglyPPEVSeSSFAAASRKTDIWCF 448
Cdd:cd14164  121 IVHRDLKCENILLSADDRK--IKIADFGFARFVEDYpELSTTF-CGSRAYT--------PPEVI-LGTPYDPKKYDVWSL 188
                        170
                 ....*....|
gi 63054755  449 GLLVLQMLCG 458
Cdd:cd14164  189 GVVLYVMVTG 198
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
351-473 4.60e-04

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: 44.18  E-value: 4.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  351 VRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLrdmnashpfNINSQSITNILPEGLY-PP 429
Cdd:cd07870  100 VRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGE---LKLADFGLARAK---------SIPSQTYSSEVVTLWYrPP 167
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 63054755  430 EVSESSfAAASRKTDIWCFGLLVLQMLCG----AHVLNKFSSLKLIMT 473
Cdd:cd07870  168 DVLLGA-TDYSSALDIWGAGCIFIEMLQGqpafPGVSDVFEQLEKIWT 214
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
282-401 4.68e-04

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: 43.68  E-value: 4.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  282 DGKREIQEL-EYELESLKVIRHDLLASIYEYQLEREtrgygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILE 360
Cdd:cd14087   35 ETKCRGREVcESELNVLRRVRHTNIIQLIEVFETKE------RVYMVMELATGGELFDRIIAKGSFTERDATRVLQMVLD 108
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 63054755  361 GLAELHRLGISHKSLHLDNVVLFHSGHRTFAKLMDFGFTRT 401
Cdd:cd14087  109 GVKYLHGLGITHRDLKPENLLYYHPGPDSKIMITDFGLAST 149
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
289-458 4.81e-04

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: 44.01  E-value: 4.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  289 ELEYELESLKVIRHDLLasIYEYQLERETRGYGwrlyVLQEYSPKFTLFSLLQTVLTL-DVETVRAFSNnILEGLAELHR 367
Cdd:cd14076   52 KIMREINILKGLTHPNI--VRLLDVLKTKKYIG----IVLEFVSGGELFDYILARRRLkDSVACRLFAQ-LISGVAYLHK 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  368 LGISHKSLHLDNVVLfhSGHRTFAkLMDFGFTRTLrDMNASHPFNINSQSITNILPEGLyppeVSESSFAAasRKTDIWC 447
Cdd:cd14076  125 KGVVHRDLKLENLLL--DKNRNLV-ITDFGFANTF-DHFNGDLMSTSCGSPCYAAPELV----VSDSMYAG--RKADIWS 194
                        170
                 ....*....|.
gi 63054755  448 FGLLVLQMLCG 458
Cdd:cd14076  195 CGVILYAMLAG 205
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
286-500 5.33e-04

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 43.67  E-value: 5.33e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755     286 EIQELEYELESLKVIRHDLLASIYEYQLEREtrgygwRLYVLQEYSPKFTLFSLLQ-TVLTLDVETVRAFSNNILEGLAE 364
Cdd:smart00219   44 QIEEFLREARIMRKLDHPNVVKLLGVCTEEE------PLYIVMEYMEGGDLLSYLRkNRPKLSLSDLLSFALQIARGMEY 117
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755     365 LHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDMNashpfnINSQSITNiLPEGLYPPEV-SESSFaaaSRKT 443
Cdd:smart00219  118 LESKNFIHRDLAARNCLVGENLV---VKISDFGLSRDLYDDD------YYRKRGGK-LPIRWMAPESlKEGKF---TSKS 184
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63054755     444 DIWCFGLLVLQMLCGAHVLNKFSSLKLIMTHVI--------PLLPGSYQDLVRRCLMRDSRKRPS 500
Cdd:smart00219  185 DVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLKngyrlpqpPNCPPELYDLMLQCWAEDPEDRPT 249
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
323-458 5.72e-04

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


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 44.02  E-value: 5.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  323 RLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTl 402
Cdd:cd05591   70 RLFFVMEYVNGGDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGH---CKLADFGMCKE- 145
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  403 rdmnashpfNINSQSITNIL---PEGLYPPEVSESSFAAAsrkTDIWCFGLLVLQMLCG 458
Cdd:cd05591  146 ---------GILNGKTTTTFcgtPDYIAPEILQELEYGPS---VDWWALGVLMYEMMAG 192
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
324-458 5.82e-04

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: 44.23  E-value: 5.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  324 LYVLQEYSPKFTLFSLLQTvltLDV--ETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGftrT 401
Cdd:cd05622  148 LYMVMEYMPGGDLVNLMSN---YDVpeKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGH---LKLADFG---T 218
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  402 LRDMNASHPFNINSQSITnilPEGLyPPEV--SESSFAAASRKTDIWCFGLLVLQMLCG 458
Cdd:cd05622  219 CMKMNKEGMVRCDTAVGT---PDYI-SPEVlkSQGGDGYYGRECDWWSVGVFLYEMLVG 273
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
284-506 6.40e-04

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: 43.25  E-value: 6.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755    284 KREIQELEYELESLKVIRHDLLASIYEYQLERETrgygwrLYVLQEYSPKFTLFSLLQTVL-TLDVETVRAFSNNILEGL 362
Cdd:pfam07714   42 EEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEP------LYIVTEYMPGGDLLDFLRKHKrKLTLKDLLSMALQIAKGM 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755    363 AELHRLGISHKSLHLDNVVLfhsGHRTFAKLMDFGFTRTLRDmnashpfNINSQSITN-ILPEGLYPPEV-SESSFaaaS 440
Cdd:pfam07714  116 EYLESKNFVHRDLAARNCLV---SENLVVKISDFGLSRDIYD-------DDYYRKRGGgKLPIKWMAPESlKDGKF---T 182
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63054755    441 RKTDIWCFGLLVLQMLCGAHV----LNKFSSLKLIMT---HVIPLL-PGSYQDLVRRCLMRDSRKRPSAIDLLS 506
Cdd:pfam07714  183 SKSDVWSFGVLLWEIFTLGEQpypgMSNEEVLEFLEDgyrLPQPENcPDELYDLMKQCWAYDPEDRPTFSELVE 256
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
324-458 6.91e-04

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: 43.87  E-value: 6.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  324 LYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGF----- 398
Cdd:cd05628   76 LYLIMEFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGH---VKLSDFGLctglk 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  399 ----TRTLRDMNASHPFNINSQSI-------------------TNILPEGLYPPEVSESSFaaaSRKTDIWCFGLLVLQM 455
Cdd:cd05628  153 kahrTEFYRNLNHSLPSDFTFQNMnskrkaetwkrnrrqlafsTVGTPDYIAPEVFMQTGY---NKLCDWWSLGVIMYEM 229

                 ...
gi 63054755  456 LCG 458
Cdd:cd05628  230 LIG 232
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
357-507 7.33e-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: 43.38  E-value: 7.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  357 NILEGLAELHRLGISHKSLHLDNvVLFHSGHRTFaKLMDFGFTrtlrdmnashpFNINSQSITNILPEGLYPPEVS-ESS 435
Cdd:cd14020  118 DVLEALAFLHHEGYVHADLKPRN-ILWSAEDECF-KLIDFGLS-----------FKEGNQDVKYIQTDGYRAPEAElQNC 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  436 FAAA--------SRKTDIWCFGLLVLQMLCGAHVLNKFSSLK------LIMTHVI-------PLLPGSY-QDLVRRCLMR 493
Cdd:cd14020  185 LAQAglqsetecTSAVDLWSLGIVLLEMFSGMKLKHTVRSQEwkdnssAIIDHIFasnavvnPAIPAYHlRDLIKSMLHN 264
                        170
                 ....*....|....
gi 63054755  494 DSRKRPSAIDLLSS 507
Cdd:cd14020  265 DPGKRATAEAALCS 278
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
356-458 7.44e-04

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: 43.56  E-value: 7.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  356 NNILEGLAELHRLGISHKSLHLDNVVLFHSGHRTFAKLMDFGFtrtlrdmnASHPFnINSQSITNI-LPEGLYP------ 428
Cdd:cd14090  107 RDIASALDFLHDKGIAHRDLKPENILCESMDKVSPVKICDFDL--------GSGIK-LSSTSMTPVtTPELLTPvgsaey 177
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 63054755  429 --PEVSESSFAAAS---RKTDIWCFGLLVLQMLCG 458
Cdd:cd14090  178 maPEVVDAFVGEALsydKRCDLWSLGVILYIMLCG 212
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
326-506 8.57e-04

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: 43.03  E-value: 8.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  326 VLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVL-FHSGHrtfAKLMDFGFTRTLRD 404
Cdd:cd14100   83 VLERPEPVQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIdLNTGE---LKLIDFGSGALLKD 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  405 MnashpfninsqSITNILPEGLYPPEVSESSFAAASRKTDIWCFGLLVLQMLCGAHVLNKFSSLKLIMTHVIPLLPGSYQ 484
Cdd:cd14100  160 T-----------VYTDFDGTRVYSPPEWIRFHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIRGQVFFRQRVSSECQ 228
                        170       180
                 ....*....|....*....|..
gi 63054755  485 DLVRRCLMRDSRKRPSAIDLLS 506
Cdd:cd14100  229 HLIKWCLALRPSDRPSFEDIQN 250
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
323-458 8.93e-04

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: 43.47  E-value: 8.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  323 RLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRT- 401
Cdd:cd05617   90 RLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGH---IKLTDYGMCKEg 166
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  402 LRDMNASHPFninSQSITNILPEGLYPPEVSESsfaaasrkTDIWCFGLLVLQMLCG 458
Cdd:cd05617  167 LGPGDTTSTF---CGTPNYIAPEILRGEEYGFS--------VDWWALGVLMFEMMAG 212
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
293-498 1.06e-03

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: 42.76  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  293 ELESLKVIRHDLLASIYEYQlerETRGYgwrLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISH 372
Cdd:cd14071   49 EVQIMKMLNHPHIIKLYQVM---ETKDM---LYLVTEYASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVH 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  373 KSLHLDNVVLFHSGHrtfAKLMDFGF------TRTLRDMNASHPFNinsqsitnilpeglyPPEVSESSfAAASRKTDIW 446
Cdd:cd14071  123 RDLKAENLLLDANMN---IKIADFGFsnffkpGELLKTWCGSPPYA---------------APEVFEGK-EYEGPQLDIW 183
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  447 CFGLLVLQMLCGAHVLNKfSSLKLIMTHV------IP-LLPGSYQDLVRRCLMRDSRKR 498
Cdd:cd14071  184 SLGVVLYVLVCGALPFDG-STLQTLRDRVlsgrfrIPfFMSTDCEHLIRRMLVLDPSKR 241
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
319-501 1.08e-03

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


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 42.87  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  319 GYGWRLYVLQEYSPkFTLFSLLQTVlTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVL-FHSGHRTFAKLMDFG 397
Cdd:cd14018  110 GHNRTLFLVMKNYP-CTLRQYLWVN-TPSYRLARVMILQLLEGVDHLVRHGIAHRDLKSDNILLeLDFDGCPWLVIADFG 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  398 FTRTLRDMNASHPFniNSQSITNILPEGLYPPEVSESS---FAAAS-RKTDIWCFGLLVLQMLCGAhvlNKFSSLKLIMT 473
Cdd:cd14018  188 CCLADDSIGLQLPF--SSWYVDRGGNACLMAPEVSTAVpgpGVVINySKADAWAVGAIAYEIFGLS---NPFYGLGDTML 262
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 63054755  474 HV-------IPLLPGS----YQDLVRRCLMRDSRKRPSA 501
Cdd:cd14018  263 ESrsyqesqLPALPSAvppdVRQVVKDLLQRDPNKRVSA 301
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
323-506 1.16e-03

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: 42.60  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  323 RLYVLqEYSPKFTLFSLLQ----TVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLF--HSGHRTFAKLMDF 396
Cdd:cd14000   83 LMLVL-ELAPLGSLDHLLQqdsrSFASLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLVWtlYPNSAIIIKIADY 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  397 GFTRTlrdmnaSHPFNINSQSITnilpEGLYPPEVSESSfAAASRKTDIWCFGLLVLQMLCGAHVL---NKFSSLKLIMT 473
Cdd:cd14000  162 GISRQ------CCRMGAKGSEGT----PGFRAPEIARGN-VIYNEKVDVFSFGMLLYEILSGGAPMvghLKFPNEFDIHG 230
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 63054755  474 HVIPLL-------PGSYQDLVRRCLMRDSRKRPSAIDLLS 506
Cdd:cd14000  231 GLRPPLkqyecapWPEVEVLMKKCWKENPQQRPTAVTVVS 270
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
362-506 1.22e-03

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: 42.49  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  362 LAELHR-LGISHKSLHLDNVVLfhsGHRTFAKLMDFGFTRTLRDmnashpfniNSQSITNILPEGLYP-PEVSESSfaAA 439
Cdd:cd08528  126 LRYLHKeKQIVHRDLKPNNIML---GEDDKVTITDFGLAKQKGP---------ESSKMTSVVGTILYScPEIVQNE--PY 191
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63054755  440 SRKTDIWCFGLLVLQMLCGAHVLNKFSSLKLIMTHV----IPLLPGSYQD----LVRRCLMRDSRKRPSAIDLLS 506
Cdd:cd08528  192 GEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVeaeyEPLPEGMYSDditfVIRSCLTPDPEARPDIVEVSS 266
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
324-507 1.34e-03

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: 42.44  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  324 LYVLQEYSPKFTLFSLLQTVL-TLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLfhsGHRTFAKLMDFGFTR-T 401
Cdd:cd05059   74 IFIVTEYMANGCLLNYLRERRgKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLV---GEQNVVKVSDFGLARyV 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  402 LRDMNAShpfninsqSITNILPEGLYPPEVSesSFAAASRKTDIWCFGLLVLQML-CGAHVLNKFSSLKLI----MTHVI 476
Cdd:cd05059  151 LDDEYTS--------SVGTKFPVKWSPPEVF--MYSKFSSKSDVWSFGVLMWEVFsEGKMPYERFSNSEVVehisQGYRL 220
                        170       180       190
                 ....*....|....*....|....*....|....
gi 63054755  477 P---LLPGSYQDLVRRCLMRDSRKRPSAIDLLSS 507
Cdd:cd05059  221 YrphLAPTEVYTIMYSCWHEKPEERPTFKILLSQ 254
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
323-498 1.44e-03

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: 42.56  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  323 RLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRtl 402
Cdd:cd05585   68 KLYLVLAFINGGELFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGH---IALCDFGLCK-- 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  403 rdmnashpFNINSQSITNIL---PEGLYPPEVSESSFaaaSRKTDIWCFGLLVLQMLCGA---HVLNKFSSLKLIMTHvi 476
Cdd:cd05585  143 --------LNMKDDDKTNTFcgtPEYLAPELLLGHGY---TKAVDWWTLGVLLYEMLTGLppfYDENTNEMYRKILQE-- 209
                        170       180
                 ....*....|....*....|....*..
gi 63054755  477 PLL-----PGSYQDLVRRCLMRDSRKR 498
Cdd:cd05585  210 PLRfpdgfDRDAKDLLIGLLNRDPTKR 236
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
360-507 1.86e-03

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 41.97  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  360 EGLAELHRLGISHKSLHLDNVVLFHSghrTFAKLMDFGFTRTLRDMNASHPFNINSQSITNILPEGLYPPEVSESSFaaa 439
Cdd:cd14151  115 QGMDYLHAKSIIHRDLKSNNIFLHED---LTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSF--- 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  440 srKTDIWCFGLLVLQMLCGA----HVLNKFSSLKLI--------MTHVIPLLPGSYQDLVRRCLMRDSRKRPSAIDLLSS 507
Cdd:cd14151  189 --QSDVYAFGIVLYELMTGQlpysNINNRDQIIFMVgrgylspdLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILAS 266
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
322-458 1.97e-03

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: 42.05  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  322 WRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRT 401
Cdd:cd14077   86 NHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGN---IKIIDFGLSNL 162
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054755  402 LRDMNASHPFninSQSITNILPEGLYP-----PEVsessfaaasrktDIWCFGLLVLQMLCG 458
Cdd:cd14077  163 YDPRRLLRTF---CGSLYFAAPELLQAqpytgPEV------------DVWSFGVVLYVLVCG 209
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
281-505 2.03e-03

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: 41.84  E-value: 2.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  281 EDGKREIQELEYELESLKVIRHDllaSIYEYQ-LERETRGYGWRLyvLQEYSPKFTLFSLL-QTVLTLDVETVRAFSNNI 358
Cdd:cd05079   44 ESGGNHIADLKKEIEILRNLYHE---NIVKYKgICTEDGGNGIKL--IMEFLPSGSLKEYLpRNKNKINLKQQLKYAVQI 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  359 LEGLAELHRLGISHKSLHLDNVvLFHSGHRTfaKLMDFGFTRTLRDMNASHPFNINSQSitnilPEGLYPPE-VSESSFA 437
Cdd:cd05079  119 CKGMDYLGSRQYVHRDLAARNV-LVESEHQV--KIGDFGLTKAIETDKEYYTVKDDLDS-----PVFWYAPEcLIQSKFY 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  438 AASrktDIWCFGLLVLQML--CGAHVLNKFSSLKLI--------MTHVIPLL------------PGSYQDLVRRCLMRDS 495
Cdd:cd05079  191 IAS---DVWSFGVTLYELLtyCDSESSPMTLFLKMIgpthgqmtVTRLVRVLeegkrlprppncPEEVYQLMRKCWEFQP 267
                        250
                 ....*....|
gi 63054755  496 RKRPSAIDLL 505
Cdd:cd05079  268 SKRTTFQNLI 277
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
309-508 2.08e-03

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: 42.35  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  309 YEYQLEREtrgygwrLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHr 388
Cdd:cd05627   69 YSFQDKRN-------LYLIMEFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGH- 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  389 tfAKLMDFGF---------TRTLRDMNASHPFNINSQSI-------------------TNILPEGLYPPEVSESSFaaaS 440
Cdd:cd05627  141 --VKLSDFGLctglkkahrTEFYRNLTHNPPSDFSFQNMnskrkaetwkknrrqlaysTVGTPDYIAPEVFMQTGY---N 215
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  441 RKTDIWCFGLLVLQMLCG---------AHVLNKFSSLK--LIMTHVIPLLPGSYQDLVRRCLMRDSRKRPSAIDLLSSH 508
Cdd:cd05627  216 KLCDWWSLGVIMYEMLIGyppfcsetpQETYRKVMNWKetLVFPPEVPISEKAKDLILRFCTDAENRIGSNGVEEIKSH 294
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
358-505 2.20e-03

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: 41.61  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  358 ILEGLAELHRLG---ISHKSLHLDNVVLF-----HSGHRTFAKLMDFGFTRTLrdmnashpfninsQSITNILPEGLY-- 427
Cdd:cd14061  101 IARGMNYLHNEApvpIIHRDLKSSNILILeaienEDLENKTLKITDFGLAREW-------------HKTTRMSAAGTYaw 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  428 -PPEVSESS-FAAASrktDIWCFGLLVLQMLCGAHVLNKFSSLKLI-------MTHVIP-LLPGSYQDLVRRCLMRDSRK 497
Cdd:cd14061  168 mAPEVIKSStFSKAS---DVWSYGVLLWELLTGEVPYKGIDGLAVAygvavnkLTLPIPsTCPEPFAQLMKDCWQPDPHD 244

                 ....*...
gi 63054755  498 RPSAIDLL 505
Cdd:cd14061  245 RPSFADIL 252
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
323-505 2.32e-03

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: 41.74  E-value: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  323 RLYVLQEYSPKFTLFSLLQTV-LTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHRTFAKLMDFGFTRT 401
Cdd:cd14156   62 KLHPILEYVSGGCLEELLAREeLPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGREAVVTDFGLARE 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  402 LRDMNASHPfninSQSITNILPEGLYPPEVSESSfaAASRKTDIWCFGLLVLQML----CGAHVLNKFSSLKLIMT---H 474
Cdd:cd14156  142 VGEMPANDP----ERKLSLVGSAFWMAPEMLRGE--PYDRKVDVFSFGIVLCEILaripADPEVLPRTGDFGLDVQafkE 215
                        170       180       190
                 ....*....|....*....|....*....|.
gi 63054755  475 VIPLLPGSYQDLVRRCLMRDSRKRPSAIDLL 505
Cdd:cd14156  216 MVPGCPEPFLDLAASCCRMDAFKRPSFAELL 246
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
288-455 2.57e-03

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: 41.47  E-value: 2.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  288 QELEYELESLKVIRHDLLASIYEYQLERETrgygwrLYVLQEYSPKFTLFSLLQTVL-TLDVETVRAFSNNILEGLAELH 366
Cdd:cd05112   44 EDFIEEAEVMMKLSHPKLVQLYGVCLEQAP------ICLVFEFMEHGCLSDYLRTQRgLFSAETLLGMCLDVCEGMAYLE 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  367 RLGISHKSLHLDNVVLfhsGHRTFAKLMDFGFTRTLRDmnashpfNINSQSITNILPEGLYPPEVSesSFAAASRKTDIW 446
Cdd:cd05112  118 EASVIHRDLAARNCLV---GENQVVKVSDFGMTRFVLD-------DQYTSSTGTKFPVKWSSPEVF--SFSRYSSKSDVW 185

                 ....*....
gi 63054755  447 CFGLLVLQM 455
Cdd:cd05112  186 SFGVLMWEV 194
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
297-458 2.64e-03

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: 41.87  E-value: 2.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  297 LKVIRHDLLASI-YEYQLERetrgygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSL 375
Cdd:cd05604   51 LKNVKHPFLVGLhYSFQTTD-------KLYFVLDFVNGGELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDL 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  376 HLDNVVLFHSGHRTfakLMDFGFTRTlrdmnashpfNINSQSITNIL---PEGLYPPEVSESSFaaaSRKTDIWCFGLLV 452
Cdd:cd05604  124 KPENILLDSQGHIV---LTDFGLCKE----------GISNSDTTTTFcgtPEYLAPEVIRKQPY---DNTVDWWCLGSVL 187

                 ....*.
gi 63054755  453 LQMLCG 458
Cdd:cd05604  188 YEMLYG 193
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
324-397 2.66e-03

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


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 39.73  E-value: 2.66e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63054755  324 LYVLQEYSPKFTLFSLLQTVlTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLfhsGHRTFAKLMDFG 397
Cdd:cd13968   67 NILLMELVKGGTLIAYTQEE-ELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILL---SEDGNVKLIDFG 136
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
293-501 2.78e-03

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: 41.61  E-value: 2.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  293 ELESLKVIRHDLLASIYEYQLEREtrgygwRLYVLQEYSPKFTLFSLL-QTVLTLDVETVRAFSNNILEGLAELHR-LGI 370
Cdd:cd13992   46 ELNQLKELVHDNLNKFIGICINPP------NIAVVTEYCTRGSLQDVLlNREIKMDWMFKSSFIKDIVKGMNYLHSsSIG 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  371 SHKSLHLDNVVLfhsGHRTFAKLMDFGFTRTLRDmnashpfNINSQSITNILPEGLY--PPEVSESSFAAASR--KTDIW 446
Cdd:cd13992  120 YHGRLKSSNCLV---DSRWVVKLTDFGLRNLLEE-------QTNHQLDEDAQHKKLLwtAPELLRGSLLEVRGtqKGDVY 189
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  447 CFGLLVLQMLC----GAHVLNKFSSLKLIMTHVIPLLPG----------SYQDLVRRCLMRDSRKRPSA 501
Cdd:cd13992  190 SFAIILYEILFrsdpFALEREVAIVEKVISGGNKPFRPElavlldefppRLVLLVKQCWAENPEKRPSF 258
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
279-456 2.96e-03

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: 41.41  E-value: 2.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  279 STEDGKREIQELEYELESLKVIRHDLLASIYEYqLERETrgygwrLYVLQEYSPKFTLFSLLQTV--LTLDVETVRAFSN 356
Cdd:cd05067   38 SLKQGSMSPDAFLAEANLMKQLQHQRLVRLYAV-VTQEP------IYIITEYMENGSLVDFLKTPsgIKLTINKLLDMAA 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  357 NILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTLRDMN------ASHPfninsqsITNILPEGLyppe 430
Cdd:cd05067  111 QIAEGMAFIEERNYIHRDLRAANILVSDTLS---CKIADFGLARLIEDNEytaregAKFP-------IKWTAPEAI---- 176
                        170       180
                 ....*....|....*....|....*.
gi 63054755  431 vsesSFAAASRKTDIWCFGLLVLQML 456
Cdd:cd05067  177 ----NYGTFTIKSDVWSFGILLTEIV 198
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
354-458 2.97e-03

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: 41.49  E-value: 2.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  354 FSNNILEGLAELHRLGISHKSLHLDNVVLF-HSGHRTfaKLMDFGFTRTLRdmnASHPFNINSQSitnilPEGLyPPEVS 432
Cdd:cd14192  107 FTRQICEGVHYLHQHYILHLDLKPENILCVnSTGNQI--KIIDFGLARRYK---PREKLKVNFGT-----PEFL-APEVV 175
                         90       100
                 ....*....|....*....|....*.
gi 63054755  433 ESSFaaASRKTDIWCFGLLVLQMLCG 458
Cdd:cd14192  176 NYDF--VSFPTDMWSVGVITYMLLSG 199
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
324-508 3.05e-03

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: 41.07  E-value: 3.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  324 LYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNvvlFHSGHRTFAKLMDFGFTRTLr 403
Cdd:cd14189   76 IYIFLELCSRKSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGN---FFINENMELKVGDFGLAARL- 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  404 dmnasHPFNINSQSITNIlPEGLYPPEVSESSFAAASrktDIWCFGLLVLQMLCGAhvlNKFSSLKLIMTH-----VIPL 478
Cdd:cd14189  152 -----EPPEQRKKTICGT-PNYLAPEVLLRQGHGPES---DVWSLGCVMYTLLCGN---PPFETLDLKETYrcikqVKYT 219
                        170       180       190
                 ....*....|....*....|....*....|....
gi 63054755  479 LPGSY----QDLVRRCLMRDSRKRPSaIDLLSSH 508
Cdd:cd14189  220 LPASLslpaRHLLAGILKRNPGDRLT-LDQILEH 252
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
297-458 3.97e-03

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: 41.15  E-value: 3.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  297 LKVIRHDLLASI-YEYQlereTRGygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSL 375
Cdd:cd05575   50 LKNVKHPFLVGLhYSFQ----TKD---KLYFVLDYVNGGELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDL 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  376 HLDNVVLFHSGHrtfAKLMDFGFTRTlrdmnashpfNINSQSITNIL---PEGLyPPEVSESSfaAASRKTDIWCFGLLV 452
Cdd:cd05575  123 KPENILLDSQGH---VVLTDFGLCKE----------GIEPSDTTSTFcgtPEYL-APEVLRKQ--PYDRTVDWWCLGAVL 186

                 ....*.
gi 63054755  453 LQMLCG 458
Cdd:cd05575  187 YEMLYG 192
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
285-462 4.10e-03

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: 41.01  E-value: 4.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  285 REIQeleyeleSLKVIRHDLLASIYEYQLERETRGYGWRLYVLQEYSPkFTLFSLL-QTVLTLDVETVRAFSNNILEGLA 363
Cdd:cd07840   47 REIK-------LLQKLDHPNVVRLKEIVTSKGSAKYKGSIYMVFEYMD-HDLTGLLdNPEVKFTESQIKCYMKQLLEGLQ 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  364 ELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRTlrdMNASHPFNINSQSITniL----PEGL-----YPPEVses 434
Cdd:cd07840  119 YLHSNGILHRDIKGSNILINNDGV---LKLADFGLARP---YTKENNADYTNRVIT--LwyrpPELLlgatrYGPEV--- 187
                        170       180
                 ....*....|....*....|....*...
gi 63054755  435 sfaaasrktDIWCFGLLVLQMLCGAHVL 462
Cdd:cd07840  188 ---------DMWSVGCILAELFTGKPIF 206
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
323-508 4.50e-03

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: 41.23  E-value: 4.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  323 RLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTR-T 401
Cdd:cd05582   71 KLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGH---IKLTDFGLSKeS 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  402 LRDMNASHPFNINSQSITnilpeglypPEVSES---SFAAasrktDIWCFGLLVLQMLCGA---------HVLNKFSSLK 469
Cdd:cd05582  148 IDHEKKAYSFCGTVEYMA---------PEVVNRrghTQSA-----DWWSFGVLMFEMLTGSlpfqgkdrkETMTMILKAK 213
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 63054755  470 LIMTHvipLLPGSYQDLVRRCLMRDSRKR----PSAIDLLSSH 508
Cdd:cd05582  214 LGMPQ---FLSPEAQSLLRALFKRNPANRlgagPDGVEEIKRH 253
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
358-508 4.61e-03

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: 40.70  E-value: 4.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  358 ILEGLAELHRLGISHKSLHLDNvVLFHSGHRTfaKLMDFG-------FTR--TLRDMNASHPFNinsqsitnilpeglyP 428
Cdd:cd14119  106 LIDGLEYLHSQGIIHKDIKPGN-LLLTTDGTL--KISDFGvaealdlFAEddTCTTSQGSPAFQ---------------P 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  429 PEVS--ESSFAAasRKTDIWCFGLLVLQMLCGAH------VLNKFSSLKLIMTHVIPLLPGSYQDLVRRCLMRDSRKRPS 500
Cdd:cd14119  168 PEIAngQDSFSG--FKVDIWSAGVTLYNMTTGKYpfegdnIYKLFENIGKGEYTIPDDVDPDLQDLLRGMLEKDPEKRFT 245

                 ....*...
gi 63054755  501 aIDLLSSH 508
Cdd:cd14119  246 -IEQIRQH 252
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
283-458 4.73e-03

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: 41.17  E-value: 4.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  283 GKREIQELEYELESLKVIRHDLLASI-YEYQLERetrgygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEG 361
Cdd:cd05594   65 AKDEVAHTLTENRVLQNSRHPFLTALkYSFQTHD-------RLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSA 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  362 LAELH-RLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRT-LRDMNASHPFNINsqsitnilPEGLYPPEVSESSFAaa 439
Cdd:cd05594  138 LDYLHsEKNVVYRDLKLENLMLDKDGH---IKITDFGLCKEgIKDGATMKTFCGT--------PEYLAPEVLEDNDYG-- 204
                        170
                 ....*....|....*....
gi 63054755  440 sRKTDIWCFGLLVLQMLCG 458
Cdd:cd05594  205 -RAVDWWGLGVVMYEMMCG 222
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
297-458 5.32e-03

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


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 40.80  E-value: 5.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  297 LKVIRHDLLASI-YEYQLERetrgygwRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSL 375
Cdd:cd05571   49 LQNTRHPFLTSLkYSFQTND-------RLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDL 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  376 HLDNVVLFHSGHrtfAKLMDFG-------FTRTLRDMNAShpfninsqsitnilPEGLyPPEVSESSfaAASRKTDIWCF 448
Cdd:cd05571  122 KLENLLLDKDGH---IKITDFGlckeeisYGATTKTFCGT--------------PEYL-APEVLEDN--DYGRAVDWWGL 181
                        170
                 ....*....|
gi 63054755  449 GLLVLQMLCG 458
Cdd:cd05571  182 GVVMYEMMCG 191
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
323-458 5.61e-03

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: 40.79  E-value: 5.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  323 RLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFTRT- 401
Cdd:cd05618   95 RLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGH---IKLTDYGMCKEg 171
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 63054755  402 LRDMNASHPFninSQSITNILPEGLYPPEVSESsfaaasrkTDIWCFGLLVLQMLCG 458
Cdd:cd05618  172 LRPGDTTSTF---CGTPNYIAPEILRGEDYGFS--------VDWWALGVLMFEMMAG 217
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
324-399 6.09e-03

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: 40.99  E-value: 6.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054755  324 LYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFGFT 399
Cdd:cd05629   76 LYLIMEFLPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGH---IKLSDFGLS 148
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
324-397 6.48e-03

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: 40.79  E-value: 6.48e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63054755  324 LYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHrtfAKLMDFG 397
Cdd:cd05600   86 VYLAMEYVPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGH---IKLTDFG 156
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
358-507 7.26e-03

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


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 40.02  E-value: 7.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  358 ILEGLAELHRLGISHKSLHLDNVVLfhSGHRTfAKLMDFGFTRtlrDMNASHPFNINSQSItniLPEGLYPPE-VSESSF 436
Cdd:cd05032  128 IADGMAYLAAKKFVHRDLAARNCMV--AEDLT-VKIGDFGMTR---DIYETDYYRKGGKGL---LPVRWMAPEsLKDGVF 198
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63054755  437 AAASrktDIWCFGLLVLQMLCGAHV----LNKFSSLKLIMT-HVIPL---LPGSYQDLVRRCLMRDSRKRPSAIDLLSS 507
Cdd:cd05032  199 TTKS---DVWSFGVVLWEMATLAEQpyqgLSNEEVLKFVIDgGHLDLpenCPDKLLELMRMCWQYNPKMRPTFLEIVSS 274
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
323-458 9.68e-03

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: 40.05  E-value: 9.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054755  323 RLYVLQEYSP---------------KFTLFSLLQTVLTLDVetvrafsnnileglaeLHRLGISHKSLHLDNVVLFHSGH 387
Cdd:cd05596  100 YLYMVMDYMPggdlvnlmsnydvpeKWARFYTAEVVLALDA----------------IHSMGFVHRDVKPDNMLLDASGH 163
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054755  388 rtfAKLMDFGftrTLRDMNAshpfNINSQSITNILPEGLYPPEV--SESSFAAASRKTDIWCFGLLVLQMLCG 458
Cdd:cd05596  164 ---LKLADFG---TCMKMDK----DGLVRSDTAVGTPDYISPEVlkSQGGDGVYGRECDWWSVGVFLYEMLVG 226
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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